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.

Bibliographic Details
Main Authors:	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
Format:	Article
Language:	English
Published:	Nature Publishing Group 2016-03-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/ncomms10948

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spelling	doaj-c5964ef9df1642ba92713454e4688a632021-05-11T11:05:58ZengNature Publishing GroupNature Communications2041-17232016-03-01711910.1038/ncomms10948Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formationPaolo Arosio0Thomas C. T. Michaels1Sara Linse2Cecilia Månsson3Cecilia Emanuelsson4Jenny Presto5Jan Johansson6Michele Vendruscolo7Christopher M. Dobson8Tuomas P. J. Knowles9Department of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeDepartment of Biochemistry and Structural Biology, Lund UniversityDepartment of Biochemistry and Structural Biology, Lund UniversityDepartment of Biochemistry and Structural Biology, Lund UniversityDivision for Neurogeriatrics, Department of Neurobiology, Center for Alzheimer Research, Care Sciences and Society, Karolinska InstitutetDivision for Neurogeriatrics, Department of Neurobiology, Center for Alzheimer Research, Care Sciences and Society, Karolinska InstitutetDepartment of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeMolecular 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.https://doi.org/10.1038/ncomms10948
collection	DOAJ
language	English
format	Article
sources	DOAJ
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
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2016-03-01
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.
url	https://doi.org/10.1038/ncomms10948
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Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

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