Afficher la notice abrégée

Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils

dc.rights.licenseopenen_US
dc.contributor.authorSHARMA, Kartikay
dc.contributor.authorSTOCKERT, Fabian
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorSHENOY, Jayakrishna
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorABDUL-SHUKKOOR, Muhammed Bilal
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorSCHMIDT, Matthias
dc.contributor.authorFANDRICH, Marcus
dc.date.accessioned2025-01-20T15:22:53Z
dc.date.available2025-01-20T15:22:53Z
dc.date.issued2024-01-12
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/204415
dc.description.abstractEnThe transactive response DNA-binding protein-43 (TDP-43) is a multi-facet protein involved in phase separation, RNA-binding, and alternative splicing. In the context of neurodegenerative diseases, abnormal aggregation of TDP-43 has been linked to amyotrophic lateral sclerosis and frontotemporal lobar degeneration through the aggregation of its C-terminal domain. Here, we report a cryo-electron microscopy (cryo-EM)-based structural characterization of TDP-43 fibrils obtained from the full-length protein. We find that the fibrils are polymorphic and contain three different amyloid structures. The structures differ in the number and relative orientation of the protofilaments, although they share a similar fold containing an amyloid key motif. The observed fibril structures differ from previously described conformations of TDP-43 fibrils and help to better understand the structural landscape of the amyloid fibril structures derived from this protein.
dc.language.isoENen_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.title.enCryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s41467-023-44489-0en_US
dc.subject.halChimie/Matériauxen_US
dc.identifier.pubmed38212334en_US
bordeaux.journalNature Communicationsen_US
bordeaux.page486en_US
bordeaux.volume15en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue1en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDHorizon 2020en_US
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Communications&rft.date=2024-01-12&rft.volume=15&rft.issue=1&rft.spage=486&rft.epage=486&rft.au=SHARMA,%20Kartikay&STOCKERT,%20Fabian&SHENOY,%20Jayakrishna&BERBON,%20Melanie&ABDUL-SHUKKOOR,%20Muhammed%20Bilal&rft.genre=article


Fichier(s) constituant ce document

Thumbnail
Nom:
CBMN_NatComm_2024_Sharma.pdf
Taille:
2.424Mo
Format:
PDF
Voir/Ouvrir
Thumbnail
Nom:
license_rdf
Taille:
811octets
Format:
application/rdf+xml
Voir/Ouvrir

Ce document figure dans la(les) collection(s) suivante(s)

Afficher la notice abrégée