Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) patients have brain deposits with amyloid-like aggregates from large C-terminal fragments of the transactive response DNA-binding protein of 43 kDa (TDP-43). Here, the authors present the cryo-EM structure of amyloid fi...

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Autores principales: Qiuye Li, W. Michael Babinchak, Witold K. Surewicz
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/68d66e0dca0f4a9d85d7409936818d76
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spelling oai:doaj.org-article:68d66e0dca0f4a9d85d7409936818d762021-12-02T11:36:21ZCryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-4310.1038/s41467-021-21912-y2041-1723https://doaj.org/article/68d66e0dca0f4a9d85d7409936818d762021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21912-yhttps://doaj.org/toc/2041-1723Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) patients have brain deposits with amyloid-like aggregates from large C-terminal fragments of the transactive response DNA-binding protein of 43 kDa (TDP-43). Here, the authors present the cryo-EM structure of amyloid fibrils generated from the complete C-terminal TDP-43 low complexity domain and they discuss the effects of disease-causing mutations and phosphorylation of specific Ser residues.Qiuye LiW. Michael BabinchakWitold K. SurewiczNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Qiuye Li
W. Michael Babinchak
Witold K. Surewicz
Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
description Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) patients have brain deposits with amyloid-like aggregates from large C-terminal fragments of the transactive response DNA-binding protein of 43 kDa (TDP-43). Here, the authors present the cryo-EM structure of amyloid fibrils generated from the complete C-terminal TDP-43 low complexity domain and they discuss the effects of disease-causing mutations and phosphorylation of specific Ser residues.
format article
author Qiuye Li
W. Michael Babinchak
Witold K. Surewicz
author_facet Qiuye Li
W. Michael Babinchak
Witold K. Surewicz
author_sort Qiuye Li
title Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
title_short Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
title_full Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
title_fullStr Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
title_full_unstemmed Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
title_sort cryo-em structure of amyloid fibrils formed by the entire low complexity domain of tdp-43
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/68d66e0dca0f4a9d85d7409936818d76
work_keys_str_mv AT qiuyeli cryoemstructureofamyloidfibrilsformedbytheentirelowcomplexitydomainoftdp43
AT wmichaelbabinchak cryoemstructureofamyloidfibrilsformedbytheentirelowcomplexitydomainoftdp43
AT witoldksurewicz cryoemstructureofamyloidfibrilsformedbytheentirelowcomplexitydomainoftdp43
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