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dc.contributor.author
Strohäker, Timo
dc.contributor.author
Jung, Byung Chul
dc.contributor.author
Liou, Shu Hao
dc.contributor.author
Fernandez, Claudio Oscar
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dc.contributor.author
Riedel, Dietmar
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Becker, Stefan
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Halliday, Glenda M.
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Bennati, Marina
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Kim, Woojin S.
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Lee, Seung Jae
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Zweckstetter, Markus
dc.date.available
2023-01-26T12:47:02Z
dc.date.issued
2019-12
dc.identifier.citation
Strohäker, Timo; Jung, Byung Chul; Liou, Shu Hao; Fernandez, Claudio Oscar; Riedel, Dietmar; et al.; Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts; Nature; Nature Communications; 10; 1; 12-2019; 1-12
dc.identifier.issn
2041-1723
dc.identifier.uri
http://hdl.handle.net/11336/185711
dc.description.abstract
Parkinson’s disease (PD) and Multiple System Atrophy (MSA) are clinically distinctive diseases that feature a common neuropathological hallmark of aggregated α-synuclein. Little is known about how differences in α-synuclein aggregate structure affect disease phenotype. Here, we amplified α-synuclein aggregates from PD and MSA brain extracts and analyzed the conformational properties using fluorescent probes, NMR spectroscopy and electron paramagnetic resonance. We also generated and analyzed several in vitro α-synuclein polymorphs. We found that brain-derived α-synuclein fibrils were structurally different to all of the in vitro polymorphs analyzed. Importantly, there was a greater structural heterogeneity among α-synuclein fibrils from the PD brain compared to those from the MSA brain, possibly reflecting on the greater variability of disease phenotypes evident in PD. Our findings have significant ramifications for the use of non-brain-derived α-synuclein fibrils in PD and MSA studies, and raise important questions regarding the one disease-one strain hypothesis in the study of α-synucleinopathies.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Nature
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
Structure
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brain
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MPCA
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diversity
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Neurociencias
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dc.subject.classification
Medicina Básica
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dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
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dc.title
Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-04-28T20:41:27Z
dc.journal.volume
10
dc.journal.number
1
dc.journal.pagination
1-12
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Strohäker, Timo. Max Planck Institue For Biophysical Chemistry; Alemania
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Fil: Jung, Byung Chul. Seoul National University; Japón
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Fil: Liou, Shu Hao. Max Planck Institute for Biophysical Chemistry; Alemania
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Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina
dc.description.fil
Fil: Riedel, Dietmar. Max Planck Institue For Biophysical Chemistry; Alemania
dc.description.fil
Fil: Becker, Stefan. Max Planck Institue For Biophysical Chemistry; Alemania
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Fil: Halliday, Glenda M.. University of Western Sydney; Australia
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Fil: Bennati, Marina. Max Planck Institue For Biophysical Chemistry; Alemania
dc.description.fil
Fil: Kim, Woojin S.. University of Western Sydney; Australia
dc.description.fil
Fil: Lee, Seung Jae. Max Planck Institue For Biophysical Chemistry; Alemania
dc.description.fil
Fil: Zweckstetter, Markus. Max Planck Institue For Biophysical Chemistry; Alemania
dc.journal.title
Nature Communications
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41467-019-13564-w
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1038/s41467-019-13564-w
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