CINXE.COM

<!DOCTYPE html> <html class="client-nojs vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-feature-night-mode-enabled skin-theme-clientpref-day vector-sticky-header-enabled vector-toc-available" lang="en" dir="ltr"> <head> <meta charset="UTF-8"> <title>Amyloid - Wikipedia</title> <script>(function(){var className="client-js vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-feature-night-mode-enabled skin-theme-clientpref-day vector-sticky-header-enabled vector-toc-available";var cookie=document.cookie.match(/(?:^|; )enwikimwclientpreferences=([^;]+)/);if(cookie){cookie[1].split('%2C').forEach(function(pref){className=className.replace(new RegExp('(^| )'+pref.replace(/-clientpref-\w+$|[^\w-]+/g,'')+'-clientpref-\\w+( |$)'),'$1'+pref+'$2');});}document.documentElement.className=className;}());RLCONF={"wgBreakFrames":false,"wgSeparatorTransformTable":["",""],"wgDigitTransformTable":["",""],"wgDefaultDateFormat":"dmy","wgMonthNames":["","January","February","March","April","May","June","July","August","September","October","November","December"],"wgRequestId":"8b71080a-16ee-46d8-ad98-19548102eb90","wgCanonicalNamespace":"","wgCanonicalSpecialPageName":false,"wgNamespaceNumber":0,"wgPageName":"Amyloid","wgTitle":"Amyloid","wgCurRevisionId":1283153266,"wgRevisionId":1283153266,"wgArticleId":396724,"wgIsArticle":true,"wgIsRedirect":false,"wgAction":"view","wgUserName":null,"wgUserGroups":["*"],"wgCategories":["Articles with short description","Short description is different from Wikidata","Articles containing Latin-language text","Articles containing Ancient Greek (to 1453)-language text","All articles with unsourced statements","Articles with unsourced statements from November 2008","Commons category link is on Wikidata","Amyloidosis","Histopathology","Structural proteins"],"wgPageViewLanguage":"en","wgPageContentLanguage":"en","wgPageContentModel":"wikitext","wgRelevantPageName":"Amyloid","wgRelevantArticleId":396724,"wgIsProbablyEditable":true,"wgRelevantPageIsProbablyEditable":true,"wgRestrictionEdit":[],"wgRestrictionMove":[],"wgNoticeProject":"wikipedia","wgCiteReferencePreviewsActive":false,"wgFlaggedRevsParams":{"tags":{"status":{"levels":1}}},"wgMediaViewerOnClick":true,"wgMediaViewerEnabledByDefault":true,"wgPopupsFlags":0,"wgVisualEditor":{"pageLanguageCode":"en","pageLanguageDir":"ltr","pageVariantFallbacks":"en"},"wgMFDisplayWikibaseDescriptions":{"search":true,"watchlist":true,"tagline":false,"nearby":true},"wgWMESchemaEditAttemptStepOversample":false,"wgWMEPageLength":60000,"wgEditSubmitButtonLabelPublish":true,"wgULSPosition":"interlanguage","wgULSisCompactLinksEnabled":false,"wgVector2022LanguageInHeader":true,"wgULSisLanguageSelectorEmpty":false,"wgWikibaseItemId":"Q6740853","wgCheckUserClientHintsHeadersJsApi":["brands","architecture","bitness","fullVersionList","mobile","model","platform","platformVersion"],"GEHomepageSuggestedEditsEnableTopics":true,"wgGETopicsMatchModeEnabled":false,"wgGELevelingUpEnabledForUser":false}; RLSTATE={"ext.globalCssJs.user.styles":"ready","site.styles":"ready","user.styles":"ready","ext.globalCssJs.user":"ready","user":"ready","user.options":"loading","ext.cite.styles":"ready","ext.math.styles":"ready","skins.vector.search.codex.styles":"ready","skins.vector.styles":"ready","skins.vector.icons":"ready","jquery.tablesorter.styles":"ready","jquery.makeCollapsible.styles":"ready","ext.wikimediamessages.styles":"ready","ext.visualEditor.desktopArticleTarget.noscript":"ready","ext.uls.interlanguage":"ready","wikibase.client.init":"ready"};RLPAGEMODULES=["ext.cite.ux-enhancements","mediawiki.page.media","site","mediawiki.page.ready","jquery.tablesorter","jquery.makeCollapsible","mediawiki.toc","skins.vector.js","ext.centralNotice.geoIP","ext.centralNotice.startUp","ext.gadget.ReferenceTooltips","ext.gadget.switcher","ext.urlShortener.toolbar","ext.centralauth.centralautologin","mmv.bootstrap","ext.popups","ext.visualEditor.desktopArticleTarget.init","ext.visualEditor.targetLoader","ext.echo.centralauth","ext.eventLogging","ext.wikimediaEvents","ext.navigationTiming","ext.uls.interface","ext.cx.eventlogging.campaigns","ext.cx.uls.quick.actions","wikibase.client.vector-2022","ext.checkUser.clientHints","ext.quicksurveys.init","ext.growthExperiments.SuggestedEditSession"];</script> <script>(RLQ=window.RLQ||[]).push(function(){mw.loader.impl(function(){return["user.options@12s5i",function($,jQuery,require,module){mw.user.tokens.set({"patrolToken":"+\\","watchToken":"+\\","csrfToken":"+\\"}); }];});});</script> <link rel="stylesheet" href="/w/load.php?lang=en&modules=ext.cite.styles%7Cext.math.styles%7Cext.uls.interlanguage%7Cext.visualEditor.desktopArticleTarget.noscript%7Cext.wikimediamessages.styles%7Cjquery.makeCollapsible.styles%7Cjquery.tablesorter.styles%7Cskins.vector.icons%2Cstyles%7Cskins.vector.search.codex.styles%7Cwikibase.client.init&only=styles&skin=vector-2022"> <script async="" src="/w/load.php?lang=en&modules=startup&only=scripts&raw=1&skin=vector-2022"></script> <meta name="ResourceLoaderDynamicStyles" content=""> <link rel="stylesheet" href="/w/load.php?lang=en&modules=site.styles&only=styles&skin=vector-2022"> <meta name="generator" content="MediaWiki 1.44.0-wmf.22"> <meta name="referrer" content="origin"> <meta name="referrer" content="origin-when-cross-origin"> <meta name="robots" content="max-image-preview:standard"> <meta name="format-detection" content="telephone=no"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/6/6f/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg"> <meta property="og:image:width" content="1200"> <meta property="og:image:height" content="1118"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/thumb/6/6f/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg/800px-Small_bowel_duodenum_with_amyloid_deposition_20X.jpg"> <meta property="og:image:width" content="800"> <meta property="og:image:height" content="745"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/thumb/6/6f/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg/640px-Small_bowel_duodenum_with_amyloid_deposition_20X.jpg"> <meta property="og:image:width" content="640"> <meta property="og:image:height" content="596"> <meta name="viewport" content="width=1120"> <meta property="og:title" content="Amyloid - Wikipedia"> <meta property="og:type" content="website"> <link rel="preconnect" href="//upload.wikimedia.org"> <link rel="alternate" media="only screen and (max-width: 640px)" href="//en.m.wikipedia.org/wiki/Amyloid"> <link rel="alternate" type="application/x-wiki" title="Edit this page" href="/w/index.php?title=Amyloid&action=edit"> <link rel="apple-touch-icon" href="/static/apple-touch/wikipedia.png"> <link rel="icon" href="/static/favicon/wikipedia.ico"> <link rel="search" type="application/opensearchdescription+xml" href="/w/rest.php/v1/search" title="Wikipedia (en)"> <link rel="EditURI" type="application/rsd+xml" href="//en.wikipedia.org/w/api.php?action=rsd"> <link rel="canonical" href="https://en.wikipedia.org/wiki/Amyloid"> <link rel="license" href="https://creativecommons.org/licenses/by-sa/4.0/deed.en"> <link rel="alternate" type="application/atom+xml" title="Wikipedia Atom feed" href="/w/index.php?title=Special:RecentChanges&feed=atom"> <link rel="dns-prefetch" href="//meta.wikimedia.org" /> <link rel="dns-prefetch" href="auth.wikimedia.org"> </head> <body class="skin--responsive skin-vector skin-vector-search-vue mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject mw-editable page-Amyloid rootpage-Amyloid skin-vector-2022 action-view"><a class="mw-jump-link" href="#bodyContent">Jump to content</a> <div class="vector-header-container"> <header class="vector-header mw-header"> <div class="vector-header-start"> <nav class="vector-main-menu-landmark" aria-label="Site"> <div id="vector-main-menu-dropdown" class="vector-dropdown vector-main-menu-dropdown vector-button-flush-left vector-button-flush-right" title="Main menu" > <input type="checkbox" id="vector-main-menu-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-main-menu-dropdown" class="vector-dropdown-checkbox " aria-label="Main menu" > <label id="vector-main-menu-dropdown-label" for="vector-main-menu-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Main menu </label> <div class="vector-dropdown-content"> <div id="vector-main-menu-unpinned-container" class="vector-unpinned-container"> <div id="vector-main-menu" class="vector-main-menu vector-pinnable-element"> <div class="vector-pinnable-header vector-main-menu-pinnable-header vector-pinnable-header-unpinned" data-feature-name="main-menu-pinned" data-pinnable-element-id="vector-main-menu" data-pinned-container-id="vector-main-menu-pinned-container" data-unpinned-container-id="vector-main-menu-unpinned-container" > <div class="vector-pinnable-header-label">Main menu</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-main-menu.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-main-menu.unpin">hide</button> </div> <div id="p-navigation" class="vector-menu mw-portlet mw-portlet-navigation" > <div class="vector-menu-heading"> Navigation </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="n-mainpage-description" class="mw-list-item"><a href="/wiki/Main_Page" title="Visit the main page [z]" accesskey="z">Main page</a></li><li id="n-contents" class="mw-list-item"><a href="/wiki/Wikipedia:Contents" title="Guides to browsing Wikipedia">Contents</a></li><li id="n-currentevents" class="mw-list-item"><a href="/wiki/Portal:Current_events" title="Articles related to current events">Current events</a></li><li id="n-randompage" class="mw-list-item"><a href="/wiki/Special:Random" title="Visit a randomly selected article [x]" accesskey="x">Random article</a></li><li id="n-aboutsite" class="mw-list-item"><a href="/wiki/Wikipedia:About" title="Learn about Wikipedia and how it works">About Wikipedia</a></li><li id="n-contactpage" class="mw-list-item"><a href="//en.wikipedia.org/wiki/Wikipedia:Contact_us" title="How to contact Wikipedia">Contact us</a></li> </ul> </div> </div> <div id="p-interaction" class="vector-menu mw-portlet mw-portlet-interaction" > <div class="vector-menu-heading"> Contribute </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="n-help" class="mw-list-item"><a href="/wiki/Help:Contents" title="Guidance on how to use and edit Wikipedia">Help</a></li><li id="n-introduction" class="mw-list-item"><a href="/wiki/Help:Introduction" title="Learn how to edit Wikipedia">Learn to edit</a></li><li id="n-portal" class="mw-list-item"><a href="/wiki/Wikipedia:Community_portal" title="The hub for editors">Community portal</a></li><li id="n-recentchanges" class="mw-list-item"><a href="/wiki/Special:RecentChanges" title="A list of recent changes to Wikipedia [r]" accesskey="r">Recent changes</a></li><li id="n-upload" class="mw-list-item"><a href="/wiki/Wikipedia:File_upload_wizard" title="Add images or other media for use on Wikipedia">Upload file</a></li><li id="n-specialpages" class="mw-list-item"><a href="/wiki/Special:SpecialPages">Special pages</a></li> </ul> </div> </div> </div> </div> </div> </div> </nav> <a href="/wiki/Main_Page" class="mw-logo"> <img class="mw-logo-icon" src="/static/images/icons/wikipedia.png" alt="" aria-hidden="true" height="50" width="50"> <img class="mw-logo-wordmark" alt="Wikipedia" src="/static/images/mobile/copyright/wikipedia-wordmark-en.svg" style="width: 7.5em; height: 1.125em;"> <img class="mw-logo-tagline" alt="The Free Encyclopedia" src="/static/images/mobile/copyright/wikipedia-tagline-en.svg" width="117" height="13" style="width: 7.3125em; height: 0.8125em;"> </a> </div> <div class="vector-header-end"> <div id="p-search" role="search" class="vector-search-box-vue vector-search-box-collapses vector-search-box-show-thumbnail vector-search-box-auto-expand-width vector-search-box"> <a href="/wiki/Special:Search" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only search-toggle" title="Search Wikipedia [f]" accesskey="f"> Search </a> <div class="vector-typeahead-search-container"> <div class="cdx-typeahead-search cdx-typeahead-search--show-thumbnail cdx-typeahead-search--auto-expand-width"> <form action="/w/index.php" id="searchform" class="cdx-search-input cdx-search-input--has-end-button"> <div id="simpleSearch" class="cdx-search-input__input-wrapper" data-search-loc="header-moved"> <div class="cdx-text-input cdx-text-input--has-start-icon"> <input class="cdx-text-input__input" type="search" name="search" placeholder="Search Wikipedia" aria-label="Search Wikipedia" autocapitalize="sentences" title="Search Wikipedia [f]" accesskey="f" id="searchInput" > </div> <input type="hidden" name="title" value="Special:Search"> </div> <button class="cdx-button cdx-search-input__end-button">Search</button> </form> </div> </div> </div> <nav class="vector-user-links vector-user-links-wide" aria-label="Personal tools"> <div class="vector-user-links-main"> <div id="p-vector-user-menu-preferences" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <div id="p-vector-user-menu-userpage" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-dropdown" class="vector-dropdown " title="Change the appearance of the page's font size, width, and color" > <input type="checkbox" id="vector-appearance-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-appearance-dropdown" class="vector-dropdown-checkbox " aria-label="Appearance" > <label id="vector-appearance-dropdown-label" for="vector-appearance-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Appearance </label> <div class="vector-dropdown-content"> <div id="vector-appearance-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <div id="p-vector-user-menu-notifications" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <div id="p-vector-user-menu-overflow" class="vector-menu mw-portlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-sitesupport-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="https://donate.wikimedia.org/?wmf_source=donate&wmf_medium=sidebar&wmf_campaign=en.wikipedia.org&uselang=en" class="">Donate</a> </li> <li id="pt-createaccount-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="/w/index.php?title=Special:CreateAccount&returnto=Amyloid" title="You are encouraged to create an account and log in; however, it is not mandatory" class="">Create account</a> </li> <li id="pt-login-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="/w/index.php?title=Special:UserLogin&returnto=Amyloid" title="You're encouraged to log in; however, it's not mandatory. [o]" accesskey="o" class="">Log in</a> </li> </ul> </div> </div> </div> <div id="vector-user-links-dropdown" class="vector-dropdown vector-user-menu vector-button-flush-right vector-user-menu-logged-out" title="Log in and more options" > <input type="checkbox" id="vector-user-links-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-user-links-dropdown" class="vector-dropdown-checkbox " aria-label="Personal tools" > <label id="vector-user-links-dropdown-label" for="vector-user-links-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Personal tools </label> <div class="vector-dropdown-content"> <div id="p-personal" class="vector-menu mw-portlet mw-portlet-personal user-links-collapsible-item" title="User menu" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-sitesupport" class="user-links-collapsible-item mw-list-item"><a href="https://donate.wikimedia.org/?wmf_source=donate&wmf_medium=sidebar&wmf_campaign=en.wikipedia.org&uselang=en">Donate</a></li><li id="pt-createaccount" class="user-links-collapsible-item mw-list-item"><a href="/w/index.php?title=Special:CreateAccount&returnto=Amyloid" title="You are encouraged to create an account and log in; however, it is not mandatory"> Create account</a></li><li id="pt-login" class="user-links-collapsible-item mw-list-item"><a href="/w/index.php?title=Special:UserLogin&returnto=Amyloid" title="You're encouraged to log in; however, it's not mandatory. [o]" accesskey="o"> Log in</a></li> </ul> </div> </div> <div id="p-user-menu-anon-editor" class="vector-menu mw-portlet mw-portlet-user-menu-anon-editor" > <div class="vector-menu-heading"> Pages for logged out editors <a href="/wiki/Help:Introduction" aria-label="Learn more about editing">learn more</a> </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-anoncontribs" class="mw-list-item"><a href="/wiki/Special:MyContributions" title="A list of edits made from this IP address [y]" accesskey="y">Contributions</a></li><li id="pt-anontalk" class="mw-list-item"><a href="/wiki/Special:MyTalk" title="Discussion about edits from this IP address [n]" accesskey="n">Talk</a></li> </ul> </div> </div> </div> </div> </nav> </div> </header> </div> <div class="mw-page-container"> <div class="mw-page-container-inner"> <div class="vector-sitenotice-container"> <div id="siteNotice"></div> </div> <div class="vector-column-start"> <div class="vector-main-menu-container"> <div id="mw-navigation"> <nav id="mw-panel" class="vector-main-menu-landmark" aria-label="Site"> <div id="vector-main-menu-pinned-container" class="vector-pinned-container"> </div> </nav> </div> </div> <div class="vector-sticky-pinned-container"> <nav id="mw-panel-toc" aria-label="Contents" data-event-name="ui.sidebar-toc" class="mw-table-of-contents-container vector-toc-landmark"> <div id="vector-toc-pinned-container" class="vector-pinned-container"> <div id="vector-toc" class="vector-toc vector-pinnable-element"> <div class="vector-pinnable-header vector-toc-pinnable-header vector-pinnable-header-pinned" data-feature-name="toc-pinned" data-pinnable-element-id="vector-toc" > <h2 class="vector-pinnable-header-label">Contents</h2> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-toc.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-toc.unpin">hide</button> </div> <ul class="vector-toc-contents" id="mw-panel-toc-list"> <li id="toc-mw-content-text" class="vector-toc-list-item vector-toc-level-1"> <a href="#" class="vector-toc-link"> <div class="vector-toc-text">(Top)</div> </a> </li> <li id="toc-Definition" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Definition"> <div class="vector-toc-text"> 1 Definition </div> </a> <ul id="toc-Definition-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Proteins_forming_amyloids_in_diseases" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Proteins_forming_amyloids_in_diseases"> <div class="vector-toc-text"> 2 Proteins forming amyloids in diseases </div> </a> <ul id="toc-Proteins_forming_amyloids_in_diseases-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Non-disease_and_functional_amyloids" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Non-disease_and_functional_amyloids"> <div class="vector-toc-text"> 3 Non-disease and functional amyloids </div> </a> <ul id="toc-Non-disease_and_functional_amyloids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Structure" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Structure"> <div class="vector-toc-text"> 4 Structure </div> </a> <ul id="toc-Structure-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Formation" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Formation"> <div class="vector-toc-text"> 5 Formation </div> </a> <ul id="toc-Formation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Amino_acid_sequence_and_amyloid_formation" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Amino_acid_sequence_and_amyloid_formation"> <div class="vector-toc-text"> 6 Amino acid sequence and amyloid formation </div> </a> <ul id="toc-Amino_acid_sequence_and_amyloid_formation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Amyloid_toxicity" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Amyloid_toxicity"> <div class="vector-toc-text"> 7 Amyloid toxicity </div> </a> <ul id="toc-Amyloid_toxicity-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Histological_staining" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Histological_staining"> <div class="vector-toc-text"> 8 Histological staining </div> </a> <ul id="toc-Histological_staining-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> 9 See also </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> 10 References </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> 11 External links </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" title="Table of Contents" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Toggle the table of contents </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading">Amyloid</h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 18 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-18" aria-hidden="true" > 18 languages </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D9%86%D8%B4%D9%88%D8%A7%D9%86%D9%8A" title="نشواني – Arabic" lang="ar" hreflang="ar" data-title="نشواني" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target">العربية</a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Amiloid" title="Amiloid – Bosnian" lang="bs" hreflang="bs" data-title="Amiloid" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target">Bosanski</a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Amiloide" title="Amiloide – Catalan" lang="ca" hreflang="ca" data-title="Amiloide" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target">Català</a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Amyloid" title="Amyloid – Czech" lang="cs" hreflang="cs" data-title="Amyloid" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target">Čeština</a></li><li class="interlanguage-link interwiki-eu mw-list-item"><a href="https://eu.wikipedia.org/wiki/Amiloide" title="Amiloide – Basque" lang="eu" hreflang="eu" data-title="Amiloide" data-language-autonym="Euskara" data-language-local-name="Basque" class="interlanguage-link-target">Euskara</a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Substance_amylo%C3%AFde" title="Substance amyloïde – French" lang="fr" hreflang="fr" data-title="Substance amyloïde" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target">Français</a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Amiloide" title="Amiloide – Galician" lang="gl" hreflang="gl" data-title="Amiloide" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target">Galego</a></li><li class="interlanguage-link interwiki-he mw-list-item"><a href="https://he.wikipedia.org/wiki/%D7%A2%D7%9E%D7%99%D7%9C%D7%95%D7%90%D7%99%D7%93" title="עמילואיד – Hebrew" lang="he" hreflang="he" data-title="עמילואיד" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target">עברית</a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%A2%E3%83%9F%E3%83%AD%E3%82%A4%E3%83%89" title="アミロイド – Japanese" lang="ja" hreflang="ja" data-title="アミロイド" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target">日本語</a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Amyloid" title="Amyloid – Polish" lang="pl" hreflang="pl" data-title="Amyloid" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target">Polski</a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Amiloide" title="Amiloide – Portuguese" lang="pt" hreflang="pt" data-title="Amiloide" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target">Português</a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Amiloid" title="Amiloid – Serbian" lang="sr" hreflang="sr" data-title="Amiloid" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target">Српски / srpski</a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Amiloid" title="Amiloid – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Amiloid" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target">Srpskohrvatski / српскохрватски</a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Amyloidi" title="Amyloidi – Finnish" lang="fi" hreflang="fi" data-title="Amyloidi" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target">Suomi</a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Amyloid" title="Amyloid – Swedish" lang="sv" hreflang="sv" data-title="Amyloid" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target">Svenska</a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B9%81%E0%B8%AD%E0%B8%A1%E0%B8%B5%E0%B8%A5%E0%B8%AD%E0%B8%A2%E0%B8%94%E0%B9%8C" title="แอมีลอยด์ – Thai" lang="th" hreflang="th" data-title="แอมีลอยด์" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target">ไทย</a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%90%D0%BC%D1%96%D0%BB%D0%BE%D1%97%D0%B4" title="Амілоїд – Ukrainian" lang="uk" hreflang="uk" data-title="Амілоїд" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target">Українська</a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E9%A1%9E%E6%BE%B1%E7%B2%89%E8%9B%8B%E7%99%BD" title="類澱粉蛋白 – Chinese" lang="zh" hreflang="zh" data-title="類澱粉蛋白" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target">中文</a></li> </ul> <div class="after-portlet after-portlet-lang"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q6740853#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></div> </div> </div> </div> </header> <div class="vector-page-toolbar"> <div class="vector-page-toolbar-container"> <div id="left-navigation"> <nav aria-label="Namespaces"> <div id="p-associated-pages" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-associated-pages" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-nstab-main" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Amyloid" title="View the content page [c]" accesskey="c">Article</a></li><li id="ca-talk" class="vector-tab-noicon mw-list-item"><a href="/wiki/Talk:Amyloid" rel="discussion" title="Discuss improvements to the content page [t]" accesskey="t">Talk</a></li> </ul> </div> </div> <div id="vector-variants-dropdown" class="vector-dropdown emptyPortlet" > <input type="checkbox" id="vector-variants-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-variants-dropdown" class="vector-dropdown-checkbox " aria-label="Change language variant" > <label id="vector-variants-dropdown-label" for="vector-variants-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet" aria-hidden="true" >English </label> <div class="vector-dropdown-content"> <div id="p-variants" class="vector-menu mw-portlet mw-portlet-variants emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> </div> </div> </nav> </div> <div id="right-navigation" class="vector-collapsible"> <nav aria-label="Views"> <div id="p-views" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-views" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-view" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Amyloid">Read</a></li><li id="ca-edit" class="vector-tab-noicon mw-list-item"><a href="/w/index.php?title=Amyloid&action=edit" title="Edit this page [e]" accesskey="e">Edit</a></li><li id="ca-history" class="vector-tab-noicon mw-list-item"><a href="/w/index.php?title=Amyloid&action=history" title="Past revisions of this page [h]" accesskey="h">View history</a></li> </ul> </div> </div> </nav> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-dropdown" class="vector-dropdown vector-page-tools-dropdown" > <input type="checkbox" id="vector-page-tools-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-tools-dropdown" class="vector-dropdown-checkbox " aria-label="Tools" > <label id="vector-page-tools-dropdown-label" for="vector-page-tools-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet" aria-hidden="true" >Tools </label> <div class="vector-dropdown-content"> <div id="vector-page-tools-unpinned-container" class="vector-unpinned-container"> <div id="vector-page-tools" class="vector-page-tools vector-pinnable-element"> <div class="vector-pinnable-header vector-page-tools-pinnable-header vector-pinnable-header-unpinned" data-feature-name="page-tools-pinned" data-pinnable-element-id="vector-page-tools" data-pinned-container-id="vector-page-tools-pinned-container" data-unpinned-container-id="vector-page-tools-unpinned-container" > <div class="vector-pinnable-header-label">Tools</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-page-tools.