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overflow: hidden; text-overflow: ellipsis; -webkit-line-clamp: 3; -webkit-box-orient: vertical; }</style><div class="col-xs-12 clearfix"><div class="u-floatLeft"><h1 class="PageHeader-title u-m0x u-fs30">M Rna Processing</h1><div class="u-tcGrayDark">33 Followers</div><div class="u-tcGrayDark u-mt2x">Recent papers in <b>M Rna Processing</b></div></div></div></div></div></div><div class="TabbedNavigation"><div class="container"><div class="row"><div class="col-xs-12 clearfix"><ul class="nav u-m0x u-p0x list-inline u-displayFlex"><li class="active"><a href="https://www.academia.edu/Documents/in/M_Rna_Processing">Top Papers</a></li><li><a href="https://www.academia.edu/Documents/in/M_Rna_Processing/MostCited">Most Cited Papers</a></li><li><a href="https://www.academia.edu/Documents/in/M_Rna_Processing/MostDownloaded">Most Downloaded Papers</a></li><li><a href="https://www.academia.edu/Documents/in/M_Rna_Processing/MostRecent">Newest Papers</a></li><li><a class="" href="https://www.academia.edu/People/M_Rna_Processing">People</a></li></ul></div><style type="text/css">ul.nav{flex-direction:row}@media(max-width: 567px){ul.nav{flex-direction:column}.TabbedNavigation li{max-width:100%}.TabbedNavigation li.active{background-color:var(--background-grey, #dddde2)}.TabbedNavigation li.active:before,.TabbedNavigation li.active:after{display:none}}</style></div></div></div><div class="container"><div class="row"><div class="col-xs-12"><div class="u-displayFlex"><div class="u-flexGrow1"><div class="works"><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_61188810" data-work_id="61188810" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/61188810/The_Movement_of_Coiled_Bodies_Visualized_in_Living_Plant_Cells_by_the_Green_Fluorescent_Protein">The Movement of Coiled Bodies Visualized in Living Plant Cells by the Green Fluorescent Protein</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Coiled bodies are nuclear organelles that contain components of at least three RNA-processing pathways: pre-mRNA splicing, histone mRNA 3′- maturation, and pre-rRNA processing. Their function remains unknown. However, it has been... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_61188810" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Coiled bodies are nuclear organelles that contain components of at least three RNA-processing pathways: pre-mRNA splicing, histone mRNA 3′- maturation, and pre-rRNA processing. Their function remains unknown. However, it has been speculated that coiled bodies may be sites of splicing factor assembly and/or recycling, play a role in histone mRNA 3′-processing, or act as nuclear transport or sorting structures. To study the dynamics of coiled bodies in living cells, we have stably expressed a U2B&quot;–green fluorescent protein fusion in tobacco BY-2 cells and in Arabidopsis plants. Time-lapse confocal microscopy has shown that coiled bodies are mobile organelles in plant cells. We have observed movements of coiled bodies in the nucleolus, in the nucleoplasm, and from the periphery of the nucleus into the nucleolus, which suggests a transport function for coiled bodies. Furthermore, we have observed coalescence of coiled bodies, which suggests a mechanism for the decrease in coiled bo...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/61188810" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3f4b8d40ec3083159b1d499a65adcfaf" rel="nofollow" data-download="{"attachment_id":74309641,"asset_id":61188810,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/74309641/download_file?st=MTczMjc5NDQ5NSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="42808404" href="https://independent.academia.edu/PeterShaw19">Peter Shaw</a><script data-card-contents-for-user="42808404" type="text/json">{"id":42808404,"first_name":"Peter","last_name":"Shaw","domain_name":"independent","page_name":"PeterShaw19","display_name":"Peter Shaw","profile_url":"https://independent.academia.edu/PeterShaw19?f_ri=3702","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_61188810 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="61188810"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 61188810, container: ".js-paper-rank-work_61188810", }); 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Their function remains unknown. However, it has been speculated that coiled bodies may be sites of splicing factor assembly and/or recycling, play a role in histone mRNA 3′-processing, or act as nuclear transport or sorting structures. To study the dynamics of coiled bodies in living cells, we have stably expressed a U2B\u0026quot;–green fluorescent protein fusion in tobacco BY-2 cells and in Arabidopsis plants. Time-lapse confocal microscopy has shown that coiled bodies are mobile organelles in plant cells. We have observed movements of coiled bodies in the nucleolus, in the nucleoplasm, and from the periphery of the nucleus into the nucleolus, which suggests a transport function for coiled bodies. Furthermore, we have observed coalescence of coiled bodies, which suggests a mechanism for the decrease in coiled bo...","downloadable_attachments":[{"id":74309641,"asset_id":61188810,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":42808404,"first_name":"Peter","last_name":"Shaw","domain_name":"independent","page_name":"PeterShaw19","display_name":"Peter Shaw","profile_url":"https://independent.academia.edu/PeterShaw19?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":7700,"name":"Fluorescence Microscopy","url":"https://www.academia.edu/Documents/in/Fluorescence_Microscopy?f_ri=3702","nofollow":false},{"id":9109,"name":"Tobacco","url":"https://www.academia.edu/Documents/in/Tobacco?f_ri=3702","nofollow":false},{"id":9113,"name":"Cell 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maturation of yeast 66S preribosomes.Mol</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest">Ytm1, Nop7, and Erb1 form a complex necessary for maturation of yeast 66S preribosomes.</div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/70126502" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="80e2406097baf924707fb1f758382e26" rel="nofollow" data-download="{"attachment_id":79987592,"asset_id":70126502,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button 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Polymerase","url":"https://www.academia.edu/Documents/in/RNA_Dependent_RNA_Polymerase?f_ri=3702"},{"id":1305892,"name":"RNA Virus","url":"https://www.academia.edu/Documents/in/RNA_Virus?f_ri=3702"},{"id":1345633,"name":"RNA Replication","url":"https://www.academia.edu/Documents/in/RNA_Replication?f_ri=3702"},{"id":1939264,"name":"single stranded DNA","url":"https://www.academia.edu/Documents/in/single_stranded_DNA?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_14361824" data-work_id="14361824" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/14361824/Nucleocytoplasmic_transport_cargo_trafficking_across_the_border">Nucleocytoplasmic transport: cargo trafficking across the border</a></div></div><div 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data-has-card-for-ri="156" href="https://www.academia.edu/Documents/in/Genetics">Genetics</a>, <script data-card-contents-for-ri="156" type="text/json">{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="3702" href="https://www.academia.edu/Documents/in/M_Rna_Processing">M Rna Processing</a>, <script data-card-contents-for-ri="3702" type="text/json">{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="4987" href="https://www.academia.edu/Documents/in/Kinetics">Kinetics</a>, <script data-card-contents-for-ri="4987" type="text/json">{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="13827" href="https://www.academia.edu/Documents/in/Cell_Biology">Cell Biology</a><script data-card-contents-for-ri="13827" type="text/json">{"id":13827,"name":"Cell Biology","url":"https://www.academia.edu/Documents/in/Cell_Biology?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=14361824]'), work: {"id":14361824,"title":"Nucleocytoplasmic transport: cargo trafficking across the border","created_at":"2015-07-24T05:12:22.081-07:00","url":"https://www.academia.edu/14361824/Nucleocytoplasmic_transport_cargo_trafficking_across_the_border?f_ri=3702","dom_id":"work_14361824","summary":null,"downloadable_attachments":[{"id":44282828,"asset_id":14361824,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33305738,"first_name":"Karsten","last_name":"Weis","domain_name":"ethz","page_name":"KarstenWeis","display_name":"Karsten 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nucleus","url":"https://www.academia.edu/Documents/in/Cell_nucleus?f_ri=3702"},{"id":635694,"name":"Alternative Splicing","url":"https://www.academia.edu/Documents/in/Alternative_Splicing-1?f_ri=3702"},{"id":771343,"name":"S100 protein family","url":"https://www.academia.edu/Documents/in/S100_protein_family?f_ri=3702"},{"id":979299,"name":"Ribosomes","url":"https://www.academia.edu/Documents/in/Ribosomes?f_ri=3702"},{"id":1166930,"name":"Cytoplasm","url":"https://www.academia.edu/Documents/in/Cytoplasm?f_ri=3702"},{"id":1457054,"name":"Protein Transport","url":"https://www.academia.edu/Documents/in/Protein_Transport?f_ri=3702"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_20146958 coauthored" data-work_id="20146958" itemscope="itemscope" 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js-work-card work_4888218" data-work_id="4888218" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/4888218/The_HRPT2_Tumor_Suppressor_Gene_Product_Parafibromin_Associates_with_Human_PAF1_and_RNA_Polymerase_II">The HRPT2 Tumor Suppressor Gene Product Parafibromin Associates with Human PAF1 and RNA Polymerase II</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/4888218" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div 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sharma","profile_url":"https://bhu-in.academia.edu/shalinisharma?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=3702","nofollow":false},{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false},{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=3702","nofollow":false},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology?f_ri=3702","nofollow":false},{"id":3701,"name":"RNA","url":"https://www.academia.edu/Documents/in/RNA?f_ri=3702"},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702"},{"id":3971,"name":"Protein Folding","url":"https://www.academia.edu/Documents/in/Protein_Folding?f_ri=3702"},{"id":9113,"name":"Cell 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Acids","url":"https://www.academia.edu/Documents/in/Nucleic_Acids?f_ri=3702"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=3702"},{"id":238813,"name":"Chromatin","url":"https://www.academia.edu/Documents/in/Chromatin?f_ri=3702"},{"id":240723,"name":"Chromatin structure","url":"https://www.academia.edu/Documents/in/Chromatin_structure?f_ri=3702"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=3702"},{"id":283547,"name":"Introns","url":"https://www.academia.edu/Documents/in/Introns?f_ri=3702"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=3702"},{"id":1494061,"name":"DNA recombination","url":"https://www.academia.edu/Documents/in/DNA_recombination?