α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex for...
α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation
About this item
Full title
Author / Creator
Publisher
United States: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
United States: National Academy of Sciences
Subjects
More information
Scope and Contents
Contents
Physiologically, α-synuclein chaperones soluble NSF attachment protein receptor (SNARE) complex assembly and may also perform other functions; pathologically, in contrast, α-synuclein misfolds into neurotoxic aggregates that mediate neurodegeneration and propagate between neurons. In neurons, α-synuclein exists in an equilibrium between cytosolic a...
Alternative Titles
Full title
α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4210039
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4210039
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1416598111
