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IBB – Institut de Biotecnologia i Biomedicina
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<!-- 201704 Wordpress styles --> <header class="vl-main-header"> <div class="classDiv_header classColour"> <div class="classDiv_hTitle_fullWeight classColour"> <h1> Protein Folding and Conformational Diseases </h1> <!-- <p> <form action="https://ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/view_unitat.php" method="post" name="view_unitat"> <input type="hidden" value="40" name="CodiUnitat"/> (Unit: <a href="javascript:document.view_unitat.submit();" alt="Veure Perfil"> Applied Proteomics and Protein Engineering</a>) </form> </p> --> </div> </div> <!-- Below the header, add the "path" to the current page. E.g.: IBB > Research > Unit --> <div class="vl-path"> <a href="https://ibb.uab.cat"> IBB </a> > <a href="https://ibb.uab.cat/index.php/research/"> Research </a> > <a href="https://ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/view_unitat.php?CodiUnitat=40"> Applied Proteomics and Protein Engineering </a> > <a> Protein Folding and Conformational Diseases </a> </div><!-- path --> </header><!-- .entry-header --> <div id="infoGroup"> <div class="classDiv_headPhoto"> <a href="https://ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/view_membre.php?CodiMembre=140" alt="Veure Perfil"><div class="classDiv_imgIPbig classDiv_imgIP" style="background:white;"><img class="portrait" src="https://ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/image.php?id=140 " height="100%" alt="" style="border:none"/></div></a> </div><div class="classDiv_headInfo"> <!-- Keep the closing and the openning tags together (div). Otherwise, using "inline-blocks" understand a white-space between them --> <!--<span class="classSpan_g">Protein Folding and Conformational Diseases</span>--> <span class="classSpan_g"><a href="https://ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/view_membre.php?CodiMembre=140" alt="Veure Perfil"> Ventura Zamora, Salvador </a><br></span> <span id="tel" class="classSpan_g"> <a href="tel:935868956"> 935868956 </a> </span> <span id="mail" class="classSpan_g"> <a href="mailto:salvador.ventura@uab.es"> salvador.ventura@uab.es </a> </span> <span id="web" class="classSpan_g"> <a href="//ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/view_grup.php?CodiGrup=36" title='Group website' target=""> ibb.uab.cat/wp-content/themes/viral/modules/ibb_membres/view_grup.php?CodiGrup=36 </a> </span> </div> </div> <div id="infoContent"> <!-- 201704 Hack: use a hidden-checkbox + related-label to deal with the label-content in CSS as it was a link (onClick...) --> <input type="checkbox" id="btnControl_tinfo"/> <label class="btn" for="btnControl_tinfo"> <div id="idDiv_tinfo" class="classDiv_t"> <div class="plus"></div> <div class="classDiv_sHeader"> <div>Research lines</div> </div> <div class="classDiv_tContent"> <p><p>Our lab uses a multidisciplinary approach to address fundamental aspects of protein folding, misfolding and aggregation. In addition to define the basic mechanistic principles underlying these processes, we aim to understand how their deregulation leads to the onset of human conformational diseases and to develop innovative therapeutics to target these pathologies. Moreover, this knowledge should allow us to design and produce novel and better protein-based biopharmaceuticals as well as the development of new self-assembled materials for nanotechnology applications.