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_11029553" data-work_id="11029553" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/11029553/Unwinding_RNA_in_Saccharomyces_cerevisiae_DEAD_box_proteins_and_related_families">Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/11029553" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="64b425ea8444d3721bb12a1da01d2fa4" 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11029553; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_11029553"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_11029553 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="11029553"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 11029553; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=11029553]").text(description); $(".js-view-count-work_11029553").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_11029553").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="11029553"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">10</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="145" href="https://www.academia.edu/Documents/in/Biochemistry">Biochemistry</a>, <script data-card-contents-for-ri="145" type="text/json">{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="371" href="https://www.academia.edu/Documents/in/Functional_Analysis">Functional Analysis</a>, <script data-card-contents-for-ri="371" type="text/json">{"id":371,"name":"Functional Analysis","url":"https://www.academia.edu/Documents/in/Functional_Analysis?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="3702" href="https://www.academia.edu/Documents/in/M_Rna_Processing">M Rna Processing</a>, <script data-card-contents-for-ri="3702" type="text/json">{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="15719" href="https://www.academia.edu/Documents/in/Mitochondria">Mitochondria</a><script data-card-contents-for-ri="15719" type="text/json">{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=11029553]'), work: {"id":11029553,"title":"Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and 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Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=3702","nofollow":false},{"id":30347,"name":"Translation","url":"https://www.academia.edu/Documents/in/Translation?f_ri=3702"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=3702"},{"id":49123,"name":"Saccharomyces cerevisiae","url":"https://www.academia.edu/Documents/in/Saccharomyces_cerevisiae?f_ri=3702"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=3702"},{"id":979299,"name":"Ribosomes","url":"https://www.academia.edu/Documents/in/Ribosomes?f_ri=3702"},{"id":1588981,"name":"Protein Biosynthesis","url":"https://www.academia.edu/Documents/in/Protein_Biosynthesis?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_9623693" data-work_id="9623693" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/9623693/Identification_of_a_cytoskeleton_associated_120_kDa_RNA_binding_protein_in_developing_rice_seeds">Identification of a cytoskeleton-associated 120 kDa RNA-binding protein in developing rice seeds</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">During rice seed development, prolamine RNAs are localized to the surface of the prolamine storage protein bodies (PBs), organelles bounded by the endoplasmic reticulum (ER). The exact mechanism by which prolamine RNAs are enriched on... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_9623693" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">During rice seed development, prolamine RNAs are localized to the surface of the prolamine storage protein bodies (PBs), organelles bounded by the endoplasmic reticulum (ER). The exact mechanism by which prolamine RNAs are enriched on this ER subdomain is not known but recent evidence indicates the directed transport and targeting of prolamine RNAs to the prolamine PBs. As such a process involves RNA signal determinants and cytoskeleton-interacting proteins that recognize these signals, we obtained an enriched cytoskeleton-PB fraction and identified a prominent RNA-binding activity, Rp120, by RNA-binding UV-cross-linking assay. Recombinant cDNA clones of Rp120 revealed that the primary sequence shared considerable structural homology to the human transcriptional coactivator p100 and possessed a modular organization, four nucleic acid-binding SN domains, a tudor domain and a coil-coil domain. Consistent with the presence of SN domains, Rp120 binds a variety of RNAs including prolamine RNA. Interaction with the latter RNA, however, was specific as binding activity was evident only to the prolamine 3′ UTR and not to the 5′ UTR or coding sequences. Rp120 is also able to interact with other proteins as its sedimentation behavior in sucrose density gradient suggests an association with the cytoskeleton. The presence of a tudor domain, suggested to have a role in RNA processing or transport, together with the SN and coiled-coil domains are consistent with the view that Rp120 may be involved in RNA sorting in rice endosperm.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/9623693" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="0595592332a359d063b11ce5b2392797" rel="nofollow" data-download="{"attachment_id":47701885,"asset_id":9623693,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/47701885/download_file?st=MTczMjc5NDQ5NSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="22900815" href="https://independent.academia.edu/YujiaWu2">Yujia Wu</a><script data-card-contents-for-user="22900815" type="text/json">{"id":22900815,"first_name":"Yujia","last_name":"Wu","domain_name":"independent","page_name":"YujiaWu2","display_name":"Yujia Wu","profile_url":"https://independent.academia.edu/YujiaWu2?f_ri=3702","photo":"https://0.academia-photos.com/22900815/6216461/7042252/s65_yujia.wu.jpg_oh_f7ab251af8eebac9661f6374039bfdc5_oe_550854be___gda___1426442039_5957347afae716188d9a3feb628a0bad"}</script></span></span></li><li class="js-paper-rank-work_9623693 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="9623693"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 9623693, container: ".js-paper-rank-work_9623693", }); 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The exact mechanism by which prolamine RNAs are enriched on this ER subdomain is not known but recent evidence indicates the directed transport and targeting of prolamine RNAs to the prolamine PBs. As such a process involves RNA signal determinants and cytoskeleton-interacting proteins that recognize these signals, we obtained an enriched cytoskeleton-PB fraction and identified a prominent RNA-binding activity, Rp120, by RNA-binding UV-cross-linking assay. Recombinant cDNA clones of Rp120 revealed that the primary sequence shared considerable structural homology to the human transcriptional coactivator p100 and possessed a modular organization, four nucleic acid-binding SN domains, a tudor domain and a coil-coil domain. Consistent with the presence of SN domains, Rp120 binds a variety of RNAs including prolamine RNA. Interaction with the latter RNA, however, was specific as binding activity was evident only to the prolamine 3′ UTR and not to the 5′ UTR or coding sequences. Rp120 is also able to interact with other proteins as its sedimentation behavior in sucrose density gradient suggests an association with the cytoskeleton. The presence of a tudor domain, suggested to have a role in RNA processing or transport, together with the SN and coiled-coil domains are consistent with the view that Rp120 may be involved in RNA sorting in rice endosperm.","downloadable_attachments":[{"id":47701885,"asset_id":9623693,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":22900815,"first_name":"Yujia","last_name":"Wu","domain_name":"independent","page_name":"YujiaWu2","display_name":"Yujia Wu","profile_url":"https://independent.academia.edu/YujiaWu2?f_ri=3702","photo":"https://0.academia-photos.com/22900815/6216461/7042252/s65_yujia.wu.jpg_oh_f7ab251af8eebac9661f6374039bfdc5_oe_550854be___gda___1426442039_5957347afae716188d9a3feb628a0bad"}],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":5541,"name":"Plant Biology","url":"https://www.academia.edu/Documents/in/Plant_Biology?f_ri=3702","nofollow":false},{"id":25657,"name":"Plant Molecular Biology","url":"https://www.academia.edu/Documents/in/Plant_Molecular_Biology?f_ri=3702","nofollow":false},{"id":37508,"name":"Cytoskeleton","url":"https://www.academia.edu/Documents/in/Cytoskeleton?f_ri=3702"},{"id":67484,"name":"Sequence alignment","url":"https://www.academia.edu/Documents/in/Sequence_alignment?f_ri=3702"},{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum?f_ri=3702"},{"id":142577,"name":"Seed Development","url":"https://www.academia.edu/Documents/in/Seed_Development?f_ri=3702"},{"id":149368,"name":"Oryza Sativa","url":"https://www.academia.edu/Documents/in/Oryza_Sativa?f_ri=3702"},{"id":286419,"name":"Density gradient","url":"https://www.academia.edu/Documents/in/Density_gradient?f_ri=3702"},{"id":386438,"name":"Seeds","url":"https://www.academia.edu/Documents/in/Seeds?f_ri=3702"},{"id":420908,"name":"RNA-binding proteins","url":"https://www.academia.edu/Documents/in/RNA-binding_proteins?f_ri=3702"},{"id":695018,"name":"Molecular weight","url":"https://www.academia.edu/Documents/in/Molecular_weight?f_ri=3702"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence?f_ri=3702"},{"id":965027,"name":"Subcellular Fractions","url":"https://www.academia.edu/Documents/in/Subcellular_Fractions?f_ri=3702"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=3702"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=3702"},{"id":1727314,"name":"Nucleic Acid","url":"https://www.academia.edu/Documents/in/Nucleic_Acid?f_ri=3702"},{"id":2058817,"name":"Immunoblotting","url":"https://www.academia.edu/Documents/in/Immunoblotting?f_ri=3702"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_17478935" data-work_id="17478935" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/17478935/The_snRNP_associated_U1A_levels_change_following_IL_6_stimulation_of_human_B_cells">The snRNP-associated U1A levels change following IL-6 stimulation of human B-cells</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li 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Milcarek","profile_url":"https://independent.academia.edu/ChristineMilcarek?