A molecular mechanism for transthyretin amyloidogenesis

A number of disease-causing human transthyretin (TTR) mutations are known to lead to amyloid formation. Here the authors combine neutron crystallography, native mass spectrometry and modelling studies to characterize the T119M and S52P-TTR mutants, providing mechanistic insights into TTR amyloidosis...

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Autores principales:	Ai Woon Yee, Matteo Aldeghi, Matthew P. Blakeley, Andreas Ostermann, Philippe J. Mas, Martine Moulin, Daniele de Sanctis, Matthew W. Bowler, Christoph Mueller-Dieckmann, Edward P. Mitchell, Michael Haertlein, Bert L. de Groot, Elisabetta Boeri Erba, V. Trevor Forsyth
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d3204d9671444e838d043f4321cfd3bb
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spelling	oai:doaj.org-article:d3204d9671444e838d043f4321cfd3bb2021-12-02T16:58:07ZA molecular mechanism for transthyretin amyloidogenesis10.1038/s41467-019-08609-z2041-1723https://doaj.org/article/d3204d9671444e838d043f4321cfd3bb2019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08609-zhttps://doaj.org/toc/2041-1723A number of disease-causing human transthyretin (TTR) mutations are known to lead to amyloid formation. Here the authors combine neutron crystallography, native mass spectrometry and modelling studies to characterize the T119M and S52P-TTR mutants, providing mechanistic insights into TTR amyloidosis.Ai Woon YeeMatteo AldeghiMatthew P. BlakeleyAndreas OstermannPhilippe J. MasMartine MoulinDaniele de SanctisMatthew W. BowlerChristoph Mueller-DieckmannEdward P. MitchellMichael HaertleinBert L. de GrootElisabetta Boeri ErbaV. Trevor ForsythNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ai Woon Yee Matteo Aldeghi Matthew P. Blakeley Andreas Ostermann Philippe J. Mas Martine Moulin Daniele de Sanctis Matthew W. Bowler Christoph Mueller-Dieckmann Edward P. Mitchell Michael Haertlein Bert L. de Groot Elisabetta Boeri Erba V. Trevor Forsyth A molecular mechanism for transthyretin amyloidogenesis
description	A number of disease-causing human transthyretin (TTR) mutations are known to lead to amyloid formation. Here the authors combine neutron crystallography, native mass spectrometry and modelling studies to characterize the T119M and S52P-TTR mutants, providing mechanistic insights into TTR amyloidosis.
format	article
author	Ai Woon Yee Matteo Aldeghi Matthew P. Blakeley Andreas Ostermann Philippe J. Mas Martine Moulin Daniele de Sanctis Matthew W. Bowler Christoph Mueller-Dieckmann Edward P. Mitchell Michael Haertlein Bert L. de Groot Elisabetta Boeri Erba V. Trevor Forsyth
author_facet	Ai Woon Yee Matteo Aldeghi Matthew P. Blakeley Andreas Ostermann Philippe J. Mas Martine Moulin Daniele de Sanctis Matthew W. Bowler Christoph Mueller-Dieckmann Edward P. Mitchell Michael Haertlein Bert L. de Groot Elisabetta Boeri Erba V. Trevor Forsyth
author_sort	Ai Woon Yee
title	A molecular mechanism for transthyretin amyloidogenesis
title_short	A molecular mechanism for transthyretin amyloidogenesis
title_full	A molecular mechanism for transthyretin amyloidogenesis
title_fullStr	A molecular mechanism for transthyretin amyloidogenesis
title_full_unstemmed	A molecular mechanism for transthyretin amyloidogenesis
title_sort	molecular mechanism for transthyretin amyloidogenesis
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/d3204d9671444e838d043f4321cfd3bb
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A molecular mechanism for transthyretin amyloidogenesis

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