Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS

The low-complexity (LC) domain mediates liquid-liquid phase separation and fibril formation of the RNA-binding protein FUS (FUsed in Sarcoma). Here, the authors combine cryo-EM, solid-state NMR measurements and MD simulations to structurally characterise the fibrils formed by the C-terminal half of...

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Autores principales:	Myungwoon Lee, Ujjayini Ghosh, Kent R. Thurber, Masato Kato, Robert Tycko
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8142805573524157b65818c9f357da0e
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spelling	oai:doaj.org-article:8142805573524157b65818c9f357da0e2021-12-02T17:32:27ZMolecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS10.1038/s41467-020-19512-32041-1723https://doaj.org/article/8142805573524157b65818c9f357da0e2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19512-3https://doaj.org/toc/2041-1723The low-complexity (LC) domain mediates liquid-liquid phase separation and fibril formation of the RNA-binding protein FUS (FUsed in Sarcoma). Here, the authors combine cryo-EM, solid-state NMR measurements and MD simulations to structurally characterise the fibrils formed by the C-terminal half of the FUS LC domain and discuss stabilizing interactions within the fibril core.Myungwoon LeeUjjayini GhoshKent R. ThurberMasato KatoRobert TyckoNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Myungwoon Lee Ujjayini Ghosh Kent R. Thurber Masato Kato Robert Tycko Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
description	The low-complexity (LC) domain mediates liquid-liquid phase separation and fibril formation of the RNA-binding protein FUS (FUsed in Sarcoma). Here, the authors combine cryo-EM, solid-state NMR measurements and MD simulations to structurally characterise the fibrils formed by the C-terminal half of the FUS LC domain and discuss stabilizing interactions within the fibril core.
format	article
author	Myungwoon Lee Ujjayini Ghosh Kent R. Thurber Masato Kato Robert Tycko
author_facet	Myungwoon Lee Ujjayini Ghosh Kent R. Thurber Masato Kato Robert Tycko
author_sort	Myungwoon Lee
title	Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
title_short	Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
title_full	Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
title_fullStr	Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
title_full_unstemmed	Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
title_sort	molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from fus
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/8142805573524157b65818c9f357da0e
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Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS

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