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":1290,"name":"Immunology","url":"https://www.academia.edu/Documents/in/Immunology?f_ri=3702","nofollow":false},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":6599,"name":"Flow Cytometry","url":"https://www.academia.edu/Documents/in/Flow_Cytometry?f_ri=3702","nofollow":false},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line?f_ri=3702","nofollow":false},{"id":63332,"name":"Molecular Immunology","url":"https://www.academia.edu/Documents/in/Molecular_Immunology?f_ri=3702"},{"id":420908,"name":"RNA-binding proteins","url":"https://www.academia.edu/Documents/in/RNA-binding_proteins?f_ri=3702"},{"id":678853,"name":"B 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href="https://www.academia.edu/Documents/in/Gene_expression">Gene expression</a>, <script data-card-contents-for-ri="27784" type="text/json">{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="57808" href="https://www.academia.edu/Documents/in/Cell_line">Cell line</a><script data-card-contents-for-ri="57808" type="text/json">{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=70230894]'), work: {"id":70230894,"title":"p53 inhibits mRNA 3′ processing through its interaction with the CstF/BARD1 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itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/30150816/The_DEAD_box_protein_family_of_RNA_helicases">The DEAD-box protein family of RNA helicases</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/30150816" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="f126e4d8a48c20660c6fc4b12bf88413" rel="nofollow" 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u-positionRelative">26</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="156" href="https://www.academia.edu/Documents/in/Genetics">Genetics</a>, <script data-card-contents-for-ri="156" type="text/json">{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="3702" href="https://www.academia.edu/Documents/in/M_Rna_Processing">M Rna Processing</a>, <script data-card-contents-for-ri="3702" type="text/json">{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="16612" href="https://www.academia.edu/Documents/in/RNP">RNP</a>, <script data-card-contents-for-ri="16612" type="text/json">{"id":16612,"name":"RNP","url":"https://www.academia.edu/Documents/in/RNP?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="33441" href="https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography">Macromolecular X-Ray Crystallography</a><script data-card-contents-for-ri="33441" type="text/json">{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=30150816]'), work: {"id":30150816,"title":"The DEAD-box protein family of RNA 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itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="56985363" href="https://sheffield.academia.edu/PhilipJMitchell">Philip J Mitchell</a><script data-card-contents-for-user="56985363" type="text/json">{"id":56985363,"first_name":"Philip J","last_name":"Mitchell","domain_name":"sheffield","page_name":"PhilipJMitchell","display_name":"Philip J Mitchell","profile_url":"https://sheffield.academia.edu/PhilipJMitchell?f_ri=3702","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-29994640">+1</span><div class="hidden js-additional-users-29994640"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/ChristineAllmang">Christine Allmang</a></span></div></div></span><script>(function(){ var popoverSettings = { el: 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class="InlineList-item-text" data-has-card-for-ri="49123" href="https://www.academia.edu/Documents/in/Saccharomyces_cerevisiae">Saccharomyces cerevisiae</a>, <script data-card-contents-for-ri="49123" type="text/json">{"id":49123,"name":"Saccharomyces cerevisiae","url":"https://www.academia.edu/Documents/in/Saccharomyces_cerevisiae?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="368872" href="https://www.academia.edu/Documents/in/snoRNA">snoRNA</a><script data-card-contents-for-ri="368872" type="text/json">{"id":368872,"name":"snoRNA","url":"https://www.academia.edu/Documents/in/snoRNA?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=29994640]'), work: {"id":29994640,"title":"Functions of the exosome in rRNA, snoRNA and snRNA 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class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/5101693/Cotranscriptional_Recognition_of_Human_Intronic_Box_H_ACA_snoRNAs_Occurs_in_a_Splicing_Independent_Manner">Cotranscriptional Recognition of Human Intronic Box H/ACA snoRNAs Occurs in a Splicing-Independent Manner</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/5101693" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="dcda218e76c861530b8dc7cd1c213fd7" rel="nofollow" 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point","url":"https://www.academia.edu/Documents/in/Branch_point?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_25803320" data-work_id="25803320" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/25803320/A_comprehensive_evolutionary_classification_of_proteins_encoded_in_complete_eukaryotic_genomes">A comprehensive evolutionary classification of proteins encoded in complete eukaryotic genomes</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Sequencing the genomes of multiple, taxonomically diverse eukaryotes enables in-depth comparative-genomic analysis which is expected to help in reconstructing ancestral eukaryotic genomes and major events in eukaryotic evolution and in... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_25803320" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Sequencing the genomes of multiple, taxonomically diverse eukaryotes enables in-depth comparative-genomic analysis which is expected to help in reconstructing ancestral eukaryotic genomes and major events in eukaryotic evolution and in making functional predictions for currently uncharacterized conserved genes. We examined functional and evolutionary patterns in the recently constructed set of 5,873 clusters of predicted orthologs (eukaryotic orthologous groups or KOGs) from seven eukaryotic genomes: Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Arabidopsis thaliana, Saccharomyces cerevisiae, Schizosaccharomyces pombe and Encephalitozoon cuniculi. Conservation of KOGs through the phyletic range of eukaryotes strongly correlates with their functions and with the effect of gene knockout on the organism&#39;s viability. The approximately 40% of KOGs that are represented in six or seven species are enriched in proteins responsible for housekeeping functions, particularl...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/25803320" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3e5527d18ca3ec126f13f4810ebabc6a" rel="nofollow" data-download="{"attachment_id":46167232,"asset_id":25803320,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46167232/download_file?st=MTczMjc5NDQ5NSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="49569170" href="https://thebody.academia.edu/AvivaJacobs">Aviva Jacobs</a><script data-card-contents-for-user="49569170" type="text/json">{"id":49569170,"first_name":"Aviva","last_name":"Jacobs","domain_name":"thebody","page_name":"AvivaJacobs","display_name":"Aviva Jacobs","profile_url":"https://thebody.academia.edu/AvivaJacobs?f_ri=3702","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_25803320 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="25803320"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 25803320, container: ".js-paper-rank-work_25803320", }); 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$(".js-view-count[data-work-id=25803320]").text(description); $(".js-view-count-work_25803320").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_25803320").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="25803320"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">21</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="2889" href="https://www.academia.edu/Documents/in/Caenorhabditis_elegans">Caenorhabditis elegans</a>, <script data-card-contents-for-ri="2889" type="text/json">{"id":2889,"name":"Caenorhabditis elegans","url":"https://www.academia.edu/Documents/in/Caenorhabditis_elegans?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="3702" href="https://www.academia.edu/Documents/in/M_Rna_Processing">M Rna Processing</a>, <script data-card-contents-for-ri="3702" type="text/json">{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="4967" href="https://www.academia.edu/Documents/in/Molecular_Evolution">Molecular Evolution</a>, <script data-card-contents-for-ri="4967" type="text/json">{"id":4967,"name":"Molecular Evolution","url":"https://www.academia.edu/Documents/in/Molecular_Evolution?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="5504" href="https://www.academia.edu/Documents/in/Comparative_Genomics">Comparative Genomics</a><script data-card-contents-for-ri="5504" type="text/json">{"id":5504,"name":"Comparative Genomics","url":"https://www.academia.edu/Documents/in/Comparative_Genomics?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=25803320]'), work: {"id":25803320,"title":"A comprehensive evolutionary classification of proteins encoded in complete eukaryotic genomes","created_at":"2016-06-02T07:04:27.777-07:00","url":"https://www.academia.edu/25803320/A_comprehensive_evolutionary_classification_of_proteins_encoded_in_complete_eukaryotic_genomes?f_ri=3702","dom_id":"work_25803320","summary":"Sequencing the genomes of multiple, taxonomically diverse eukaryotes enables in-depth comparative-genomic analysis which is expected to help in reconstructing ancestral eukaryotic genomes and major events in eukaryotic evolution and in making functional predictions for currently uncharacterized conserved genes. 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The approximately 40% of KOGs that are represented in six or seven species are enriched in proteins responsible for housekeeping functions, particularl...","downloadable_attachments":[{"id":46167232,"asset_id":25803320,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":49569170,"first_name":"Aviva","last_name":"Jacobs","domain_name":"thebody","page_name":"AvivaJacobs","display_name":"Aviva Jacobs","profile_url":"https://thebody.academia.edu/AvivaJacobs?