Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding

The calcium binding protein S100B is an abundantly expressed protein in the brain and has neuro-protective functions by inhibiting Aβ aggregation and metal ion toxicity. Here, the authors combine cell biology and biochemical experiments with chemical kinetics and NMR measurements and show that S100B...

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Autores principales:	Guilherme G. Moreira, François-Xavier Cantrelle, Andrea Quezada, Filipa S. Carvalho, Joana S. Cristóvão, Urmi Sengupta, Nicha Puangmalai, Ana P. Carapeto, Mário S. Rodrigues, Isabel Cardoso, Güenter Fritz, Federico Herrera, Rakez Kayed, Isabelle Landrieu, Cláudio M. Gomes
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c84f299d39b043bfadec87ae6bbc7bf3
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spelling	oai:doaj.org-article:c84f299d39b043bfadec87ae6bbc7bf32021-11-08T11:07:22ZDynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding10.1038/s41467-021-26584-22041-1723https://doaj.org/article/c84f299d39b043bfadec87ae6bbc7bf32021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26584-2https://doaj.org/toc/2041-1723The calcium binding protein S100B is an abundantly expressed protein in the brain and has neuro-protective functions by inhibiting Aβ aggregation and metal ion toxicity. Here, the authors combine cell biology and biochemical experiments with chemical kinetics and NMR measurements and show that S100B protein is an extracellular Tau chaperone and further characterize the interactions between S100B and Tau.Guilherme G. MoreiraFrançois-Xavier CantrelleAndrea QuezadaFilipa S. CarvalhoJoana S. CristóvãoUrmi SenguptaNicha PuangmalaiAna P. CarapetoMário S. RodriguesIsabel CardosoGüenter FritzFederico HerreraRakez KayedIsabelle LandrieuCláudio M. GomesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Guilherme G. Moreira François-Xavier Cantrelle Andrea Quezada Filipa S. Carvalho Joana S. Cristóvão Urmi Sengupta Nicha Puangmalai Ana P. Carapeto Mário S. Rodrigues Isabel Cardoso Güenter Fritz Federico Herrera Rakez Kayed Isabelle Landrieu Cláudio M. Gomes Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
description	The calcium binding protein S100B is an abundantly expressed protein in the brain and has neuro-protective functions by inhibiting Aβ aggregation and metal ion toxicity. Here, the authors combine cell biology and biochemical experiments with chemical kinetics and NMR measurements and show that S100B protein is an extracellular Tau chaperone and further characterize the interactions between S100B and Tau.
format	article
author	Guilherme G. Moreira François-Xavier Cantrelle Andrea Quezada Filipa S. Carvalho Joana S. Cristóvão Urmi Sengupta Nicha Puangmalai Ana P. Carapeto Mário S. Rodrigues Isabel Cardoso Güenter Fritz Federico Herrera Rakez Kayed Isabelle Landrieu Cláudio M. Gomes
author_facet	Guilherme G. Moreira François-Xavier Cantrelle Andrea Quezada Filipa S. Carvalho Joana S. Cristóvão Urmi Sengupta Nicha Puangmalai Ana P. Carapeto Mário S. Rodrigues Isabel Cardoso Güenter Fritz Federico Herrera Rakez Kayed Isabelle Landrieu Cláudio M. Gomes
author_sort	Guilherme G. Moreira
title	Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
title_short	Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
title_full	Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
title_fullStr	Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
title_full_unstemmed	Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
title_sort	dynamic interactions and ca2+-binding modulate the holdase-type chaperone activity of s100b preventing tau aggregation and seeding
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c84f299d39b043bfadec87ae6bbc7bf3
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Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding

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