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-page-tools.unpin">hide</button> </div> <div id="p-cactions" class="vector-menu mw-portlet mw-portlet-cactions emptyPortlet vector-has-collapsible-items" title="More options" > <div class="vector-menu-heading"> Actions </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-more-view" class="selected vector-more-collapsible-item mw-list-item"><a href="/wiki/Amyloid">Read</a></li><li id="ca-more-edit" class="vector-more-collapsible-item mw-list-item"><a href="/w/index.php?title=Amyloid&action=edit" title="Edit this page [e]" accesskey="e">Edit</a></li><li id="ca-more-history" class="vector-more-collapsible-item mw-list-item"><a href="/w/index.php?title=Amyloid&action=history">View history</a></li> </ul> </div> </div> <div id="p-tb" class="vector-menu mw-portlet mw-portlet-tb" > <div class="vector-menu-heading"> General </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="t-whatlinkshere" class="mw-list-item"><a href="/wiki/Special:WhatLinksHere/Amyloid" title="List of all English Wikipedia pages containing links to this page [j]" accesskey="j">What links here</a></li><li id="t-recentchangeslinked" class="mw-list-item"><a href="/wiki/Special:RecentChangesLinked/Amyloid" rel="nofollow" title="Recent changes in pages linked from this page [k]" accesskey="k">Related changes</a></li><li id="t-upload" class="mw-list-item"><a href="//en.wikipedia.org/wiki/Wikipedia:File_Upload_Wizard" title="Upload files [u]" accesskey="u">Upload file</a></li><li id="t-permalink" class="mw-list-item"><a href="/w/index.php?title=Amyloid&oldid=1283153266" title="Permanent link to this revision of this page">Permanent link</a></li><li id="t-info" class="mw-list-item"><a href="/w/index.php?title=Amyloid&action=info" title="More information about this page">Page information</a></li><li id="t-cite" class="mw-list-item"><a href="/w/index.php?title=Special:CiteThisPage&page=Amyloid&id=1283153266&wpFormIdentifier=titleform" title="Information on how to cite this page">Cite this page</a></li><li id="t-urlshortener" class="mw-list-item"><a href="/w/index.php?title=Special:UrlShortener&url=https%3A%2F%2Fen.wikipedia.org%2Fwiki%2FAmyloid">Get shortened URL</a></li><li id="t-urlshortener-qrcode" class="mw-list-item"><a href="/w/index.php?title=Special:QrCode&url=https%3A%2F%2Fen.wikipedia.org%2Fwiki%2FAmyloid">Download QR code</a></li> </ul> </div> </div> <div id="p-coll-print_export" class="vector-menu mw-portlet mw-portlet-coll-print_export" > <div class="vector-menu-heading"> Print/export </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="coll-download-as-rl" class="mw-list-item"><a href="/w/index.php?title=Special:DownloadAsPdf&page=Amyloid&action=show-download-screen" title="Download this page as a PDF file">Download as PDF</a></li><li id="t-print" class="mw-list-item"><a href="/w/index.php?title=Amyloid&printable=yes" title="Printable version of this page [p]" accesskey="p">Printable version</a></li> </ul> </div> </div> <div id="p-wikibase-otherprojects" class="vector-menu mw-portlet mw-portlet-wikibase-otherprojects" > <div class="vector-menu-heading"> In other projects </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="wb-otherproject-link wb-otherproject-commons mw-list-item"><a href="https://commons.wikimedia.org/wiki/Category:Amyloid" hreflang="en">Wikimedia Commons</a></li><li id="t-wikibase" class="wb-otherproject-link wb-otherproject-wikibase-dataitem mw-list-item"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q6740853" title="Structured data on this page hosted by Wikidata [g]" accesskey="g">Wikidata item</a></li> </ul> </div> </div> </div> </div> </div> </div> </nav> </div> </div> </div> <div class="vector-column-end"> <div class="vector-sticky-pinned-container"> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-pinned-container" class="vector-pinned-container"> </div> </nav> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-pinned-container" class="vector-pinned-container"> <div id="vector-appearance" class="vector-appearance vector-pinnable-element"> <div class="vector-pinnable-header vector-appearance-pinnable-header vector-pinnable-header-pinned" data-feature-name="appearance-pinned" data-pinnable-element-id="vector-appearance" data-pinned-container-id="vector-appearance-pinned-container" data-unpinned-container-id="vector-appearance-unpinned-container" > <div class="vector-pinnable-header-label">Appearance</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-appearance.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-appearance.unpin">hide</button> </div> </div> </div> </nav> </div> </div> <div id="bodyContent" class="vector-body" aria-labelledby="firstHeading" data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Insoluble protein aggregate with a fibrillar morphology</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">For other uses, see <a href="/wiki/Amyloid_(disambiguation)" class="mw-disambig" title="Amyloid (disambiguation)">Amyloid (disambiguation)</a>.</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Small_bowel_duodenum_with_amyloid_deposition_20X.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6f/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg/220px-Small_bowel_duodenum_with_amyloid_deposition_20X.jpg" decoding="async" width="220" height="205" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6f/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg/330px-Small_bowel_duodenum_with_amyloid_deposition_20X.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/6f/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg/440px-Small_bowel_duodenum_with_amyloid_deposition_20X.jpg 2x" data-file-width="1200" data-file-height="1118" /></a><figcaption><a href="/wiki/Micrograph" title="Micrograph">Micrograph</a> showing amyloid deposits (pink) in <a href="/wiki/Small_bowel" class="mw-redirect" title="Small bowel">small bowel</a>. Duodenum with amyloid deposition in lamina propria. Amyloid shows up as homogeneous pink material in lamina propria and around blood vessels. 20× magnification. </figcaption></figure> Amyloids are aggregates of <a href="/wiki/Protein" title="Protein">proteins</a> characterised by a <a href="/wiki/Fibril" title="Fibril">fibrillar</a> morphology of typically 7–13 <a href="/wiki/Nanometer" class="mw-redirect" title="Nanometer">nm</a> in <a href="/wiki/Diameter" title="Diameter">diameter</a>, a <a href="/wiki/Beta_sheet" title="Beta sheet">β-sheet</a> <a href="/wiki/Secondary_structure_of_proteins" class="mw-redirect" title="Secondary structure of proteins">secondary structure</a> (known as cross-β) and ability to be <a href="/wiki/Staining" title="Staining">stained</a> by particular dyes, such as <a href="/wiki/Congo_red" title="Congo red">Congo red</a>.<a href="#cite_note-pmid9356260-1">[1]</a> In the <a href="/wiki/Human_body" title="Human body">human body</a>, amyloids have been linked to the development of various <a href="/wiki/Disease" title="Disease">diseases</a>.<a href="#cite_note-pmid28498720-2">[2]</a> Pathogenic amyloids form when previously healthy proteins lose their normal <a href="/wiki/Protein_structure" title="Protein structure">structure</a> and <a href="/wiki/Physiology" title="Physiology">physiological</a> functions (<a href="/wiki/Protein_misfolding" class="mw-redirect" title="Protein misfolding">misfolding</a>) and form fibrous deposits within and around cells. These protein misfolding and deposition processes disrupt the healthy function of tissues and organs. Such amyloids have been associated with (but not necessarily as the cause of) more than 50<a href="#cite_note-pmid28498720-2">[2]</a><a href="#cite_note-pmid30614283-3">[3]</a> human diseases, known as <a href="/wiki/Amyloidosis" title="Amyloidosis">amyloidosis</a>, and may play a role in some <a href="/wiki/Neurodegenerative_diseases" class="mw-redirect" title="Neurodegenerative diseases">neurodegenerative diseases</a>.<a href="#cite_note-pmid28498720-2">[2]</a><a href="#cite_note-4">[4]</a> Some of these diseases are mainly sporadic and only a few cases are <a href="/wiki/Genetic_disorder" title="Genetic disorder">familial</a>. Others are only <a href="/wiki/Genetic_disorder" title="Genetic disorder">familial</a>. Some <a href="/wiki/Iatrogenic" class="mw-redirect" title="Iatrogenic">result from medical treatment</a>. <a href="/wiki/Prion" title="Prion">Prions</a> are an <a href="/wiki/Infectious" class="mw-redirect" title="Infectious">infectious</a> form of amyloids that can act as a template to convert other non-infectious forms.<a href="#cite_note-5">[5]</a> Amyloids may also have normal biological functions; for example, in the formation of <a href="/wiki/Fimbria_(bacteriology)" class="mw-redirect" title="Fimbria (bacteriology)">fimbriae</a> in some <a href="/wiki/Genus" title="Genus">genera</a> of <a href="/wiki/Bacteria" title="Bacteria">bacteria</a>, transmission of epigenetic traits in fungi, as well as pigment deposition and hormone release in humans.<a href="#cite_note-ann_rev_biochem_2011-6">[6]</a> Amyloids have been known to arise from many different proteins.<a href="#cite_note-pmid28498720-2">[2]</a><a href="#cite_note-7">[7]</a> These polypeptide chains generally form <a href="/wiki/Beta_sheet" title="Beta sheet">β-sheet</a> structures that aggregate into long fibers; however, identical polypeptides can fold into multiple distinct amyloid conformations.<a href="#cite_note-pm11076514-8">[8]</a> The diversity of the conformations may have led to different forms of the <a href="/wiki/Prion" title="Prion">prion</a> diseases.<a href="#cite_note-ann_rev_biochem_2011-6">[6]</a> An unusual secondary structure named <a href="/wiki/Alpha_sheet" title="Alpha sheet">α sheet</a> has been proposed as the toxic constituent of amyloid precursor proteins,<a href="#cite_note-alphasheet-9">[9]</a> but this idea is not widely accepted at present. <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:2rnm.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/45/2rnm.jpg/240px-2rnm.jpg" decoding="async" width="240" height="192" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/45/2rnm.jpg/360px-2rnm.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/45/2rnm.jpg/480px-2rnm.jpg 2x" data-file-width="1000" data-file-height="800" /></a><figcaption>Amyloid of HET-s(218-289) prion pentamer, Podospora anserina (<a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/2rnm">2rnm</a>)</figcaption></figure> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Definition">Definition</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=1" title="Edit section: Definition">edit</a>]</div> The name amyloid comes from the early mistaken identification by <a href="/wiki/Rudolf_Virchow" title="Rudolf Virchow">Rudolf Virchow</a> of the substance as <a href="/wiki/Starch" title="Starch">starch</a> (amylum in <a href="/wiki/Latin" title="Latin">Latin</a>, from <a href="/wiki/Ancient_Greek_language" class="mw-redirect" title="Ancient Greek language">Ancient Greek</a>: ἄμυλον, <a href="/wiki/Romanization_of_Ancient_Greek" class="mw-redirect" title="Romanization of Ancient Greek">romanized</a>: amylon), based on crude <a href="/wiki/Iodine-staining" class="mw-redirect" title="Iodine-staining">iodine-staining</a> techniques. For a period, the scientific community debated whether or not amyloid deposits are <a href="/wiki/Lipid" title="Lipid">fatty</a> deposits or <a href="/wiki/Carbohydrate" title="Carbohydrate">carbohydrate</a> deposits until it was finally found (in 1859) that they are, in fact, deposits of <a href="/wiki/Albumin" title="Albumin">albumoid</a> proteinaceous material.<a href="#cite_note-10">[10]</a> <ul><li>The classical, <a href="/wiki/Histopathology" title="Histopathology">histopathological</a> definition of amyloid is an extracellular, proteinaceous <a href="/wiki/Fibrillar" class="mw-redirect" title="Fibrillar">fibrillar</a> deposit exhibiting <a href="/wiki/%CE%92-sheet" class="mw-redirect" title="Β-sheet">β-sheet</a> <a href="/wiki/Secondary_structure_of_proteins" class="mw-redirect" title="Secondary structure of proteins">secondary structure</a> and identified by apple-green <a href="/wiki/Birefringence" title="Birefringence">birefringence</a> when stained with <a href="/wiki/Congo_red" title="Congo red">congo red</a> under <a href="/wiki/Polarization_(waves)" title="Polarization (waves)">polarized light</a>. These deposits often recruit various sugars and other components such as <a href="/wiki/Serum_amyloid_P_component" title="Serum amyloid P component">serum amyloid P component</a>, resulting in complex, and sometimes inhomogeneous structures.<a href="#cite_note-11">[11]</a> Recently this definition has come into question as some classic, amyloid species have been observed in distinctly intracellular locations.<a href="#cite_note-pmid17353506-12">[12]</a></li> <li>A more recent, <a href="/wiki/Biophysics" title="Biophysics">biophysical</a> definition is broader, including any polypeptide that polymerizes to form a cross-β structure, in vivo or in vitro, inside or outside <a href="/wiki/Cell_(biology)" title="Cell (biology)">cells</a>. <a href="/wiki/Microbiologists" class="mw-redirect" title="Microbiologists">Microbiologists</a>, <a href="/wiki/Biochemists" class="mw-redirect" title="Biochemists">biochemists</a>, <a href="/wiki/Biophysicists" class="mw-redirect" title="Biophysicists">biophysicists</a>, <a href="/wiki/Chemists" class="mw-redirect" title="Chemists">chemists</a> and <a href="/wiki/Physicists" class="mw-redirect" title="Physicists">physicists</a> have largely adopted this definition,<a href="#cite_note-pmid15283924-13">[13]</a><a href="#cite_note-pmid17530168-14">[14]</a> leading to some conflict in the biological community over an <a href="/wiki/Linguistic_prescription" title="Linguistic prescription">issue of language</a>.</li></ul> <div class="mw-heading mw-heading2"><h2 id="Proteins_forming_amyloids_in_diseases">Proteins forming amyloids in diseases</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=2" title="Edit section: Proteins forming amyloids in diseases">edit</a>]</div> To date, 37 human <a href="/wiki/Proteins" class="mw-redirect" title="Proteins">proteins</a> have been found to form amyloid in <a href="/wiki/Pathology" title="Pathology">pathology</a> and be associated with well-defined <a href="/wiki/Diseases" class="mw-redirect" title="Diseases">diseases</a>.<a href="#cite_note-pmid28498720-2">[2]</a> The International Society of Amyloidosis classifies amyloid fibrils and their associated diseases based upon associated proteins (for example ATTR is the group of diseases and associated fibrils formed by <a href="/wiki/Transthyretin" title="Transthyretin">TTR</a>).<a href="#cite_note-pmid30614283-3">[3]</a> A table is included below. <table class="sortable wikitable"> <tbody><tr> <th>Protein </th> <th>Diseases </th> <th>Official abbreviation </th></tr> <tr> <td><a href="/wiki/%CE%92_amyloid" class="mw-redirect" title="Β amyloid">β amyloid peptide</a> (<a href="/wiki/Beta_amyloid" class="mw-redirect" title="Beta amyloid">Aβ</a>) from <a href="/wiki/Amyloid_precursor_protein" class="mw-redirect" title="Amyloid precursor protein">Amyloid precursor protein</a><a href="#cite_note-pmid18781964-15">[15]</a><a href="#cite_note-pmid18368143-16">[16]</a><a href="#cite_note-pmid17505973-17">[17]</a><a href="#cite_note-pmid22813427-18">[18]</a> </td> <td><a href="/wiki/Alzheimer%27s_disease" title="Alzheimer's disease">Alzheimer's disease</a>, <a href="/wiki/Hereditary_cystatin_C_amyloid_angiopathy" title="Hereditary cystatin C amyloid angiopathy">Hereditary cerebral haemorrhage with amyloidosis</a> </td> <td>Aβ </td></tr> <tr> <td><a href="/wiki/%CE%91-synuclein" class="mw-redirect" title="Α-synuclein">α-synuclein</a><a href="#cite_note-pmid18368143-16">[16]</a> </td> <td><a href="/wiki/Parkinson%27s_disease" title="Parkinson's disease">Parkinson's disease</a>, <a href="/wiki/Parkinson%27s_disease_dementia" title="Parkinson's disease dementia">Parkinson's disease dementia</a>, <a href="/wiki/Dementia_with_Lewy_bodies" title="Dementia with Lewy bodies">Dementia with Lewy bodies</a>, <a href="/wiki/Multiple_system_atrophy" title="Multiple system atrophy">Multiple system atrophy</a> </td> <td>AαSyn </td></tr> <tr> <td><a href="/wiki/Prion" title="Prion">PrPSc</a><a href="#cite_note-19">[19]</a> </td> <td><a href="/wiki/Transmissible_spongiform_encephalopathy" title="Transmissible spongiform encephalopathy">Transmissible spongiform encephalopathy</a> (e.g. <a href="/wiki/Fatal_familial_insomnia" class="mw-redirect" title="Fatal familial insomnia">Fatal familial insomnia</a>, <a href="/wiki/Gerstmann-Str%C3%A4ussler-Scheinker_disease" class="mw-redirect" title="Gerstmann-Sträussler-Scheinker disease">Gerstmann-Sträussler-Scheinker disease</a>, <a href="/wiki/Creutzfeldt%E2%80%93Jakob_disease" title="Creutzfeldt–Jakob disease">Creutzfeldt–Jakob disease</a>, <a href="/wiki/New_variant_Creutzfeldt-Jakob_disease" class="mw-redirect" title="New variant Creutzfeldt-Jakob disease">New variant Creutzfeldt–Jakob disease</a>) </td> <td>APrP </td></tr> <tr> <td><a href="/wiki/Microtubule-associated_protein_tau" class="mw-redirect" title="Microtubule-associated protein tau">Microtubule-associated protein tau</a> </td> <td>Various forms of <a href="/wiki/Tauopathies" class="mw-redirect" title="Tauopathies">tauopathies</a> (e.g. <a href="/wiki/Pick%27s_disease" class="mw-redirect" title="Pick's disease">Pick's disease</a>, <a href="/wiki/Progressive_supranuclear_palsy" title="Progressive supranuclear palsy">Progressive supranuclear palsy</a>, <a href="/wiki/Corticobasal_degeneration" title="Corticobasal degeneration">Corticobasal degeneration</a>, <a href="/wiki/Frontotemporal_dementia_with_parkinsonism" class="mw-redirect" title="Frontotemporal dementia with parkinsonism">Frontotemporal dementia with parkinsonism linked to chromosome 17</a>, <a href="/wiki/Argyrophilic_grain_disease" class="mw-redirect" title="Argyrophilic grain disease">Argyrophilic grain disease</a>) </td> <td>ATau </td></tr> <tr> <td><a href="/wiki/Huntingtin" title="Huntingtin">Huntingtin exon 1</a><a href="#cite_note-pmid18637947-20">[20]</a><a href="#cite_note-pmid16848688-21">[21]</a> </td> <td><a href="/wiki/Huntington%27s_disease" title="Huntington's disease">Huntington's disease</a> </td> <td>HTTex1 </td></tr> <tr> <td><a href="/wiki/ITM2B" title="ITM2B">ABri peptide</a> </td> <td><a href="/wiki/Familial_British_dementia" title="Familial British dementia">Familial British dementia</a> </td> <td>ABri </td></tr> <tr> <td><a href="/wiki/ITM2B" title="ITM2B">ADan peptide</a> </td> <td><a href="/wiki/Familial_Danish_dementia" title="Familial Danish dementia">Familial Danish dementia</a> </td> <td>ADan </td></tr> <tr> <td>Fragments of <a href="/wiki/Immunoglobulin_light_chains" class="mw-redirect" title="Immunoglobulin light chains">immunoglobulin light chains</a><a href="#cite_note-emedicine.medscape.com-22">[22]</a> </td> <td><a href="/wiki/Primary_systemic_amyloidosis" class="mw-redirect" title="Primary systemic amyloidosis">Light chain amyloidosis</a> </td> <td>AL </td></tr> <tr> <td>Fragments of <a href="/wiki/Immunoglobulin_heavy_chains" class="mw-redirect" title="Immunoglobulin heavy chains">immunoglobulin heavy chains</a><a href="#cite_note-emedicine.medscape.com-22">[22]</a> </td> <td>Heavy chain amyloidosis </td> <td>AH </td></tr> <tr> <td>full length of N-terminal fragments of <a href="/wiki/Serum_amyloid_A_protein" class="mw-redirect" title="Serum amyloid A protein">Serum amyloid A protein</a> </td> <td><a href="/wiki/AA_amyloidosis" title="AA amyloidosis">AA amyloidosis</a> </td> <td>AA </td></tr> <tr> <td><a href="/wiki/Transthyretin" title="Transthyretin">Transthyretin</a> </td> <td><a href="/wiki/Senile_systemic_amyloidosis" class="mw-redirect" title="Senile systemic amyloidosis">Senile systemic amyloidosis</a>, <a href="/wiki/Familial_amyloid_polyneuropathy" title="Familial amyloid polyneuropathy">Familial amyloid polyneuropathy</a>, <a href="/wiki/Familial_amyloid_cardiomyopathy" title="Familial amyloid cardiomyopathy">Familial amyloid cardiomyopathy</a>, <a href="/wiki/Leptomeningeal_amyloidosis" class="mw-redirect" title="Leptomeningeal amyloidosis">Leptomeningeal amyloidosis</a> </td> <td>ATTR </td></tr> <tr> <td><a href="/wiki/Beta-2_microglobulin" title="Beta-2 microglobulin">β-2 microglobulin</a> </td> <td><a href="/wiki/Dialysis_related_amyloidosis" class="mw-redirect" title="Dialysis related amyloidosis">Dialysis related amyloidosis</a>, <a href="/wiki/Familial_visceral_amyloidosis" class="mw-redirect" title="Familial visceral amyloidosis">Hereditary visceral amyloidosis</a> (familial) </td> <td>Aβ2M </td></tr> <tr> <td>N-terminal fragments of <a href="/wiki/Apolipoprotein_AI" title="Apolipoprotein AI">Apolipoprotein AI</a> </td> <td>ApoAI amyloidosis </td> <td>AApoAI </td></tr> <tr> <td>C-terminally extended <a href="/wiki/Apolipoprotein_A2" class="mw-redirect" title="Apolipoprotein A2">Apolipoprotein AII</a> </td> <td>ApoAII amyloidosis </td> <td>AApoAII </td></tr> <tr> <td>N-terminal fragments of <a href="/w/index.php?title=Apolipoprotein_A4&action=edit&redlink=1" class="new" title="Apolipoprotein A4 (page does not exist)">Apolipoprotein AIV</a> </td> <td>ApoAIV amyloidosis </td> <td>AApoAIV </td></tr> <tr> <td><a href="/wiki/Apolipoprotein_C2" class="mw-redirect" title="Apolipoprotein C2">Apolipoprotein C-II</a> </td> <td>ApoCII amyloidosis </td> <td>AApoCII </td></tr> <tr> <td><a href="/wiki/Apolipoprotein_C3" class="mw-redirect" title="Apolipoprotein C3">Apolipoprotein C-III</a> </td> <td>ApoCIII amyloidosis </td> <td>AApoCIII </td></tr> <tr> <td>fragments of <a href="/wiki/Gelsolin" title="Gelsolin">Gelsolin</a> </td> <td><a href="/wiki/Finnish_type_amyloidosis" class="mw-redirect" title="Finnish type amyloidosis">Familial amyloidosis, Finnish type</a> </td> <td>AGel </td></tr> <tr> <td><a href="/wiki/Lysozyme" title="Lysozyme">Lysozyme</a> </td> <td><a href="/wiki/Hereditary_non-neuropathic_systemic_amyloidosis" class="mw-redirect" title="Hereditary non-neuropathic systemic amyloidosis">Hereditary non-neuropathic systemic amyloidosis</a> </td> <td>ALys </td></tr> <tr> <td>fragments of <a href="/w/index.php?title=Fibrinogen_%CE%B1_chain&action=edit&redlink=1" class="new" title="Fibrinogen α chain (page does not exist)">Fibrinogen α chain</a> </td> <td>Fibrinogen amyloidosis </td> <td>AFib </td></tr> <tr> <td>N-terminally truncated <a href="/wiki/Cystatin_C" title="Cystatin C">Cystatin C</a> </td> <td>Hereditary cerebral hemorrhage with amyloidosis, Icelandic type </td> <td>ACys </td></tr> <tr> <td><a href="/wiki/Amylin" title="Amylin">IAPP (Amylin)</a><a href="#cite_note-pmid18314421-23">[23]</a><a href="#cite_note-pmid10933741-24">[24]</a> </td> <td><a href="/wiki/Diabetes_mellitus_type_2" class="mw-redirect" title="Diabetes mellitus type 2">Diabetes mellitus type 2</a>, Insulinoma </td> <td>AIAPP </td></tr> <tr> <td><a href="/wiki/Calcitonin" title="Calcitonin">Calcitonin</a><a href="#cite_note-emedicine.medscape.com-22">[22]</a> </td> <td><a href="/wiki/Medullary_thyroid_cancer" title="Medullary thyroid cancer">Medullary carcinoma of the thyroid</a> </td> <td>ACal </td></tr> <tr> <td><a href="/wiki/Atrial_natriuretic_factor" class="mw-redirect" title="Atrial natriuretic factor">Atrial natriuretic factor</a> </td> <td><a href="/wiki/Cardiac_arrhythmias" class="mw-redirect" title="Cardiac arrhythmias">Cardiac arrhythmias</a>, <a href="/wiki/Isolated_atrial_amyloidosis" title="Isolated atrial amyloidosis">Isolated atrial amyloidosis</a> </td> <td>AANF </td></tr> <tr> <td><a href="/wiki/Prolactin" title="Prolactin">Prolactin</a> </td> <td><a href="/wiki/Prolactinoma" title="Prolactinoma">Pituitary prolactinoma</a> </td> <td>APro </td></tr> <tr> <td><a href="/wiki/Insulin" title="Insulin">Insulin</a> </td> <td>Injection-localized amyloidosis </td> <td>AIns </td></tr> <tr> <td><a href="/wiki/Lactadherin" class="mw-redirect" title="Lactadherin">Lactadherin</a> / <a href="/wiki/Lactadherin" class="mw-redirect" title="Lactadherin">Medin</a> </td> <td><a href="/w/index.php?title=Aortic_medial_amyloidosis&action=edit&redlink=1" class="new" title="Aortic medial amyloidosis (page does not exist)">Aortic medial amyloidosis</a> </td> <td>AMed </td></tr> <tr> <td><a href="/wiki/Lactotransferrin" class="mw-redirect" title="Lactotransferrin">Lactotransferrin</a> / <a href="/wiki/Lactoferrin" title="Lactoferrin">Lactoferrin</a> </td> <td><a href="/wiki/Gelatinous_drop-like_corneal_dystrophy" title="Gelatinous drop-like corneal dystrophy">Gelatinous drop-like corneal dystrophy</a> </td> <td>ALac </td></tr> <tr> <td>Odontogenic ameloblast-associated protein </td> <td>Calcifying epithelial odontogenic tumors </td> <td>AOAAP </td></tr> <tr> <td><a href="/wiki/Pulmonary_surfactant-associated_protein_C" class="mw-redirect" title="Pulmonary surfactant-associated protein C">Pulmonary surfactant-associated protein C</a> (SP-C) </td> <td><a href="/wiki/Pulmonary_alveolar_proteinosis" title="Pulmonary alveolar proteinosis">Pulmonary alveolar proteinosis</a> </td> <td>ASPC </td></tr> <tr> <td><a href="/wiki/LECT2" title="LECT2">Leukocyte cell-derived chemotaxin-2</a> (<a href="/wiki/LECT2" title="LECT2">LECT-2</a>) </td> <td><a href="/wiki/LECT2_amyloidosis" title="LECT2 amyloidosis">Renal LECT2 amyloidosis</a> </td> <td>ALECT2 </td></tr> <tr> <td><a href="/wiki/Galectin-7" title="Galectin-7">Galectin-7</a> </td> <td><a href="/wiki/Lichen_amyloidosis" class="mw-redirect" title="Lichen amyloidosis">Lichen amyloidosis</a>, <a href="/wiki/Macular_amyloidosis" class="mw-redirect" title="Macular amyloidosis">Macular amyloidosis</a> </td> <td>AGal7 </td></tr> <tr> <td><a href="/wiki/Corneodesmosin" title="Corneodesmosin">Corneodesmosin</a> </td> <td><a href="/w/index.php?title=Hypotrichosis_simplex_of_the_scalp&action=edit&redlink=1" class="new" title="Hypotrichosis simplex of the scalp (page does not exist)">Hypotrichosis simplex of the scalp</a> </td> <td>ACor </td></tr> <tr> <td>C-terminal fragments of <a href="/wiki/TGFBI" title="TGFBI">TGFBI</a>/<a href="/wiki/Keratoepithelin" class="mw-redirect" title="Keratoepithelin">Keratoepithelin</a> </td> <td><a href="/wiki/Lattice_corneal_dystrophy_type_I" class="mw-redirect" title="Lattice corneal dystrophy type I">Lattice corneal dystrophy type I</a>, Lattice corneal dystrophy type 3A, Lattice corneal dystrophy Avellino type </td> <td>AKer </td></tr> <tr> <td><a href="/wiki/Semenogelin_I" title="Semenogelin I">Semenogelin-1</a> (SGI) </td> <td>Seminal vesicle amyloidosis </td> <td>ASem1 </td></tr> <tr> <td><a href="/wiki/S100_protein" title="S100 protein">Proteins S100A8/A9</a> </td> <td><a href="/wiki/Prostate_cancer" title="Prostate cancer">Prostate cancer</a> </td> <td>none </td></tr> <tr> <td><a href="/wiki/Enfuvirtide" title="Enfuvirtide">Enfuvirtide</a> </td> <td>Injection-localized amyloidosis </td> <td>AEnf </td></tr> </tbody></table> <div class="mw-heading mw-heading2"><h2 id="Non-disease_and_functional_amyloids">Non-disease and functional amyloids</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=3" title="Edit section: Non-disease and functional amyloids">edit</a>]</div> Many examples of non-pathological amyloid with a well-defined physiological role have been identified in various organisms, including <a href="/wiki/Homo_sapiens" class="mw-redirect" title="Homo sapiens">human</a>. These may be termed as functional or physiological or native amyloid.