Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program

Author summary TDP-43 aggregation is linked to various diseases including amyotrophic lateral sclerosis. Here the authors show that acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism tha...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Ping Wang, Connor M. Wander, Chao-Xing Yuan, Michael S. Bereman, Todd J. Cohen
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
Materias:
Q
Acceso en línea:https://doaj.org/article/46fad8dc2b444576bc81981652f2f6f9
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:46fad8dc2b444576bc81981652f2f6f9
record_format dspace
spelling oai:doaj.org-article:46fad8dc2b444576bc81981652f2f6f92021-12-02T13:57:44ZAcetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program10.1038/s41467-017-00088-42041-1723https://doaj.org/article/46fad8dc2b444576bc81981652f2f6f92017-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00088-4https://doaj.org/toc/2041-1723Author summary TDP-43 aggregation is linked to various diseases including amyotrophic lateral sclerosis. Here the authors show that acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein.Ping WangConnor M. WanderChao-Xing YuanMichael S. BeremanTodd J. CohenNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ping Wang
Connor M. Wander
Chao-Xing Yuan
Michael S. Bereman
Todd J. Cohen
Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
description Author summary TDP-43 aggregation is linked to various diseases including amyotrophic lateral sclerosis. Here the authors show that acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein.
format article
author Ping Wang
Connor M. Wander
Chao-Xing Yuan
Michael S. Bereman
Todd J. Cohen
author_facet Ping Wang
Connor M. Wander
Chao-Xing Yuan
Michael S. Bereman
Todd J. Cohen
author_sort Ping Wang
title Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
title_short Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
title_full Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
title_fullStr Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
title_full_unstemmed Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
title_sort acetylation-induced tdp-43 pathology is suppressed by an hsf1-dependent chaperone program
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/46fad8dc2b444576bc81981652f2f6f9
work_keys_str_mv AT pingwang acetylationinducedtdp43pathologyissuppressedbyanhsf1dependentchaperoneprogram
AT connormwander acetylationinducedtdp43pathologyissuppressedbyanhsf1dependentchaperoneprogram
AT chaoxingyuan acetylationinducedtdp43pathologyissuppressedbyanhsf1dependentchaperoneprogram
AT michaelsbereman acetylationinducedtdp43pathologyissuppressedbyanhsf1dependentchaperoneprogram
AT toddjcohen acetylationinducedtdp43pathologyissuppressedbyanhsf1dependentchaperoneprogram
_version_ 1718392256822509568