</p> <p> </p> <p><a href="#linea1ID"><img class="alignnone wp-image-1140" src="http://ibb.uab.cat/wp-content/uploads/linea1v2-300x200.jpg" alt="" width="281" height="187" /></a><a href="#linea2ID"><img class="alignnone wp-image-1141" src="http://ibb.uab.cat/wp-content/uploads/linea2-300x200.jpg" alt="" width="281" height="187" /></a><a href="#linea3ID"><img class="alignnone wp-image-1148" src="http://ibb.uab.cat/wp-content/uploads/linea3v2-300x200.jpg" alt="" width="281" height="187" /></a></p> <p><a href="#linea4ID"><img class="alignnone wp-image-1146" src="http://ibb.uab.cat/wp-content/uploads/linea4v2-300x200.jpg" alt="" width="281" height="187" /></a><a href="#linea5ID"><img class="alignnone wp-image-1144" src="http://ibb.uab.cat/wp-content/uploads/linea5-300x200.jpg" alt="" width="281" height="187" /></a><a href="#linea6ID"> <img class="alignnone wp-image-1147" src="http://ibb.uab.cat/wp-content/uploads/linea6-300x200.jpg" alt="" width="281" height="187" /></a></p> <p> </p> <hr /> <p> </p> <p style="text-align: justify;"><a id="linea1ID"></a><img class="wp-image-1140 alignleft" src="http://ibb.uab.cat/wp-content/uploads/linea1v2-300x200.jpg" alt="" width="281" height="187" /></p> <p> </p> <p style="text-align: justify;">For most proteins, biological function requires folding into a unique structure, in which they remain during their lifetime. There is, however, an emerging class of proteins that adopt a specific structure to function, but are otherwise disordered, the so-called conditionally disordered proteins (CDPs). The structure and activity of CDPs is tightly regulated by the environment. Some CDPs, use oxidation of their redox-sensitive cysteines to reversibly convert large disordered regions into defined structural domains. This is the case of proteins synthesized on cytosolic ribosomes and targeted to the intermembrane space (IMS) of mitochondria as reduced and disordered species. They become oxidized and folded into their functional forms only after entering this organelle. This redox-controlled folding, acts as a folding-trap that drives their translocation to the IMS. We use an integrated structural approach to decipher the molecular determinants of these massive structural rearrangements, which determine the function of mitochondrial proteins linked to diseases like Parkinson鈥檚, Huntington鈥檚 or cardiomyopathies</p> <p><a id="linea2ID"></a><img class="wp-image-1141 alignleft" src="http://ibb.uab.cat/wp-content/uploads/linea2-300x200.jpg" alt="" width="281" height="187" /></p> <p> </p> <p> </p> <p style="text-align: justify;">Parkinson's disease (PD) is the second most common neurodegenerative disorder and is still incurable. PD is associated with the death of dopaminergic neurons in the brain. There is substantial evidence supporting the aggregation of the protein a-Synuclein (a-Syn) as a key event in pathogenesis of PD, emerging thus as a privileged therapeutic target. We have recently identified and designed small compounds and peptides able to inhibit a-Syn aggregation with extremely high potency <em>in vitro</em> and in animal models.聽 We aim to develop these molecules into lead compounds for the therapeutics of PD.</p> <p style="text-align: justify;">Early detection of PD is a long pursued objective. A predictive test would revolutionize clinical care, research and treatment. Biochemical analysis evidenced an elevation of a-Syn aggregates in the biofluids of patients, suggesting that this feature might be used as a diagnostic biomarker for PD. We aim to develop an orthogonal approach towards the development of a sensitive automated diagnostic assay based on the specific detection of early a-Syn aggregates in biofluids.</p> <p> </p> <p style="text-align: justify;"><a id="linea3ID"></a><img class="size-medium wp-image-1148 alignleft" src="http://ibb.uab.cat/wp-content/uploads/linea3v2-300x200.jpg" alt="" width="300" height="200" />Transthyretin amyloidosis (ATTR) is the most common form of familial amyloidosis. In ATTR, destabilizing mutations in the protein transthyretin (TTR) causes amyloid fibres to build up, which, depending on the mutation, are deposited in different organs, such as the brain, the nerves or the myocardium, causing them to malfunction and bringing the various forms of the disease. To prevent disease progress, a liver transplant or heart transplant is needed. However, the use of pharmacologic chaperones that stabilize the structure of TTR is emerging as a non-invasive therapeutic means to halt the disease. In this context, we have repurposed