<a href="#cite_note-pmid18487849-25">[25]</a><a href="#cite_note-pmid17412596-26">[26]</a><a href="#cite_note-pmid28498720-2">[2]</a> <ul><li>Functional amyloid in <a href="/wiki/Homo_sapiens" class="mw-redirect" title="Homo sapiens">Homo sapiens</a>: <ul><li>Intralumenal domain of melanocyte protein <a href="/wiki/PMEL_(gene)" title="PMEL (gene)">PMEL</a><a href="#cite_note-pmid16300414-27">[27]</a></li> <li>Peptide/protein hormones stored as amyloids within endocrine secretory granules<a href="#cite_note-28">[28]</a></li> <li>Receptor-interacting serine/threonine-protein kinase 1/3 (<a href="/w/index.php?title=RIP1_(protein)&action=edit&redlink=1" class="new" title="RIP1 (protein) (page does not exist)">RIP1</a>/<a href="/w/index.php?title=RIP3&action=edit&redlink=1" class="new" title="RIP3 (page does not exist)">RIP3</a>)<a href="#cite_note-pmid22817896-29">[29]</a></li> <li>Fragments of <a href="/wiki/Prostatic_acid_phosphatase" title="Prostatic acid phosphatase">prostatic acid phosphatase</a> and <a href="/wiki/Semenogelin" title="Semenogelin">semenogelins</a><a href="#cite_note-pmid24691351-30">[30]</a></li></ul></li> <li>Functional amyloid in other organisms: <ul><li><a href="/wiki/Pilus#Curli" title="Pilus">Curli</a> <a href="/wiki/Fimbria_(bacteriology)" class="mw-redirect" title="Fimbria (bacteriology)">fibrils</a> produced by <a href="/wiki/E._coli" class="mw-redirect" title="E. coli">E. coli</a>, <a href="/wiki/Salmonella" title="Salmonella">Salmonella</a>, and a few other members of the <a href="/wiki/Enterobacteriales" class="mw-redirect" title="Enterobacteriales">Enterobacteriales</a> (Csg). The genetic elements (<a href="/wiki/Operons" class="mw-redirect" title="Operons">operons</a>) encoding the curli system are phylogenetic widespread and can be found in at least four bacterial phyla.<a href="#cite_note-31">[31]</a> This suggest that many more bacteria may express curli fibrils.</li> <li>GvpA, forming the walls of particular <a href="/wiki/Gas_vesicle" title="Gas vesicle">Gas vesicles</a>, i.e. the buoyancy organelles of aquatic archaea and eubacteria<a href="#cite_note-32">[32]</a></li> <li>Fap fibrils in various species of <a href="/wiki/Pseudomonas" title="Pseudomonas">Pseudomonas</a><a href="#cite_note-33">[33]</a><a href="#cite_note-34">[34]</a></li> <li>Chaplins from <a href="/wiki/Streptomyces_coelicolor" class="mw-redirect" title="Streptomyces coelicolor">Streptomyces coelicolor</a><a href="#cite_note-pmid12832396-35">[35]</a></li> <li><a href="/wiki/Spidroin" title="Spidroin">Spidroin</a> from <a href="/wiki/Trichonephila_edulis" title="Trichonephila edulis">Trichonephila edulis</a> (<a href="/wiki/Spider" title="Spider">spider</a>) (<a href="/wiki/Spider_silk" title="Spider silk">Spider silk</a>)<a href="#cite_note-pmid12180993-36">[36]</a></li> <li><a href="/wiki/Hydrophobin" title="Hydrophobin">Hydrophobins</a> from <a href="/wiki/Neurospora_crassa" title="Neurospora crassa">Neurospora crassa</a> and other fungi<a href="#cite_note-pmid11250193-37">[37]</a></li> <li>Fungal cell adhesion proteins forming cell surface amyloid regions with greatly increased binding strength<a href="#cite_note-38">[38]</a><a href="#cite_note-39">[39]</a></li> <li>Environmental <a href="/wiki/Biofilm" title="Biofilm">biofilms</a> according to staining with amyloid specific dyes and antibodies.<a href="#cite_note-40">[40]</a></li> <li>Tubular sheaths encasing <a href="/wiki/Methanosaeta" title="Methanosaeta">Methanosaeta</a> thermophila filaments<a href="#cite_note-41">[41]</a></li></ul></li> <li>Functional amyloid acting as prions <ul><li>Several <a href="/wiki/Yeast_prions" class="mw-redirect" title="Yeast prions">yeast prions</a> are based on an infectious amyloid, e.g. [PSI+] (<a href="/wiki/Sup35p" title="Sup35p">Sup35p</a>); [URE3] (<a href="/wiki/Ure2p" title="Ure2p">Ure2p</a>); [PIN+] or [RNQ+] (Rnq1p); [SWI1+] (Swi1p) and [OCT8+] (Cyc8p)</li> <li>Prion HET-s from <a href="/wiki/Podospora_anserina" title="Podospora anserina">Podospora anserina</a><a href="#cite_note-pmid9275200-42">[42]</a></li> <li>Neuron-specific isoform of CPEB from <a href="/wiki/Aplysia_californica" class="mw-redirect" title="Aplysia californica">Aplysia californica</a> (marine snail)<a href="#cite_note-pmid14697205-43">[43]</a></li></ul></li></ul> <div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=4" title="Edit section: Structure">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Protofilament_of_Beta_Amyloid.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/7/76/Protofilament_of_Beta_Amyloid.jpg/220px-Protofilament_of_Beta_Amyloid.jpg" decoding="async" width="220" height="209" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/76/Protofilament_of_Beta_Amyloid.jpg/330px-Protofilament_of_Beta_Amyloid.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/76/Protofilament_of_Beta_Amyloid.jpg/440px-Protofilament_of_Beta_Amyloid.jpg 2x" data-file-width="964" data-file-height="916" /></a><figcaption>Structure of a fibril, consisting of one single protofilament, of the amyloid β peptide viewed down the long axis of the fibril (<a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/2mlq">2mlq</a>)<a href="#cite_note-pmid19015532-44">[44]</a></figcaption></figure> Amyloids are formed of long unbranched fibers that are characterized by an extended <a href="/wiki/%CE%92_sheet" class="mw-redirect" title="Β sheet">β-sheet secondary structure</a> in which individual <a href="/wiki/Beta_strand" class="mw-redirect" title="Beta strand">β strands</a> (β-strands) (coloured arrows in the adjacent figure) are arranged in an orientation perpendicular to the long axis of the fiber. Such a structure is known as cross-β structure. Each individual fiber may be 7–13 <a href="/wiki/Nanometre" title="Nanometre">nanometres</a> in width and a few <a href="/wiki/Micrometre" title="Micrometre">micrometres</a> in length.<a href="#cite_note-ann_rev_biochem_2011-6">[6]</a><a href="#cite_note-pmid28498720-2">[2]</a> The main hallmarks recognised by different disciplines to classify protein aggregates as amyloid is the presence of a fibrillar morphology with the expected diameter, detected using <a href="/wiki/Transmission_electron_microscopy" title="Transmission electron microscopy">transmission electron microscopy</a> (TEM) or <a href="/wiki/Atomic_force_microscopy" title="Atomic force microscopy">atomic force microscopy</a> (AFM), the presence of a cross-β secondary structure, determined with <a href="/wiki/Circular_dichroism" title="Circular dichroism">circular dichroism</a>, <a href="/wiki/Fourier_transform_infrared_spectroscopy" class="mw-redirect" title="Fourier transform infrared spectroscopy">FTIR</a>, <a href="/wiki/Solid-state_nuclear_magnetic_resonance" title="Solid-state nuclear magnetic resonance">solid-state nuclear magnetic resonance</a> (ssNMR), <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a>, or <a href="/wiki/X-ray_diffraction" title="X-ray diffraction">X-ray fiber diffraction</a> (often considered the "gold-standard" test to see whether a structure contains cross-β fibres), and an ability to stain with specific dyes, such as <a href="/wiki/Congo_red" title="Congo red">Congo red</a>, <a href="/wiki/Thioflavin_T" class="mw-redirect" title="Thioflavin T">thioflavin T</a> or <a href="/wiki/Thioflavin_S" class="mw-redirect" title="Thioflavin S">thioflavin S</a>.<a href="#cite_note-pmid28498720-2">[2]</a> The term "cross-β" was based on the observation of two sets of diffraction lines, one longitudinal and one transverse, that form a characteristic "cross" pattern.<a href="#cite_note-45">[45]</a> There are two characteristic scattering diffraction signals produced at 4.7 and 10 <a href="/wiki/%C3%85ngstrom" class="mw-redirect" title="Ångstrom">Å</a> (0.47 nm and 1.0 nm), corresponding to the interstrand and stacking distances in β sheets.<a href="#cite_note-pmid9356260-1">[1]</a> The "stacks" of β sheet are short and traverse the breadth of the amyloid fibril; the length of the amyloid fibril is built by aligned β-strands. The cross-β pattern is considered a diagnostic hallmark of amyloid structure.<a href="#cite_note-ann_rev_biochem_2011-6">[6]</a> Amyloid fibrils are generally composed of 1–8 protofilaments (one protofilament also corresponding to a fibril is shown in the figure), each 2–7 nm in diameter, that interact laterally as flat ribbons that maintain the height of 2–7 nm (that of a single protofilament) and are up to 30 nm wide; more often protofilaments twist around each other to form the typically 7–13 nm wide fibrils.<a href="#cite_note-pmid28498720-2">[2]</a> Each protofilament possesses the typical cross-β structure and may be formed by 1–6 β-sheets (six are shown in the figure) stacked on each other. Each individual protein molecule can contribute one to several β-strands in each protofilament and the strands can be arranged in antiparallel β-sheets, but more often in parallel β-sheets. Only a fraction of the polypeptide chain is in a β-strand conformation in the fibrils, the remainder forms structured or unstructured loops or tails. For a long time our knowledge of the atomic-level structure of amyloid fibrils was limited by the fact that they are unsuitable for the most traditional methods for studying protein structures. Recent years have seen progress in experimental methods, including <a href="/wiki/Solid-state_NMR" class="mw-redirect" title="Solid-state NMR">solid-state NMR</a> spectroscopy and <a href="/wiki/Cryo-electron_microscopy" class="mw-redirect" title="Cryo-electron microscopy">cryo-electron microscopy</a>. Combined, these methods have provided 3D atomic structures of amyloid fibrils formed by amyloid β peptides, α-synuclein, tau, and the FUS protein, associated with various neurodegenerative diseases.<a href="#cite_note-46">[46]</a><a href="#cite_note-47">[47]</a> <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray diffraction studies of microcrystals</a> revealed <a href="/wiki/Atomistics" class="mw-redirect" title="Atomistics">atomistic</a> details of core region of amyloid, although only for simplified peptides having a length remarkably shorter than that of peptides or proteins involved in disease.<a href="#cite_note-Nelson2005-48">[48]</a><a href="#cite_note-Sawaya2007-49">[49]</a> The crystallographic structures show that short stretches from amyloid-prone regions of amyloidogenic proteins run perpendicular to the filament axis, consistent with the "cross-β" feature of amyloid structure. They also reveal a number of characteristics of amyloid structures – neighboring β-sheets are tightly packed together via an interface devoid of water (therefore referred to as dry interface), with the opposing β-strands slightly offset from each other such that their side-chains interdigitate. This compact dehydrated interface created was termed a steric-zipper interface.<a href="#cite_note-ann_rev_biochem_2011-6">[6]</a> There are eight theoretical classes of steric-zipper interfaces, dictated by the directionality of the β-sheets (parallel and anti-parallel) and symmetry between adjacent β-sheets. A limitation of X-ray crystallography for solving amyloid structure is represented by the need to form microcrystals, which can be achieved only with peptides shorter than those associated with disease. Although bona fide amyloid structures always are based on intermolecular β-sheets, different types of "higher order" tertiary folds have been observed or proposed. The β-sheets may form a <a href="/wiki/Beta-sandwich" title="Beta-sandwich">β-sandwich</a>, or a β-solenoid which may be either <a href="/wiki/Beta_helix" title="Beta helix">β-helix</a> or β-roll. Native-like amyloid fibrils in which native β-sheet containing proteins maintain their native-like structure in the fibrils have also been proposed.<a href="#cite_note-PMID12219081-50">[50]</a> There are few developed ideas on how the complex backbone topologies of disulfide-constrained proteins, which are prone to form amyloid fibrils (such as insulin and lysozyme), adopt the amyloid β-sheet motif. The presence of multiple constraints significantly reduces the accessible conformational space, making computational simulations of amyloid structures more feasible.<a href="#cite_note-51">[51]</a> One complicating factor in studies of amyloidogenic polypeptides is that identical polypeptides can fold into multiple distinct amyloid conformations.<a href="#cite_note-ann_rev_biochem_2011-6">[6]</a> This phenomenon is typically described as amyloid polymorphism.<a href="#cite_note-pm11076514-8">[8]</a><a href="#cite_note-pm17056725-52">[52]</a><a href="#cite_note-pm12023906-53">[53]</a> It has notable biological consequences given that it is thought to explain the <a href="/wiki/Prion" title="Prion">prion</a> strain phenomenon. <div class="mw-heading mw-heading2"><h2 id="Formation">Formation</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=5" title="Edit section: Formation">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Three_phases_of_amyloid_fibril_formation.tif" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Three_phases_of_amyloid_fibril_formation.tif/lossless-page1-300px-Three_phases_of_amyloid_fibril_formation.tif.png" decoding="async" width="300" height="213" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Three_phases_of_amyloid_fibril_formation.tif/lossless-page1-450px-Three_phases_of_amyloid_fibril_formation.tif.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Three_phases_of_amyloid_fibril_formation.tif/lossless-page1-600px-Three_phases_of_amyloid_fibril_formation.tif.png 2x" data-file-width="1356" data-file-height="964" /></a><figcaption>Three phases of amyloid fibril formation: <a href="/wiki/Incubation_period" title="Incubation period">lag phase</a>, <a href="/wiki/Exponential_function" title="Exponential function">exponential phase</a> and <a href="/wiki/Plateau_effect" title="Plateau effect">plateau phase</a></figcaption></figure> Amyloid is formed through the <a href="/wiki/Polymerization" title="Polymerization">polymerization</a> of hundreds to thousands of monomeric <a href="/wiki/Peptides" class="mw-redirect" title="Peptides">peptides</a> or <a href="/wiki/Proteins" class="mw-redirect" title="Proteins">proteins</a> into long fibers. Amyloid formation involves a <a href="/wiki/Incubation_period" title="Incubation period">lag</a> phase (also called <a href="/wiki/Nucleation" title="Nucleation">nucleation</a> phase), an <a href="/wiki/Exponential_growth" title="Exponential growth">exponential</a> phase (also called growth phase) and a <a href="/wiki/Plateau_effect" title="Plateau effect">plateau</a> phase (also called saturation phase), as shown in the figure.<a href="#cite_note-pmid8490014-54">[54]</a><a href="#cite_note-pmid10507029-55">[55]</a><a href="#cite_note-pmid19071235-56">[56]</a><a href="#cite_note-pmid20007899-57">[57]</a> Indeed, when the quantity of fibrils is plotted versus time, a <a href="/wiki/Sigmoid_function" title="Sigmoid function">sigmoidal</a> time course is observed reflecting the three distinct phases. In the simplest model of 'nucleated polymerization' (marked by red arrows in the figure below), individual unfolded or partially unfolded <a href="/wiki/Polypeptide_chains" class="mw-redirect" title="Polypeptide chains">polypeptide chains</a> (monomers) convert into a <a href="/wiki/Cell_nucleus" title="Cell nucleus">nucleus</a> (<a href="/wiki/Monomer" title="Monomer">monomer</a> or <a href="/wiki/Oligomer" title="Oligomer">oligomer</a>) via a <a href="/wiki/Thermodynamics" title="Thermodynamics">thermodynamically</a> unfavourable process that occurs early in the lag phase.<a href="#cite_note-pmid19071235-56">[56]</a> Fibrils grow subsequently from these <a href="/wiki/Nucleation" title="Nucleation">nuclei</a> through the addition of <a href="/wiki/Monomer" title="Monomer">monomers</a> in the exponential phase.<a href="#cite_note-pmid19071235-56">[56]</a> A different model, called 'nucleated conformational conversion' and marked by blue arrows in the figure below, was introduced later on to fit some experimental observations: monomers have often been found to convert rapidly into misfolded and highly disorganized oligomers distinct from nuclei.<a href="#cite_note-pmid10958771-58">[58]</a> Only later on, will these aggregates reorganise structurally into nuclei, on which other disorganised oligomers will add and reorganise through a templating or induced-fit mechanism (this 'nucleated conformational conversion' model), eventually forming fibrils.<a href="#cite_note-pmid10958771-58">[58]</a> Normally <a href="/wiki/Folded_proteins" class="mw-redirect" title="Folded proteins">folded proteins</a> have to unfold partially before aggregation can take place through one of these mechanisms.<a href="#cite_note-pmid19088715-59">[59]</a> In some cases, however, folded proteins can aggregate without crossing the major <a href="/wiki/Energy_barrier" class="mw-redirect" title="Energy barrier">energy barrier</a> for unfolding, by populating native-like conformations as a consequence of <a href="/wiki/Thermal_fluctuations" title="Thermal fluctuations">thermal fluctuations</a>, ligand release or local unfolding occurring in particular circumstances.<a href="#cite_note-pmid19088715-59">[59]</a> In these native-like conformations, segments that are normally buried or structured in the fully folded and possessing a high propensity to aggregate become exposed to the solvent or flexible, allowing the formation of native-like aggregates, which convert subsequently into nuclei and fibrils. This process is called 'native-like aggregation' (green arrows in the figure) and is similar to the 'nucleated conformational conversion' model. A more recent, modern and thorough model of amyloid fibril formation involves the intervention of secondary events, such as 'fragmentation', in which a fibril breaks into two or more shorter fibrils, and 'secondary nucleation', in which fibril surfaces (not fibril ends) catalyze the formation of new nuclei.<a href="#cite_note-pmid20007899-57">[57]</a> Both secondary events increase the number of fibril ends able to recruit new monomers or oligomers, therefore accelerating fibril formation through a positive feedback mechanism. These events add to the well recognised steps of primary nucleation (formation of the nucleus from the monomers through one of models described above), fibril elongation (addition of monomers or oligomers to growing fibril ends) and dissociation (opposite process). Such a new model is described in the figure on the right and involves the utilization of a <a href="/wiki/Master_equation" title="Master equation">master equation</a> that includes all steps of amyloid fibril formation, i.e. primary nucleation, fibril elongation, secondary nucleation and fibril fragmentation.<a href="#cite_note-pmid20007899-57">[57]</a><a href="#cite_note-:0-60">[60]</a> The <a href="/wiki/Rate_constant" class="mw-redirect" title="Rate constant">rate constants</a> of the various steps can be determined from a global fit of a number of time courses of aggregation (for example <a href="/wiki/Thioflavin" title="Thioflavin">ThT fluorescence</a> emission versus time) recorded at different protein concentrations.<a href="#cite_note-pmid20007899-57">[57]</a> The general master equation approach to amyloid fibril formation with secondary pathways has been developed by <a href="/wiki/Tuomas_Knowles" title="Tuomas Knowles">Knowles</a>, <a href="/wiki/Michele_Vendruscolo" title="Michele Vendruscolo">Vendruscolo</a>, Cohen, Michaels and coworkers and considers the time evolution of the concentration <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle f(t,j)}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo stretchy="false">)</mo> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle f(t,j)}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/343e635092c0903da01d3a4d04ec54c5d06d9e04" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.838ex; width:5.92ex; height:2.843ex;" alt="{\displaystyle f(t,j)}" /> of fibrils of length <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle j}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>j</mi> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle j}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/2f461e54f5c093e92a55547b9764291390f0b5d0" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.671ex; margin-left: -0.027ex; width:0.985ex; height:2.509ex;" alt="{\displaystyle j}" /> (here <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle j}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>j</mi> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle j}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/2f461e54f5c093e92a55547b9764291390f0b5d0" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.671ex; margin-left: -0.027ex; width:0.985ex; height:2.509ex;" alt="{\displaystyle j}" /> represents the number of monomers in an aggregate).