Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein

To better understand the specific cascade of protein interactions that lead to the pathological aggregation of α-synuclein (wild-type and mutant forms), Leitão et al. present a method to measure interactions of monomeric, oligomeric, and fibrillar forms of α-syn with 65 proteins that were previously...

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Autores principales:	André D. G. Leitão, Paulina Rudolffi-Soto, Alexandre Chappard, Akshay Bhumkar, Derrick Lau, Dominic J. B. Hunter, Yann Gambin, Emma Sierecki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/aca601966a214f07a960669aebb2ca79
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spelling	oai:doaj.org-article:aca601966a214f07a960669aebb2ca792021-12-02T18:48:42ZSelectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein10.1038/s42003-021-02624-x2399-3642https://doaj.org/article/aca601966a214f07a960669aebb2ca792021-09-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02624-xhttps://doaj.org/toc/2399-3642To better understand the specific cascade of protein interactions that lead to the pathological aggregation of α-synuclein (wild-type and mutant forms), Leitão et al. present a method to measure interactions of monomeric, oligomeric, and fibrillar forms of α-syn with 65 proteins that were previously shown to be components of Lewy bodies. This approach is useful to understand the sequence of protein-binding events that lead to α-syn aggregation.André D. G. LeitãoPaulina Rudolffi-SotoAlexandre ChappardAkshay BhumkarDerrick LauDominic J. B. HunterYann GambinEmma SiereckiNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 André D. G. Leitão Paulina Rudolffi-Soto Alexandre Chappard Akshay Bhumkar Derrick Lau Dominic J. B. Hunter Yann Gambin Emma Sierecki Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein
description	To better understand the specific cascade of protein interactions that lead to the pathological aggregation of α-synuclein (wild-type and mutant forms), Leitão et al. present a method to measure interactions of monomeric, oligomeric, and fibrillar forms of α-syn with 65 proteins that were previously shown to be components of Lewy bodies. This approach is useful to understand the sequence of protein-binding events that lead to α-syn aggregation.
format	article
author	André D. G. Leitão Paulina Rudolffi-Soto Alexandre Chappard Akshay Bhumkar Derrick Lau Dominic J. B. Hunter Yann Gambin Emma Sierecki
author_facet	André D. G. Leitão Paulina Rudolffi-Soto Alexandre Chappard Akshay Bhumkar Derrick Lau Dominic J. B. Hunter Yann Gambin Emma Sierecki
author_sort	André D. G. Leitão
title	Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein
title_short	Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein
title_full	Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein
title_fullStr	Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein
title_full_unstemmed	Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein
title_sort	selectivity of lewy body protein interactions along the aggregation pathway of α-synuclein
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/aca601966a214f07a960669aebb2ca79
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Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein

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