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2889,"name":"Caenorhabditis elegans","url":"https://www.academia.edu/Documents/in/Caenorhabditis_elegans?f_ri=3702","nofollow":false},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":4967,"name":"Molecular Evolution","url":"https://www.academia.edu/Documents/in/Molecular_Evolution?f_ri=3702","nofollow":false},{"id":5504,"name":"Comparative 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Prediction","url":"https://www.academia.edu/Documents/in/Protein_Function_Prediction?f_ri=3702"},{"id":663045,"name":"Yeasts","url":"https://www.academia.edu/Documents/in/Yeasts?f_ri=3702"},{"id":771990,"name":"Eukaryotic Cells","url":"https://www.academia.edu/Documents/in/Eukaryotic_Cells?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_22162794 coauthored" data-work_id="22162794" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/22162794/Enrichment_of_ultraconserved_elements_among_genomic_imbalances_causing_mental_delay_and_congenital_anomalies">Enrichment of ultraconserved elements among genomic imbalances causing mental delay and congenital anomalies</a></div></div><div class="u-pb4x u-mt3x"></div><ul 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js-work-more-authors-22162794">+1</span><div class="hidden js-additional-users-22162794"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/RamiroQuiroga2">Ramiro Quiroga</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-22162794'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-22162794').html(); } } new HoverPopover(popoverSettings); })();</script></li><li class="js-paper-rank-work_22162794 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="22162794"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 22162794, container: ".js-paper-rank-work_22162794", }); });</script></li><li class="js-percentile-work_22162794 InlineList-item 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href="https://www.academia.edu/Documents/in/Genomics">Genomics</a>, <script data-card-contents-for-ri="3216" type="text/json">{"id":3216,"name":"Genomics","url":"https://www.academia.edu/Documents/in/Genomics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="3702" href="https://www.academia.edu/Documents/in/M_Rna_Processing">M Rna Processing</a>, <script data-card-contents-for-ri="3702" type="text/json">{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="12757" href="https://www.academia.edu/Documents/in/Transcription_regulation_of_development">Transcription regulation of development</a><script data-card-contents-for-ri="12757" type="text/json">{"id":12757,"name":"Transcription regulation of development","url":"https://www.academia.edu/Documents/in/Transcription_regulation_of_development?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=22162794]'), work: {"id":22162794,"title":"Enrichment of ultraconserved elements among genomic imbalances causing mental delay and congenital anomalies","created_at":"2016-02-18T22:50:44.708-08:00","url":"https://www.academia.edu/22162794/Enrichment_of_ultraconserved_elements_among_genomic_imbalances_causing_mental_delay_and_congenital_anomalies?f_ri=3702","dom_id":"work_22162794","summary":null,"downloadable_attachments":[{"id":42825464,"asset_id":22162794,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":43512460,"first_name":"Carmen","last_name":"Orellana","domain_name":"independent","page_name":"CarmenOrellana4","display_name":"Carmen Orellana","profile_url":"https://independent.academia.edu/CarmenOrellana4?f_ri=3702","photo":"/images/s65_no_pic.png"},{"id":43780521,"first_name":"Ramiro","last_name":"Quiroga","domain_name":"independent","page_name":"RamiroQuiroga2","display_name":"Ramiro Quiroga","profile_url":"https://independent.academia.edu/RamiroQuiroga2?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false},{"id":3216,"name":"Genomics","url":"https://www.academia.edu/Documents/in/Genomics?f_ri=3702","nofollow":false},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":12757,"name":"Transcription regulation of development","url":"https://www.academia.edu/Documents/in/Transcription_regulation_of_development?f_ri=3702","nofollow":false},{"id":171144,"name":"Mental Disorders","url":"https://www.academia.edu/Documents/in/Mental_Disorders?f_ri=3702"},{"id":293558,"name":"Congenital Anomalies","url":"https://www.academia.edu/Documents/in/Congenital_Anomalies?f_ri=3702"},{"id":309981,"name":"Human Genome","url":"https://www.academia.edu/Documents/in/Human_Genome?f_ri=3702"},{"id":712943,"name":"Genome Rearrangement","url":"https://www.academia.edu/Documents/in/Genome_Rearrangement?f_ri=3702"},{"id":809882,"name":"Base Sequence","url":"https://www.academia.edu/Documents/in/Base_Sequence?f_ri=3702"},{"id":844352,"name":"Neurodevelopmental Disorder Autism","url":"https://www.academia.edu/Documents/in/Neurodevelopmental_Disorder_Autism?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_16154426" data-work_id="16154426" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/16154426/Structural_basis_for_group_A_trichothiodystrophy">Structural basis for group A trichothiodystrophy</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Patients with the rare neurodevelopmental repair syndrome known as group A trichothiodystrophy (TTD-A) carry mutations in the gene encoding the p8 subunit of the transcription and DNA repair factor TFIIH. Here we describe the crystal... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_16154426" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Patients with the rare neurodevelopmental repair syndrome known as group A trichothiodystrophy (TTD-A) carry mutations in the gene encoding the p8 subunit of the transcription and DNA repair factor TFIIH. Here we describe the crystal structure of a minimal complex between Tfb5, the yeast ortholog of p8, and the C-terminal domain of Tfb2, the yeast p52 subunit of TFIIH. The structure revealed that these two polypeptides adopt the same fold, forming a compact pseudosymmetric heterodimer via a beta-strand addition and coiled coils interactions between terminal alpha-helices. Furthermore, Tfb5 protects a hydrophobic surface in Tfb2 from solvent, providing a rationale for the influence of p8 in the stabilization of p52 and explaining why mutations that weaken p8-p52 interactions lead to a reduced intracellular TFIIH concentration and a defect in nucleotide-excision repair, a common feature of TTD cells.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/16154426" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="2058d50c68daa1d21d96d09de3f4e426" rel="nofollow" data-download="{"attachment_id":41162738,"asset_id":16154426,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/41162738/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="35265921" href="https://independent.academia.edu/JeanmarcEgly">Jean-marc Egly</a><script data-card-contents-for-user="35265921" type="text/json">{"id":35265921,"first_name":"Jean-marc","last_name":"Egly","domain_name":"independent","page_name":"JeanmarcEgly","display_name":"Jean-marc Egly","profile_url":"https://independent.academia.edu/JeanmarcEgly?f_ri=3702","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_16154426 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="16154426"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 16154426, container: ".js-paper-rank-work_16154426", }); 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$(".js-view-count[data-work-id=16154426]").text(description); $(".js-view-count-work_16154426").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_16154426").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="16154426"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">34</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="145" href="https://www.academia.edu/Documents/in/Biochemistry">Biochemistry</a>, <script data-card-contents-for-ri="145" type="text/json">{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="156" href="https://www.academia.edu/Documents/in/Genetics">Genetics</a>, <script data-card-contents-for-ri="156" type="text/json">{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="502" href="https://www.academia.edu/Documents/in/Biophysics">Biophysics</a>, <script data-card-contents-for-ri="502" type="text/json">{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="2513" href="https://www.academia.edu/Documents/in/Molecular_Biology">Molecular Biology</a><script data-card-contents-for-ri="2513" type="text/json">{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=16154426]'), work: {"id":16154426,"title":"Structural basis for group A trichothiodystrophy","created_at":"2015-09-24T23:38:00.230-07:00","url":"https://www.academia.edu/16154426/Structural_basis_for_group_A_trichothiodystrophy?f_ri=3702","dom_id":"work_16154426","summary":"Patients with the rare neurodevelopmental repair syndrome known as group A trichothiodystrophy (TTD-A) carry mutations in the gene encoding the p8 subunit of the transcription and DNA repair factor TFIIH. Here we describe the crystal structure of a minimal complex between Tfb5, the yeast ortholog of p8, and the C-terminal domain of Tfb2, the yeast p52 subunit of TFIIH. The structure revealed that these two polypeptides adopt the same fold, forming a compact pseudosymmetric heterodimer via a beta-strand addition and coiled coils interactions between terminal alpha-helices. Furthermore, Tfb5 protects a hydrophobic surface in Tfb2 from solvent, providing a rationale for the influence of p8 in the stabilization of p52 and explaining why mutations that weaken p8-p52 interactions lead to a reduced intracellular TFIIH concentration and a defect in nucleotide-excision repair, a common feature of TTD cells.","downloadable_attachments":[{"id":41162738,"asset_id":16154426,"asset_type":"Work","always_allow_download":false},{"id":41212269,"asset_id":16154426,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":35265921,"first_name":"Jean-marc","last_name":"Egly","domain_name":"independent","page_name":"JeanmarcEgly","display_name":"Jean-marc Egly","profile_url":"https://independent.academia.edu/JeanmarcEgly?