<a href="#cite_note-:0-60">[60]</a> <math display="block" xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\begin{aligned}{\frac {\partial f(t,j)}{\partial t}}&=2k_{+}m(t)f(t,j-1)-2k_{+}m(t)f(t,j)\\&+2k_{\rm {off}}f(t,j+1)-2k_{\rm {off}}f(t,j)\\&+k_{-}\sum _{i=j+1}^{\infty }f(t,i)-k_{-}(j-1)f(t,j)\\&+k_{1}m(t)^{n_{1}}\delta _{j,n_{1}}+k_{2}m(t)^{n_{2}}M(t)\delta _{j,n_{2}}\\\\\end{aligned}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mtable columnalign="right left right left right left right left right left right left" rowspacing="3pt" columnspacing="0em 2em 0em 2em 0em 2em 0em 2em 0em 2em 0em" displaystyle="true"> <mtr> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mi mathvariant="normal">∂</mi> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo stretchy="false">)</mo> </mrow> <mrow> <mi mathvariant="normal">∂</mi> <mi>t</mi> </mrow> </mfrac> </mrow> </mtd> <mtd> <mi></mi> <mo>=</mo> <mn>2</mn> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>+</mo> </mrow> </msub> <mi>m</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo stretchy="false">)</mo> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo>−</mo> <mn>1</mn> <mo stretchy="false">)</mo> <mo>−</mo> <mn>2</mn> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>+</mo> </mrow> </msub> <mi>m</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo stretchy="false">)</mo> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo stretchy="false">)</mo> </mtd> </mtr> <mtr> <mtd></mtd> <mtd> <mi></mi> <mo>+</mo> <mn>2</mn> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mi mathvariant="normal">o</mi> <mi mathvariant="normal">f</mi> <mi mathvariant="normal">f</mi> </mrow> </mrow> </msub> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo>+</mo> <mn>1</mn> <mo stretchy="false">)</mo> <mo>−</mo> <mn>2</mn> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mi mathvariant="normal">o</mi> <mi mathvariant="normal">f</mi> <mi mathvariant="normal">f</mi> </mrow> </mrow> </msub> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo stretchy="false">)</mo> </mtd> </mtr> <mtr> <mtd></mtd> <mtd> <mi></mi> <mo>+</mo> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </msub> <munderover> <mo>∑</mo> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> <mo>=</mo> <mi>j</mi> <mo>+</mo> <mn>1</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mi mathvariant="normal">∞</mi> </mrow> </munderover> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>i</mi> <mo stretchy="false">)</mo> <mo>−</mo> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </msub> <mo stretchy="false">(</mo> <mi>j</mi> <mo>−</mo> <mn>1</mn> <mo stretchy="false">)</mo> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo stretchy="false">)</mo> </mtd> </mtr> <mtr> <mtd></mtd> <mtd> <mi></mi> <mo>+</mo> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>1</mn> </mrow> </msub> <mi>m</mi> <mo stretchy="false">(</mo> <mi>t</mi> <msup> <mo stretchy="false">)</mo> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>n</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>1</mn> </mrow> </msub> </mrow> </msup> <msub> <mi>δ</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>j</mi> <mo>,</mo> <msub> <mi>n</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>1</mn> </mrow> </msub> </mrow> </msub> <mo>+</mo> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> </msub> <mi>m</mi> <mo stretchy="false">(</mo> <mi>t</mi> <msup> <mo stretchy="false">)</mo> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>n</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> </msub> </mrow> </msup> <mi>M</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo stretchy="false">)</mo> <msub> <mi>δ</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>j</mi> <mo>,</mo> <msub> <mi>n</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> </msub> </mrow> </msub> </mtd> </mtr> <mtr> <mtd></mtd> </mtr> </mtable> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\begin{aligned}{\frac {\partial f(t,j)}{\partial t}}&=2k_{+}m(t)f(t,j-1)-2k_{+}m(t)f(t,j)\\&+2k_{\rm {off}}f(t,j+1)-2k_{\rm {off}}f(t,j)\\&+k_{-}\sum _{i=j+1}^{\infty }f(t,i)-k_{-}(j-1)f(t,j)\\&+k_{1}m(t)^{n_{1}}\delta _{j,n_{1}}+k_{2}m(t)^{n_{2}}M(t)\delta _{j,n_{2}}\\\\\end{aligned}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/0c6834f840a81fd14c02c7ffbd621f08588a8f23" class="mwe-math-fallback-image-display mw-invert skin-invert" aria-hidden="true" style="vertical-align: -10.671ex; width:47.753ex; height:22.509ex;" alt="{\displaystyle {\begin{aligned}{\frac {\partial f(t,j)}{\partial t}}&=2k_{+}m(t)f(t,j-1)-2k_{+}m(t)f(t,j)\\&+2k_{\rm {off}}f(t,j+1)-2k_{\rm {off}}f(t,j)\\&+k_{-}\sum _{i=j+1}^{\infty }f(t,i)-k_{-}(j-1)f(t,j)\\&+k_{1}m(t)^{n_{1}}\delta _{j,n_{1}}+k_{2}m(t)^{n_{2}}M(t)\delta _{j,n_{2}}\\\\\end{aligned}}}" />where <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle \delta _{i,j}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>δ</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> <mo>,</mo> <mi>j</mi> </mrow> </msub> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle \delta _{i,j}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/40e421f3ef0893f646c999fcc309a25ad6bad1f5" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -1.005ex; width:2.967ex; height:3.009ex;" alt="{\displaystyle \delta _{i,j}}" /> denotes the <a href="/wiki/Kronecker_delta" title="Kronecker delta">Kronecker delta</a>. The physical interpretation of the various terms in the above master equation is straight forward: the terms on the first line describe the growth of fibrils via monomer addition with rate constant <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle k_{+}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>+</mo> </mrow> </msub> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle k_{+}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/101dd91e4318a4dfb09d3701fe87fc5ad31e13e2" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.671ex; width:2.722ex; height:2.509ex;" alt="{\displaystyle k_{+}}" /> (elongation). The terms on the second line describe monomer dissociation, i.e. the inverse process of elongation. <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle k_{\rm {off}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mi mathvariant="normal">o</mi> <mi mathvariant="normal">f</mi> <mi mathvariant="normal">f</mi> </mrow> </mrow> </msub> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle k_{\rm {off}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/aa9f6d7a8ffd70e800a12e736a82690b0598c02e" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.671ex; width:3.489ex; height:2.509ex;" alt="{\displaystyle k_{\rm {off}}}" /> is the rate constant of monomer dissociation. The terms on the third line describe the effect of fragmentation, which is assumed to occur homogeneously along fibrils with rate constant <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle k_{-}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>k</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </msub> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle k_{-}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/f58e4fd8179e5a65b9754737155e05c1a8077baf" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.671ex; width:2.722ex; height:2.509ex;" alt="{\displaystyle k_{-}}" />. Finally, the terms on the last line describe primary and secondary nucleation respectively. Note that the rate of secondary nucleation is proportional to the mass of aggregates, defined as <math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle M(t)=\sum _{j=n_{1}}^{\infty }jf(t,j)}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>M</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo stretchy="false">)</mo> <mo>=</mo> <munderover> <mo>∑</mo> <mrow class="MJX-TeXAtom-ORD"> <mi>j</mi> <mo>=</mo> <msub> <mi>n</mi> <mrow class="MJX-TeXAtom-ORD"> <mn>1</mn> </mrow> </msub> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mi mathvariant="normal">∞</mi> </mrow> </munderover> <mi>j</mi> <mi>f</mi> <mo stretchy="false">(</mo> <mi>t</mi> <mo>,</mo> <mi>j</mi> <mo stretchy="false">)</mo> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle M(t)=\sum _{j=n_{1}}^{\infty }jf(t,j)}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/4831e3d325af10aff1060148d2e07bc582b3bcda" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.338ex; width:19.228ex; height:7.176ex;" alt="{\displaystyle M(t)=\sum _{j=n_{1}}^{\infty }jf(t,j)}" />. Following this analytical approach, it has become apparent that the lag phase does not correspond necessarily to only nucleus formation, but rather results from a combination of various steps. Similarly, the exponential phase is not only fibril elongation, but results from a combination of various steps, involving primary nucleation, fibril elongation, but also secondary events. A significant quantity of fibrils resulting from primary nucleation and fibril elongation may be formed during the lag phase and secondary steps, rather than only fibril elongation, can be the dominant processes contributing to fibril growth during the exponential phase. With this new model, any perturbing agents of amyloid fibril formation, such as putative <a href="/wiki/Drugs" class="mw-redirect" title="Drugs">drugs</a>, <a href="/wiki/Metabolites" class="mw-redirect" title="Metabolites">metabolites</a>, <a href="/wiki/Amino_acid_replacement" title="Amino acid replacement">mutations</a>, <a href="/wiki/Molecular_chaperones" class="mw-redirect" title="Molecular chaperones">chaperones</a>, etc., can be assigned to a specific step of fibril formation. <div class="mw-heading mw-heading2"><h2 id="Amino_acid_sequence_and_amyloid_formation">Amino acid sequence and amyloid formation</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=6" title="Edit section: Amino acid sequence and amyloid formation">edit</a>]</div> In general, amyloid <a href="/wiki/Polymer" title="Polymer">polymerization</a> (aggregation or non-covalent polymerization) is sequence-sensitive, that is mutations in the sequence can induce or prevent self-assembly.<a href="#cite_note-pmid12917692-61">[61]</a><a href="#cite_note-62">[62]</a> For example, humans produce <a href="/wiki/Amylin" title="Amylin">amylin</a>, an amyloidogenic peptide associated with type II diabetes, but in rats and mice prolines are substituted in critical locations and amyloidogenesis does not occur.<a href="#cite_note-63">[63]</a> Studies comparing synthetic to recombinant <a href="/wiki/%CE%92_amyloid" class="mw-redirect" title="Β amyloid">β amyloid peptide</a> in assays measuring rate of fibrillation, fibril homogeneity, and cellular toxicity showed that recombinant β amyloid peptide has a faster fibrillation rate and greater toxicity than synthetic β amyloid peptide.<a href="#cite_note-64">[64]</a> There are multiple classes of amyloid-forming polypeptide sequences.<a href="#cite_note-pm11076514-8">[8]</a><a href="#cite_note-pm17056725-52">[52]</a><a href="#cite_note-pm12023906-53">[53]</a> Glutamine-rich polypeptides are important in the amyloidogenesis of Yeast and mammalian <a href="/wiki/Prions" class="mw-redirect" title="Prions">prions</a>, as well as <a href="/wiki/Trinucleotide_repeat_disorders" class="mw-redirect" title="Trinucleotide repeat disorders">trinucleotide repeat disorders</a> including <a href="/wiki/Huntington%27s_disease" title="Huntington's disease">Huntington's disease</a>. When glutamine-rich polypeptides are in a β-sheet conformation, glutamines can brace the structure by forming inter-strand hydrogen bonding between its amide carbonyls and nitrogens of both the backbone and side chains. The onset age for Huntington's disease shows an inverse correlation with the length of the <a href="/wiki/Polyglutamine_tract" title="Polyglutamine tract">polyglutamine sequence</a>, with analogous findings in a <a href="/wiki/Caenorhabditis_elegans" title="Caenorhabditis elegans">C. elegans</a> model system with engineered polyglutamine peptides.<a href="#cite_note-65">[65]</a> Other polypeptides and proteins such as <a href="/wiki/Amylin" title="Amylin">amylin</a> and the β amyloid peptide do not have a simple consensus sequence and are thought to aggregate through the sequence segments enriched with hydrophobic residues, or residues with high propensity to form β-sheet structure.<a href="#cite_note-pmid12917692-61">[61]</a> Among the hydrophobic residues, aromatic amino-acids are found to have the highest amyloidogenic propensity.<a href="#cite_note-66">[66]</a><a href="#cite_note-PMID15925383-67">[67]</a> Cross-polymerization (fibrils of one polypeptide sequence causing other fibrils of another sequence to form) is observed in vitro and possibly in vivo. This phenomenon is important, since it would explain interspecies <a href="/wiki/Prion" title="Prion">prion</a> propagation and differential rates of prion propagation, as well as a statistical link between Alzheimer's and type 2 diabetes.<a href="#cite_note-pmid23794448-68">[68]</a> In general, the more similar the peptide sequence the more efficient cross-polymerization is, though entirely dissimilar sequences can cross-polymerize and highly similar sequences can even be "blockers" that prevent polymerization.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] <div class="mw-heading mw-heading2"><h2 id="Amyloid_toxicity">Amyloid toxicity</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=7" title="Edit section: Amyloid toxicity">edit</a>]</div> The reasons why amyloid cause diseases are unclear. In some cases, the deposits physically disrupt tissue architecture, suggesting disruption of function by some bulk process. An emerging consensus implicates prefibrillar intermediates, rather than mature amyloid fibers, in causing cell death, particularly in neurodegenerative diseases.<a href="#cite_note-pmid17505973-17">[17]</a><a href="#cite_note-69">[69]</a> The fibrils are, however, far from innocuous, as they keep the protein homeostasis network engaged, release oligomers, cause the formation of toxic oligomers via secondary nucleation, grow indefinitely spreading from district to district<a href="#cite_note-pmid28498720-2">[2]</a> and, in some cases, may be toxic themselves.<a href="#cite_note-70">[70]</a> Calcium dysregulation has been observed to occur early in cells exposed to protein oligomers. These small aggregates can form ion channels through lipid bilayer membranes and activate NMDA and AMPA receptors. Channel formation has been hypothesized to account for calcium dysregulation and mitochondrial dysfunction by allowing indiscriminate leakage of ions across cell membranes.<a href="#cite_note-71">[71]</a> Studies have shown that amyloid deposition is associated with mitochondrial dysfunction and a resulting generation of <a href="/wiki/Reactive_oxygen_species" title="Reactive oxygen species">reactive oxygen species</a> (ROS), which can initiate a signalling pathway leading to <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a>.<a href="#cite_note-72">[72]</a> There are reports that indicate amyloid polymers (such as those of huntingtin, associated with Huntington's disease) can induce the polymerization of essential amyloidogenic proteins, which should be deleterious to cells. Also, interaction partners of these essential proteins can also be sequestered.<a href="#cite_note-73">[73]</a> All these mechanisms of toxicity are likely to play a role. In fact, the aggregation of a protein generates a variety of aggregates, all of which are likely to be toxic to some degree. A wide variety of biochemical, physiological and cytological perturbations has been identified following the exposure of cells and animals to such species, independently of their identity. The oligomers have also been reported to interact with a variety of molecular targets. Hence, it is unlikely that there is a unique mechanism of toxicity or a unique cascade of cellular events. The misfolded nature of protein aggregates causes a multitude of aberrant interactions with a multitude of cellular components, including membranes, protein receptors, soluble proteins, RNAs, small metabolites, etc. <div class="mw-heading mw-heading2"><h2 id="Histological_staining">Histological staining</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=8" title="Edit section: Histological staining">edit</a>]</div> In the clinical setting, amyloid diseases are typically identified by a change in the spectroscopic properties of planar <a href="/wiki/Aromatic" class="mw-redirect" title="Aromatic">aromatic</a> <a href="/wiki/Dye" title="Dye">dyes</a> such as <a href="/wiki/Thioflavin_T" class="mw-redirect" title="Thioflavin T">thioflavin T</a>, <a href="/wiki/Congo_red" title="Congo red">congo red</a> or NIAD-4.<a href="#cite_note-74">[74]</a> In general, this is attributed to the environmental change, as these dyes <a href="/wiki/Intercalation_(biochemistry)" title="Intercalation (biochemistry)">intercalate</a> between β-strands to confine their structure.<a href="#cite_note-75">[75]</a> Congo Red positivity remains the gold standard for diagnosis of <a href="/wiki/Amyloidosis" title="Amyloidosis">amyloidosis</a>. In general, binding of Congo Red to amyloid plaques produces a typical apple-green <a href="/wiki/Birefringence" title="Birefringence">birefringence</a> when viewed under cross-polarized light. Recently, significant enhancement of fluorescence quantum yield of NIAD-4 was exploited to <a href="/wiki/Super-resolution" class="mw-redirect" title="Super-resolution">super-resolution</a> fluorescence imaging of amyloid fibrils<a href="#cite_note-76">[76]</a> and oligomers.<a href="#cite_note-77">[77]</a> To avoid nonspecific staining, other <a href="/wiki/Histology" title="Histology">histology</a> stains, such as the <a href="/wiki/H%26E_stain" title="H&E stain">hematoxylin and eosin</a> stain, are used to quench the dyes' activity in other places such as the nucleus, where the dye might bind. Modern antibody technology and <a href="/wiki/Immunohistochemistry" title="Immunohistochemistry">immunohistochemistry</a> has made specific staining easier, but often this can cause trouble because epitopes can be concealed in the amyloid fold; in general, an amyloid protein structure is a different conformation from the one that the antibody recognizes. <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=9" title="Edit section: See also">edit</a>]</div> <ul><li><a href="/wiki/JUNQ_and_IPOD" title="JUNQ and IPOD">JUNQ and IPOD</a></li> <li><a href="/wiki/Proteopathy" class="mw-redirect" title="Proteopathy">Proteopathy</a></li> <li><a href="/wiki/Protein_aggregation_predictors" title="Protein aggregation predictors">Protein aggregation predictors</a></li> <li><a href="/wiki/Alzheimer%27s_disease" title="Alzheimer's disease">Alzheimer's disease</a></li> <li><a href="/wiki/Amyloid_plaque" class="mw-redirect" title="Amyloid plaque">Amyloid plaque</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=10" title="Edit section: References">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist reflist-columns references-column-width" style="column-width: 30em;"> <ol class="references"> <li id="cite_note-pmid9356260-1">^ <a href="#cite_ref-pmid9356260_1-0">a</a> <a href="#cite_ref-pmid9356260_1-1">b</a> <style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFSundeSerpellBartlamFraser1997" class="citation journal cs1">Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC (October 1997). "Common core structure of amyloid fibrils by synchrotron X-ray diffraction". Journal of Molecular Biology. 273 (3): 729–39. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1006%2Fjmbi.1997.1348">10.1006/jmbi.1997.1348</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9356260">9356260</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:19394482">19394482</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Molecular+Biology&rft.atitle=Common+core+structure+of+amyloid+fibrils+by+synchrotron+X-ray+diffraction&rft.volume=273&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E729-%3C%2Fspan%3E39&rft.date=1997-10&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A19394482%23id-name%3DS2CID&rft_id=info%3Apmid%2F9356260&rft_id=info%3Adoi%2F10.1006%2Fjmbi.1997.1348&rft.aulast=Sunde&rft.aufirst=M&rft.au=Serpell%2C+LC&rft.au=Bartlam%2C+M&rft.au=Fraser%2C+PE&rft.au=Pepys%2C+MB&rft.au=Blake%2C+CC&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid28498720-2">^ <a href="#cite_ref-pmid28498720_2-0">a</a> <a href="#cite_ref-pmid28498720_2-1">b</a> <a href="#cite_ref-pmid28498720_2-2">c</a> <a href="#cite_ref-pmid28498720_2-3">d</a> <a href="#cite_ref-pmid28498720_2-4">e</a> <a href="#cite_ref-pmid28498720_2-5">f</a> <a href="#cite_ref-pmid28498720_2-6">g</a> <a href="#cite_ref-pmid28498720_2-7">h</a> <a href="#cite_ref-pmid28498720_2-8">i</a> <a href="#cite_ref-pmid28498720_2-9">j</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFChitiDobson2017" class="citation journal cs1">Chiti F, Dobson CM (June 2017). "Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade". Annual Review of Biochemistry. 86: 27–68. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev-biochem-061516-045115">10.1146/annurev-biochem-061516-045115</a>. <a href="/wiki/Hdl_(identifier)" class="mw-redirect" title="Hdl (identifier)">hdl</a>:<a rel="nofollow" class="external text" href="https://hdl.handle.net/2158%2F1117236">2158/1117236</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28498720">28498720</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annual+Review+of+Biochemistry&rft.atitle=Protein+Misfolding%2C+Amyloid+Formation%2C+and+Human+Disease%3A+A+Summary+of+Progress+Over+the+Last+Decade&rft.volume=86&rft.pages=%3Cspan+class%3D%22nowrap%22%3E27-%3C%2Fspan%3E68&rft.date=2017-06&rft_id=info%3Ahdl%2F2158%2F1117236&rft_id=info%3Apmid%2F28498720&rft_id=info%3Adoi%2F10.1146%2Fannurev-biochem-061516-045115&rft.aulast=Chiti&rft.aufirst=F&rft.au=Dobson%2C+CM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid30614283-3">^ <a href="#cite_ref-pmid30614283_3-0">a</a> <a href="#cite_ref-pmid30614283_3-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBensonBuxbaumEisenbergMerlini2018" class="citation journal cs1">Benson MD, Buxbaum JN, Eisenberg DS, Merlini G, Saraiva MJ, Sekijima Y, et al. (December 2018). <a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F13506129.2018.1549825">"Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee"</a>. Amyloid. 25 (4): 215–219. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F13506129.2018.1549825">10.1080/13506129.2018.1549825</a>. <a href="/wiki/Hdl_(identifier)" class="mw-redirect" title="Hdl (identifier)">hdl</a>:<a rel="nofollow" class="external text" href="https://hdl.handle.net/1805%2F20251">1805/20251</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30614283">30614283</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Amyloid&rft.atitle=Amyloid+nomenclature+2018%3A+recommendations+by+the+International+Society+of+Amyloidosis+%28ISA%29+nomenclature+committee&rft.volume=25&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E215-%3C%2Fspan%3E219&rft.date=2018-12&rft_id=info%3Ahdl%2F1805%2F20251&rft_id=info%3Apmid%2F30614283&rft_id=info%3Adoi%2F10.1080%2F13506129.2018.1549825&rft.aulast=Benson&rft.aufirst=MD&rft.au=Buxbaum%2C+JN&rft.au=Eisenberg%2C+DS&rft.au=Merlini%2C+G&rft.au=Saraiva%2C+MJ&rft.au=Sekijima%2C+Y&rft.au=Sipe%2C+JD&rft.au=Westermark%2C+P&rft_id=https%3A%2F%2Fdoi.org%2F10.1080%252F13506129.2018.1549825&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-4"><a href="#cite_ref-4">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPulawskiGhoshdastiderAndrisanoFilipek2012" class="citation journal cs1">Pulawski W, Ghoshdastider U, Andrisano V, Filipek S (April 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3324686">"Ubiquitous amyloids"</a>. Applied Biochemistry and Biotechnology. 166 (7): 1626–43. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs12010-012-9549-3">10.1007/s12010-012-9549-3</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3324686">3324686</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22350870">22350870</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Applied+Biochemistry+and+Biotechnology&rft.atitle=Ubiquitous+amyloids&rft.volume=166&rft.issue=7&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1626-%3C%2Fspan%3E43&rft.date=2012-04&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3324686%23id-name%3DPMC&rft_id=info%3Apmid%2F22350870&rft_id=info%3Adoi%2F10.1007%2Fs12010-012-9549-3&rft.aulast=Pulawski&rft.aufirst=W&rft.au=Ghoshdastider%2C+U&rft.au=Andrisano%2C+V&rft.au=Filipek%2C+S&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3324686&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-5"><a href="#cite_ref-5">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSotoEstradaCastilla2006" class="citation journal cs1">Soto C, Estrada L, Castilla J (March 2006). "Amyloids, prions and the inherent infectious nature of misfolded protein aggregates". Trends in Biochemical Sciences. 31 (3): 150–5. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.tibs.2006.01.002">10.1016/j.tibs.2006.01.002</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16473510">16473510</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Biochemical+Sciences&rft.atitle=Amyloids%2C+prions+and+the+inherent+infectious+nature+of+misfolded+protein+aggregates&rft.volume=31&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E150-%3C%2Fspan%3E5&rft.date=2006-03&rft_id=info%3Adoi%2F10.1016%2Fj.tibs.2006.01.002&rft_id=info%3Apmid%2F16473510&rft.aulast=Soto&rft.aufirst=C&rft.au=Estrada%2C+L&rft.au=Castilla%2C+J&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-ann_rev_biochem_2011-6">^ <a href="#cite_ref-ann_rev_biochem_2011_6-0">a</a> <a href="#cite_ref-ann_rev_biochem_2011_6-1">b</a> <a href="#cite_ref-ann_rev_biochem_2011_6-2">c</a> <a href="#cite_ref-ann_rev_biochem_2011_6-3">d</a> <a href="#cite_ref-ann_rev_biochem_2011_6-4">e</a> <a href="#cite_ref-ann_rev_biochem_2011_6-5">f</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFToyamaWeissman2011" class="citation journal cs1">Toyama BH, Weissman JS (2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3817101">"Amyloid structure: conformational diversity and consequences"</a>. Annual Review of Biochemistry. 80: 557–85. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev-biochem-090908-120656">10.1146/annurev-biochem-090908-120656</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3817101">3817101</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21456964">21456964</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annual+Review+of+Biochemistry&rft.atitle=Amyloid+structure%3A+conformational+diversity+and+consequences&rft.volume=80&rft.pages=%3Cspan+class%3D%22nowrap%22%3E557-%3C%2Fspan%3E85&rft.date=2011&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3817101%23id-name%3DPMC&rft_id=info%3Apmid%2F21456964&rft_id=info%3Adoi%2F10.1146%2Fannurev-biochem-090908-120656&rft.aulast=Toyama&rft.aufirst=BH&rft.au=Weissman%2C+JS&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3817101&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-7"><a href="#cite_ref-7">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFRamirez-AlvaradoMerkelRegan2000" class="citation journal cs1">Ramirez-Alvarado M, Merkel JS, Regan L (August 2000). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16807">"A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro"</a>. Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 8979–84. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2000PNAS...97.8979R">2000PNAS...97.8979R</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.150091797">10.1073/pnas.150091797</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16807">16807</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10908649">10908649</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=A+systematic+exploration+of+the+influence+of+the+protein+stability+on+amyloid+fibril+formation+in+vitro&rft.volume=97&rft.issue=16&rft.pages=%3Cspan+class%3D%22nowrap%22%3E8979-%3C%2Fspan%3E84&rft.date=2000-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC16807%23id-name%3DPMC&rft_id=info%3Apmid%2F10908649&rft_id=info%3Adoi%2F10.1073%2Fpnas.150091797&rft_id=info%3Abibcode%2F2000PNAS...97.8979R&rft.aulast=Ramirez-Alvarado&rft.aufirst=M&rft.au=Merkel%2C+JS&rft.au=Regan%2C+L&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC16807&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pm11076514-8">^ <a href="#cite_ref-pm11076514_8-0">a</a> <a href="#cite_ref-pm11076514_8-1">b</a> <a href="#cite_ref-pm11076514_8-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBalbachIshiiAntzutkinLeapman2000" class="citation journal cs1">Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, et al. (November 2000). "Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR". Biochemistry. 39 (45): 13748–59. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fbi0011330">10.1021/bi0011330</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11076514">11076514</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:17232045">17232045</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochemistry&rft.atitle=Amyloid+fibril+formation+by+A%CE%B216-22%2C+a+seven-residue+fragment+of+the+Alzheimer%27s+%CE%B2-amyloid+peptide%2C+and+structural+characterization+by+solid+state+NMR&rft.volume=39&rft.issue=45&rft.pages=%3Cspan+class%3D%22nowrap%22%3E13748-%3C%2Fspan%3E59&rft.date=2000-11&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A17232045%23id-name%3DS2CID&rft_id=info%3Apmid%2F11076514&rft_id=info%3Adoi%2F10.1021%2Fbi0011330&rft.aulast=Balbach&rft.aufirst=JJ&rft.au=Ishii%2C+Y&rft.au=Antzutkin%2C+ON&rft.au=Leapman%2C+RD&rft.au=Rizzo%2C+NW&rft.au=Dyda%2C+F&rft.au=Reed%2C+J&rft.au=Tycko%2C+R&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-alphasheet-9"><a href="#cite_ref-alphasheet_9-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFArmenDemarcoAlonsoDaggett2004" class="citation journal cs1">Armen RS, Demarco ML, Alonso DO, Daggett V (2004). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC511030">"Pauling and Coreys α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease"</a>. Proceedings of the National Academy of Sciences of the United States of America. 101 (1): 11622–11627. