Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

Molecular chaperones are recognized to interfere with protein aggregation, yet the underlying mechanisms are largely unknown. Here, the authors develop a kinetic model that reveals the variety of distinct microscopic mechanisms through which molecular chaperones act to suppress amyloid formation.

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Autores principales:	Paolo Arosio, Thomas C. T. Michaels, Sara Linse, Cecilia Månsson, Cecilia Emanuelsson, Jenny Presto, Jan Johansson, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c5964ef9df1642ba92713454e4688a63
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spelling	oai:doaj.org-article:c5964ef9df1642ba92713454e4688a632021-12-02T14:39:53ZKinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation10.1038/ncomms109482041-1723https://doaj.org/article/c5964ef9df1642ba92713454e4688a632016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms10948https://doaj.org/toc/2041-1723Molecular chaperones are recognized to interfere with protein aggregation, yet the underlying mechanisms are largely unknown. Here, the authors develop a kinetic model that reveals the variety of distinct microscopic mechanisms through which molecular chaperones act to suppress amyloid formation.Paolo ArosioThomas C. T. MichaelsSara LinseCecilia MånssonCecilia EmanuelssonJenny PrestoJan JohanssonMichele VendruscoloChristopher M. DobsonTuomas P. J. KnowlesNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Paolo Arosio Thomas C. T. Michaels Sara Linse Cecilia Månsson Cecilia Emanuelsson Jenny Presto Jan Johansson Michele Vendruscolo Christopher M. Dobson Tuomas P. J. Knowles Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
description	Molecular chaperones are recognized to interfere with protein aggregation, yet the underlying mechanisms are largely unknown. Here, the authors develop a kinetic model that reveals the variety of distinct microscopic mechanisms through which molecular chaperones act to suppress amyloid formation.
format	article
author	Paolo Arosio Thomas C. T. Michaels Sara Linse Cecilia Månsson Cecilia Emanuelsson Jenny Presto Jan Johansson Michele Vendruscolo Christopher M. Dobson Tuomas P. J. Knowles
author_facet	Paolo Arosio Thomas C. T. Michaels Sara Linse Cecilia Månsson Cecilia Emanuelsson Jenny Presto Jan Johansson Michele Vendruscolo Christopher M. Dobson Tuomas P. J. Knowles
author_sort	Paolo Arosio
title	Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
title_short	Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
title_full	Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
title_fullStr	Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
title_full_unstemmed	Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
title_sort	kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/c5964ef9df1642ba92713454e4688a63
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_version_	1718390501346902016

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

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