Structural basis of synaptic vesicle assembly promoted by α-synuclein

α-synuclein, a protein associated to Parkinson's disease, is involved in synaptic vesicle interaction and assembly. Here, the authors use NMR spectroscopy and super-resolution microscopy to unveil the nature and molecular mechanism of α-synuclein-mediated synaptic vesicle clustering.

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Autores principales:	Giuliana Fusco, Tillmann Pape, Amberley D. Stephens, Pierre Mahou, Ana Rita Costa, Clemens F. Kaminski, Gabriele S. Kaminski Schierle, Michele Vendruscolo, Gianluigi Veglia, Christopher M. Dobson, Alfonso De Simone
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b6df8c3334454adeab13d8b8305bc6e2
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spelling	oai:doaj.org-article:b6df8c3334454adeab13d8b8305bc6e22021-12-02T17:31:18ZStructural basis of synaptic vesicle assembly promoted by α-synuclein10.1038/ncomms125632041-1723https://doaj.org/article/b6df8c3334454adeab13d8b8305bc6e22016-09-01T00:00:00Zhttps://doi.org/10.1038/ncomms12563https://doaj.org/toc/2041-1723α-synuclein, a protein associated to Parkinson's disease, is involved in synaptic vesicle interaction and assembly. Here, the authors use NMR spectroscopy and super-resolution microscopy to unveil the nature and molecular mechanism of α-synuclein-mediated synaptic vesicle clustering.Giuliana FuscoTillmann PapeAmberley D. StephensPierre MahouAna Rita CostaClemens F. KaminskiGabriele S. Kaminski SchierleMichele VendruscoloGianluigi VegliaChristopher M. DobsonAlfonso De SimoneNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Giuliana Fusco Tillmann Pape Amberley D. Stephens Pierre Mahou Ana Rita Costa Clemens F. Kaminski Gabriele S. Kaminski Schierle Michele Vendruscolo Gianluigi Veglia Christopher M. Dobson Alfonso De Simone Structural basis of synaptic vesicle assembly promoted by α-synuclein
description	α-synuclein, a protein associated to Parkinson's disease, is involved in synaptic vesicle interaction and assembly. Here, the authors use NMR spectroscopy and super-resolution microscopy to unveil the nature and molecular mechanism of α-synuclein-mediated synaptic vesicle clustering.
format	article
author	Giuliana Fusco Tillmann Pape Amberley D. Stephens Pierre Mahou Ana Rita Costa Clemens F. Kaminski Gabriele S. Kaminski Schierle Michele Vendruscolo Gianluigi Veglia Christopher M. Dobson Alfonso De Simone
author_facet	Giuliana Fusco Tillmann Pape Amberley D. Stephens Pierre Mahou Ana Rita Costa Clemens F. Kaminski Gabriele S. Kaminski Schierle Michele Vendruscolo Gianluigi Veglia Christopher M. Dobson Alfonso De Simone
author_sort	Giuliana Fusco
title	Structural basis of synaptic vesicle assembly promoted by α-synuclein
title_short	Structural basis of synaptic vesicle assembly promoted by α-synuclein
title_full	Structural basis of synaptic vesicle assembly promoted by α-synuclein
title_fullStr	Structural basis of synaptic vesicle assembly promoted by α-synuclein
title_full_unstemmed	Structural basis of synaptic vesicle assembly promoted by α-synuclein
title_sort	structural basis of synaptic vesicle assembly promoted by α-synuclein
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/b6df8c3334454adeab13d8b8305bc6e2
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_version_	1718380694771597312

Structural basis of synaptic vesicle assembly promoted by α-synuclein

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