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2004PNAS..10111622A">2004PNAS..10111622A</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.0401781101">10.1073/pnas.0401781101</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC511030">511030</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15280548">15280548</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=Pauling+and+Coreys+%CE%B1-pleated+sheet+structure+may+define+the+prefibrillar+amyloidogenic+intermediate+in+amyloid+disease&rft.volume=101&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E11622-%3C%2Fspan%3E11627&rft.date=2004&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC511030%23id-name%3DPMC&rft_id=info%3Apmid%2F15280548&rft_id=info%3Adoi%2F10.1073%2Fpnas.0401781101&rft_id=info%3Abibcode%2F2004PNAS..10111622A&rft.aulast=Armen&rft.aufirst=RS&rft.au=Demarco%2C+ML&rft.au=Alonso%2C+DO&rft.au=Daggett%2C+V&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC511030&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-10"><a href="#cite_ref-10">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKyle2001" class="citation journal cs1">Kyle RA (September 2001). "Amyloidosis: a convoluted story". British Journal of Haematology. 114 (3): 529–38. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1046%2Fj.1365-2141.2001.02999.x">10.1046/j.1365-2141.2001.02999.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11552976">11552976</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:23111535">23111535</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=British+Journal+of+Haematology&rft.atitle=Amyloidosis%3A+a+convoluted+story&rft.volume=114&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E529-%3C%2Fspan%3E38&rft.date=2001-09&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A23111535%23id-name%3DS2CID&rft_id=info%3Apmid%2F11552976&rft_id=info%3Adoi%2F10.1046%2Fj.1365-2141.2001.02999.x&rft.aulast=Kyle&rft.aufirst=RA&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-11"><a href="#cite_ref-11">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSipeCohen2000" class="citation journal cs1">Sipe JD, Cohen AS (June 2000). "Review: history of the amyloid fibril". Journal of Structural Biology. 130 (2–3): 88–98. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1006%2Fjsbi.2000.4221">10.1006/jsbi.2000.4221</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10940217">10940217</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:16442783">16442783</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Structural+Biology&rft.atitle=Review%3A+history+of+the+amyloid+fibril&rft.volume=130&rft.issue=%3Cspan+class%3D%22nowrap%22%3E2%E2%80%93%3C%2Fspan%3E3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E88-%3C%2Fspan%3E98&rft.date=2000-06&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A16442783%23id-name%3DS2CID&rft_id=info%3Apmid%2F10940217&rft_id=info%3Adoi%2F10.1006%2Fjsbi.2000.4221&rft.aulast=Sipe&rft.aufirst=JD&rft.au=Cohen%2C+AS&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid17353506-12"><a href="#cite_ref-pmid17353506_12-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLinGurloKayedButler2007" class="citation journal cs1">Lin CY, Gurlo T, Kayed R, Butler AE, Haataja L, Glabe CG, Butler PC (May 2007). <a rel="nofollow" class="external text" href="https://doi.org/10.2337%2Fdb06-1579">"Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced β-cell apoptosis in h-IAPP transgenic mice"</a>. Diabetes. 56 (5): 1324–32. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2337%2Fdb06-1579">10.2337/db06-1579</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17353506">17353506</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Diabetes&rft.atitle=Toxic+human+islet+amyloid+polypeptide+%28h-IAPP%29+oligomers+are+intracellular%2C+and+vaccination+to+induce+anti-toxic+oligomer+antibodies+does+not+prevent+h-IAPP-induced+%CE%B2-cell+apoptosis+in+h-IAPP+transgenic+mice&rft.volume=56&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1324-%3C%2Fspan%3E32&rft.date=2007-05&rft_id=info%3Adoi%2F10.2337%2Fdb06-1579&rft_id=info%3Apmid%2F17353506&rft.aulast=Lin&rft.aufirst=CY&rft.au=Gurlo%2C+T&rft.au=Kayed%2C+R&rft.au=Butler%2C+AE&rft.au=Haataja%2C+L&rft.au=Glabe%2C+CG&rft.au=Butler%2C+PC&rft_id=https%3A%2F%2Fdoi.org%2F10.2337%252Fdb06-1579&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid15283924-13"><a href="#cite_ref-pmid15283924_13-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFNilsson2004" class="citation journal cs1">Nilsson MR (September 2004). "Techniques to study amyloid fibril formation in vitro". Methods. 34 (1): 151–60. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ymeth.2004.03.012">10.1016/j.ymeth.2004.03.012</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15283924">15283924</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Methods&rft.atitle=Techniques+to+study+amyloid+fibril+formation+in+vitro&rft.volume=34&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E151-%3C%2Fspan%3E60&rft.date=2004-09&rft_id=info%3Adoi%2F10.1016%2Fj.ymeth.2004.03.012&rft_id=info%3Apmid%2F15283924&rft.aulast=Nilsson&rft.aufirst=MR&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid17530168-14"><a href="#cite_ref-pmid17530168_14-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFändrich2007" class="citation journal cs1">Fändrich M (August 2007). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11138455">"On the structural definition of amyloid fibrils and other polypeptide aggregates"</a>. Cellular and Molecular Life Sciences. 64 (16): 2066–78. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs00018-007-7110-2">10.1007/s00018-007-7110-2</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11138455">11138455</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17530168">17530168</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:32667968">32667968</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cellular+and+Molecular+Life+Sciences&rft.atitle=On+the+structural+definition+of+amyloid+fibrils+and+other+polypeptide+aggregates&rft.volume=64&rft.issue=16&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2066-%3C%2Fspan%3E78&rft.date=2007-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC11138455%23id-name%3DPMC&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A32667968%23id-name%3DS2CID&rft_id=info%3Apmid%2F17530168&rft_id=info%3Adoi%2F10.1007%2Fs00018-007-7110-2&rft.aulast=F%C3%A4ndrich&rft.aufirst=M&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC11138455&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid18781964-15"><a href="#cite_ref-pmid18781964_15-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFChiangLamLuo2008" class="citation journal cs1">Chiang PK, Lam MA, Luo Y (September 2008). "The many faces of amyloid β in Alzheimer's disease". Current Molecular Medicine. 8 (6): 580–4. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F156652408785747951">10.2174/156652408785747951</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18781964">18781964</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Molecular+Medicine&rft.atitle=The+many+faces+of+amyloid+%CE%B2+in+Alzheimer%27s+disease&rft.volume=8&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E580-%3C%2Fspan%3E4&rft.date=2008-09&rft_id=info%3Adoi%2F10.2174%2F156652408785747951&rft_id=info%3Apmid%2F18781964&rft.aulast=Chiang&rft.aufirst=PK&rft.au=Lam%2C+MA&rft.au=Luo%2C+Y&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid18368143-16">^ <a href="#cite_ref-pmid18368143_16-0">a</a> <a href="#cite_ref-pmid18368143_16-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFIrvineEl-AgnafShankarWalsh2008" class="citation journal cs1">Irvine GB, El-Agnaf OM, Shankar GM, Walsh DM (2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2274891">"Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases"</a>. Molecular Medicine. 14 (7–8): 451–64. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2119%2F2007-00100.Irvine">10.2119/2007-00100.Irvine</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2274891">2274891</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18368143">18368143</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Molecular+Medicine&rft.atitle=Protein+aggregation+in+the+brain%3A+the+molecular+basis+for+Alzheimer%27s+and+Parkinson%27s+diseases&rft.volume=14&rft.issue=%3Cspan+class%3D%22nowrap%22%3E7%E2%80%93%3C%2Fspan%3E8&rft.pages=%3Cspan+class%3D%22nowrap%22%3E451-%3C%2Fspan%3E64&rft.date=2008&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2274891%23id-name%3DPMC&rft_id=info%3Apmid%2F18368143&rft_id=info%3Adoi%2F10.2119%2F2007-00100.Irvine&rft.aulast=Irvine&rft.aufirst=GB&rft.au=El-Agnaf%2C+OM&rft.au=Shankar%2C+GM&rft.au=Walsh%2C+DM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2274891&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid17505973-17">^ <a href="#cite_ref-pmid17505973_17-0">a</a> <a href="#cite_ref-pmid17505973_17-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFerreiraVieiraDe_Felice2007" class="citation journal cs1">Ferreira ST, Vieira MN, De Felice FG (2007). <a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F15216540701283882">"Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases"</a>. IUBMB Life. 59 (4–5): 332–45. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F15216540701283882">10.1080/15216540701283882</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17505973">17505973</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:7489461">7489461</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=IUBMB+Life&rft.atitle=Soluble+protein+oligomers+as+emerging+toxins+in+Alzheimer%27s+and+other+amyloid+diseases&rft.volume=59&rft.issue=%3Cspan+class%3D%22nowrap%22%3E4%E2%80%93%3C%2Fspan%3E5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E332-%3C%2Fspan%3E45&rft.date=2007&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A7489461%23id-name%3DS2CID&rft_id=info%3Apmid%2F17505973&rft_id=info%3Adoi%2F10.1080%2F15216540701283882&rft.aulast=Ferreira&rft.aufirst=ST&rft.au=Vieira%2C+MN&rft.au=De+Felice%2C+FG&rft_id=https%3A%2F%2Fdoi.org%2F10.1080%252F15216540701283882&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid22813427-18"><a href="#cite_ref-pmid22813427_18-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHamley2012" class="citation journal cs1">Hamley IW (October 2012). <a rel="nofollow" class="external text" href="http://centaur.reading.ac.uk/30230/2/AbetaRevisednew%20-IWH%20%281%29.pdf">"The amyloid β peptide: a chemist's perspective. Role in Alzheimer's and fibrillization"</a> (PDF). Chemical Reviews. 112 (10): 5147–92. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fcr3000994">10.1021/cr3000994</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22813427">22813427</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemical+Reviews&rft.atitle=The+amyloid+%CE%B2+peptide%3A+a+chemist%27s+perspective.+Role+in+Alzheimer%27s+and+fibrillization&rft.volume=112&rft.issue=10&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5147-%3C%2Fspan%3E92&rft.date=2012-10&rft_id=info%3Adoi%2F10.1021%2Fcr3000994&rft_id=info%3Apmid%2F22813427&rft.aulast=Hamley&rft.aufirst=IW&rft_id=http%3A%2F%2Fcentaur.reading.ac.uk%2F30230%2F2%2FAbetaRevisednew%2520-IWH%2520%25281%2529.pdf&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-19"><a href="#cite_ref-19">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite class="citation journal cs1"><a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F86132">"More than just mad cow disease"</a>. Nature Structural Biology. 8 (4): 281. April 2001. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F86132">10.1038/86132</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11276238">11276238</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Structural+Biology&rft.atitle=More+than+just+mad+cow+disease&rft.volume=8&rft.issue=4&rft.pages=281&rft.date=2001-04&rft_id=info%3Adoi%2F10.1038%2F86132&rft_id=info%3Apmid%2F11276238&rft_id=https%3A%2F%2Fdoi.org%2F10.1038%252F86132&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid18637947-20"><a href="#cite_ref-pmid18637947_20-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFTruantAtwalDesmondMunsie2008" class="citation journal cs1">Truant R, Atwal RS, Desmond C, Munsie L, Tran T (September 2008). <a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1742-4658.2008.06561.x">"Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases"</a>. The FEBS Journal. 275 (17): 4252–62. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1742-4658.2008.06561.x">10.1111/j.1742-4658.2008.06561.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18637947">18637947</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:11510408">11510408</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+FEBS+Journal&rft.atitle=Huntington%27s+disease%3A+revisiting+the+aggregation+hypothesis+in+polyglutamine+neurodegenerative+diseases&rft.volume=275&rft.issue=17&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4252-%3C%2Fspan%3E62&rft.date=2008-09&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A11510408%23id-name%3DS2CID&rft_id=info%3Apmid%2F18637947&rft_id=info%3Adoi%2F10.1111%2Fj.1742-4658.2008.06561.x&rft.aulast=Truant&rft.aufirst=R&rft.au=Atwal%2C+RS&rft.au=Desmond%2C+C&rft.au=Munsie%2C+L&rft.au=Tran%2C+T&rft_id=https%3A%2F%2Fdoi.org%2F10.1111%252Fj.1742-4658.2008.06561.x&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid16848688-21"><a href="#cite_ref-pmid16848688_21-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFWeydtLa_Spada2006" class="citation journal cs1">Weydt P, La Spada AR (August 2006). "Targeting protein aggregation in neurodegeneration--lessons from polyglutamine disorders". Expert Opinion on Therapeutic Targets. 10 (4): 505–13. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1517%2F14728222.10.4.505">10.1517/14728222.10.4.505</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16848688">16848688</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:24483289">24483289</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Expert+Opinion+on+Therapeutic+Targets&rft.atitle=Targeting+protein+aggregation+in+neurodegeneration--lessons+from+polyglutamine+disorders&rft.volume=10&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E505-%3C%2Fspan%3E13&rft.date=2006-08&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A24483289%23id-name%3DS2CID&rft_id=info%3Apmid%2F16848688&rft_id=info%3Adoi%2F10.1517%2F14728222.10.4.505&rft.aulast=Weydt&rft.aufirst=P&rft.au=La+Spada%2C+AR&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-emedicine.medscape.com-22">^ <a href="#cite_ref-emedicine.medscape.com_22-0">a</a> <a href="#cite_ref-emedicine.medscape.com_22-1">b</a> <a href="#cite_ref-emedicine.medscape.com_22-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHolmesEdisonBaethgeJacobson2018" class="citation journal cs1">Holmes RO, Edison J, Baethge BA, Jacobson DR (10 October 2018). <a rel="nofollow" class="external text" href="https://emedicine.medscape.com/article/335414-overview">"Amyloidosis: Definition of Amyloid and Amyloidosis, Classification Systems, Systemic Amyloidoses"</a>. Medscape.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Medscape&rft.atitle=Amyloidosis%3A+Definition+of+Amyloid+and+Amyloidosis%2C+Classification+Systems%2C+Systemic+Amyloidoses&rft.date=2018-10-10&rft.aulast=Holmes&rft.aufirst=RO&rft.au=Edison%2C+J&rft.au=Baethge%2C+BA&rft.au=Jacobson%2C+DR&rft_id=https%3A%2F%2Femedicine.medscape.com%2Farticle%2F335414-overview&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid18314421-23"><a href="#cite_ref-pmid18314421_23-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHaatajaGurloHuangButler2008" class="citation journal cs1">Haataja L, Gurlo T, Huang CJ, Butler PC (May 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2528855">"Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis"</a>. Endocrine Reviews. 29 (3): 303–16. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1210%2Fer.2007-0037">10.1210/er.2007-0037</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2528855">2528855</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18314421">18314421</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Endocrine+Reviews&rft.atitle=Islet+amyloid+in+type+2+diabetes%2C+and+the+toxic+oligomer+hypothesis&rft.volume=29&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E303-%3C%2Fspan%3E16&rft.date=2008-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2528855%23id-name%3DPMC&rft_id=info%3Apmid%2F18314421&rft_id=info%3Adoi%2F10.1210%2Fer.2007-0037&rft.aulast=Haataja&rft.aufirst=L&rft.au=Gurlo%2C+T&rft.au=Huang%2C+CJ&rft.au=Butler%2C+PC&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2528855&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid10933741-24"><a href="#cite_ref-pmid10933741_24-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHöppenerAhrénLips2000" class="citation journal cs1">Höppener JW, Ahrén B, Lips CJ (August 2000). "Islet amyloid and type 2 diabetes mellitus". The New England Journal of Medicine. 343 (6): 411–9. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1056%2FNEJM200008103430607">10.1056/NEJM200008103430607</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10933741">10933741</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+New+England+Journal+of+Medicine&rft.atitle=Islet+amyloid+and+type+2+diabetes+mellitus&rft.volume=343&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E411-%3C%2Fspan%3E9&rft.date=2000-08&rft_id=info%3Adoi%2F10.1056%2FNEJM200008103430607&rft_id=info%3Apmid%2F10933741&rft.aulast=H%C3%B6ppener&rft.aufirst=JW&rft.au=Ahr%C3%A9n%2C+B&rft.au=Lips%2C+CJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid18487849-25"><a href="#cite_ref-pmid18487849_25-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHammerWangMcGuffieChapman2008" class="citation journal cs1">Hammer ND, Wang X, McGuffie BA, Chapman MR (May 2008). <a rel="nofollow" class="external text" href="https://archive.today/20130103210811/http://iospress.metapress.com/openurl.asp?genre=article&issn=1387-2877&volume=13&issue=4&spage=407">"Amyloids: friend or foe?"</a>. Journal of Alzheimer's Disease. 13 (4): 407–19. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.3233%2FJAD-2008-13406">10.3233/JAD-2008-13406</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2674399">2674399</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18487849">18487849</a>. Archived from <a rel="nofollow" class="external text" href="http://iospress.metapress.com/openurl.asp?genre=article&issn=1387-2877&volume=13&issue=4&spage=407">the original</a> on 2013-01-03.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Alzheimer%27s+Disease&rft.atitle=Amyloids%3A+friend+or+foe%3F&rft.volume=13&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E407-%3C%2Fspan%3E19&rft.date=2008-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2674399%23id-name%3DPMC&rft_id=info%3Apmid%2F18487849&rft_id=info%3Adoi%2F10.3233%2FJAD-2008-13406&rft.aulast=Hammer&rft.aufirst=ND&rft.au=Wang%2C+X&rft.au=McGuffie%2C+BA&rft.au=Chapman%2C+MR&rft_id=http%3A%2F%2Fiospress.metapress.com%2Fopenurl.asp%3Fgenre%3Darticle%26issn%3D1387-2877%26volume%3D13%26issue%3D4%26spage%3D407&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid17412596-26"><a href="#cite_ref-pmid17412596_26-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFowlerKoulovBalchKelly2007" class="citation journal cs1">Fowler DM, Koulov AV, Balch WE, Kelly JW (May 2007). "Functional amyloid--from bacteria to humans". Trends in Biochemical Sciences. 32 (5): 217–24. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.tibs.2007.03.003">10.1016/j.tibs.2007.03.003</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17412596">17412596</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Biochemical+Sciences&rft.atitle=Functional+amyloid--from+bacteria+to+humans&rft.volume=32&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E217-%3C%2Fspan%3E24&rft.date=2007-05&rft_id=info%3Adoi%2F10.1016%2Fj.tibs.2007.03.003&rft_id=info%3Apmid%2F17412596&rft.aulast=Fowler&rft.aufirst=DM&rft.au=Koulov%2C+AV&rft.au=Balch%2C+WE&rft.au=Kelly%2C+JW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid16300414-27"><a href="#cite_ref-pmid16300414_27-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFowlerKoulovAlory-JostMarks2006" class="citation journal cs1">Fowler DM, Koulov AV, Alory-Jost C, Marks MS, Balch WE, Kelly JW (January 2006). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1288039">"Functional amyloid formation within mammalian tissue"</a>. PLOS Biology. 4 (1): e6. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1371%2Fjournal.pbio.0040006">10.1371/journal.pbio.0040006</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1288039">1288039</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16300414">16300414</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PLOS+Biology&rft.atitle=Functional+amyloid+formation+within+mammalian+tissue&rft.volume=4&rft.issue=1&rft.pages=e6&rft.date=2006-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1288039%23id-name%3DPMC&rft_id=info%3Apmid%2F16300414&rft_id=info%3Adoi%2F10.1371%2Fjournal.pbio.0040006&rft.aulast=Fowler&rft.aufirst=DM&rft.au=Koulov%2C+AV&rft.au=Alory-Jost%2C+C&rft.au=Marks%2C+MS&rft.au=Balch%2C+WE&rft.au=Kelly%2C+JW&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1288039&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-28"><a href="#cite_ref-28">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMajiPerrinSawayaJessberger2009" class="citation journal cs1">Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, Rissman RA, et al. (July 2009). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2865899">"Functional amyloids as natural storage of peptide hormones in pituitary secretory granules"</a>. Science. 325 (5938): 328–32. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2009Sci...325..328M">2009Sci...325..328M</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1126%2Fscience.1173155">10.1126/science.1173155</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2865899">2865899</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19541956">19541956</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Science&rft.atitle=Functional+amyloids+as+natural+storage+of+peptide+hormones+in+pituitary+secretory+granules&rft.volume=325&rft.issue=5938&rft.pages=%3Cspan+class%3D%22nowrap%22%3E328-%3C%2Fspan%3E32&rft.date=2009-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2865899%23id-name%3DPMC&rft_id=info%3Apmid%2F19541956&rft_id=info%3Adoi%2F10.1126%2Fscience.1173155&rft_id=info%3Abibcode%2F2009Sci...325..328M&rft.aulast=Maji&rft.aufirst=SK&rft.au=Perrin%2C+MH&rft.au=Sawaya%2C+MR&rft.au=Jessberger%2C+S&rft.au=Vadodaria%2C+K&rft.au=Rissman%2C+RA&rft.au=Singru%2C+PS&rft.au=Nilsson%2C+KP&rft.au=Simon%2C+R&rft.au=Schubert%2C+D&rft.au=Eisenberg%2C+D&rft.au=Rivier%2C+J&rft.au=Sawchenko%2C+P&rft.au=Vale%2C+W&rft.au=Riek%2C+R&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2865899&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid22817896-29"><a href="#cite_ref-pmid22817896_29-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLiMcQuadeSiemerNapetschnig2012" class="citation journal cs1">Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, et al. (July 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3664196">"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis"</a>. Cell. 150 (2): 339–50. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.cell.2012.06.019">10.1016/j.cell.2012.06.019</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3664196">3664196</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22817896">22817896</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cell&rft.atitle=The+RIP1%2FRIP3+necrosome+forms+a+functional+amyloid+signaling+complex+required+for+programmed+necrosis&rft.volume=150&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E339-%3C%2Fspan%3E50&rft.date=2012-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3664196%23id-name%3DPMC&rft_id=info%3Apmid%2F22817896&rft_id=info%3Adoi%2F10.1016%2Fj.cell.2012.06.019&rft.aulast=Li&rft.aufirst=J&rft.au=McQuade%2C+T&rft.au=Siemer%2C+AB&rft.au=Napetschnig%2C+J&rft.au=Moriwaki%2C+K&rft.au=Hsiao%2C+YS&rft.au=Damko%2C+E&rft.au=Moquin%2C+D&rft.au=Walz%2C+T&rft.au=McDermott%2C+A&rft.au=Chan%2C+FK&rft.au=Wu%2C+H&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3664196&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid24691351-30"><a href="#cite_ref-pmid24691351_30-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFUsmaniZirafiMüllerSandi-Monroy2014" class="citation journal cs1">Usmani SM, Zirafi O, Müller JA, Sandi-Monroy NL, Yadav JK, Meier C, et al. (April 2014). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4129123">"Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen"</a>. Nature Communications. 5: 3508. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2014NatCo...5.3508U">2014NatCo...5.3508U</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fncomms4508">10.1038/ncomms4508</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4129123">4129123</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/24691351">24691351</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Communications&rft.atitle=Direct+visualization+of+HIV-enhancing+endogenous+amyloid+fibrils+in+human+semen&rft.volume=5&rft.pages=3508&rft.date=2014-04&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4129123%23id-name%3DPMC&rft_id=info%3Apmid%2F24691351&rft_id=info%3Adoi%2F10.1038%2Fncomms4508&rft_id=info%3Abibcode%2F2014NatCo...5.3508U&rft.aulast=Usmani&rft.aufirst=SM&rft.au=Zirafi%2C+O&rft.au=M%C3%BCller%2C+JA&rft.au=Sandi-Monroy%2C+NL&rft.au=Yadav%2C+JK&rft.au=Meier%2C+C&rft.au=Weil%2C+T&rft.au=Roan%2C+NR&rft.au=Greene%2C+WC&rft.au=Walther%2C+P&rft.au=Nilsson%2C+KP&rft.au=Hammarstr%C3%B6m%2C+P&rft.au=Wetzel%2C+R&rft.au=Pilcher%2C+CD&rft.au=Gagsteiger%2C+F&rft.au=F%C3%A4ndrich%2C+M&rft.au=Kirchhoff%2C+F&rft.au=M%C3%BCnch%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4129123&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-31"><a href="#cite_ref-31">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDueholmAlbertsenOtzenNielsen2012" class="citation journal cs1">Dueholm MS, Albertsen M, Otzen D, Nielsen PH (2012). Webber MA (ed.). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3521004">"Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure"</a>. PLOS ONE. 7 (12): e51274. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2012PLoSO...751274D">2012PLoSO...751274D</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1371%2Fjournal.pone.0051274">10.1371/journal.pone.0051274</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3521004">3521004</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23251478">23251478</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PLOS+ONE&rft.atitle=Curli+functional+amyloid+systems+are+phylogenetically+widespread+and+display+large+diversity+in+operon+and+protein+structure&rft.volume=7&rft.issue=12&rft.pages=e51274&rft.date=2012&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3521004%23id-name%3DPMC&rft_id=info%3Apmid%2F23251478&rft_id=info%3Adoi%2F10.1371%2Fjournal.pone.0051274&rft_id=info%3Abibcode%2F2012PLoSO...751274D&rft.aulast=Dueholm&rft.aufirst=MS&rft.au=Albertsen%2C+M&rft.au=Otzen%2C+D&rft.au=Nielsen%2C+PH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3521004&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-32"><a href="#cite_ref-32">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBayroDavisoBelenkyGriffin2012" class="citation journal cs1">Bayro MJ, Daviso E, Belenky M, Griffin RG, Herzfeld J (January 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3271001">"An amyloid organelle, solid-state NMR evidence for cross-β assembly of gas vesicles"</a>. The Journal of Biological Chemistry. 287 (5): 3479–84. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M111.313049">10.1074/jbc.M111.313049</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3271001">3271001</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22147705">22147705</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=An+amyloid+organelle%2C+solid-state+NMR+evidence+for+cross-%CE%B2+assembly+of+gas+vesicles&rft.volume=287&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E3479-%3C%2Fspan%3E84&rft.date=2012-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3271001%23id-name%3DPMC&rft_id=info%3Apmid%2F22147705&rft_id=info%3Adoi%2F10.1074%2Fjbc.M111.313049&rft.aulast=Bayro&rft.aufirst=MJ&rft.au=Daviso%2C+E&rft.au=Belenky%2C+M&rft.au=Griffin%2C+RG&rft.au=Herzfeld%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3271001&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-33"><a href="#cite_ref-33">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDueholmPetersenSønderkærLarsen2010" class="citation journal cs1">Dueholm MS, Petersen SV, Sønderkær M, Larsen P, Christiansen G, Hein KL, et al. (August 2010). <a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1365-2958.2010.07269.x">"Functional amyloid in Pseudomonas"</a>. Molecular Microbiology. 77 (4): 1009–20. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1365-2958.2010.07269.x">10.1111/j.1365-2958.2010.07269.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20572935">20572935</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:205368641">205368641</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Molecular+Microbiology&rft.atitle=Functional+amyloid+in+Pseudomonas&rft.volume=77&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1009-%3C%2Fspan%3E20&rft.date=2010-08&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A205368641%23id-name%3DS2CID&rft_id=info%3Apmid%2F20572935&rft_id=info%3Adoi%2F10.1111%2Fj.1365-2958.2010.07269.x&rft.aulast=Dueholm&rft.aufirst=MS&rft.au=Petersen%2C+SV&rft.au=S%C3%B8nderk%C3%A6r%2C+M&rft.au=Larsen%2C+P&rft.au=Christiansen%2C+G&rft.au=Hein%2C+KL&rft.au=Enghild%2C+JJ&rft.au=Nielsen%2C+JL&rft.au=Nielsen%2C+KL&rft.au=Nielsen%2C+PH&rft.au=Otzen%2C+DE&rft_id=https%3A%2F%2Fdoi.org%2F10.1111%252Fj.1365-2958.2010.07269.x&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-34"><a href="#cite_ref-34">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDueholmSøndergaardNilssonChristiansen2013" class="citation journal cs1">Dueholm MS, Søndergaard MT, Nilsson M, Christiansen G, Stensballe A, Overgaard MT, et al. (June 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3684753">"Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation"</a>. MicrobiologyOpen. 2 (3): 365–82. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fmbo3.81">10.1002/mbo3.81</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3684753">3684753</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23504942">23504942</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=MicrobiologyOpen&rft.atitle=Expression+of+Fap+amyloids+in+Pseudomonas+aeruginosa%2C+P.+fluorescens%2C+and+P.+putida+results+in+aggregation+and+increased+biofilm+formation&rft.volume=2&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E365-%3C%2Fspan%3E82&rft.date=2013-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3684753%23id-name%3DPMC&rft_id=info%3Apmid%2F23504942&rft_id=info%3Adoi%2F10.1002%2Fmbo3.81&rft.aulast=Dueholm&rft.aufirst=MS&rft.au=S%C3%B8ndergaard%2C+MT&rft.au=Nilsson%2C+M&rft.au=Christiansen%2C+G&rft.au=Stensballe%2C+A&rft.au=Overgaard%2C+MT&rft.au=Givskov%2C+M&rft.au=Tolker-Nielsen%2C+T&rft.au=Otzen%2C+DE&rft.au=Nielsen%2C+PH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3684753&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid12832396-35"><a href="#cite_ref-pmid12832396_35-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFClaessenRinkde_JongSiebring2003" class="citation journal cs1">Claessen D, Rink R, de Jong W, Siebring J, de Vreugd P, Boersma FG, et al. (July 2003). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC196180">"A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils"</a>. Genes & Development. 17 (14): 1714–26. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1101%2Fgad.264303">10.1101/gad.264303</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC196180">196180</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12832396">12832396</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Genes+%26+Development&rft.atitle=A+novel+class+of+secreted+hydrophobic+proteins+is+involved+in+aerial+hyphae+formation+in+Streptomyces+coelicolor+by+forming+amyloid-like+fibrils&rft.volume=17&rft.issue=14&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1714-%3C%2Fspan%3E26&rft.date=2003-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC196180%23id-name%3DPMC&rft_id=info%3Apmid%2F12832396&rft_id=info%3Adoi%2F10.1101%2Fgad.264303&rft.aulast=Claessen&rft.aufirst=D&rft.au=Rink%2C+R&rft.au=de+Jong%2C+W&rft.au=Siebring%2C+J&rft.au=de+Vreugd%2C+P&rft.au=Boersma%2C+FG&rft.au=Dijkhuizen%2C+L&rft.au=Wosten%2C+HA&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC196180&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid12180993-36"><a href="#cite_ref-pmid12180993_36-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKenneyKnightWiseVollrath2002" class="citation journal cs1">Kenney JM, Knight D, Wise MJ, Vollrath F (August 2002). <a rel="nofollow" class="external text" href="https://doi.org/10.1046%2Fj.1432-1033.2002.03112.x">"Amyloidogenic nature of spider silk"</a>. European Journal of Biochemistry. 269 (16): 4159–63. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1046%2Fj.1432-1033.2002.03112.x">10.1046/j.1432-1033.2002.03112.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12180993">12180993</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=European+Journal+of+Biochemistry&rft.atitle=Amyloidogenic+nature+of+spider+silk&rft.volume=269&rft.issue=16&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4159-%3C%2Fspan%3E63&rft.date=2002-08&rft_id=info%3Adoi%2F10.1046%2Fj.1432-1033.2002.03112.x&rft_id=info%3Apmid%2F12180993&rft.aulast=Kenney&rft.aufirst=JM&rft.au=Knight%2C+D&rft.au=Wise%2C+MJ&rft.au=Vollrath%2C+F&rft_id=https%3A%2F%2Fdoi.org%2F10.1046%252Fj.1432-1033.2002.03112.x&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid11250193-37"><a href="#cite_ref-pmid11250193_37-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMackayMatthewsWinefieldMackay2001" class="citation journal cs1">Mackay JP, Matthews JM, Winefield RD, Mackay LG, Haverkamp RG, Templeton MD (February 2001). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0969-2126%2800%2900559-1">"The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures"</a>. Structure. 9 (2): 83–91. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0969-2126%2800%2900559-1">10.1016/s0969-2126(00)00559-1</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11250193">11250193</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Structure&rft.atitle=The+hydrophobin+EAS+is+largely+unstructured+in+solution+and+functions+by+forming+amyloid-like+structures&rft.volume=9&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E83-%3C%2Fspan%3E91&rft.date=2001-02&rft_id=info%3Adoi%2F10.1016%2Fs0969-2126%2800%2900559-1&rft_id=info%3Apmid%2F11250193&rft.aulast=Mackay&rft.aufirst=JP&rft.au=Matthews%2C+JM&rft.au=Winefield%2C+RD&rft.au=Mackay%2C+LG&rft.au=Haverkamp%2C+RG&rft.au=Templeton%2C+MD&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252Fs0969-2126%252800%252900559-1&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-38"><a href="#cite_ref-38">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGarciaLeeRamsookAlsteens2011" class="citation journal cs1">Garcia MC, Lee JT, Ramsook CB, Alsteens D, Dufrêne YF, Lipke PN (March 2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3050909">"A role for amyloid in cell aggregation and biofilm formation"</a>. PLOS ONE. 6 (3): e17632. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2011PLoSO...617632G">2011PLoSO...617632G</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1371%2Fjournal.pone.0017632">10.1371/journal.pone.0017632</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3050909">3050909</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21408122">21408122</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PLOS+ONE&rft.atitle=A+role+for+amyloid+in+cell+aggregation+and+biofilm+formation&rft.volume=6&rft.issue=3&rft.pages=e17632&rft.date=2011-03&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3050909%23id-name%3DPMC&rft_id=info%3Apmid%2F21408122&rft_id=info%3Adoi%2F10.1371%2Fjournal.pone.0017632&rft_id=info%3Abibcode%2F2011PLoSO...617632G&rft.aulast=Garcia&rft.aufirst=MC&rft.au=Lee%2C+JT&rft.au=Ramsook%2C+CB&rft.au=Alsteens%2C+D&rft.au=Dufr%C3%AAne%2C+YF&rft.au=Lipke%2C+PN&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3050909&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-39"><a href="#cite_ref-39">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLipkeGarciaAlsteensRamsook2012" class="citation journal cs1">Lipke PN, Garcia MC, Alsteens D, Ramsook CB, Klotz SA, Dufrêne YF (February 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3278544">"Strengthening relationships: amyloids create adhesion nanodomains in yeasts"</a>. Trends in Microbiology. 20 (2): 59–65. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.tim.2011.10.002">10.1016/j.tim.2011.10.002</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3278544">3278544</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22099004">22099004</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Microbiology&rft.atitle=Strengthening+relationships%3A+amyloids+create+adhesion+nanodomains+in+yeasts&rft.volume=20&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E59-%3C%2Fspan%3E65&rft.date=2012-02&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3278544%23id-name%3DPMC&rft_id=info%3Apmid%2F22099004&rft_id=info%3Adoi%2F10.1016%2Fj.tim.2011.10.002&rft.aulast=Lipke&rft.aufirst=PN&rft.au=Garcia%2C+MC&rft.au=Alsteens%2C+D&rft.au=Ramsook%2C+CB&rft.au=Klotz%2C+SA&rft.au=Dufr%C3%AAne%2C+YF&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3278544&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-40"><a href="#cite_ref-40">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLarsenNielsenDueholmWetzel2007" class="citation journal cs1">Larsen P, Nielsen JL, Dueholm MS, Wetzel R, Otzen D, Nielsen PH (December 2007). "Amyloid adhesins are abundant in natural biofilms". Environmental Microbiology. 9 (12): 3077–90. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2007EnvMi...9.3077L">2007EnvMi...9.3077L</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1462-2920.2007.01418.x">10.1111/j.1462-2920.2007.01418.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17991035">17991035</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Environmental+Microbiology&rft.atitle=Amyloid+adhesins+are+abundant+in+natural+biofilms&rft.volume=9&rft.issue=12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E3077-%3C%2Fspan%3E90&rft.date=2007-12&rft_id=info%3Apmid%2F17991035&rft_id=info%3Adoi%2F10.1111%2Fj.1462-2920.2007.01418.x&rft_id=info%3Abibcode%2F2007EnvMi...9.3077L&rft.aulast=Larsen&rft.aufirst=P&rft.au=Nielsen%2C+JL&rft.au=Dueholm%2C+MS&rft.au=Wetzel%2C+R&rft.au=Otzen%2C+D&rft.au=Nielsen%2C+PH&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-41"><a href="#cite_ref-41">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDueholmLarsenFinsterStenvang2015" class="citation journal cs1">Dueholm MS, Larsen P, Finster K, Stenvang MR, Christiansen G, Vad BS, et al. (August 2015). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4536462">"The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids"</a>. The Journal of Biological Chemistry. 290 (33): 20590–600. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M115.654780">10.1074/jbc.M115.654780</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4536462">4536462</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/26109065">26109065</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=The+Tubular+Sheaths+Encasing+Methanosaeta+thermophila+Filaments+Are+Functional+Amyloids&rft.volume=290&rft.issue=33&rft.pages=%3Cspan+class%3D%22nowrap%22%3E20590-%3C%2Fspan%3E600&rft.date=2015-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4536462%23id-name%3DPMC&rft_id=info%3Apmid%2F26109065&rft_id=info%3Adoi%2F10.1074%2Fjbc.M115.654780&rft.aulast=Dueholm&rft.aufirst=MS&rft.au=Larsen%2C+P&rft.au=Finster%2C+K&rft.au=Stenvang%2C+MR&rft.au=Christiansen%2C+G&rft.au=Vad%2C+BS&rft.au=B%C3%B8ggild%2C+A&rft.au=Otzen%2C+DE&rft.au=Nielsen%2C+PH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4536462&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid9275200-42"><a href="#cite_ref-pmid9275200_42-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFCoustouDeleuSaupeBegueret1997" class="citation journal cs1">Coustou V, Deleu C, Saupe S, Begueret J (September 1997). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23266">"The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog"</a>. Proceedings of the National Academy of Sciences of the United States of America. 94 (18): 9773–8. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1997PNAS...94.9773C">1997PNAS...94.9773C</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.94.18.9773">10.1073/pnas.94.18.9773</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23266">23266</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9275200">9275200</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=The+protein+product+of+the+het-s+heterokaryon+incompatibility+gene+of+the+fungus+Podospora+anserina+behaves+as+a+prion+analog&rft.volume=94&rft.issue=18&rft.pages=%3Cspan+class%3D%22nowrap%22%3E9773-%3C%2Fspan%3E8&rft.date=1997-09&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC23266%23id-name%3DPMC&rft_id=info%3Apmid%2F9275200&rft_id=info%3Adoi%2F10.1073%2Fpnas.94.18.9773&rft_id=info%3Abibcode%2F1997PNAS...94.9773C&rft.aulast=Coustou&rft.aufirst=V&rft.au=Deleu%2C+C&rft.au=Saupe%2C+S&rft.au=Begueret%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC23266&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid14697205-43"><a href="#cite_ref-pmid14697205_43-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSiLindquistKandel2003" class="citation journal cs1">Si K, Lindquist S, Kandel ER (December 2003). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0092-8674%2803%2901020-1">"A neuronal isoform of the aplysia CPEB has prion-like properties"</a>. Cell. 115 (7): 879–91. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0092-8674%2803%2901020-1">10.1016/s0092-8674(03)01020-1</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14697205">14697205</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:3060439">3060439</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cell&rft.atitle=A+neuronal+isoform+of+the+aplysia+CPEB+has+prion-like+properties&rft.volume=115&rft.issue=7&rft.pages=%3Cspan+class%3D%22nowrap%22%3E879-%3C%2Fspan%3E91&rft.date=2003-12&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A3060439%23id-name%3DS2CID&rft_id=info%3Apmid%2F14697205&rft_id=info%3Adoi%2F10.1016%2Fs0092-8674%2803%2901020-1&rft.aulast=Si&rft.aufirst=K&rft.au=Lindquist%2C+S&rft.au=Kandel%2C+ER&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252Fs0092-8674%252803%252901020-1&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid19015532-44"><a href="#cite_ref-pmid19015532_44-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFParavastuLeapmanYauTycko2008" class="citation journal cs1">Paravastu AK, Leapman RD, Yau WM, Tycko R (25 November 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2587602">"Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils"</a>. PNAS. 105 (47): 18349–54. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2008PNAS..10518349P">2008PNAS..10518349P</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.0806270105">10.1073/pnas.0806270105</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2587602">2587602</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19015532">19015532</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PNAS&rft.atitle=Molecular+structural+basis+for+polymorphism+in+Alzheimer%27s+%CE%B2-amyloid+fibrils&rft.volume=105&rft.issue=47&rft.pages=%3Cspan+class%3D%22nowrap%22%3E18349-%3C%2Fspan%3E54&rft.date=2008-11-25&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2587602%23id-name%3DPMC&rft_id=info%3Apmid%2F19015532&rft_id=info%3Adoi%2F10.1073%2Fpnas.0806270105&rft_id=info%3Abibcode%2F2008PNAS..10518349P&rft.aulast=Paravastu&rft.aufirst=AK&rft.au=Leapman%2C+RD&rft.au=Yau%2C+WM&rft.au=Tycko%2C+R&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2587602&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-45"><a href="#cite_ref-45">^</a> Wormell RL. New fibres from proteins. Academic Press, 1954, p. 106. </li> <li id="cite_note-46"><a href="#cite_ref-46">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMeierRiekBöckmann2017" class="citation journal cs1">Meier BH, Riek R, Böckmann A (October 2017). "Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR". Trends in Biochemical Sciences. 42 (10): 777–787. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.tibs.2017.08.001">10.1016/j.tibs.2017.08.001</a>. <a href="/wiki/Hdl_(identifier)" class="mw-redirect" title="Hdl (identifier)">hdl</a>:<a rel="nofollow" class="external text" href="https://hdl.handle.net/20.500.11850%2F193533">20.500.11850/193533</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28916413">28916413</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Biochemical+Sciences&rft.atitle=Emerging+Structural+Understanding+of+Amyloid+Fibrils+by+Solid-State+NMR&rft.volume=42&rft.issue=10&rft.pages=%3Cspan+class%3D%22nowrap%22%3E777-%3C%2Fspan%3E787&rft.date=2017-10&rft_id=info%3Ahdl%2F20.500.11850%2F193533&rft_id=info%3Apmid%2F28916413&rft_id=info%3Adoi%2F10.1016%2Fj.tibs.2017.08.001&rft.aulast=Meier&rft.aufirst=BH&rft.au=Riek%2C+R&rft.au=B%C3%B6ckmann%2C+A&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-47"><a href="#cite_ref-47">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFitzpatrickFalconHeMurzin2017" class="citation journal cs1">Fitzpatrick AW, Falcon B, He S, Murzin AG, Murshudov G, Garringer HJ, et al. (July 2017). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5552202">"Cryo-EM structures of tau filaments from Alzheimer's disease"</a>. Nature. 547 (7662): 185–190. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2017Natur.547..185F">2017Natur.547..185F</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnature23002">10.1038/nature23002</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5552202">5552202</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28678775">28678775</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=Cryo-EM+structures+of+tau+filaments+from+Alzheimer%27s+disease&rft.volume=547&rft.issue=7662&rft.pages=%3Cspan+class%3D%22nowrap%22%3E185-%3C%2Fspan%3E190&rft.date=2017-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5552202%23id-name%3DPMC&rft_id=info%3Apmid%2F28678775&rft_id=info%3Adoi%2F10.1038%2Fnature23002&rft_id=info%3Abibcode%2F2017Natur.547..185F&rft.aulast=Fitzpatrick&rft.aufirst=AW&rft.au=Falcon%2C+B&rft.au=He%2C+S&rft.au=Murzin%2C+AG&rft.au=Murshudov%2C+G&rft.au=Garringer%2C+HJ&rft.au=Crowther%2C+RA&rft.au=Ghetti%2C+B&rft.au=Goedert%2C+M&rft.au=Scheres%2C+SH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5552202&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-Nelson2005-48"><a href="#cite_ref-Nelson2005_48-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFNelsonSawayaBalbirnieMadsen2005" class="citation journal cs1">Nelson R, Sawaya MR, Balbirnie M, Madsen AØ, Riekel C, Grothe R, Eisenberg D (June 2005). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1479801">"Structure of the cross-β spine of amyloid-like fibrils"</a>. Nature. 435 (7043): 773–8. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2005Natur.435..773N">2005Natur.435..773N</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnature03680">10.1038/nature03680</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1479801">1479801</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15944695">15944695</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=Structure+of+the+cross-%CE%B2+spine+of+amyloid-like+fibrils&rft.volume=435&rft.issue=7043&rft.pages=%3Cspan+class%3D%22nowrap%22%3E773-%3C%2Fspan%3E8&rft.date=2005-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1479801%23id-name%3DPMC&rft_id=info%3Apmid%2F15944695&rft_id=info%3Adoi%2F10.1038%2Fnature03680&rft_id=info%3Abibcode%2F2005Natur.435..773N&rft.aulast=Nelson&rft.aufirst=R&rft.au=Sawaya%2C+MR&rft.au=Balbirnie%2C+M&rft.au=Madsen%2C+A%C3%98&rft.au=Riekel%2C+C&rft.au=Grothe%2C+R&rft.au=Eisenberg%2C+D&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1479801&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-Sawaya2007-49"><a href="#cite_ref-Sawaya2007_49-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSawayaSambashivanNelsonIvanova2007" class="citation journal cs1">Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, et al. (May 2007). "Atomic structures of amyloid cross-β spines reveal varied steric zippers". Nature. 447 (7143): 453–7. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2007Natur.447..453S">2007Natur.447..453S</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnature05695">10.1038/nature05695</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17468747">17468747</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4400866">4400866</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=Atomic+structures+of+amyloid+cross-%CE%B2+spines+reveal+varied+steric+zippers&rft.volume=447&rft.issue=7143&rft.pages=%3Cspan+class%3D%22nowrap%22%3E453-%3C%2Fspan%3E7&rft.date=2007-05&rft_id=info%3Adoi%2F10.1038%2Fnature05695&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A4400866%23id-name%3DS2CID&rft_id=info%3Apmid%2F17468747&rft_id=info%3Abibcode%2F2007Natur.447..453S&rft.aulast=Sawaya&rft.aufirst=MR&rft.au=Sambashivan%2C+S&rft.au=Nelson%2C+R&rft.au=Ivanova%2C+MI&rft.au=Sievers%2C+SA&rft.au=Apostol%2C+MI&rft.au=Thompson%2C+MJ&rft.au=Balbirnie%2C+M&rft.au=Wiltzius%2C+JJ&rft.au=McFarlane%2C+HT&rft.au=Madsen%2C+A%C3%98&rft.au=Riekel%2C+C&rft.au=Eisenberg%2C+D&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-PMID12219081-50"><a href="#cite_ref-PMID12219081_50-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSeragAltenbachGingeryHubbell2002" class="citation journal cs1">Serag AA, Altenbach C, Gingery M, Hubbell WL, Yeates TO (October 2002). "Arrangement of subunits and ordering of β-strands in an amyloid sheet". Nature Structural Biology. 9 (10): 734–9. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnsb838">10.1038/nsb838</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12219081">12219081</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:23926428">23926428</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Structural+Biology&rft.atitle=Arrangement+of+subunits+and+ordering+of+%CE%B2-strands+in+an+amyloid+sheet&rft.volume=9&rft.issue=10&rft.pages=%3Cspan+class%3D%22nowrap%22%3E734-%3C%2Fspan%3E9&rft.date=2002-10&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A23926428%23id-name%3DS2CID&rft_id=info%3Apmid%2F12219081&rft_id=info%3Adoi%2F10.1038%2Fnsb838&rft.aulast=Serag&rft.aufirst=AA&rft.au=Altenbach%2C+C&rft.au=Gingery%2C+M&rft.au=Hubbell%2C+WL&rft.au=Yeates%2C+TO&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-51"><a href="#cite_ref-51">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPuławskiDzwolak2022" class="citation journal cs1">Puławski, W; Dzwolak, W (7 June 2022). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9178918">"Virtual Quasi-2D Intermediates as Building Blocks for Plausible Structural Models of Amyloid Fibrils from Proteins with Complex Topologies: A Case Study of Insulin"</a>. Langmuir. 38 (22): 7024–7034. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Facs.langmuir.2c00699">10.1021/acs.langmuir.2c00699</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9178918">9178918</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/35617668">35617668</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Langmuir&rft.atitle=Virtual+Quasi-2D+Intermediates+as+Building+Blocks+for+Plausible+Structural+Models+of+Amyloid+Fibrils+from+Proteins+with+Complex+Topologies%3A+A+Case+Study+of+Insulin.&rft.volume=38&rft.issue=22&rft.pages=%3Cspan+class%3D%22nowrap%22%3E7024-%3C%2Fspan%3E7034&rft.date=2022-06-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC9178918%23id-name%3DPMC&rft_id=info%3Apmid%2F35617668&rft_id=info%3Adoi%2F10.1021%2Facs.langmuir.2c00699&rft.aulast=Pu%C5%82awski&rft.aufirst=W&rft.au=Dzwolak%2C+W&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC9178918&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pm17056725-52">^ <a href="#cite_ref-pm17056725_52-0">a</a> <a href="#cite_ref-pm17056725_52-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBuShiCallawayTycko2007" class="citation journal cs1">Bu Z, Shi Y, Callaway DJ, Tycko R (January 2007). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1751388">"Molecular alignment within β-sheets in Aβ14-23 fibrils: solid-state NMR experiments and theoretical predictions"</a>. Biophysical Journal. 92 (2): 594–602. