{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Whiten DR"],"funding":["Christ’s College, Cambridge, UK","Cambridge Centre for Misfolding Diseases","Fondazione Umberto Veronesi","Herchel Smith fellowship","Royal Society","UK Biotechnology and Biochemical Sciences Research Council","Australian Research Council","Australian Postgraduate Award","European Research Council","Medical Research Council","Wellcome Trust","Boehringer Ingelheim Fonds","Marie Curie"],"pagination":["3492-3500"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6024880"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(12)"],"pubmed_abstract":["The aberrant aggregation of α-synuclein is associated with several human diseases, collectively termed the α-synucleinopathies, which includes Parkinson's disease. The progression of these diseases is, in part, mediated by extracellular α-synuclein oligomers that may exert effects through several mechanisms, including prion-like transfer, direct cytotoxicity, and pro-inflammatory actions. In this study, we show that two abundant extracellular chaperones, clusterin and α<sub>2</sub>-macroglobulin, directly bind to exposed hydrophobic regions on the surface of α-synuclein oligomers. Using single-molecule fluorescence techniques, we found that clusterin, unlike α<sub>2</sub>-macroglobulin, exhibits differential binding to α-synuclein oligomers that may be related to structural differences bet"],"journal":["Cell reports"],"pubmed_title":["Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers."],"pmcid":["PMC6024880"],"funding_grant_id":["DP160100011","669237","UKDRI-2003"],"pubmed_authors":["Tosatto L","Flagmeier P","Dobson CM","Cox D","De S","Taylor CG","Whiten DR","Wilson MR","Ecroyd H","Kumita JR","Horrocks MH","Klenerman D"],"additional_accession":[]},"is_claimable":false,"name":"Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers.","description":"The aberrant aggregation of α-synuclein is associated with several human diseases, collectively termed the α-synucleinopathies, which includes Parkinson's disease. The progression of these diseases is, in part, mediated by extracellular α-synuclein oligomers that may exert effects through several mechanisms, including prion-like transfer, direct cytotoxicity, and pro-inflammatory actions. In this study, we show that two abundant extracellular chaperones, clusterin and α<sub>2</sub>-macroglobulin, directly bind to exposed hydrophobic regions on the surface of α-synuclein oligomers. Using single-molecule fluorescence techniques, we found that clusterin, unlike α<sub>2</sub>-macroglobulin, exhibits differential binding to α-synuclein oligomers that may be related to structural differences bet","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jun","modification":"2025-04-25T21:16:07.419Z","creation":"2019-03-26T23:44:43Z"},"accession":"S-EPMC6024880","cross_references":{"pubmed":["29924993"],"doi":["10.1016/j.celrep.2018.05.074"]}}