a molecule originally intended to treat Parkinson鈥檚, as perhaps, the most effective drug for these diseases, already in clinical trials. We pursue both to test its efficacy for previously unaddressed forms of ATTR, with special emphasis of those occurring in the brain, and to use structure based design to generate second generation, more powerful, drugs</p> <p><img class="size-medium wp-image-1146 alignleft" src="http://ibb.uab.cat/wp-content/uploads/linea4v2-300x200.jpg" alt="" width="300" height="200" /></p> <p> </p> <p style="text-align: justify;"><a id="linea4ID"></a>Amyloids become infectious in prion diseases. Nevertheless, not all prion proteins are disease-related; in yeast, they help for environmental adaptation. Most yeast prions contain a low complexity (LC) prion domain responsible for their self-assembly and propagation. Proteins from other organisms such as bacteria, plants and humans do also bear prion-like domains indicating that their aggregated state might also be beneficial for the cell. Human prion-like proteins are involved in the formation of membraneless intracellular compartments through liquid-liquid phase separation using their LC domains to favor functional interactions between specific partners. However, these proteins are inherently aggregation-prone and the liquid state can revert into an aberrant solid state responsible for several pathologies including inflammatory and neurodegenerative disorders and cancer. We have recently developed a set of novel algorithms aimed to uncover novel proteins with prion-like behavior in order to characterize the functional pathways in which they are involved as well as their association to disease.</p> <p> </p> <p style="text-align: justify;"><img class="size-medium wp-image-1144 alignleft" src="http://ibb.uab.cat/wp-content/uploads/linea5-300x200.jpg" alt="" width="300" height="200" /><a id="linea5ID"></a>The extraordinary stability and tunable assembly of amyloid fibrils make them very attractive targets in nanotechnology. Most efforts so far have been focused on the use of short synthetic peptides as the bioactive components of such materials, and an analogous approach for inducing globular proteins to assemble into functional nanofibres has been much less explored. The main limitations to create mono- or multi-component nanofibres that contain functional globular proteins come from the requirement to prevent their aggregation during expression, to maintain them in a soluble state during purification and storage, and to be able to induce their assembly at a desired time and place. We aim to exploit our combined computational/experimental expertise to design and produce new molecules fulfilling these properties for a range of biomedical and biotechnological applications, including enzyme catalysis, biosensors, electronics, tissue engineering, drug delivery and immunotherapy.</p> <p><img class="size-medium wp-image-1147 alignleft" src="http://ibb.uab.cat/wp-content/uploads/linea6-300x200.jpg" alt="" width="300" height="200" /></p> <p> </p> <p style="text-align: justify;"><a id="linea6ID"></a>The fast development of protein therapeutics- monoclonal antibodies, replacement enzymes and hormones- is providing improved therapies for a wide range of human diseases, taking advantage of their high specificity towards their targets. One of the major challenges that one should face during the development of protein-based biopharmaceuticals is their inherent propensity to aggregate. Indeed, protein therapeutic agents are both stored and typically administered at very high concentrations. Under these conditions they can easily aggregate, impacting the product's developability, stability, formulation, and immunogenicity. Traditionally, attempts to improve protein solubility have exploited experimental trial and error approaches.