Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent exposed the N-terminus of aSyn is, the more aggregation pron...

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Autores principales:	Amberley D. Stephens, Maria Zacharopoulou, Rani Moons, Giuliana Fusco, Neeleema Seetaloo, Anass Chiki, Philippa J. Woodhams, Ioanna Mela, Hilal A. Lashuel, Jonathan J. Phillips, Alfonso De Simone, Frank Sobott, Gabriele S. Kaminski Schierle
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/06df908e29ff4c6a9479ca48a333babb
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spelling	oai:doaj.org-article:06df908e29ff4c6a9479ca48a333babb2021-12-02T17:51:04ZExtent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity10.1038/s41467-020-16564-32041-1723https://doaj.org/article/06df908e29ff4c6a9479ca48a333babb2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16564-3https://doaj.org/toc/2041-1723In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent exposed the N-terminus of aSyn is, the more aggregation prone its conformation becomes, and further show how PD mutations and post translational modifications influence the extent of the N-terminus solvent exposure.Amberley D. StephensMaria ZacharopoulouRani MoonsGiuliana FuscoNeeleema SeetalooAnass ChikiPhilippa J. WoodhamsIoanna MelaHilal A. LashuelJonathan J. PhillipsAlfonso De SimoneFrank SobottGabriele S. Kaminski SchierleNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Amberley D. Stephens Maria Zacharopoulou Rani Moons Giuliana Fusco Neeleema Seetaloo Anass Chiki Philippa J. Woodhams Ioanna Mela Hilal A. Lashuel Jonathan J. Phillips Alfonso De Simone Frank Sobott Gabriele S. Kaminski Schierle Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
description	In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent exposed the N-terminus of aSyn is, the more aggregation prone its conformation becomes, and further show how PD mutations and post translational modifications influence the extent of the N-terminus solvent exposure.
format	article
author	Amberley D. Stephens Maria Zacharopoulou Rani Moons Giuliana Fusco Neeleema Seetaloo Anass Chiki Philippa J. Woodhams Ioanna Mela Hilal A. Lashuel Jonathan J. Phillips Alfonso De Simone Frank Sobott Gabriele S. Kaminski Schierle
author_facet	Amberley D. Stephens Maria Zacharopoulou Rani Moons Giuliana Fusco Neeleema Seetaloo Anass Chiki Philippa J. Woodhams Ioanna Mela Hilal A. Lashuel Jonathan J. Phillips Alfonso De Simone Frank Sobott Gabriele S. Kaminski Schierle
author_sort	Amberley D. Stephens
title	Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
title_short	Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
title_full	Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
title_fullStr	Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
title_full_unstemmed	Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
title_sort	extent of n-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/06df908e29ff4c6a9479ca48a333babb
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Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

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