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Wei Ping Gai
Researcher at Flinders University
Publications - 75
Citations - 8533
Wei Ping Gai is an academic researcher from Flinders University. The author has contributed to research in topics: Alpha-synuclein & Lewy body. The author has an hindex of 44, co-authored 74 publications receiving 7557 citations. Previous affiliations of Wei Ping Gai include Sewanee: The University of the South & Flinders Medical Centre.
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Journal ArticleDOI
Idiopathic Parkinson's disease: possible routes by which vulnerable neuronal types may be subject to neuroinvasion by an unknown pathogen.
TL;DR: The here hypothesized mechanism offers one possible explanation for the sequential and apparently uninterrupted manner in which vulnerable brain regions, subcortical grays and cortical areas become involved in idiopathic Parkinson's disease.
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Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease
John P. Anderson,Donald Walker,Jason Goldstein,Rian de Laat,Kelly Banducci,Russell J. Caccavello,Robin Barbour,Jiping Huang,Kristin Kling,Michael K. Lee,Linnea Diep,Pamela S. Keim,Xiaofeng Shen,Tim Chataway,Michael G. Schlossmacher,Peter A. Seubert,Dale B. Schenk,Sukanto Sinha,Wei Ping Gai,Tamie J. Chilcote +19 more
TL;DR: A comprehensive, unbiased inventory of synuclein forms present in Lewy bodies from patients with dementia with Lewy body was carried out using two-dimensional immunoblot analysis, novel enzyme-linked immunosorbent assays with modification-specific Synuclein antibodies, and mass spectroscopy as mentioned in this paper.
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Proteasomal Inhibition by α-Synuclein Filaments and Oligomers
Evo Lindersson,Rasmus Beedholm,Peter Højrup,Torben Moos,Wei Ping Gai,Klavs B. Hendil,Poul Henning Jensen +6 more
TL;DR: It is demonstrated that α-synuclein and 20 S proteasome components co-localize in Lewy bodies and that subunits from 20 S Proteasome particles, in contrast to subunits of the 19 S regulatory complex, bind efficiently to aggregated filamentous but not monomeric α- synuclein.
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Parkin Localizes to the Lewy Bodies of Parkinson Disease and Dementia with Lewy Bodies
Michael G. Schlossmacher,Matthew P. Frosch,Wei Ping Gai,Miguel Medina,Nutan Sharma,Lysia S. Forno,Tomoyo Ochiishi,Hideki Shimura,Ronit Sharon,Nobutaka Hattori,J. William Langston,Yoshikuni Mizuno,Bradley T. Hyman,Dennis J. Selkoe,Kenneth S. Kosik +14 more
TL;DR: It is concluded that parkin and UbcH7 are present with alphaS in subcellular compartments of normal brain and that park in frequently co-localizes with alpha S aggregates in the characteristic LB inclusions of PD and DLB.
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In Situ and in Vitro Study of Colocalization and Segregation of α-Synuclein, Ubiquitin, and Lipids in Lewy Bodies
TL;DR: The results suggest that Lewy bodies are heterogeneous in their subregional composition, and the segregation of alpha-synuclein to Lewy body peripheral domain is consistent with the hypothesis that alpha- Synuclein is continually deposited ontoLewy bodies.