Dataset Information
ATP synthase nLC-MSMS - α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Rattus Norvegicus (rat)
TISSUE(S): Brain
SUBMITTER: 
Morana Jaganjac
LAB HEAD: Morana Jaganjac
PROVIDER: PXD009416 | Pride | 2018-06-18
REPOSITORIES: Pride
Dataset's files
Publications
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease.
Nature communications 20180612 1
Protein aggregation causes α-synuclein to switch from its physiological role to a pathological toxic gain of function. Under physiological conditions, monomeric α-synuclein improves ATP synthase efficiency. Here, we report that aggregation of monomers generates beta sheet-rich oligomers that localise to the mitochondria in close proximity to several mitochondrial proteins including ATP synthase. Oligomeric α-synuclein impairs complex I-dependent respiration. Oligomers induce selective oxidation ...[more]
