Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/6362
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dc.contributor.authorEschmann, Neil A.-
dc.contributor.authorGeorgieva, Elka R.-
dc.contributor.authorGanguly, Pritam-
dc.contributor.authorBorbat, Peter P.-
dc.contributor.authorRappaport, Maxime D.-
dc.contributor.authorAkdoğan, Yaşar-
dc.contributor.authorFreed, Jack H.-
dc.contributor.authorShea, Joan-Emma-
dc.contributor.authorHan, Songi-
dc.date.accessioned2017-10-16T11:27:22Z
dc.date.available2017-10-16T11:27:22Z
dc.date.issued2017-03
dc.identifier.citationEschmann, N. A., Georgieva, E. R., Ganguly, P., Borbat, P. P., Rappaport, M. D., Akdoğan, Y., Freed, J. H., Shea, J.-E., and Han, S. (2017). Signature of an aggregation-prone conformation of tau. Scientific Reports, 7. doi:10.1038/srep44739en_US
dc.identifier.issn2045-2322
dc.identifier.issn2045-2322-
dc.identifier.urihttp://doi.org/10.1038/srep44739
dc.identifier.urihttp://hdl.handle.net/11147/6362
dc.description.abstractThe self-assembly of the microtubule associated tau protein into fibrillar cell inclusions is linked to a number of devastating neurodegenerative disorders collectively known as tauopathies. The mechanism by which tau self-assembles into pathological entities is a matter of much debate, largely due to the lack of direct experimental insights into the earliest stages of aggregation. We present pulsed double electron-electron resonance measurements of two key fibril-forming regions of tau, PHF6 and PHF6∗, in transient as aggregation happens. By monitoring the end-to-end distance distribution of these segments as a function of aggregation time, we show that the PHF6 (∗) regions dramatically extend to distances commensurate with extended β-strand structures within the earliest stages of aggregation, well before fibril formation. Combined with simulations, our experiments show that the extended β-strand conformational state of PHF6 (∗) is readily populated under aggregating conditions, constituting a defining signature of aggregation-prone tau, and as such, a possible target for therapeutic interventions.en_US
dc.description.sponsorshipNIH (S10 RR028992); NIH Innovator award; NIH/NIGMS (R21EB022731-- P41-GM103521), NSF (MCB 1158577); NSF MRSEC Program (DMR 1121053); Center for Scientific Computing at the UCSB CNSI (CNS-0960316); Extreme Science and Engineering Discovery Environment-XSEDE - NSF (TG-MCA05S027--ACI-1053575); University of California; Santa Barbara; University of California, Office of the Presidenten_US
dc.language.isoenen_US
dc.publisherNature Publishing Groupen_US
dc.relation.ispartofScientific Reportsen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectTau proteinen_US
dc.subjectIntrinsically disordered proteinen_US
dc.subjectNeurofibrillary tanglesen_US
dc.subjectAggregationen_US
dc.titleSignature of an aggregation-prone conformation of tauen_US
dc.typeArticleen_US
dc.authoridTR180857en_US
dc.institutionauthorAkdoğan, Yaşar-
dc.departmentİzmir Institute of Technology. Materials Science and Engineeringen_US
dc.identifier.volume7en_US
dc.identifier.wosWOS:000396647000001en_US
dc.identifier.scopus2-s2.0-85015721684en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1038/srep44739-
dc.identifier.pmid28303942en_US
dc.relation.doi10.1038/srep44739en_US
dc.coverage.doi10.1038/srep44739en_US
dc.identifier.wosqualityQ1-
dc.identifier.scopusqualityQ1-
dc.identifier.wosqualityttpTop10%en_US
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextopen-
crisitem.author.dept03.09. Department of Materials Science and Engineering-
Appears in Collections:Materials Science and Engineering / Malzeme Bilimi ve Mühendisliği
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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