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2007BpJ....92..594B">2007BpJ....92..594B</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1529%2Fbiophysj.106.091017">10.1529/biophysj.106.091017</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1751388">1751388</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17056725">17056725</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biophysical+Journal&rft.atitle=Molecular+alignment+within+%CE%B2-sheets+in+A%CE%B2%3Csub%3E14-23%3C%2Fsub%3E+fibrils%3A+solid-state+NMR+experiments+and+theoretical+predictions&rft.volume=92&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E594-%3C%2Fspan%3E602&rft.date=2007-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1751388%23id-name%3DPMC&rft_id=info%3Apmid%2F17056725&rft_id=info%3Adoi%2F10.1529%2Fbiophysj.106.091017&rft_id=info%3Abibcode%2F2007BpJ....92..594B&rft.aulast=Bu&rft.aufirst=Z&rft.au=Shi%2C+Y&rft.au=Callaway%2C+DJ&rft.au=Tycko%2C+R&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1751388&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pm12023906-53">^ <a href="#cite_ref-pm12023906_53-0">a</a> <a href="#cite_ref-pm12023906_53-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFTjernbergTjernbergBarkShi2002" class="citation journal cs1">Tjernberg LO, Tjernberg A, Bark N, Shi Y, Ruzsicska BP, Bu Z, et al. (August 2002). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222771">"Assembling amyloid fibrils from designed structures containing a significant amyloid β-peptide fragment"</a>. The Biochemical Journal. 366 (Pt 1): 343–51. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1042%2FBJ20020229">10.1042/BJ20020229</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222771">1222771</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12023906">12023906</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Biochemical+Journal&rft.atitle=Assembling+amyloid+fibrils+from+designed+structures+containing+a+significant+amyloid+%CE%B2-peptide+fragment&rft.volume=366&rft.issue=Pt+1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E343-%3C%2Fspan%3E51&rft.date=2002-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1222771%23id-name%3DPMC&rft_id=info%3Apmid%2F12023906&rft_id=info%3Adoi%2F10.1042%2FBJ20020229&rft.aulast=Tjernberg&rft.aufirst=LO&rft.au=Tjernberg%2C+A&rft.au=Bark%2C+N&rft.au=Shi%2C+Y&rft.au=Ruzsicska%2C+BP&rft.au=Bu%2C+Z&rft.au=Thyberg%2C+J&rft.au=Callaway%2C+DJ&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1222771&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid8490014-54"><a href="#cite_ref-pmid8490014_54-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFJarrettBergerLansbury1993" class="citation journal cs1">Jarrett JT, Berger EP, Lansbury PT (May 1993). "The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease". Biochemistry. 32 (18): 4693–7. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fbi00069a001">10.1021/bi00069a001</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/8490014">8490014</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochemistry&rft.atitle=The+carboxy+terminus+of+the+%CE%B2+amyloid+protein+is+critical+for+the+seeding+of+amyloid+formation%3A+implications+for+the+pathogenesis+of+Alzheimer%27s+disease&rft.volume=32&rft.issue=18&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4693-%3C%2Fspan%3E7&rft.date=1993-05&rft_id=info%3Adoi%2F10.1021%2Fbi00069a001&rft_id=info%3Apmid%2F8490014&rft.aulast=Jarrett&rft.aufirst=JT&rft.au=Berger%2C+EP&rft.au=Lansbury%2C+PT&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid10507029-55"><a href="#cite_ref-pmid10507029_55-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFerrone1999" class="citation book cs1">Ferrone F (1999). "Analysis of protein aggregation kinetics". Amyloid, Prions, and Other Protein Aggregates. Methods in Enzymology. Vol. 309. pp. 256–74. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0076-6879%2899%2909019-9">10.1016/s0076-6879(99)09019-9</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/9780121822101" title="Special:BookSources/9780121822101"><bdi>9780121822101</bdi></a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10507029">10507029</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Analysis+of+protein+aggregation+kinetics&rft.btitle=Amyloid%2C+Prions%2C+and+Other+Protein+Aggregates&rft.series=Methods+in+Enzymology&rft.pages=%3Cspan+class%3D%22nowrap%22%3E256-%3C%2Fspan%3E74&rft.date=1999&rft_id=info%3Apmid%2F10507029&rft_id=info%3Adoi%2F10.1016%2Fs0076-6879%2899%2909019-9&rft.isbn=9780121822101&rft.aulast=Ferrone&rft.aufirst=F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid19071235-56">^ <a href="#cite_ref-pmid19071235_56-0">a</a> <a href="#cite_ref-pmid19071235_56-1">b</a> <a href="#cite_ref-pmid19071235_56-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMorrisWatzkyFinke2009" class="citation journal cs1">Morris AM, Watzky MA, Finke RG (March 2009). "Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794 (3): 375–97. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbapap.2008.10.016">10.1016/j.bbapap.2008.10.016</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19071235">19071235</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Proteins+and+Proteomics&rft.atitle=Protein+aggregation+kinetics%2C+mechanism%2C+and+curve-fitting%3A+a+review+of+the+literature&rft.volume=1794&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E375-%3C%2Fspan%3E97&rft.date=2009-03&rft_id=info%3Adoi%2F10.1016%2Fj.bbapap.2008.10.016&rft_id=info%3Apmid%2F19071235&rft.aulast=Morris&rft.aufirst=AM&rft.au=Watzky%2C+MA&rft.au=Finke%2C+RG&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid20007899-57">^ <a href="#cite_ref-pmid20007899_57-0">a</a> <a href="#cite_ref-pmid20007899_57-1">b</a> <a href="#cite_ref-pmid20007899_57-2">c</a> <a href="#cite_ref-pmid20007899_57-3">d</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKnowlesWaudbyDevlinCohen2009" class="citation journal cs1">Knowles TP, Waudby CA, Devlin GL, Cohen SI, Aguzzi A, Vendruscolo M, et al. (December 2009). "An analytical solution to the kinetics of breakable filament assembly". Science. 326 (5959): 1533–7. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2009Sci...326.1533K">2009Sci...326.1533K</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1126%2Fscience.1178250">10.1126/science.1178250</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20007899">20007899</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:6267152">6267152</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Science&rft.atitle=An+analytical+solution+to+the+kinetics+of+breakable+filament+assembly&rft.volume=326&rft.issue=5959&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1533-%3C%2Fspan%3E7&rft.date=2009-12&rft_id=info%3Adoi%2F10.1126%2Fscience.1178250&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A6267152%23id-name%3DS2CID&rft_id=info%3Apmid%2F20007899&rft_id=info%3Abibcode%2F2009Sci...326.1533K&rft.aulast=Knowles&rft.aufirst=TP&rft.au=Waudby%2C+CA&rft.au=Devlin%2C+GL&rft.au=Cohen%2C+SI&rft.au=Aguzzi%2C+A&rft.au=Vendruscolo%2C+M&rft.au=Terentjev%2C+EM&rft.au=Welland%2C+ME&rft.au=Dobson%2C+CM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid10958771-58">^ <a href="#cite_ref-pmid10958771_58-0">a</a> <a href="#cite_ref-pmid10958771_58-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSerioCashikarKowalSawicki2000" class="citation journal cs1">Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, et al. (August 2000). "Nucleated conformational conversion and the replication of conformational information by a prion determinant". Science. 289 (5483): 1317–21. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2000Sci...289.1317S">2000Sci...289.1317S</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1126%2Fscience.289.5483.1317">10.1126/science.289.5483.1317</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10958771">10958771</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Science&rft.atitle=Nucleated+conformational+conversion+and+the+replication+of+conformational+information+by+a+prion+determinant&rft.volume=289&rft.issue=5483&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1317-%3C%2Fspan%3E21&rft.date=2000-08&rft_id=info%3Apmid%2F10958771&rft_id=info%3Adoi%2F10.1126%2Fscience.289.5483.1317&rft_id=info%3Abibcode%2F2000Sci...289.1317S&rft.aulast=Serio&rft.aufirst=TR&rft.au=Cashikar%2C+AG&rft.au=Kowal%2C+AS&rft.au=Sawicki%2C+GJ&rft.au=Moslehi%2C+JJ&rft.au=Serpell%2C+L&rft.au=Arnsdorf%2C+MF&rft.au=Lindquist%2C+SL&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid19088715-59">^ <a href="#cite_ref-pmid19088715_59-0">a</a> <a href="#cite_ref-pmid19088715_59-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFChitiDobson2009" class="citation journal cs1">Chiti F, Dobson CM (January 2009). "Amyloid formation by globular proteins under native conditions". Nature Chemical Biology. 5 (1): 15–22. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnchembio.131">10.1038/nchembio.131</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19088715">19088715</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Chemical+Biology&rft.atitle=Amyloid+formation+by+globular+proteins+under+native+conditions&rft.volume=5&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E15-%3C%2Fspan%3E22&rft.date=2009-01&rft_id=info%3Adoi%2F10.1038%2Fnchembio.131&rft_id=info%3Apmid%2F19088715&rft.aulast=Chiti&rft.aufirst=F&rft.au=Dobson%2C+CM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-:0-60">^ <a href="#cite_ref-:0_60-0">a</a> <a href="#cite_ref-:0_60-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMichaelsŠarićHabchiChia2018" class="citation journal cs1">Michaels TC, Šarić A, Habchi J, Chia S, Meisl G, Vendruscolo M, et al. (April 2018). <a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev-physchem-050317-021322">"Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation"</a>. Annual Review of Physical Chemistry. 69 (1): 273–298. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2018ARPC...69..273M">2018ARPC...69..273M</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev-physchem-050317-021322">10.1146/annurev-physchem-050317-021322</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29490200">29490200</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annual+Review+of+Physical+Chemistry&rft.atitle=Chemical+Kinetics+for+Bridging+Molecular+Mechanisms+and+Macroscopic+Measurements+of+Amyloid+Fibril+Formation&rft.volume=69&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E273-%3C%2Fspan%3E298&rft.date=2018-04&rft_id=info%3Apmid%2F29490200&rft_id=info%3Adoi%2F10.1146%2Fannurev-physchem-050317-021322&rft_id=info%3Abibcode%2F2018ARPC...69..273M&rft.aulast=Michaels&rft.aufirst=TC&rft.au=%C5%A0ari%C4%87%2C+A&rft.au=Habchi%2C+J&rft.au=Chia%2C+S&rft.au=Meisl%2C+G&rft.au=Vendruscolo%2C+M&rft.au=Dobson%2C+CM&rft.au=Knowles%2C+TP&rft_id=https%3A%2F%2Fdoi.org%2F10.1146%252Fannurev-physchem-050317-021322&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid12917692-61">^ <a href="#cite_ref-pmid12917692_61-0">a</a> <a href="#cite_ref-pmid12917692_61-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFChitiStefaniTaddeiRamponi2003" class="citation journal cs1">Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (August 2003). "Rationalization of the effects of mutations on peptide and protein aggregation rates". Nature. 424 (6950): 805–8. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2003Natur.424..805C">2003Natur.424..805C</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnature01891">10.1038/nature01891</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12917692">12917692</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4421180">4421180</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=Rationalization+of+the+effects+of+mutations+on+peptide+and+protein+aggregation+rates&rft.volume=424&rft.issue=6950&rft.pages=%3Cspan+class%3D%22nowrap%22%3E805-%3C%2Fspan%3E8&rft.date=2003-08&rft_id=info%3Adoi%2F10.1038%2Fnature01891&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A4421180%23id-name%3DS2CID&rft_id=info%3Apmid%2F12917692&rft_id=info%3Abibcode%2F2003Natur.424..805C&rft.aulast=Chiti&rft.aufirst=F&rft.au=Stefani%2C+M&rft.au=Taddei%2C+N&rft.au=Ramponi%2C+G&rft.au=Dobson%2C+CM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-62"><a href="#cite_ref-62">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGileadGazit2004" class="citation journal cs1">Gilead S, Gazit E (August 2004). "Inhibition of amyloid fibril formation by peptide analogues modified with α-aminoisobutyric acid". Angewandte Chemie. 43 (31): 4041–4. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fanie.200353565">10.1002/anie.200353565</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15300690">15300690</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Angewandte+Chemie&rft.atitle=Inhibition+of+amyloid+fibril+formation+by+peptide+analogues+modified+with+%CE%B1-aminoisobutyric+acid&rft.volume=43&rft.issue=31&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4041-%3C%2Fspan%3E4&rft.date=2004-08&rft_id=info%3Adoi%2F10.1002%2Fanie.200353565&rft_id=info%3Apmid%2F15300690&rft.aulast=Gilead&rft.aufirst=S&rft.au=Gazit%2C+E&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-63"><a href="#cite_ref-63">^</a> Lutz, T.A.: Creating the amylin story. Appetite 172 (2022) 105965, doi:10.1016/j.appet.2022.105965 </li> <li id="cite_note-64"><a href="#cite_ref-64">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFinderVodopivecNitschGlockshuber2010" class="citation journal cs1">Finder VH, Vodopivec I, Nitsch RM, Glockshuber R (February 2010). "The recombinant amyloid-β peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ-42". Journal of Molecular Biology. 396 (1): 9–18. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.jmb.2009.12.016">10.1016/j.jmb.2009.12.016</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20026079">20026079</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Molecular+Biology&rft.atitle=The+recombinant+amyloid-%CE%B2+peptide+A%CE%B21-42+aggregates+faster+and+is+more+neurotoxic+than+synthetic+A%CE%B2-42&rft.volume=396&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E9-%3C%2Fspan%3E18&rft.date=2010-02&rft_id=info%3Adoi%2F10.1016%2Fj.jmb.2009.12.016&rft_id=info%3Apmid%2F20026079&rft.aulast=Finder&rft.aufirst=VH&rft.au=Vodopivec%2C+I&rft.au=Nitsch%2C+RM&rft.au=Glockshuber%2C+R&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-65"><a href="#cite_ref-65">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMorleyBrignullWeyersMorimoto2002" class="citation journal cs1">Morley JF, Brignull HR, Weyers JJ, Morimoto RI (August 2002). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC124929">"The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans"</a>. Proceedings of the National Academy of Sciences of the United States of America. 99 (16): 10417–22. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2002PNAS...9910417M">2002PNAS...9910417M</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.152161099">10.1073/pnas.152161099</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC124929">124929</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12122205">12122205</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=The+threshold+for+polyglutamine-expansion+protein+aggregation+and+cellular+toxicity+is+dynamic+and+influenced+by+aging+in+Caenorhabditis+elegans&rft.volume=99&rft.issue=16&rft.pages=%3Cspan+class%3D%22nowrap%22%3E10417-%3C%2Fspan%3E22&rft.date=2002-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC124929%23id-name%3DPMC&rft_id=info%3Apmid%2F12122205&rft_id=info%3Adoi%2F10.1073%2Fpnas.152161099&rft_id=info%3Abibcode%2F2002PNAS...9910417M&rft.aulast=Morley&rft.aufirst=JF&rft.au=Brignull%2C+HR&rft.au=Weyers%2C+JJ&rft.au=Morimoto%2C+RI&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC124929&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-66"><a href="#cite_ref-66">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGazit2002" class="citation journal cs1">Gazit E (January 2002). <a rel="nofollow" class="external text" href="https://doi.org/10.1096%2Ffj.01-0442hyp">"A possible role for pi-stacking in the self-assembly of amyloid fibrils"</a>. FASEB Journal. 16 (1): 77–83. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1096%2Ffj.01-0442hyp">10.1096/fj.01-0442hyp</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11772939">11772939</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:27896962">27896962</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=FASEB+Journal&rft.atitle=A+possible+role+for+pi-stacking+in+the+self-assembly+of+amyloid+fibrils&rft.volume=16&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E77-%3C%2Fspan%3E83&rft.date=2002-01&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A27896962%23id-name%3DS2CID&rft_id=info%3Apmid%2F11772939&rft_id=info%3Adoi%2F10.1096%2Ffj.01-0442hyp&rft.aulast=Gazit&rft.aufirst=E&rft_id=https%3A%2F%2Fdoi.org%2F10.1096%252Ffj.01-0442hyp&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-PMID15925383-67"><a href="#cite_ref-PMID15925383_67-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPawarDubayZurdoChiti2005" class="citation journal cs1">Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM (July 2005). "Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases". Journal of Molecular Biology. 350 (2): 379–92. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.jmb.2005.04.016">10.1016/j.jmb.2005.04.016</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15925383">15925383</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Molecular+Biology&rft.atitle=Prediction+of+%22aggregation-prone%22+and+%22aggregation-susceptible%22+regions+in+proteins+associated+with+neurodegenerative+diseases&rft.volume=350&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E379-%3C%2Fspan%3E92&rft.date=2005-07&rft_id=info%3Adoi%2F10.1016%2Fj.jmb.2005.04.016&rft_id=info%3Apmid%2F15925383&rft.aulast=Pawar&rft.aufirst=AP&rft.au=Dubay%2C+KF&rft.au=Zurdo%2C+J&rft.au=Chiti%2C+F&rft.au=Vendruscolo%2C+M&rft.au=Dobson%2C+CM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-pmid23794448-68"><a href="#cite_ref-pmid23794448_68-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFJacksonBarisoneDiazJin2013" class="citation journal cs1">Jackson K, Barisone GA, Diaz E, Jin LW, DeCarli C, Despa F (October 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818462">"Amylin deposition in the brain: A second amyloid in Alzheimer disease?"</a>. Annals of Neurology. 74 (4): 517–26. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fana.23956">10.1002/ana.23956</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818462">3818462</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23794448">23794448</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annals+of+Neurology&rft.atitle=Amylin+deposition+in+the+brain%3A+A+second+amyloid+in+Alzheimer+disease%3F&rft.volume=74&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E517-%3C%2Fspan%3E26&rft.date=2013-10&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3818462%23id-name%3DPMC&rft_id=info%3Apmid%2F23794448&rft_id=info%3Adoi%2F10.1002%2Fana.23956&rft.aulast=Jackson&rft.aufirst=K&rft.au=Barisone%2C+GA&rft.au=Diaz%2C+E&rft.au=Jin%2C+LW&rft.au=DeCarli%2C+C&rft.au=Despa%2C+F&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3818462&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-69"><a href="#cite_ref-69">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDemuroMinaKayedMilton2005" class="citation journal cs1">Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (April 2005). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M500997200">"Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers"</a>. The Journal of Biological Chemistry. 280 (17): 17294–300. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M500997200">10.1074/jbc.M500997200</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15722360">15722360</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=Calcium+dysregulation+and+membrane+disruption+as+a+ubiquitous+neurotoxic+mechanism+of+soluble+amyloid+oligomers&rft.volume=280&rft.issue=17&rft.pages=%3Cspan+class%3D%22nowrap%22%3E17294-%3C%2Fspan%3E300&rft.date=2005-04&rft_id=info%3Adoi%2F10.1074%2Fjbc.M500997200&rft_id=info%3Apmid%2F15722360&rft.aulast=Demuro&rft.aufirst=A&rft.au=Mina%2C+E&rft.au=Kayed%2C+R&rft.au=Milton%2C+SC&rft.au=Parker%2C+I&rft.au=Glabe%2C+CG&rft_id=https%3A%2F%2Fdoi.org%2F10.1074%252Fjbc.M500997200&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-70"><a href="#cite_ref-70">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGathBoussetHabensteinMelki2014" class="citation journal cs1">Gath J, Bousset L, Habenstein B, Melki R, Böckmann A, Meier BH (March 5, 2014). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944079">"Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity"</a>. PLOS ONE. 9 (3): e90659. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2014PLoSO...990659G">2014PLoSO...990659G</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1371%2Fjournal.pone.0090659">10.1371/journal.pone.0090659</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944079">3944079</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/24599158">24599158</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PLOS+ONE&rft.atitle=Unlike+twins%3A+an+NMR+comparison+of+two+%CE%B1-synuclein+polymorphs+featuring+different+toxicity&rft.volume=9&rft.issue=3&rft.pages=e90659&rft.date=2014-03-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3944079%23id-name%3DPMC&rft_id=info%3Apmid%2F24599158&rft_id=info%3Adoi%2F10.1371%2Fjournal.pone.0090659&rft_id=info%3Abibcode%2F2014PLoSO...990659G&rft.aulast=Gath&rft.aufirst=J&rft.au=Bousset%2C+L&rft.au=Habenstein%2C+B&rft.au=Melki%2C+R&rft.au=B%C3%B6ckmann%2C+A&rft.au=Meier%2C+BH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3944079&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-71"><a href="#cite_ref-71">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKaganAzimovAzimova2004" class="citation journal cs1">Kagan BL, Azimov R, Azimova R (November 2004). "Amyloid peptide channels". The Journal of Membrane Biology. 202 (1): 1–10. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs00232-004-0709-4">10.1007/s00232-004-0709-4</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15702375">15702375</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:23771650">23771650</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Membrane+Biology&rft.atitle=Amyloid+peptide+channels&rft.volume=202&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1-%3C%2Fspan%3E10&rft.date=2004-11&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A23771650%23id-name%3DS2CID&rft_id=info%3Apmid%2F15702375&rft_id=info%3Adoi%2F10.1007%2Fs00232-004-0709-4&rft.aulast=Kagan&rft.aufirst=BL&rft.au=Azimov%2C+R&rft.au=Azimova%2C+R&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-72"><a href="#cite_ref-72">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKadowakiNishitohUranoSadamitsu2005" class="citation journal cs1">Kadowaki H, Nishitoh H, Urano F, Sadamitsu C, Matsuzawa A, Takeda K, et al. (January 2005). <a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fsj.cdd.4401528">"Amyloid β induces neuronal cell death through ROS-mediated ASK1 activation"</a>. Cell Death and Differentiation. 12 (1): 19–24. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fsj.cdd.4401528">10.1038/sj.cdd.4401528</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15592360">15592360</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cell+Death+and+Differentiation&rft.atitle=Amyloid+%CE%B2+induces+neuronal+cell+death+through+ROS-mediated+ASK1+activation&rft.volume=12&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E19-%3C%2Fspan%3E24&rft.date=2005-01&rft_id=info%3Adoi%2F10.1038%2Fsj.cdd.4401528&rft_id=info%3Apmid%2F15592360&rft.aulast=Kadowaki&rft.aufirst=H&rft.au=Nishitoh%2C+H&rft.au=Urano%2C+F&rft.au=Sadamitsu%2C+C&rft.au=Matsuzawa%2C+A&rft.au=Takeda%2C+K&rft.au=Masutani%2C+H&rft.au=Yodoi%2C+J&rft.au=Urano%2C+Y&rft.au=Nagano%2C+T&rft.au=Ichijo%2C+H&rft_id=https%3A%2F%2Fdoi.org%2F10.1038%252Fsj.cdd.4401528&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-73"><a href="#cite_ref-73">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKochneva-PervukhovaAlexandrovTer-Avanesyan2012" class="citation journal cs1">Kochneva-Pervukhova NV, Alexandrov AI, Ter-Avanesyan MD (2012). Tuite MF (ed.). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256205">"Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast"</a>. PLOS ONE. 7 (1): e29832. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2012PLoSO...729832K">2012PLoSO...729832K</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1371%2Fjournal.pone.0029832">10.1371/journal.pone.0029832</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256205">3256205</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22253794">22253794</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PLOS+ONE&rft.atitle=Amyloid-mediated+sequestration+of+essential+proteins+contributes+to+mutant+huntingtin+toxicity+in+yeast&rft.volume=7&rft.issue=1&rft.pages=e29832&rft.date=2012&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3256205%23id-name%3DPMC&rft_id=info%3Apmid%2F22253794&rft_id=info%3Adoi%2F10.1371%2Fjournal.pone.0029832&rft_id=info%3Abibcode%2F2012PLoSO...729832K&rft.aulast=Kochneva-Pervukhova&rft.aufirst=NV&rft.au=Alexandrov%2C+AI&rft.au=Ter-Avanesyan%2C+MD&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3256205&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-74"><a href="#cite_ref-74">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFNesterovSkochHymanKlunk2005" class="citation journal cs1">Nesterov EE, Skoch J, Hyman BT, Klunk WE, Bacskai BJ, Swager TM (August 2005). "In vivo optical imaging of amyloid aggregates in brain: design of fluorescent markers". Angewandte Chemie. 44 (34): 5452–6. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fanie.200500845">10.1002/anie.200500845</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16059955">16059955</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:42217289">42217289</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Angewandte+Chemie&rft.atitle=In+vivo+optical+imaging+of+amyloid+aggregates+in+brain%3A+design+of+fluorescent+markers&rft.volume=44&rft.issue=34&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5452-%3C%2Fspan%3E6&rft.date=2005-08&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A42217289%23id-name%3DS2CID&rft_id=info%3Apmid%2F16059955&rft_id=info%3Adoi%2F10.1002%2Fanie.200500845&rft.aulast=Nesterov&rft.aufirst=EE&rft.au=Skoch%2C+J&rft.au=Hyman%2C+BT&rft.au=Klunk%2C+WE&rft.au=Bacskai%2C+BJ&rft.au=Swager%2C+TM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-75"><a href="#cite_ref-75">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBaeLimHwangHuh2015" class="citation journal cs1">Bae S, Lim E, Hwang D, Huh H, Kim SK (2015). "Torsion-dependent fluorescence switching of amyloid-binding dye NIAD-4". Chemical Physics Letters. 