聽 However, they are expensive, difficult to perform and time consuming. We have overcome these limitations developing AGGRESCAN3D, a very efficient computational tool for the automated design of protein structures displaying improved solubility, without compromising their thermodynamic stability and function. We aim to use this approach to assist the production of novel and better protein therapeutics.</p> <p> </p> <p> </p> <p> </p> <p> </p> <p> </p></p> </div> </div> </label> <input type="checkbox" id="btnControl_tmembres"/> <label class="btn" for="btnControl_tmembres"> <div id="idDiv_tmembres" class="classDiv_t"> <div class="plus"></div> <div class="classDiv_sHeader"> <div>Group members</div> </div> <div class="classDiv_tContent"> <br><h3>Head of the Group:</h3><ul><a href="view_membre.php?CodiMembre=140" alt="Veure Perfil"> Ventura Zamora, Salvador</a><br></ul><br><h3>Members:</h3><ul>Becari associat: <a href="view_membre.php?CodiMembre=532" alt="Veure Perfil"> Iglesias Mas, Valentin</a><br>Estudiant col路laborador: <a href="view_membre.php?CodiMembre=751" alt="Veure Perfil"> Behbahanipour , Molood</a><br>Investigador en formaci贸 (M脿ster): <a href="view_membre.php?CodiMembre=750" alt="Veure Perfil"> Bartolom茅 Nafr铆a, Andrea</a><br>Investigador en formaci贸 (M脿ster): <a href="view_membre.php?CodiMembre=701" alt="Veure Perfil"> Fornt Su帽茅, Marc</a><br>Investigador en formaci贸 (M脿ster): <a href="view_membre.php?CodiMembre=749" alt="Veure Perfil"> Manglano Artu帽edo, Zoe</a><br>Investigador postdoctoral: <a href="view_membre.php?CodiMembre=829" alt="Veure Perfil"> Burdukiewicz , Michal Jan</a><br>Investigador predoctoral en formaci贸 (PhD): <a href="view_membre.php?CodiMembre=794" alt="Veure Perfil"> B谩rcenas L贸pez, Oriol</a><br>Investigador predoctoral en formaci贸 (PhD): <a href="view_membre.php?CodiMembre=810" alt="Veure Perfil"> Goldin , Carla Jimena</a><br>Investigador predoctoral en formaci贸 (PhD): <a href="view_membre.php?CodiMembre=728" alt="Veure Perfil"> Pintado Grima, Carlos</a><br>PostDoc: <a href="view_membre.php?CodiMembre=265" alt="Veure Perfil"> Garc铆a Pardo, Javier</a><br>PostDoc: <a href="view_membre.php?CodiMembre=292" alt="Veure Perfil"> Navarro Cantero, Susanna</a><br>Professor Titular: <a href="view_membre.php?CodiMembre=451" alt="Veure Perfil"> Pallar猫s Goitiz, Irantzu</a><br>T猫cnic de Suport a la Recerca: <a href="view_membre.php?CodiMembre=271" alt="Veure Perfil"> Serra Hartmann, Xavier</a><br></ul> </div> </div> </label> <input type="checkbox" id="btnControl_tarticles"/> <label class="btn" for="btnControl_tarticles"> <div id="idDiv_tarticles" class="classDiv_t"> <div class="plus"></div> <div class="classDiv_sHeader"> <div>Publications</div> </div> <div class="classDiv_tContent"> <p><p><span style="font-size: 14pt; color: #993300; font-family: trebuchet ms,geneva,sans-serif;"><em><strong>Selected publications</strong></em></span></p> <table style="height: 82px;" width="936"> <tbody> <tr> <td style="width: 227px; text-align: center;"> <p><a href="https://pubs.acs.org/doi/10.1021/acsnano.8b00417"><img class="alignnone wp-image-3149" src="https://ibb.uab.cat/wp-content/uploads/COVER_ACS-ancac3_v008i009-226x300.jpg" alt="" width="140" height="186" /></a></p> </td> <td style="width: 227px; text-align: center;"><a href="http://www.sciencedirect.com/science/article/pii/S2213231717301258?via%3Dihub"><br /> </a><a href="https://www.cell.com/cell-reports/fulltext/S2211-1247(19)31745-0?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS2211124719317450%3Fshowall%3Dtrue"><img class="alignnone wp-image-3150" src="https://ibb.uab.cat/wp-content/uploads/cover-1-231x300.jpg" alt="" width="140" height="182" /></a>聽</td> <td style="width: 227px;"><a href="https://www.pnas.org/content/115/41/10481.long"><img class="alignnone wp-image-3151" src="https://ibb.uab.cat/wp-content/uploads/16.cover-source-224x300.jpg" alt="" width="140" height="187" /></a></td> <td style="width: 227px;"><a href="https://academic.oup.com/nar/article/47/W1/W300/5485072"><img class="alignnone wp-image-3152" src="https://ibb.uab.cat/wp-content/uploads/coverfig-233x300.jpg" alt="" width="140" height="180" /></a></td> <td style="width: 227px;"><a href="https://www.cell.com/trends/molecular-medicine/pdf/S1471-4914(20)30031-9.pdf?