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

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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Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2019-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-13564-w
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spelling doaj-645030a3102e4d44bda780706743ff0d2021-05-11T12:08:51ZengNature Publishing GroupNature Communications2041-17232019-12-0110111210.1038/s41467-019-13564-wStructural heterogeneity of α-synuclein fibrils amplified from patient brain extractsTimo Strohäker0Byung Chul Jung1Shu-Hao Liou2Claudio O. Fernandez3Dietmar Riedel4Stefan Becker5Glenda M. Halliday6Marina Bennati7Woojin S. Kim8Seung-Jae Lee9Markus Zweckstetter10German Center for Neurodegenerative Diseases (DZNE)Department of Biomedical Sciences, Neuroscience Research Institute, College of Medicine, Seoul National UniversityRG EPR Spectroscopy, Max Planck Institute for Biophysical ChemistryMax Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario (MPLbioR, UNR-MPIbpC)Department for Electron Microscopy, Max Planck Institute for Biophysical ChemistryDepartment for NMR-based Structural Biology, Max Planck Institute for Biophysical ChemistryBrain and Mind Centre and Central Clinical School, Faculty of Medicine and Health, The University of SydneyRG EPR Spectroscopy, Max Planck Institute for Biophysical ChemistryBrain and Mind Centre and Central Clinical School, Faculty of Medicine and Health, The University of SydneyDepartment of Biomedical Sciences, Neuroscience Research Institute, College of Medicine, Seoul National UniversityGerman Center for Neurodegenerative Diseases (DZNE)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.https://doi.org/10.1038/s41467-019-13564-w
collection DOAJ
language English
format Article
sources DOAJ
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
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-12-01
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.
url https://doi.org/10.1038/s41467-019-13564-w
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