title: Targeting alpha-synuclein in Parkinson's disease.
abstract: alpha-Synuclein aggregation into fibrils is associated with the pathogenesis of Parkinson's disease (PD). Li et al. provide strong evidence that rifampicin interacts with alpha-synuclein and inhibits its fibrillization. Rifampicin could be a promising candidate for therapeutic application for PD.
authors.affiliation: Laboratory of Bioorganic and Medicinal Chemistry, Institute of Biochemistry, University Hospital of the RWTH Aachen, Pauwelstrasse 30, D-52074 Aachen, Germany.
authors.forename: Aphrodite
authors.initials: A
authors.lastname: Kapurniotu
mesh_terms: D016503:Drug Delivery Systems; D006801:Humans; D009419:Nerve Tissue Proteins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D010300:Parkinson Disease / Q000188:drug therapy*; D012293:Rifampin / Q000378:metabolism / Q000627:therapeutic use*; D051843:Synucleins; D051844:alpha-Synuclein
chemical_list: D009419:Nerve Tissue Proteins; C497604:SNCA protein, human; D051843:Synucleins; D051844:alpha-Synuclein; D012293:Rifampin