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Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein : Quaternary structure of patient-homogenate amplified alpha-synuclein fibrils modulates seeding of endogenous alpha-synuclein
DC Field | Value | Language |
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dc.contributor.author | Frieg, Benedikt | - |
dc.contributor.author | Geraets, James A. | - |
dc.contributor.author | Strohaeker, Timo | - |
dc.contributor.author | Dienemann, Christian | - |
dc.contributor.author | Mavroeidi, Panagiota | - |
dc.contributor.author | Jung, Byung Chul | - |
dc.contributor.author | Kim, Woojin S. | - |
dc.contributor.author | Lee, Seung-Jae | - |
dc.contributor.author | Xilouri, Maria | - |
dc.contributor.author | Zweckstetter, Markus | - |
dc.contributor.author | Schroeder, Gunnar F. | - |
dc.date.accessioned | 2022-11-23T00:38:52Z | - |
dc.date.available | 2022-11-23T00:38:52Z | - |
dc.date.created | 2022-10-18 | - |
dc.date.issued | 2022-09 | - |
dc.identifier.citation | Communications Biology, Vol.5 No.1, p. 1040 | - |
dc.identifier.issn | 2399-3642 | - |
dc.identifier.uri | https://hdl.handle.net/10371/187197 | - |
dc.description.abstract | Parkinson's disease (PD) and Multiple System Atrophy (MSA) are progressive and unremitting neurological diseases that are neuropathologically characterized by alpha-synuclein inclusions. Increasing evidence supports the aggregation of alpha-synuclein in specific brain areas early in the disease course, followed by the spreading of alpha-synuclein pathology to multiple brain regions. However, little is known about how the structure of alpha-synuclein fibrils influence its ability to seed endogenous alpha-synuclein in recipient cells. Here, we aggregated alpha-synuclein by seeding with homogenates of PD- and MSA-confirmed brain tissue, determined the resulting alpha-synuclein fibril structures by cryo-electron microscopy, and characterized their seeding potential in mouse primary oligodendroglial cultures. The combined analysis shows that the two patient material-amplified alpha-synuclein fibrils share a similar protofilament fold but differ in their inter-protofilament interface and their ability to recruit endogenous alpha-synuclein. Our study indicates that the quaternary structure of alpha-synuclein fibrils modulates the seeding of alpha-synuclein pathology inside recipient cells. It thus provides an important advance in the quest to understand the connection between the structure of alpha-synuclein fibrils, cellular seeding/spreading, and ultimately the clinical manifestations of different synucleinopathies. Quaternary structure of alpha-synuclein fibrils characterized from human patients with Parkinson's disease and Multiple System Atrophy modulates seeding in mouse primary oligodendroglial cultures. | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein | - |
dc.title.alternative | Quaternary structure of patient-homogenate amplified alpha-synuclein fibrils modulates seeding of endogenous alpha-synuclein | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/s42003-022-03948-y | - |
dc.citation.journaltitle | Communications Biology | - |
dc.identifier.wosid | 000862402500005 | - |
dc.identifier.scopusid | 2-s2.0-85139180248 | - |
dc.citation.number | 1 | - |
dc.citation.startpage | 1040 | - |
dc.citation.volume | 5 | - |
dc.description.isOpenAccess | N | - |
dc.contributor.affiliatedAuthor | Lee, Seung-Jae | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
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