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=3702","nofollow":false},{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false},{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=3702","nofollow":false},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology?f_ri=3702","nofollow":false},{"id":3701,"name":"RNA","url":"https://www.academia.edu/Documents/in/RNA?f_ri=3702"},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702"},{"id":3971,"name":"Protein Folding","url":"https://www.academia.edu/Documents/in/Protein_Folding?f_ri=3702"},{"id":9113,"name":"Cell Cycle","url":"https://www.academia.edu/Documents/in/Cell_Cycle?f_ri=3702"},{"id":11929,"name":"DNA replication","url":"https://www.academia.edu/Documents/in/DNA_replication?f_ri=3702"},{"id":13827,"name":"Cell Biology","url":"https://www.academia.edu/Documents/in/Cell_Biology?f_ri=3702"},{"id":23067,"name":"DNA repair","url":"https://www.academia.edu/Documents/in/DNA_repair?f_ri=3702"},{"id":24731,"name":"Apoptosis","url":"https://www.academia.edu/Documents/in/Apoptosis?f_ri=3702"},{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=3702"},{"id":30347,"name":"Translation","url":"https://www.academia.edu/Documents/in/Translation?f_ri=3702"},{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography?f_ri=3702"},{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=3702"},{"id":42132,"name":"Transcription","url":"https://www.academia.edu/Documents/in/Transcription?f_ri=3702"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=3702"},{"id":49123,"name":"Saccharomyces cerevisiae","url":"https://www.academia.edu/Documents/in/Saccharomyces_cerevisiae?f_ri=3702"},{"id":50157,"name":"Molecular","url":"https://www.academia.edu/Documents/in/Molecular?f_ri=3702"},{"id":50630,"name":"Crystal structure","url":"https://www.academia.edu/Documents/in/Crystal_structure?f_ri=3702"},{"id":74780,"name":"Mutation","url":"https://www.academia.edu/Documents/in/Mutation?f_ri=3702"},{"id":94729,"name":"RNAi","url":"https://www.academia.edu/Documents/in/RNAi?f_ri=3702"},{"id":135658,"name":"Chromatin remodeling","url":"https://www.academia.edu/Documents/in/Chromatin_remodeling?f_ri=3702"},{"id":149210,"name":"Mechanism","url":"https://www.academia.edu/Documents/in/Mechanism?f_ri=3702"},{"id":168760,"name":"Macromolecules","url":"https://www.academia.edu/Documents/in/Macromolecules?f_ri=3702"},{"id":169771,"name":"Nucleotide Excision Repair","url":"https://www.academia.edu/Documents/in/Nucleotide_Excision_Repair?f_ri=3702"},{"id":178906,"name":"Nucleic Acids","url":"https://www.academia.edu/Documents/in/Nucleic_Acids?f_ri=3702"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=3702"},{"id":238813,"name":"Chromatin","url":"https://www.academia.edu/Documents/in/Chromatin?f_ri=3702"},{"id":240723,"name":"Chromatin structure","url":"https://www.academia.edu/Documents/in/Chromatin_structure?f_ri=3702"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=3702"},{"id":990417,"name":"Recombinant Proteins","url":"https://www.academia.edu/Documents/in/Recombinant_Proteins?f_ri=3702"},{"id":1494061,"name":"DNA recombination","url":"https://www.academia.edu/Documents/in/DNA_recombination?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_18043936" data-work_id="18043936" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/18043936/tRNA_punctuation_model_of_RNA_processing_in_human_mitochondria">tRNA punctuation model of RNA processing in human mitochondria</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">A 3&amp;#39;-end proximal segment of most of the putative mRNAs encoded in the heavy strand of HeLa cell mtDNA has been partially sequences and aligned with the DNA sequence. In all cases, the 3&amp;#39;-end nucleotide of the individual... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_18043936" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">A 3&amp;#39;-end proximal segment of most of the putative mRNAs encoded in the heavy strand of HeLa cell mtDNA has been partially sequences and aligned with the DNA sequence. In all cases, the 3&amp;#39;-end nucleotide of the individual mRNA coding sequences has been found to be immediately contiguous to a tRNA gene or another mRNA coding sequence. These and previous results indicate that the heavy (H) strand sequences coding for the rRNA, poly(A)-containing RNA and tRNA species form a continuum extending over almost the entire length of this strand. We propose that the H strand is transcribed into a single polycistronic RNA molecule, which is processed later into mature species by precise endonucleolytic cleavages which occur, in most cases, immediately before and after a tRNA sequence.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/18043936" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="10ed207cf97ba3a3e660d3be78298b79" rel="nofollow" data-download="{"attachment_id":42204024,"asset_id":18043936,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42204024/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="37982119" href="https://independent.academia.edu/GiuseppeAttardi">Giuseppe Attardi</a><script data-card-contents-for-user="37982119" type="text/json">{"id":37982119,"first_name":"Giuseppe","last_name":"Attardi","domain_name":"independent","page_name":"GiuseppeAttardi","display_name":"Giuseppe Attardi","profile_url":"https://independent.academia.edu/GiuseppeAttardi?f_ri=3702","photo":"https://gravatar.com/avatar/6e3b2ce85360a7027620ee3993980aa3?s=65"}</script></span></span></li><li class="js-paper-rank-work_18043936 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="18043936"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 18043936, container: ".js-paper-rank-work_18043936", }); 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In all cases, the 3\u0026amp;#39;-end nucleotide of the individual mRNA coding sequences has been found to be immediately contiguous to a tRNA gene or another mRNA coding sequence. These and previous results indicate that the heavy (H) strand sequences coding for the rRNA, poly(A)-containing RNA and tRNA species form a continuum extending over almost the entire length of this strand. We propose that the H strand is transcribed into a single polycistronic RNA molecule, which is processed later into mature species by precise endonucleolytic cleavages which occur, in most cases, immediately before and after a tRNA sequence.","downloadable_attachments":[{"id":42204024,"asset_id":18043936,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":37982119,"first_name":"Giuseppe","last_name":"Attardi","domain_name":"independent","page_name":"GiuseppeAttardi","display_name":"Giuseppe Attardi","profile_url":"https://independent.academia.edu/GiuseppeAttardi?f_ri=3702","photo":"https://gravatar.com/avatar/6e3b2ce85360a7027620ee3993980aa3?s=65"}],"research_interests":[{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=3702","nofollow":false},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary?f_ri=3702","nofollow":false},{"id":33319,"name":"Nature","url":"https://www.academia.edu/Documents/in/Nature?f_ri=3702","nofollow":false},{"id":63093,"name":"Mitochondrial DNA","url":"https://www.academia.edu/Documents/in/Mitochondrial_DNA?f_ri=3702"},{"id":129386,"name":"DNA sequence design","url":"https://www.academia.edu/Documents/in/DNA_sequence_design?f_ri=3702"},{"id":224794,"name":"Genetic linkage analysis","url":"https://www.academia.edu/Documents/in/Genetic_linkage_analysis?f_ri=3702"},{"id":233229,"name":"Genes","url":"https://www.academia.edu/Documents/in/Genes?f_ri=3702"},{"id":422325,"name":"HeLa cells","url":"https://www.academia.edu/Documents/in/HeLa_cells?f_ri=3702"},{"id":998170,"name":"Poly A","url":"https://www.academia.edu/Documents/in/Poly_A?f_ri=3702"},{"id":1597877,"name":"Nucleotides","url":"https://www.academia.edu/Documents/in/Nucleotides?f_ri=3702"},{"id":1763968,"name":"Gene Expression Regulation","url":"https://www.academia.edu/Documents/in/Gene_Expression_Regulation?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_75052599" data-work_id="75052599" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/75052599/Mechanistic_insights_on_the_Dicer_independent_AGO2_mediated_processing_of_AgoshRNAs">Mechanistic insights on the Dicer-independent AGO2-mediated processing of AgoshRNAs</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Short hairpin RNAs (shRNAs) are widely used for gene knockdown by inducing the RNA interference (RNAi) mechanism, both for research and therapeutic purposes. The shRNA precursor is processed by the RNase III-like enzyme Dicer into... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_75052599" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Short hairpin RNAs (shRNAs) are widely used for gene knockdown by inducing the RNA interference (RNAi) mechanism, both for research and therapeutic purposes. The shRNA precursor is processed by the RNase III-like enzyme Dicer into biologically active small interfering RNA (siRNA). This effector molecule subsequently targets a complementary mRNA for destruction via the Argonaute 2 (AGO2) complex. The cellular role of Dicer concerns the processing of pre-miRNAs into mature microRNA (miRNA). Recently, a non-canonical pathway was reported for the biogenesis of miR-451, which bypasses Dicer and is processed instead by the slicer activity of AGO2, followed by the regular AGO2-mediated mRNA targeting step. Interestingly, shRNA designs that are characterized by a relatively short basepaired stem also bypass Dicer to be processed by AGO2. We named this design AgoshRNA as these molecules depend on AGO2 both for processing and silencing activity. In this study, we investigated diverse mechanis...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/75052599" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3cedd0a8ce3d5f8c23d61aad0c691c81" rel="nofollow" data-download="{"attachment_id":82977726,"asset_id":75052599,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/82977726/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="35284927" href="https://independent.academia.edu/BenBerkhout">Ben Berkhout</a><script data-card-contents-for-user="35284927" type="text/json">{"id":35284927,"first_name":"Ben","last_name":"Berkhout","domain_name":"independent","page_name":"BenBerkhout","display_name":"Ben Berkhout","profile_url":"https://independent.academia.edu/BenBerkhout?f_ri=3702","photo":"https://gravatar.com/avatar/dac4ceeea9187b597bf7b5b4b7198479?s=65"}</script></span></span></li><li class="js-paper-rank-work_75052599 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="75052599"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 75052599, container: ".js-paper-rank-work_75052599", }); 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The shRNA precursor is processed by the RNase III-like enzyme Dicer into biologically active small interfering RNA (siRNA). This effector molecule subsequently targets a complementary mRNA for destruction via the Argonaute 2 (AGO2) complex. The cellular role of Dicer concerns the processing of pre-miRNAs into mature microRNA (miRNA). Recently, a non-canonical pathway was reported for the biogenesis of miR-451, which bypasses Dicer and is processed instead by the slicer activity of AGO2, followed by the regular AGO2-mediated mRNA targeting step. Interestingly, shRNA designs that are characterized by a relatively short basepaired stem also bypass Dicer to be processed by AGO2. We named this design AgoshRNA as these molecules depend on AGO2 both for processing and silencing activity. In this study, we investigated diverse mechanis...","downloadable_attachments":[{"id":82977726,"asset_id":75052599,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":35284927,"first_name":"Ben","last_name":"Berkhout","domain_name":"independent","page_name":"BenBerkhout","display_name":"Ben Berkhout","profile_url":"https://independent.academia.edu/BenBerkhout?f_ri=3702","photo":"https://gravatar.com/avatar/dac4ceeea9187b597bf7b5b4b7198479?s=65"}],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology?f_ri=3702","nofollow":false},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine?f_ri=3702","nofollow":false},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line?f_ri=3702"},{"id":165677,"name":"shRNA","url":"https://www.academia.edu/Documents/in/shRNA?f_ri=3702"},{"id":722685,"name":"RNA biology","url":"https://www.academia.edu/Documents/in/RNA_biology?