Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chaperone activities depending on its quaternary struct...

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Autores principales:	Gefei Chen, Axel Abelein, Harriet E. Nilsson, Axel Leppert, Yuniesky Andrade-Talavera, Simone Tambaro, Lovisa Hemmingsson, Firoz Roshan, Michael Landreh, Henrik Biverstål, Philip J. B. Koeck, Jenny Presto, Hans Hebert, André Fisahn, Jan Johansson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/54f4eca3feec44a6b3d1e292c044e1a5
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spelling	oai:doaj.org-article:54f4eca3feec44a6b3d1e292c044e1a52021-12-02T17:06:06ZBri2 BRICHOS client specificity and chaperone activity are governed by assembly state10.1038/s41467-017-02056-42041-1723https://doaj.org/article/54f4eca3feec44a6b3d1e292c044e1a52017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02056-4https://doaj.org/toc/2041-1723The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chaperone activities depending on its quaternary structure.Gefei ChenAxel AbeleinHarriet E. NilssonAxel LeppertYuniesky Andrade-TalaveraSimone TambaroLovisa HemmingssonFiroz RoshanMichael LandrehHenrik BiverstålPhilip J. B. KoeckJenny PrestoHans HebertAndré FisahnJan JohanssonNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Gefei Chen Axel Abelein Harriet E. Nilsson Axel Leppert Yuniesky Andrade-Talavera Simone Tambaro Lovisa Hemmingsson Firoz Roshan Michael Landreh Henrik Biverstål Philip J. B. Koeck Jenny Presto Hans Hebert André Fisahn Jan Johansson Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
description	The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chaperone activities depending on its quaternary structure.
format	article
author	Gefei Chen Axel Abelein Harriet E. Nilsson Axel Leppert Yuniesky Andrade-Talavera Simone Tambaro Lovisa Hemmingsson Firoz Roshan Michael Landreh Henrik Biverstål Philip J. B. Koeck Jenny Presto Hans Hebert André Fisahn Jan Johansson
author_facet	Gefei Chen Axel Abelein Harriet E. Nilsson Axel Leppert Yuniesky Andrade-Talavera Simone Tambaro Lovisa Hemmingsson Firoz Roshan Michael Landreh Henrik Biverstål Philip J. B. Koeck Jenny Presto Hans Hebert André Fisahn Jan Johansson
author_sort	Gefei Chen
title	Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
title_short	Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
title_full	Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
title_fullStr	Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
title_full_unstemmed	Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
title_sort	bri2 brichos client specificity and chaperone activity are governed by assembly state
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/54f4eca3feec44a6b3d1e292c044e1a5
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Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

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