633: 109–13. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2015CPL...633..109B">2015CPL...633..109B</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.cplett.2015.05.010">10.1016/j.cplett.2015.05.010</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemical+Physics+Letters&rft.atitle=Torsion-dependent+fluorescence+switching+of+amyloid-binding+dye+NIAD-4&rft.volume=633&rft.pages=%3Cspan+class%3D%22nowrap%22%3E109-%3C%2Fspan%3E13&rft.date=2015&rft_id=info%3Adoi%2F10.1016%2Fj.cplett.2015.05.010&rft_id=info%3Abibcode%2F2015CPL...633..109B&rft.aulast=Bae&rft.aufirst=S&rft.au=Lim%2C+E&rft.au=Hwang%2C+D&rft.au=Huh%2C+H&rft.au=Kim%2C+SK&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-76"><a href="#cite_ref-76">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFRiesUdayarSoragniHornemann2013" class="citation journal cs1">Ries J, Udayar V, Soragni A, Hornemann S, Nilsson KP, Riek R, et al. (July 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3715833">"Superresolution imaging of amyloid fibrils with binding-activated probes"</a>. ACS Chemical Neuroscience. 4 (7): 1057–61. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fcn400091m">10.1021/cn400091m</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3715833">3715833</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23594172">23594172</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=ACS+Chemical+Neuroscience&rft.atitle=Superresolution+imaging+of+amyloid+fibrils+with+binding-activated+probes&rft.volume=4&rft.issue=7&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1057-%3C%2Fspan%3E61&rft.date=2013-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3715833%23id-name%3DPMC&rft_id=info%3Apmid%2F23594172&rft_id=info%3Adoi%2F10.1021%2Fcn400091m&rft.aulast=Ries&rft.aufirst=J&rft.au=Udayar%2C+V&rft.au=Soragni%2C+A&rft.au=Hornemann%2C+S&rft.au=Nilsson%2C+KP&rft.au=Riek%2C+R&rft.au=Hock%2C+C&rft.au=Ewers%2C+H&rft.au=Aguzzi%2C+AA&rft.au=Rajendran%2C+L&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3715833&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> <li id="cite_note-77"><a href="#cite_ref-77">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHuhLeeKimHohng2017" class="citation journal cs1">Huh H, Lee J, Kim HJ, Hohng S, Kim SK (2017). "Morphological analysis of oligomeric vs. fibrillar forms of α-synuclein aggregates with super-resolution BALM imaging". Chemical Physics Letters. 690: 62–67. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2017CPL...690...62H">2017CPL...690...62H</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.cplett.2017.10.034">10.1016/j.cplett.2017.10.034</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemical+Physics+Letters&rft.atitle=Morphological+analysis+of+oligomeric+vs.+fibrillar+forms+of+%CE%B1-synuclein+aggregates+with+super-resolution+BALM+imaging&rft.volume=690&rft.pages=%3Cspan+class%3D%22nowrap%22%3E62-%3C%2Fspan%3E67&rft.date=2017&rft_id=info%3Adoi%2F10.1016%2Fj.cplett.2017.10.034&rft_id=info%3Abibcode%2F2017CPL...690...62H&rft.aulast=Huh&rft.aufirst=H&rft.au=Lee%2C+J&rft.au=Kim%2C+HJ&rft.au=Hohng%2C+S&rft.au=Kim%2C+SK&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmyloid" class="Z3988"> </li> </ol></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2>[<a href="/w/index.php?title=Amyloid&action=edit&section=11" title="Edit section: External links">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1235681985">.mw-parser-output .side-box{margin:4px 0;box-sizing:border-box;border:1px solid #aaa;font-size:88%;line-height:1.25em;background-color:var(--background-color-interactive-subtle,#f8f9fa);display:flow-root}.mw-parser-output .side-box-abovebelow,.mw-parser-output .side-box-text{padding:0.25em 0.9em}.mw-parser-output .side-box-image{padding:2px 0 2px 0.9em;text-align:center}.mw-parser-output .side-box-imageright{padding:2px 0.9em 2px 0;text-align:center}@media(min-width:500px){.mw-parser-output .side-box-flex{display:flex;align-items:center}.mw-parser-output .side-box-text{flex:1;min-width:0}}@media(min-width:720px){.mw-parser-output .side-box{width:238px}.mw-parser-output .side-box-right{clear:right;float:right;margin-left:1em}.mw-parser-output .side-box-left{margin-right:1em}}</style><style data-mw-deduplicate="TemplateStyles:r1237033735">@media print{body.ns-0 .mw-parser-output .sistersitebox{display:none!important}}@media screen{html.skin-theme-clientpref-night .mw-parser-output .sistersitebox img[src*="Wiktionary-logo-en-v2.svg"]{background-color:white}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .sistersitebox img[src*="Wiktionary-logo-en-v2.svg"]{background-color:white}}</style><div class="side-box side-box-right plainlinks sistersitebox"><style data-mw-deduplicate="TemplateStyles:r1126788409">.mw-parser-output .plainlist ol,.mw-parser-output .plainlist ul{line-height:inherit;list-style:none;margin:0;padding:0}.mw-parser-output .plainlist ol li,.mw-parser-output .plainlist ul li{margin-bottom:0}</style> <div class="side-box-flex"> <div class="side-box-image"><a href="/wiki/File:Commons-logo.svg" class="mw-file-description"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/40px-Commons-logo.svg.png" decoding="async" width="30" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/60px-Commons-logo.svg.png 1.5x" data-file-width="1024" data-file-height="1376" /></a></div> <div class="side-box-text plainlist">Wikimedia Commons has media related to <a href="https://commons.wikimedia.org/wiki/Category:Amyloid" class="extiw" title="commons:Category:Amyloid">Amyloid</a>.</div></div> </div> <ul><li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20081210070634/http://scivee.tv/node/7266">Bacterial Inclusion Bodies Contain Amyloid-Like Structure</a> at <a href="/wiki/SciVee" title="SciVee">SciVee</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20090219204637/http://wiki.iop.kcl.ac.uk/default.aspx/Neurodegeneration/Amyloid%20Cascade%20Hypothesis.html">Amyloid Cascade Hypothesis</a></li> <li><a rel="nofollow" class="external text" href="https://www.tandfonline.com/journals/iamy20">Amyloid: Journal of Protein Folding Disorders web page</a></li> <li><a rel="nofollow" class="external text" href="https://medicalxpress.com/news/2007-01-role-anesthetics-alzheimer-disease-molecular.html">Role of anesthetics in Alzheimer's disease: Molecular details revealed</a></li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl ol,.mw-parser-output .hlist dl ul,.mw-parser-output .hlist ol dl,.mw-parser-output .hlist ol ol,.mw-parser-output .hlist ol ul,.mw-parser-output .hlist ul dl,.mw-parser-output .hlist ul ol,.mw-parser-output .hlist ul ul{display:inline}.mw-parser-output .hlist .mw-empty-li{display:none}.mw-parser-output .hlist dt::after{content:": "}.mw-parser-output .hlist dd::after,.mw-parser-output .hlist li::after{content:" · ";font-weight:bold}.mw-parser-output .hlist dd:last-child::after,.mw-parser-output .hlist dt:last-child::after,.mw-parser-output .hlist li:last-child::after{content:none}.mw-parser-output .hlist dd dd:first-child::before,.mw-parser-output .hlist dd dt:first-child::before,.mw-parser-output .hlist dd li:first-child::before,.mw-parser-output .hlist dt dd:first-child::before,.mw-parser-output .hlist dt dt:first-child::before,.mw-parser-output .hlist dt li:first-child::before,.mw-parser-output .hlist li dd:first-child::before,.mw-parser-output .hlist li dt:first-child::before,.mw-parser-output .hlist li li:first-child::before{content:" (";font-weight:normal}.mw-parser-output .hlist dd dd:last-child::after,.mw-parser-output .hlist dd dt:last-child::after,.mw-parser-output .hlist dd li:last-child::after,.mw-parser-output .hlist dt dd:last-child::after,.mw-parser-output .hlist dt dt:last-child::after,.mw-parser-output .hlist dt li:last-child::after,.mw-parser-output .hlist li dd:last-child::after,.mw-parser-output .hlist li dt:last-child::after,.mw-parser-output .hlist li li:last-child::after{content:")";font-weight:normal}.mw-parser-output .hlist ol{counter-reset:listitem}.mw-parser-output .hlist ol>li{counter-increment:listitem}.mw-parser-output .hlist ol>li::before{content:" "counter(listitem)"\a0 "}.mw-parser-output .hlist dd ol>li:first-child::before,.mw-parser-output .hlist dt ol>li:first-child::before,.mw-parser-output .hlist li ol>li:first-child::before{content:" ("counter(listitem)"\a0 "}</style><style data-mw-deduplicate="TemplateStyles:r1236075235">.mw-parser-output .navbox{box-sizing:border-box;border:1px solid #a2a9b1;width:100%;clear:both;font-size:88%;text-align:center;padding:1px;margin:1em auto 0}.mw-parser-output .navbox .navbox{margin-top:0}.mw-parser-output .navbox+.navbox,.mw-parser-output .navbox+.navbox-styles+.navbox{margin-top:-1px}.mw-parser-output .navbox-inner,.mw-parser-output .navbox-subgroup{width:100%}.mw-parser-output .navbox-group,.mw-parser-output .navbox-title,.mw-parser-output .navbox-abovebelow{padding:0.25em 1em;line-height:1.5em;text-align:center}.mw-parser-output .navbox-group{white-space:nowrap;text-align:right}.mw-parser-output .navbox,.mw-parser-output .navbox-subgroup{background-color:#fdfdfd}.mw-parser-output .navbox-list{line-height:1.5em;border-color:#fdfdfd}.mw-parser-output .navbox-list-with-group{text-align:left;border-left-width:2px;border-left-style:solid}.mw-parser-output tr+tr>.navbox-abovebelow,.mw-parser-output tr+tr>.navbox-group,.mw-parser-output tr+tr>.navbox-image,.mw-parser-output tr+tr>.navbox-list{border-top:2px solid #fdfdfd}.mw-parser-output .navbox-title{background-color:#ccf}.mw-parser-output .navbox-abovebelow,.mw-parser-output .navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Amyloidosis99" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><style data-mw-deduplicate="TemplateStyles:r1239400231">.mw-parser-output .navbar{display:inline;font-size:88%;font-weight:normal}.mw-parser-output .navbar-collapse{float:left;text-align:left}.mw-parser-output .navbar-boxtext{word-spacing:0}.mw-parser-output .navbar ul{display:inline-block;white-space:nowrap;line-height:inherit}.mw-parser-output .navbar-brackets::before{margin-right:-0.125em;content:"[ "}.mw-parser-output .navbar-brackets::after{margin-left:-0.125em;content:" ]"}.mw-parser-output .navbar li{word-spacing:-0.125em}.mw-parser-output .navbar a>span,.mw-parser-output .navbar a>abbr{text-decoration:inherit}.mw-parser-output .navbar-mini abbr{font-variant:small-caps;border-bottom:none;text-decoration:none;cursor:inherit}.mw-parser-output .navbar-ct-full{font-size:114%;margin:0 7em}.mw-parser-output .navbar-ct-mini{font-size:114%;margin:0 4em}html.skin-theme-clientpref-night .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}@media(prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}}@media print{.mw-parser-output .navbar{display:none!important}}</style><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Amyloidosis" title="Template:Amyloidosis"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Amyloidosis" title="Template talk:Amyloidosis"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Amyloidosis" title="Special:EditPage/Template:Amyloidosis"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Amyloidosis99" style="font-size:114%;margin:0 4em"><a href="/wiki/Amyloidosis" title="Amyloidosis">Amyloidosis</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Common <a class="mw-selflink selflink">amyloid</a> forming proteins</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Serum_amyloid_A" title="Serum amyloid A">AA</a></li> <li><a href="/wiki/Transthyretin" title="Transthyretin">ATTR</a></li> <li><a href="/wiki/Beta-2_microglobulin" title="Beta-2 microglobulin">Aβ2M</a></li> <li><a href="/wiki/Bence_Jones_protein" title="Bence Jones protein">AL</a></li> <li><a href="/wiki/Beta_amyloid" class="mw-redirect" title="Beta amyloid">Aβ</a>/<a href="/wiki/Amyloid_precursor_protein" class="mw-redirect" title="Amyloid precursor protein">APP</a></li> <li><a href="/wiki/Amylin" title="Amylin">AIAPP</a></li> <li><a href="/wiki/Calcitonin" title="Calcitonin">ACal</a></li> <li><a href="/wiki/Prolactin" title="Prolactin">APro</a></li> <li><a href="/wiki/Atrial_natriuretic_peptide" title="Atrial natriuretic peptide">AANF</a></li> <li><a href="/wiki/Cystatin_C" title="Cystatin C">ACys</a></li> <li><a href="/wiki/ITM2B" title="ITM2B">ABri</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Systemic amyloidosis</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/AL_amyloidosis" title="AL amyloidosis">AL amyloidosis</a></li> <li><a href="/wiki/AA_amyloidosis" title="AA amyloidosis">AA amyloidosis</a></li> <li><a href="/wiki/Haemodialysis-associated_amyloidosis" title="Haemodialysis-associated amyloidosis">Aβ2M/Haemodialysis-associated</a></li> <li><a href="/wiki/Finnish_type_amyloidosis" class="mw-redirect" title="Finnish type amyloidosis">AGel/Finnish type</a></li> <li><a href="/wiki/Familial_Mediterranean_fever" title="Familial Mediterranean fever">AA/Familial Mediterranean fever</a></li> <li><a href="/wiki/Transthyretin-related_hereditary_amyloidosis" class="mw-redirect" title="Transthyretin-related hereditary amyloidosis">ATTR/Transthyretin-related hereditary</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Organ-limited_amyloidosis" title="Organ-limited amyloidosis">Organ-limited amyloidosis</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Human_heart" class="mw-redirect" title="Human heart">Heart</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"><a href="/wiki/Isolated_atrial_amyloidosis" title="Isolated atrial amyloidosis">AANF/Isolated atrial</a></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Human_brain" title="Human brain">Brain</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Familial_amyloid_neuropathy" title="Familial amyloid neuropathy">Familial amyloid neuropathy</a></li> <li><a href="/wiki/Cerebral_amyloid_angiopathy" title="Cerebral amyloid angiopathy">ACys+ABri/Cerebral amyloid angiopathy</a></li> <li><a href="/wiki/Alzheimer%27s_disease" title="Alzheimer's disease">Aβ/Alzheimer's disease</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Kidney" title="Kidney">Kidney</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Familial_renal_amyloidosis" title="Familial renal amyloidosis">AApoA1+AFib+ALys/Familial renal</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Human_skin" title="Human skin">Skin</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Primary_cutaneous_amyloidosis" title="Primary cutaneous amyloidosis">Primary cutaneous amyloidosis</a></li> <li><a href="/wiki/Amyloid_purpura" title="Amyloid purpura">Amyloid purpura</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Endocrine_system" title="Endocrine system">Endocrine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <dl><dt><a href="/wiki/Thyroid" title="Thyroid">Thyroid</a></dt> <dd><a href="/wiki/Medullary_thyroid_cancer" title="Medullary thyroid cancer">ACal/Medullary thyroid cancer</a></dd></dl> <dl><dt><a href="/wiki/Pituitary_gland" title="Pituitary gland">Pituitary</a></dt> <dd><a href="/wiki/Prolactinoma" title="Prolactinoma">APro/Prolactinoma</a></dd></dl> <dl><dt><a href="/wiki/Pancreas" title="Pancreas">Pancreas</a></dt> <dd><a href="/wiki/Insulinoma" title="Insulinoma">AIAPP/Insulinoma</a></dd> <dd><a href="/wiki/Type_2_diabetes" title="Type 2 diabetes">Type 2 diabetes</a></dd></dl> </div></td></tr></tbody></table><div></div></td></tr></tbody></table></div>    </div><noscript><img src="https://auth.wikimedia.org/loginwiki/wiki/Special:CentralAutoLogin/start?useformat=desktop&type=1x1&usesul3=1" alt="" width="1" height="1" style="border: none; position: absolute;"></noscript> <div class="printfooter" data-nosnippet="">Retrieved from "<a dir="ltr" href="https://en.wikipedia.org/w/index.php?title=Amyloid&oldid=1283153266">https://en.wikipedia.org/w/index.php?title=Amyloid&oldid=1283153266</a>"</div></div> <div id="catlinks" class="catlinks" data-mw="interface"><div id="mw-normal-catlinks" class="mw-normal-catlinks"><a href="/wiki/Help:Category" title="Help:Category">Categories</a>: <ul><li><a href="/wiki/Category:Amyloidosis" title="Category:Amyloidosis">Amyloidosis</a></li><li><a href="/wiki/Category:Histopathology" title="Category:Histopathology">Histopathology</a></li><li><a href="/wiki/Category:Structural_proteins" title="Category:Structural proteins">Structural proteins</a></li></ul></div><div id="mw-hidden-catlinks" class="mw-hidden-catlinks mw-hidden-cats-hidden">Hidden categories: <ul><li><a href="/wiki/Category:Articles_with_short_description" title="Category:Articles with short description">Articles with short description</a></li><li><a href="/wiki/Category:Short_description_is_different_from_Wikidata" title="Category:Short description is different from Wikidata">Short description is different from Wikidata</a></li><li><a href="/wiki/Category:Articles_containing_Latin-language_text" title="Category:Articles containing Latin-language text">Articles containing Latin-language text</a></li><li><a href="/wiki/Category:Articles_containing_Ancient_Greek_(to_1453)-language_text" title="Category:Articles containing Ancient Greek (to 1453)-language text">Articles containing Ancient Greek (to 1453)-language text</a></li><li><a href="/wiki/Category:All_articles_with_unsourced_statements" title="Category:All articles with unsourced statements">All articles with unsourced statements</a></li><li><a href="/wiki/Category:Articles_with_unsourced_statements_from_November_2008" title="Category:Articles with unsourced statements from November 2008">Articles with unsourced statements from November 2008</a></li><li><a href="/wiki/Category:Commons_category_link_is_on_Wikidata" title="Category:Commons category link is on Wikidata">Commons category link is on Wikidata</a></li></ul></div></div> </div> </main> </div> <div class="mw-footer-container"> <footer id="footer" class="mw-footer" > <ul id="footer-info"> <li id="footer-info-lastmod"> This page was last edited on 30 March 2025, at 19:13 (UTC).</li> <li id="footer-info-copyright">Text is available under the <a href="/wiki/Wikipedia:Text_of_the_Creative_Commons_Attribution-ShareAlike_4.0_International_License" title="Wikipedia:Text of the Creative Commons Attribution-ShareAlike 4.0 International License">Creative Commons Attribution-ShareAlike 4.0 License</a>; additional terms may apply. By using this site, you agree to the <a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Terms_of_Use" class="extiw" title="foundation:Special:MyLanguage/Policy:Terms of Use">Terms of Use</a> and <a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Privacy_policy" class="extiw" title="foundation:Special:MyLanguage/Policy:Privacy policy">Privacy Policy</a>. Wikipedia® is a registered trademark of the <a rel="nofollow" class="external text" href="https://wikimediafoundation.org/">Wikimedia Foundation, Inc.</a>, a non-profit organization.</li> </ul> <ul id="footer-places"> <li id="footer-places-privacy"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Privacy_policy">Privacy policy</a></li> <li id="footer-places-about"><a href="/wiki/Wikipedia:About">About Wikipedia</a></li> <li id="footer-places-disclaimers"><a href="/wiki/Wikipedia:General_disclaimer">Disclaimers</a></li> <li id="footer-places-contact"><a href="//en.wikipedia.org/wiki/Wikipedia:Contact_us">Contact Wikipedia</a></li> <li id="footer-places-wm-codeofconduct"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Universal_Code_of_Conduct">Code of Conduct</a></li> <li id="footer-places-developers"><a href="https://developer.wikimedia.org">Developers</a></li> <li id="footer-places-statslink"><a href="https://stats.wikimedia.org/#/en.wikipedia.org">Statistics</a></li> <li id="footer-places-cookiestatement"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Cookie_statement">Cookie statement</a></li> <li id="footer-places-mobileview"><a href="//en.m.wikipedia.org/w/index.php?title=Amyloid&mobileaction=toggle_view_mobile" class="noprint stopMobileRedirectToggle">Mobile view</a></li> </ul> <ul id="footer-icons" class="noprint"> <li id="footer-copyrightico"><a href="https://www.wikimedia.org/" class="cdx-button cdx-button--fake-button cdx-button--size-large cdx-button--fake-button--enabled"><picture><source media="(min-width: 500px)" srcset="/static/images/footer/wikimedia-button.svg" width="84" height="29"><img src="/static/images/footer/wikimedia.svg" width="25" height="25" alt="Wikimedia Foundation" lang="en" loading="lazy"></picture></a></li> <li id="footer-poweredbyico"><a href="https://www.mediawiki.org/" class="cdx-button cdx-button--fake-button cdx-button--size-large cdx-button--fake-button--enabled"><picture><source media="(min-width: 500px)" srcset="/w/resources/assets/poweredby_mediawiki.svg" width="88" height="31"><img src="/w/resources/assets/mediawiki_compact.svg" alt="Powered by MediaWiki" lang="en" width="25" height="25" loading="lazy"></picture></a></li> </ul> </footer> </div> </div> </div> <div class="vector-header-container vector-sticky-header-container"> <div id="vector-sticky-header" class="vector-sticky-header"> <div class="vector-sticky-header-start"> <div class="vector-sticky-header-icon-start vector-button-flush-left vector-button-flush-right" aria-hidden="true"> <button class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-sticky-header-search-toggle" tabindex="-1" data-event-name="ui.vector-sticky-search-form.icon"> Search </button> </div> <div role="search" class="vector-search-box-vue vector-search-box-show-thumbnail vector-search-box"> <div class="vector-typeahead-search-container"> <div class="cdx-typeahead-search cdx-typeahead-search--show-thumbnail"> <form action="/w/index.php" id="vector-sticky-search-form" class="cdx-search-input cdx-search-input--has-end-button"> <div class="cdx-search-input__input-wrapper" data-search-loc="header-moved"> <div class="cdx-text-input cdx-text-input--has-start-icon"> <input class="cdx-text-input__input" type="search" name="search" placeholder="Search Wikipedia"> </div> <input type="hidden" name="title" value="Special:Search"> </div> <button class="cdx-button cdx-search-input__end-button">Search</button> </form> </div> </div> </div> <div class="vector-sticky-header-context-bar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-sticky-header-toc" class="vector-dropdown mw-portlet mw-portlet-sticky-header-toc vector-sticky-header-toc vector-button-flush-left" > <input type="checkbox" id="vector-sticky-header-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-sticky-header-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-sticky-header-toc-label" for="vector-sticky-header-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Toggle the table of contents </label> <div class="vector-dropdown-content"> <div id="vector-sticky-header-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <div class="vector-sticky-header-context-bar-primary" aria-hidden="true" >Amyloid</div> </div> </div> <div class="vector-sticky-header-end" aria-hidden="true"> <div class="vector-sticky-header-icons"> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-talk-sticky-header" tabindex="-1" data-event-name="talk-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-subject-sticky-header" tabindex="-1" data-event-name="subject-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-history-sticky-header" tabindex="-1" data-event-name="history-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only mw-watchlink" id="ca-watchstar-sticky-header" tabindex="-1" data-event-name="watch-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-edit-sticky-header" tabindex="-1" data-event-name="wikitext-edit-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-ve-edit-sticky-header" tabindex="-1" data-event-name="ve-edit-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-viewsource-sticky-header" tabindex="-1" data-event-name="ve-edit-protected-sticky-header"> </a> </div> <div class="vector-sticky-header-buttons"> <button class="cdx-button cdx-button--weight-quiet mw-interlanguage-selector" id="p-lang-btn-sticky-header" tabindex="-1" data-event-name="ui.dropdown-p-lang-btn-sticky-header"> 18 languages </button> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive" id="ca-addsection-sticky-header" tabindex="-1" data-event-name="addsection-sticky-header"> Add topic </a> </div> <div class="vector-sticky-header-icon-end"> <div class="vector-user-links"> </div> </div> </div> </div> </div> <div class="mw-portlet mw-portlet-dock-bottom emptyPortlet" id="p-dock-bottom"> <ul> </ul> </div> <script>(RLQ=window.RLQ||[]).push(function(){mw.config.set({"wgHostname":"mw-web.codfw.main-684955989f-j7slj","wgBackendResponseTime":181,"wgPageParseReport":{"limitreport":{"cputime":"0.803","walltime":"0.970","ppvisitednodes":{"value":4877,"limit":1000000},"postexpandincludesize":{"value":238001,"limit":2097152},"templateargumentsize":{"value":1541,"limit":2097152},"expansiondepth":{"value":13,"limit":100},"expensivefunctioncount":{"value":4,"limit":500},"unstrip-depth":{"value":1,"limit":20},"unstrip-size":{"value":335089,"limit":5000000},"entityaccesscount":{"value":0,"limit":400},"timingprofile":["100.00% 782.070 1 -total"," 53.42% 417.755 1 Template:Reflist"," 45.59% 356.582 74 Template:Cite_journal"," 11.57% 90.453 1 Template:Lang"," 9.27% 72.534 1 Template:Amyloidosis"," 9.07% 70.933 2 Template:Navbox"," 7.96% 62.237 1 Template:Short_description"," 5.08% 39.744 1 Template:Commons_category"," 4.81% 37.611 1 Template:Sister_project"," 4.64% 36.321 2 Template:Pagetype"]},"scribunto":{"limitreport-timeusage":{"value":"0.520","limit":"10.000"},"limitreport-memusage":{"value":21379540,"limit":52428800}},"cachereport":{"origin":"mw-web.codfw.main-684955989f-2t95p","timestamp":"20250331175133","ttl":2592000,"transientcontent":false}}});});</script> <script type="application/ld+json">{"@context":"https:\/\/schema.org","@type":"Article","name":"Amyloid","url":"https:\/\/en.wikipedia.org\/wiki\/Amyloid","sameAs":"http:\/\/www.wikidata.org\/entity\/Q6740853","mainEntity":"http:\/\/www.wikidata.org\/entity\/Q6740853","author":{"@type":"Organization","name":"Contributors to Wikimedia projects"},"publisher":{"@type":"Organization","name":"Wikimedia Foundation, Inc.","logo":{"@type":"ImageObject","url":"https:\/\/www.wikimedia.org\/static\/images\/wmf-hor-googpub.png"}},"datePublished":"2003-12-10T23:56:52Z","dateModified":"2025-03-30T19:13:52Z","image":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/6\/6f\/Small_bowel_duodenum_with_amyloid_deposition_20X.jpg","headline":"insoluble protein aggregate"}</script> </body> </html>