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_268595" data-work_id="268595" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/268595/A_Multimeric_Assembly_Factor_Controls_the_Formation_of_Alternative_20S_Proteasomes">A Multimeric Assembly Factor Controls the Formation of Alternative 20S Proteasomes</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div 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RNase E/G and an RNase P-like activity</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/30737904" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3a2486f51dea2d5e2d411f71019a2021" rel="nofollow" data-download="{"attachment_id":51183699,"asset_id":30737904,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" 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type="text/json">{"id":18519,"name":"Glycobiology","url":"https://www.academia.edu/Documents/in/Glycobiology?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="420908" href="https://www.academia.edu/Documents/in/RNA-binding_proteins">RNA-binding proteins</a><script data-card-contents-for-ri="420908" type="text/json">{"id":420908,"name":"RNA-binding proteins","url":"https://www.academia.edu/Documents/in/RNA-binding_proteins?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=27273833]'), work: {"id":27273833,"title":"SR proteins and galectins: what's in a name?","created_at":"2016-07-26T08:13:41.052-07:00","url":"https://www.academia.edu/27273833/SR_proteins_and_galectins_whats_in_a_name?f_ri=3702","dom_id":"work_27273833","summary":null,"downloadable_attachments":[{"id":47533603,"asset_id":27273833,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":51377617,"first_name":"Kevin","last_name":"Haudek","domain_name":"independent","page_name":"KevinHaudek","display_name":"Kevin Haudek","profile_url":"https://independent.academia.edu/KevinHaudek?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":18519,"name":"Glycobiology","url":"https://www.academia.edu/Documents/in/Glycobiology?f_ri=3702","nofollow":false},{"id":47884,"name":"Biological 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href="https://www.academia.edu/10750473/Signals_pathways_and_splicing_regulation">Signals, pathways and splicing regulation</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/10750473" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="5d869c5398e7829323081194c69f6106" rel="nofollow" data-download="{"attachment_id":47154660,"asset_id":10750473,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/47154660/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="26193815" href="https://uba.academia.edu/MatiasBlaustein">Matias Blaustein</a><script data-card-contents-for-user="26193815" type="text/json">{"id":26193815,"first_name":"Matias","last_name":"Blaustein","domain_name":"uba","page_name":"MatiasBlaustein","display_name":"Matias 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$(".js-percentile-work_10750473"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_10750473 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="10750473"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 10750473; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=10750473]").text(description); $(".js-view-count-work_10750473").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_10750473").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="10750473"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">8</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="3702" href="https://www.academia.edu/Documents/in/M_Rna_Processing">M Rna Processing</a>, <script data-card-contents-for-ri="3702" type="text/json">{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="35637" href="https://www.academia.edu/Documents/in/Molecular_Mechanics">Molecular Mechanics</a>, <script data-card-contents-for-ri="35637" type="text/json">{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="38831" href="https://www.academia.edu/Documents/in/Signal_Transduction">Signal Transduction</a>, <script data-card-contents-for-ri="38831" type="text/json">{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="139002" href="https://www.academia.edu/Documents/in/Alternative_splicing">Alternative splicing</a><script data-card-contents-for-ri="139002" type="text/json">{"id":139002,"name":"Alternative splicing","url":"https://www.academia.edu/Documents/in/Alternative_splicing?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=10750473]'), work: {"id":10750473,"title":"Signals, pathways and splicing regulation","created_at":"2015-02-12T17:42:17.342-08:00","url":"https://www.academia.edu/10750473/Signals_pathways_and_splicing_regulation?f_ri=3702","dom_id":"work_10750473","summary":null,"downloadable_attachments":[{"id":47154660,"asset_id":10750473,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":26193815,"first_name":"Matias","last_name":"Blaustein","domain_name":"uba","page_name":"MatiasBlaustein","display_name":"Matias Blaustein","profile_url":"https://uba.academia.edu/MatiasBlaustein?f_ri=3702","photo":"https://0.academia-photos.com/26193815/7506590/8432047/s65_matias.blaustein.jpg"}],"research_interests":[{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=3702","nofollow":false},{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=3702","nofollow":false},{"id":139002,"name":"Alternative splicing","url":"https://www.academia.edu/Documents/in/Alternative_splicing?f_ri=3702","nofollow":false},{"id":317801,"name":"Cell nucleus","url":"https://www.academia.edu/Documents/in/Cell_nucleus?f_ri=3702"},{"id":635694,"name":"Alternative Splicing","url":"https://www.academia.edu/Documents/in/Alternative_Splicing-1?f_ri=3702"},{"id":965027,"name":"Subcellular Fractions","url":"https://www.academia.edu/Documents/in/Subcellular_Fractions?f_ri=3702"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_26606667" data-work_id="26606667" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/26606667/Nonproductive_kappa_immunoglobulin_genes_recombinational_abnormalities_and_other_lesions_affecting_transcription_RNA_processing_turnover_and_translation">Nonproductive kappa immunoglobulin genes: recombinational abnormalities and other lesions affecting transcription, RNA processing, turnover, and translation</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Six nonproductive kappa immunoglobulin genes (kappa- alleles) were cloned and sequenced. The structural abnormalities discerned from sequence analysis were correlated with functional lesions at the level of transcription, RNA processing,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_26606667" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Six nonproductive kappa immunoglobulin genes (kappa- alleles) were cloned and sequenced. The structural abnormalities discerned from sequence analysis were correlated with functional lesions at the level of transcription, RNA processing, turnover, and translation. Four kappa- alleles, three containing V kappa genes and one not, are transcribed at normal or even greater than normal rates, the defects in these genes being expressed at various posttranscriptional levels. The other two kappa- alleles, both of which lacked V genes, exhibited greatly depressed yet clearly detectable transcriptional activity. These results are consistent with a hierarchical relationship between enhancer and promoter elements in which the enhancer establishes transcriptional competence at the kappa locus and the promoter (or pseudopromoter) determines the relative level of transcriptional activity. One of the structural abnormalities discovered in this study, a large deletion which removes the entire J kapp...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/26606667" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="c2564a50b71a35842592fb77bee80977" rel="nofollow" data-download="{"attachment_id":46893290,"asset_id":26606667,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46893290/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="50542902" href="https://independent.academia.edu/LWiedemann">L. Wiedemann</a><script data-card-contents-for-user="50542902" type="text/json">{"id":50542902,"first_name":"L.","last_name":"Wiedemann","domain_name":"independent","page_name":"LWiedemann","display_name":"L. 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The structural abnormalities discerned from sequence analysis were correlated with functional lesions at the level of transcription, RNA processing, turnover, and translation. Four kappa- alleles, three containing V kappa genes and one not, are transcribed at normal or even greater than normal rates, the defects in these genes being expressed at various posttranscriptional levels. The other two kappa- alleles, both of which lacked V genes, exhibited greatly depressed yet clearly detectable transcriptional activity. These results are consistent with a hierarchical relationship between enhancer and promoter elements in which the enhancer establishes transcriptional competence at the kappa locus and the promoter (or pseudopromoter) determines the relative level of transcriptional activity. One of the structural abnormalities discovered in this study, a large deletion which removes the entire J kapp...","downloadable_attachments":[{"id":46893290,"asset_id":26606667,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":50542902,"first_name":"L.","last_name":"Wiedemann","domain_name":"independent","page_name":"LWiedemann","display_name":"L. Wiedemann","profile_url":"https://independent.academia.edu/LWiedemann?f_ri=3702","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702","nofollow":false},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=3702","nofollow":false},{"id":63067,"name":"Molecular and cellular biology","url":"https://www.academia.edu/Documents/in/Molecular_and_cellular_biology?f_ri=3702","nofollow":false},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice?f_ri=3702","nofollow":false},{"id":295728,"name":"Molecular cloning","url":"https://www.academia.edu/Documents/in/Molecular_cloning?f_ri=3702"},{"id":569028,"name":"Genetic Recombination","url":"https://www.academia.edu/Documents/in/Genetic_Recombination?f_ri=3702"},{"id":809882,"name":"Base Sequence","url":"https://www.academia.edu/Documents/in/Base_Sequence?f_ri=3702"},{"id":1588981,"name":"Protein Biosynthesis","url":"https://www.academia.edu/Documents/in/Protein_Biosynthesis?f_ri=3702"},{"id":1763968,"name":"Gene Expression Regulation","url":"https://www.academia.edu/Documents/in/Gene_Expression_Regulation?