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1471491420300319%3Fshowall%3Dtrue"><img class="alignnone wp-image-3153" src="https://ibb.uab.cat/wp-content/uploads/cover-2-231x300.jpg" alt="" width="140" height="182" /></a></td> </tr> </tbody> </table> <p> </p> <p><span style="font-size: 14pt;"><a href="https://publons.com/researcher/2878690/salvador-ventura/"><span style="color: #993300; font-family: trebuchet ms,geneva,sans-serif;"><em><strong>All publications</strong></em></span></a></span></p></p> </div> </div> </label> <input type="checkbox" id="btnControl_tfinances"/> <label class="btn" for="btnControl_tfinances"> <div id="idDiv_tfinances" class="classDiv_t"> <div class="plus"></div> <div class="classDiv_sHeader"> <div>Funding</div> </div> <div class="classDiv_tContent"> <p><p>This group receives financial support from the following sources:</p> <p> </p> <table style="height: 38px; width: 916px;"> <tbody> <tr> <td style="width: 266px;"><img class="alignnone size-medium wp-image-1177" src="http://ibb.uab.cat/wp-content/uploads/ministerio-300x68.jpg" alt="" width="300" height="68" /></td> <td style="width: 114px;"><img class=" wp-image-1178 aligncenter" src="http://ibb.uab.cat/wp-content/uploads/feder.jpg" alt="" width="74" height="77" /></td> <td style="width: 167px;"><img class="alignnone wp-image-1175" src="http://ibb.uab.cat/wp-content/uploads/descarga-300x166.png" alt="" width="169" height="94" /></td> <td style="width: 175px;"> <p>聽<img class="wp-image-1180 aligncenter" src="http://ibb.uab.cat/wp-content/uploads/logo_cost.png" alt="" width="132" height="48" /></p> <p> </p> </td> <td style="width: 170px;">聽<img class="alignnone wp-image-1181" src="http://ibb.uab.cat/wp-content/uploads/icrea-300x99.png" alt="" width="143" height="47" /></td> </tr> </tbody> </table> <p> </p> <p> </p> <ul style="list-style-type: square;"> <li>ICREA (Instituci贸 Catalana de Recerca i Estudis Avan莽ats)(Catalan Institute of Research and Advanced Studies)</li> <li>Ministerio de Econom铆a y Competitividad (MINECO)</li> <li>European Commission (EC), Fondo Europeo de Desarrollo Regional (FEDER), "Una manera de hacer Europa"</li> <li>Fundaci贸 La Marat贸 TV3</li> <li>EU Framework Programme聽</li> </ul></p> </div> </div> </label> <input type="checkbox" id="btnControl_tvideos"/> <label class="btn" for="btnControl_tvideos"> <div id="idDiv_tvideos" class="classDiv_t classDiv_tMin"> <div class="plus"></div> <div class="classDiv_sHeader"> <div>Videos</div> </div> <div class="classDiv_tContent"> <p>[embed]https://www.youtube.com/watch?v=acW-Ps-zAPc[/embed][embed]https://www.youtube.com/watch?v=acW-Ps-zAPc[/embed]<iframe src="https://www.youtube.com/embed/I0pgHEO4jVM" width="1271" height="721" frameborder="0" allowfullscreen="allowfullscreen"></iframe></p> </div> </div> </label> <input type="checkbox" id="btnControl_tsoftware"/> <label class="btn" for="btnControl_tsoftware"> <div id="idDiv_tsoftware" class="classDiv_t classDiv_tMin"> <div class="plus"></div> <div class="classDiv_sHeader"> <div>Software</div> </div> <div class="classDiv_tContent"> <p style="text-align: left;"><span style="color: #666699;"><b>聽<span style="font-size: 14pt;"> 聽 聽 聽 Bioinformatics Tools</span></b></span></p> <p> </p> <ul> <li><span style="color: #666699;"><strong><a href="http://bioinf.uab.es/aggrescan/">AGGRESCAN</a></strong><strong>:</strong></span> prediction of "hot spots" of aggregation in polypeptides (in collaboration with X. Daura, IBB-UAB)</li> <li><span style="color: #666699;"><strong><a href="http://webapps.bifi.es/prionscan">PrionScan</a>: </strong></span>an online database of predicted prion domains in complete proteomes (in collaboration with J. Sancho, UNIZAR)</li> <li><strong><a href="http://bioinf.uab.cat/prionw/">PrionW</a>:聽</strong>identification of prion-like protein domains (in collaboration with X. Daura, IBB-UAB)</li> <li><strong><a href="http://biocomp.chem.uw.edu.pl/A3D2/">Aggrescan3D (A3D)</a>:</strong>聽a server for prediction of aggregation propensity in protein structures and rational design of protein solubility (in collaboration with S. Kmiecik, Univ. of Warsaw)</li> <li><a href="http://bioinf.uab.cat/amycov04/"><b>AMYCO</b></a><b>:聽</b>A server for prediction of the impact of mutations on the aggregation propensity of prion-like proteins.