Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts

Parkinson’s disease (PD) and Multiple System Atrophy (MSA) are characterized by the pathological accumulation of α-synuclein. Here the authors employ fluorescent probes, electron microscopy and NMR spectroscopy to study the properties of α-synuclein aggregates that were amplified from patient brain...

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Autores principales:	Timo Strohäker, Byung Chul Jung, Shu-Hao Liou, Claudio O. Fernandez, Dietmar Riedel, Stefan Becker, Glenda M. Halliday, Marina Bennati, Woojin S. Kim, Seung-Jae Lee, Markus Zweckstetter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/645030a3102e4d44bda780706743ff0d
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spelling	oai:doaj.org-article:645030a3102e4d44bda780706743ff0d2021-12-02T16:57:43ZStructural heterogeneity of α-synuclein fibrils amplified from patient brain extracts10.1038/s41467-019-13564-w2041-1723https://doaj.org/article/645030a3102e4d44bda780706743ff0d2019-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13564-whttps://doaj.org/toc/2041-1723Parkinson’s disease (PD) and Multiple System Atrophy (MSA) are characterized by the pathological accumulation of α-synuclein. Here the authors employ fluorescent probes, electron microscopy and NMR spectroscopy to study the properties of α-synuclein aggregates that were amplified from patient brain extracts and observe a greater structural diversity among PD patients compared to MSA patients.Timo StrohäkerByung Chul JungShu-Hao LiouClaudio O. FernandezDietmar RiedelStefan BeckerGlenda M. HallidayMarina BennatiWoojin S. KimSeung-Jae LeeMarkus ZweckstetterNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Timo Strohäker Byung Chul Jung Shu-Hao Liou Claudio O. Fernandez Dietmar Riedel Stefan Becker Glenda M. Halliday Marina Bennati Woojin S. Kim Seung-Jae Lee Markus Zweckstetter Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
description	Parkinson’s disease (PD) and Multiple System Atrophy (MSA) are characterized by the pathological accumulation of α-synuclein. Here the authors employ fluorescent probes, electron microscopy and NMR spectroscopy to study the properties of α-synuclein aggregates that were amplified from patient brain extracts and observe a greater structural diversity among PD patients compared to MSA patients.
format	article
author	Timo Strohäker Byung Chul Jung Shu-Hao Liou Claudio O. Fernandez Dietmar Riedel Stefan Becker Glenda M. Halliday Marina Bennati Woojin S. Kim Seung-Jae Lee Markus Zweckstetter
author_facet	Timo Strohäker Byung Chul Jung Shu-Hao Liou Claudio O. Fernandez Dietmar Riedel Stefan Becker Glenda M. Halliday Marina Bennati Woojin S. Kim Seung-Jae Lee Markus Zweckstetter
author_sort	Timo Strohäker
title	Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
title_short	Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
title_full	Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
title_fullStr	Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
title_full_unstemmed	Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
title_sort	structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/645030a3102e4d44bda780706743ff0d
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Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts

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