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_12197852" data-work_id="12197852" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/12197852/The_%CE%94F508_cystic_fibrosis_mutation_impairs_domain_domain_interactions_and_arrests_post_translational_folding_of_CFTR">The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Misfolding accounts for the endoplasmic reticulum–associated degradation of mutant cystic fibrosis transmembrane conductance regulators (CFTRs), including deletion of Phe508 (ΔF508) in the nucleotide-binding domain 1 (NBD1). To study the... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_12197852" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Misfolding accounts for the endoplasmic reticulum–associated degradation of mutant cystic fibrosis transmembrane conductance regulators (CFTRs), including deletion of Phe508 (ΔF508) in the nucleotide-binding domain 1 (NBD1). To study the role of Phe508, the de novo folding and stability of NBD1, NBD2 and CFTR were compared in conjunction with mutagenesis of Phe508. ΔF508 and amino acid replacements that prevented CFTR folding</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/12197852" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="f1ad015a9aec881d8a50b961c21af577" rel="nofollow" data-download="{"attachment_id":46306795,"asset_id":12197852,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46306795/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="30657926" href="https://mcgill.academia.edu/GergelyLukacs">Gergely Lukacs</a><script data-card-contents-for-user="30657926" type="text/json">{"id":30657926,"first_name":"Gergely","last_name":"Lukacs","domain_name":"mcgill","page_name":"GergelyLukacs","display_name":"Gergely Lukacs","profile_url":"https://mcgill.academia.edu/GergelyLukacs?f_ri=3702","photo":"https://0.academia-photos.com/30657926/124895234/114255932/s65_gergely.lukacs.jpeg"}</script></span></span></li><li class="js-paper-rank-work_12197852 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="12197852"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 12197852, container: ".js-paper-rank-work_12197852", }); 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$(".js-view-count[data-work-id=12197852]").text(description); $(".js-view-count-work_12197852").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_12197852").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="12197852"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">32</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="145" href="https://www.academia.edu/Documents/in/Biochemistry">Biochemistry</a>, <script data-card-contents-for-ri="145" type="text/json">{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="156" href="https://www.academia.edu/Documents/in/Genetics">Genetics</a>, <script data-card-contents-for-ri="156" type="text/json">{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="502" href="https://www.academia.edu/Documents/in/Biophysics">Biophysics</a>, <script data-card-contents-for-ri="502" type="text/json">{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=3702","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="2513" href="https://www.academia.edu/Documents/in/Molecular_Biology">Molecular Biology</a><script data-card-contents-for-ri="2513" type="text/json">{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology?f_ri=3702","nofollow":false}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=12197852]'), work: {"id":12197852,"title":"The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR","created_at":"2015-05-02T21:48:13.923-07:00","url":"https://www.academia.edu/12197852/The_%CE%94F508_cystic_fibrosis_mutation_impairs_domain_domain_interactions_and_arrests_post_translational_folding_of_CFTR?f_ri=3702","dom_id":"work_12197852","summary":"Misfolding accounts for the endoplasmic reticulum–associated degradation of mutant cystic fibrosis transmembrane conductance regulators (CFTRs), including deletion of Phe508 (ΔF508) in the nucleotide-binding domain 1 (NBD1). To study the role of Phe508, the de novo folding and stability of NBD1, NBD2 and CFTR were compared in conjunction with mutagenesis of Phe508. ΔF508 and amino acid replacements that prevented CFTR folding","downloadable_attachments":[{"id":46306795,"asset_id":12197852,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":30657926,"first_name":"Gergely","last_name":"Lukacs","domain_name":"mcgill","page_name":"GergelyLukacs","display_name":"Gergely Lukacs","profile_url":"https://mcgill.academia.edu/GergelyLukacs?f_ri=3702","photo":"https://0.academia-photos.com/30657926/124895234/114255932/s65_gergely.lukacs.jpeg"}],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=3702","nofollow":false},{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=3702","nofollow":false},{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=3702","nofollow":false},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology?f_ri=3702","nofollow":false},{"id":3701,"name":"RNA","url":"https://www.academia.edu/Documents/in/RNA?f_ri=3702"},{"id":3702,"name":"M Rna Processing","url":"https://www.academia.edu/Documents/in/M_Rna_Processing?f_ri=3702"},{"id":3971,"name":"Protein Folding","url":"https://www.academia.edu/Documents/in/Protein_Folding?f_ri=3702"},{"id":6946,"name":"Cystic Fibrosis","url":"https://www.academia.edu/Documents/in/Cystic_Fibrosis?f_ri=3702"},{"id":9113,"name":"Cell Cycle","url":"https://www.academia.edu/Documents/in/Cell_Cycle?f_ri=3702"},{"id":11929,"name":"DNA replication","url":"https://www.academia.edu/Documents/in/DNA_replication?f_ri=3702"},{"id":13827,"name":"Cell Biology","url":"https://www.academia.edu/Documents/in/Cell_Biology?f_ri=3702"},{"id":23067,"name":"DNA repair","url":"https://www.academia.edu/Documents/in/DNA_repair?f_ri=3702"},{"id":24731,"name":"Apoptosis","url":"https://www.academia.edu/Documents/in/Apoptosis?f_ri=3702"},{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=3702"},{"id":30347,"name":"Translation","url":"https://www.academia.edu/Documents/in/Translation?f_ri=3702"},{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=3702"},{"id":42132,"name":"Transcription","url":"https://www.academia.edu/Documents/in/Transcription?f_ri=3702"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=3702"},{"id":50157,"name":"Molecular","url":"https://www.academia.edu/Documents/in/Molecular?f_ri=3702"},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line?f_ri=3702"},{"id":94729,"name":"RNAi","url":"https://www.academia.edu/Documents/in/RNAi?f_ri=3702"},{"id":135658,"name":"Chromatin remodeling","url":"https://www.academia.edu/Documents/in/Chromatin_remodeling?f_ri=3702"},{"id":149210,"name":"Mechanism","url":"https://www.academia.edu/Documents/in/Mechanism?f_ri=3702"},{"id":168760,"name":"Macromolecules","url":"https://www.academia.edu/Documents/in/Macromolecules?f_ri=3702"},{"id":178906,"name":"Nucleic Acids","url":"https://www.academia.edu/Documents/in/Nucleic_Acids?f_ri=3702"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=3702"},{"id":238813,"name":"Chromatin","url":"https://www.academia.edu/Documents/in/Chromatin?f_ri=3702"},{"id":240723,"name":"Chromatin structure","url":"https://www.academia.edu/Documents/in/Chromatin_structure?f_ri=3702"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=3702"},{"id":382339,"name":"Phenylalanine","url":"https://www.academia.edu/Documents/in/Phenylalanine?f_ri=3702"},{"id":900881,"name":"Membrane Protein","url":"https://www.academia.edu/Documents/in/Membrane_Protein?f_ri=3702"},{"id":1494061,"name":"DNA recombination","url":"https://www.academia.edu/Documents/in/DNA_recombination?f_ri=3702"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_25754251" data-work_id="25754251" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/25754251/Detection_of_novel_members_structure_function_analysis_and_evolutionary_classification_of_the_2H_phosphoesterase_family">Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase family</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">2&#39;,3&#39; Cyclic nucleotide phosphodiesterases are enzymes that catalyze at least two distinct steps in the splicing of tRNA introns in eukaryotes. Recently, the biochemistry and structure of these enzymes, from yeast and the plant... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_25754251" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">2&#39;,3&#39; Cyclic nucleotide phosphodiesterases are enzymes that catalyze at least two distinct steps in the splicing of tRNA introns in eukaryotes. Recently, the biochemistry and structure of these enzymes, from yeast and the plant Arabidopsis thaliana, have been extensively studied. They were found to share a common active site, characterized by two conserved histidines, with the bacterial tRNA-ligating enzyme LigT and the vertebrate myelin-associated 2&#39;,3&#39; phosphodiesterases. Using sensitive sequence profile analysis methods, we show that these enzymes define a large superfamily of predicted phosphoesterases with two conserved histidines (hence 2H phosphoesterase superfamily). We identify several new families of 2H phosphoesterases and present a complete evolutionary classification of this superfamily. We also carry out a structure- function analysis of these proteins and present evidence for diverse interactions for different families, within this superfamily, with RN...