</li> <li><a href="https://ppmclab.pythonanywhere.com/DispHred"><b>DispHred</b></a><b>:聽</b>A Server to Predict pH-Dependent Order鈥揇isorder Transitions in Intrinsically Disordered Proteins<b>.</b></li> <li><a href="https://ppmclab.pythonanywhere.com/SolupHred"><b>SolupHred</b></a><b><b>:聽</b></b><b></b>A Server to Predict the pH-dependent Aggregation of Intrinsically Disordered Proteins.</li> <li><a href="http://sgnn.ppmclab.com"><b>SGnn</b></a><b><b><b>:</b></b></b> A聽server for the prediction of prion-like domains recruitment to stress granules upon heat stress.聽</li> <li><b><b><b><a href="http://disphscan.ppmclab.com">DispHScan</a> :</b></b></b> A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH.</li> <li><strong><a href="http://biocomp.chem.uw.edu.pl/A3D2/hproteome">A3D database</a>:</strong> Structure-based predictions of protein aggregation for the human proteome (in collaboration with S. Kmiecik, Univ. of Warsaw).</li> <li><strong><a href="http://carsdb.ppmclab.com">CARs-DB</a> :</strong> A database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins.</li> <li><strong><a href="http://biocomp.chem.uw.edu.pl/A3D2/yeast">A3DyDB</a> :</strong> An extensive catalog of aggregation propensity predictions for the S. cerevisiae proteome (in collaboration with S. Kmiecik, Univ. of Warsaw).</li> <li><strong><a href="http://biocomp.chem.uw.edu.pl/A3D2/MODB">A3D-MODB</a> :</strong> (A3D-MODB): A database for proteome aggregation predictions in model organisms (in collaboration with S. Kmiecik, Univ. of Warsaw).</li> <li><strong><a href="https://asynpepdb.ppmclab.com">aSynPEP-DB</a> : </strong>A database of biogenic peptides for inhibiting 伪-synuclein aggregation</li> </ul> </div> </div> </label> <div style="clear:both"></div> <div id="ghost"></div> </div> <script> // 201705 SCRIPT to control the dynamic performance of this page sections (DIVs) // Create an object that will host the checkboxes value, set manually var objChecks = {}; // We'll set the values of each section-checkbox manually. 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Then, if only one // of them is shown (it'll have a "Max" class), it'll take the whole width. if( jQuery(this).hasClass('classDiv_tMax') ) { jQuery(this).css( 'width', '98.4%' ); } /*jQuery(this).animate({ //paddingBottom: "10%", width: "49%", height: '120px' });*/ jQuery(this).children('.classDiv_tContent').css('display','none'); }); jQuery('div[id^="idDiv_t"]:nth-child(even)').each(function () { jQuery(this).css({ float: 'right', clear: 'left', position: 'relative', width: "49%", height: '120px' }); // Special case: Videos and Software are optional sections. Then, if only one // of them is shown (it'll have a "Max" class), it'll take the whole width. if( jQuery(this).hasClass('classDiv_tMax') ) { jQuery(this).css( 'width', '98.4%' ); } /*jQuery(this).animate({ //paddingBottom: "10%", width: "49%", height: '120px' });*/ jQuery(this).children('.classDiv_tContent').css('display','none'); }); jQuery('#infoContent').css('height','100%'); // Workaround > We found that, when minimizing the sections (and reducing the height) // of the page, the scroll had a strange performance. It was due to the "SmoothScroll.js" // script. So, after our modification, we tell to the control-div that the heigh must // be 100% again. NOTE: the control-div had no ID, so we find it by its z-index. jQuery('div').filter(function() { return jQuery(this).css('z-index') == -10000; }).each(function() { jQuery(this).css('height','100%'); }); } else { // Apply styles // Variables var currID = thisC.id; var expSection = '84%'; var minSection = '14%'; var minHeight = 120; var nSec = jQuery('div[id^="idDiv_t"]').length - 