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The hot sites of alpha-synuclein in amyloid fibril formation
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The role of alpha-synuclein (alpha S) amyloid fibrillation has been recognized in various neurological diseases including Parkinson's Disease (PD). In early stages, fibrillation occurs by the structural transition from helix to extended states in monomeric alpha S followed by the formation of beta-sheets. This alpha-helix to beta-sheet transition (alpha beta T) speeds up the formation of amyloid fibrils through the formation of unstable and temporary configurations of the alpha S. In this study, the most important regions that act as initiating nuclei and make unstable the initial configuration were identified based on sequence and structural information. In this regard, a Targeted Molecular Dynamics (TMD) simulation was employed using explicit solvent models under physiological conditions. Identified regions are those that are in the early steps of structural opening. The trajectory was clustered the structures characterized the intermediate states. The findings of this study would help us to better understanding of the mechanism of amyloid fibril formation.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Khammari, Anahita </span> <span class="author-type"> </span> ; <span class="author-name" > Arab, Seyed Shahriar ✉ </span> <span class="author-type"> </span> ; <span class="author-name" > Ejtehadi, Mohammad Reza ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;31553379" mtid="31553379" target="_blank">The hot sites of alpha-synuclein in amyloid fibril formation</a></div> <div class="pub-info"> <span class="journal-title">SCIENTIFIC REPORTS</span> <span class="journal-volume">10</span> : <span class="journal-issue">1</span> <span class="page"> Paper: 12175 , 14 p. </span> <span class="year">(2020)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1038/s41598-020-68887-2" target="_blank" href="https://doi.org/10.1038/s41598-020-68887-2"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000556401400002" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000556401400002"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85088386488" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85088386488"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="32699326" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=32699326&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:31553379 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" >Khammari Anahita </span> ; <span class="author-name" >Arab Seyed Shahriar ✉ </span> ; <span class="author-name" >Ejtehadi Mohammad Reza ✉ </span> </div> </div> <div class="title"><a href="/gui2/?mode=browse¶ms=publication;31553379" target="_blank">The hot sites of alpha-synuclein in amyloid fibril formation</a></div> <div> <span class="journal-title">SCIENTIFIC REPORTS</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/2045-2322">2045-2322</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/2045-2322">2045-2322</a>)</span>: <span class="journal-volume">10</span> <span class="journal-issue">1</span> <span class="page"> Paper 12175. 14 p. </span> <span class="year">(2020)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1038/s41598-020-68887-2" target="_blank" href="https://doi.org/10.1038/s41598-020-68887-2"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000556401400002" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000556401400002"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85088386488" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85088386488"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="32699326" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=32699326&dopt=Abstract"> PubMed </a> </span> </span> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;31553379&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 1 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 31553379</span> | <span class="status-data status-APPROVED"> Nyilvános </span> Idéző | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">WoS-XML</span> </div> <div class="lastModified">Utolsó módosítás: 2024.02.27. 14:28 Pécsi Éva (MTMT Közp 3, admin) </div> </div></div>