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/25754251" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="4534851d54d8889c1174d22f11e2e992" rel="nofollow" data-download="{"attachment_id":46110089,"asset_id":25754251,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46110089/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="49491203" href="https://independent.academia.edu/SonaVasudevan">Sona Vasudevan</a><script data-card-contents-for-user="49491203" type="text/json">{"id":49491203,"first_name":"Sona","last_name":"Vasudevan","domain_name":"independent","page_name":"SonaVasudevan","display_name":"Sona Vasudevan","profile_url":"https://independent.academia.edu/SonaVasudevan?f_ri=3702","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_25754251 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="25754251"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 25754251, container: ".js-paper-rank-work_25754251", }); 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u-pv7x u-mb0x js-work-card work_8874121" data-work_id="8874121" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/8874121/Using_context_to_improve_protein_domain_identification">Using context to improve protein domain identification</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Background Identifying domains in protein sequences is an important step in protein structural and functional annotation. Existing domain recognition methods typically evaluate each domain prediction independently of the rest. However,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_8874121" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Background Identifying domains in protein sequences is an important step in protein structural and functional annotation. Existing domain recognition methods typically evaluate each domain prediction independently of the rest. However, the majority of proteins are multidomain, and pairwise domain co-occurrences are highly specific and non-transitive. Results Here, we demonstrate how to exploit domain co-occurrence to boost weak domain predictions that appear in previously observed combinations, while penalizing higher confidence domains if such combinations have never been observed. Our framework, Domain Prediction Using Context (dPUC), incorporates pairwise "context" scores between domains, along with traditional domain scores and thresholds, and improves domain prediction across a variety of organisms from bacteria to protozoa and metazoa. Among the genomes we tested, dPUC is most successful at improving predictions for the poorly-annotated malaria parasite Plasmodium falciparum, for which over 38% of the genome is currently unannotated. Our approach enables high-confidence annotations in this organism and the identification of orthologs to many core machinery proteins conserved in all eukaryotes, including those involved in ribosomal assembly and other RNA processing events, which surprisingly had not been previously known. Conclusions Overall, our results demonstrate that this new context-based approach will provide significant improvements in domain and function prediction, especially for poorly understood genomes for which the need for additional annotations is greatest. Source code for the algorithm is available under a GPL open source license at <a href="http://compbio.cs.princeton.edu/dpuc/" rel="nofollow">http://compbio.cs.princeton.edu/dpuc/</a>. Pre-computed results for our test organisms and a web server are also available at that location.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/8874121" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="5fce369a1c30eb74ea2a495d0e3368b8" rel="nofollow" data-download="{"attachment_id":47970971,"asset_id":8874121,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/47970971/download_file?st=MTczMjc5NDQ5Niw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="19441556" href="https://independent.academia.edu/AlejandroOchoa7">Alejandro Ochoa</a><script data-card-contents-for-user="19441556" type="text/json">{"id":19441556,"first_name":"Alejandro","last_name":"Ochoa","domain_name":"independent","page_name":"AlejandroOchoa7","display_name":"Alejandro Ochoa","profile_url":"https://independent.academia.edu/AlejandroOchoa7?f_ri=3702","photo":"https://0.academia-photos.com/19441556/6922129/7808281/s65_alejandro.ochoa.jpg_oh_db4af2df993631139837ab8c6ed61441_oe_555e7301___gda___1433090370_8a8c28a74c90907eafa90fe11c3ca2e0"}</script></span></span></li><li class="js-paper-rank-work_8874121 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="8874121"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 8874121, container: ".js-paper-rank-work_8874121", }); 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Existing domain recognition methods typically evaluate each domain prediction independently of the rest. However, the majority of proteins are multidomain, and pairwise domain co-occurrences are highly specific and non-transitive. Results Here, we demonstrate how to exploit domain co-occurrence to boost weak domain predictions that appear in previously observed combinations, while penalizing higher confidence domains if such combinations have never been observed. Our framework, Domain Prediction Using Context (dPUC), incorporates pairwise \"context\" scores between domains, along with traditional domain scores and thresholds, and improves domain prediction across a variety of organisms from bacteria to protozoa and metazoa. Among the genomes we tested, dPUC is most successful at improving predictions for the poorly-annotated malaria parasite Plasmodium falciparum, for which over 38% of the genome is currently unannotated. Our approach enables high-confidence annotations in this organism and the identification of orthologs to many core machinery proteins conserved in all eukaryotes, including those involved in ribosomal assembly and other RNA processing events, which surprisingly had not been previously known. Conclusions Overall, our results demonstrate that this new context-based approach will provide significant improvements in domain and function prediction, especially for poorly understood genomes for which the need for additional annotations is greatest. Source code for the algorithm is available under a GPL open source license at http://compbio.cs.princeton.edu/dpuc/. Pre-computed results for our test organisms and a web server are also available at that location.","downloadable_attachments":[{"id":47970971,"asset_id":8874121,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":19441556,"first_name":"Alejandro","last_name":"Ochoa","domain_name":"independent","page_name":"AlejandroOchoa7","display_name":"Alejandro Ochoa","profile_url":"https://independent.academia.edu/AlejandroOchoa7?f_ri=3702","photo":"https://0.academia-photos.com/19441556/6922129/7808281/s65_alejandro.ochoa.jpg_oh_db4af2df993631139837ab8c6ed61441_oe_555e7301___gda___1433090370_8a8c28a74c90907eafa90fe11c3ca2e0"}],"research_interests":[{"id":428,"name":"Algorithms","url":"https://www.academia.edu/Documents/in/Algorithms?f_ri=3702","nofollow":false},{"id":3216,"name":"Genomics","url":"https://www.academia.edu/Documents/in/Genomics?f_ri=3702","nofollow":false},{"id":3702,"name":"M Rna 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data-unfollow-ri-id="2183">Following</a></div></li><li class="list-group-item media_v2 u-mt0x u-p3x"><div class="media-body"><div class="u-tcGrayDarker u-fw700"><a class="u-tcGrayDarker" href="https://www.academia.edu/Documents/in/Functional_validation">Functional validation</a></div></div><div class="media-right media-middle"><a class="u-tcGreen u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-follow-ri-id="5492">Follow</a><a class="u-tcGray u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-unfollow-ri-id="5492">Following</a></div></li><li class="list-group-item media_v2 u-mt0x u-p3x"><div class="media-body"><div class="u-tcGrayDarker u-fw700"><a class="u-tcGrayDarker" href="https://www.academia.edu/Documents/in/Polyadenylation">Polyadenylation</a></div></div><div class="media-right media-middle"><a class="u-tcGreen u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-follow-ri-id="12341">Follow</a><a class="u-tcGray u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-unfollow-ri-id="12341">Following</a></div></li><li class="list-group-item media_v2 u-mt0x u-p3x"><div class="media-body"><div class="u-tcGrayDarker u-fw700"><a class="u-tcGrayDarker" href="https://www.academia.edu/Documents/in/Non_Coding_Rna">Non Coding Rna</a></div></div><div class="media-right media-middle"><a class="u-tcGreen u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-follow-ri-id="43929">Follow</a><a class="u-tcGray u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-unfollow-ri-id="43929">Following</a></div></li><li class="list-group-item media_v2 u-mt0x u-p3x"><div class="media-body"><div class="u-tcGrayDarker u-fw700"><a class="u-tcGrayDarker" href="https://www.academia.edu/Documents/in/Molecular_Biology">Molecular Biology</a></div></div><div class="media-right media-middle"><a class="u-tcGreen u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-follow-ri-id="2513">Follow</a><a class="u-tcGray u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-unfollow-ri-id="2513">Following</a></div></li><li class="list-group-item media_v2 u-mt0x u-p3x"><div class="media-body"><div class="u-tcGrayDarker u-fw700"><a class="u-tcGrayDarker" href="https://www.academia.edu/Documents/in/RNA-seq_Analysis">RNA-seq Analysis</a></div></div><div class="media-right media-middle"><a class="u-tcGreen u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-follow-ri-id="29083">Follow</a><a class="u-tcGray u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-unfollow-ri-id="29083">Following</a></div></li><li class="list-group-item media_v2 u-mt0x u-p3x"><div class="media-body"><div class="u-tcGrayDarker u-fw700"><a class="u-tcGrayDarker" href="https://www.academia.edu/Documents/in/Molecular_Virology_Biology_">Molecular Virology (Biology)</a></div></div><div class="media-right media-middle"><a class="u-tcGreen u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-follow-ri-id="170">Follow</a><a class="u-tcGray u-textDecorationNone u-linkUnstyled u-fw500 hidden" data-unfollow-ri-id="170">Following</a></div></li></ul></div></div></div></div></div></div><script>// MIT License // Copyright © 2011 Sebastian Tschan, https://blueimp.net // Permission is hereby granted, free of charge, to any person obtaining a copy of // this software and associated documentation files (the "Software"), to deal in // the Software without restriction, including without limitation the rights to // use, copy, modify, merge, publish, distribute, sublicense, and/or sell copies of // the Software, and to permit persons to whom the Software is furnished to do so, // subject to the following conditions: // The above copyright notice and this permission notice shall be included in all // copies or substantial portions of the Software. // THE SOFTWARE IS PROVIDED "AS IS", WITHOUT WARRANTY OF ANY KIND, EXPRESS OR // IMPLIED, INCLUDING BUT NOT LIMITED TO THE WARRANTIES OF MERCHANTABILITY, FITNESS // FOR A PARTICULAR PURPOSE AND NONINFRINGEMENT. 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