1; // Number of sections displayed - 1 (the opened one) // We add a class with common styles for all the sections (no min-height, with margins, etc.) jQuery('.classDiv_t').addClass("classDiv_tTemp"); if (jQuery(window).width() > 1180) { // Uncheck all the checkboxes jQuery('input[id^="btnControl_t"]').each( function () { objChecks[this] = false; jQuery(this).prop('checked', false); } ); // Check the current checkbox objChecks[thisC.id] = true; jQuery(chkbx_id).prop('checked', true); // Apply the reduced-style for the rest of sections jQuery('div[id^="idDiv_t"]').each(function () { if (this.id != currID) { jQuery(this).animate({ //paddingBottom: "10%", width: minSection, height: '120px' }); jQuery(this).css({ float: 'right', clear: 'right', position: 'relative' }); jQuery(this).children('.classDiv_tContent').css('display','none'); } }); // Apply the expanded-style for the selected section jQuery(thisC).children('.classDiv_tContent').css('display','block'); jQuery(thisC).css({ float: 'left', clear: 'left' }); // To animate the height, we must give it a static value. // To do this, we put the expanded content into a hidden <div> // and we mesure its height. jQuery("#ghost").html(jQuery(thisC).clone()); jQuery("#ghost").css({ width: expSection, overflow: 'hidden' }); jQuery("#ghost").children('.classDiv_t').css({ width: '100%', height: '100%' }); var expHeight = jQuery("#ghost").height()+90; // Althought not nice, we add +90px of height inherited from the header // Finally, and just in case, we empty the hidden <div> jQuery("#ghost").html(""); // Set the height of the section, but also, adapt the height // of the parent, since it hosts an absolute-position child var extraHeight = 1.015; // The parent container should be 1% higher var minSectionsHeight = minHeight * nSec * 1.07; // 642px = ( height*sections )*1.07 >> ~7% of margin for each section if ( (expHeight*extraHeight) > minSectionsHeight ) { jQuery('#infoContent').css('height',expHeight*extraHeight); } else { jQuery('#infoContent').css('height','auto'); } jQuery(thisC).animate({ width: expSection, height: expHeight }); // As said before, convert the section into an absolute-position // child, so we can place it to the top of the parent-div jQuery(thisC).css({ position: 'absolute', top: '0px', left: '0px' }); } else { // Uncheck all the checkboxes jQuery('input[id^="btnControl_t"]').each(function () { objChecks[this.id] = false; jQuery(this).prop('checked', false); }); // Check the current checkbox objChecks[thisC.id] = true; jQuery(chkbx_id).prop('checked', true); // Apply the reduced-style for the rest of sections jQuery('div[id^="idDiv_t"]').each(function () { jQuery(this).css({ width: '120px', height: '120px', float: 'none', clear: 'both', position: 'relative', display: 'inline-block' }); jQuery(this).children('.classDiv_tContent').css('display','none'); }); // Clear the ghost-section and create a structure inside; equivalent to the current section jQuery("#ghost").html(""); //var section = thisC.id.substr(7); // Consider that id = 'idDiv_t...' var input = '<input type="checkbox" id="btnControl_tGhost">'; var label = '<label id="ghostLabel" class="btn" for="btnControl_tGhost"></label>'; jQuery("#ghost").append(input); jQuery("#ghost").append(label); // Clone the content of the section jQuery(thisC).clone().attr('id','idDiv_tGhost').appendTo(jQuery("#ghostLabel")); // Clone the styles: background color, header (background color and/or image) //jQuery('#idDiv_tGhost').css('background-color',jQuery(this).css('background-color')); jQuery('#idDiv_tGhost').children('.classDiv_sHeader').css('background',jQuery(thisC).children('.classDiv_sHeader').css('background')); jQuery('#idDiv_tGhost').children('.classDiv_sHeader').css('background-image',jQuery(thisC).children('.classDiv_sHeader').css('background-image')); // Set the created checkbox as true jQuery("#btnControl_tGhost").prop('checked', true); // Like the other checkboxes, avoid the normal performance. 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