| Literature DB >> 24474688 |
Neal Gould1, Danielle E Mor, Richard Lightfoot, Kristen Malkus, Benoit Giasson, Harry Ischiropoulos.
Abstract
α-Synuclein aggregation is central to the pathogenesis of several brain disorders. However, the native conformations and functions of this protein in the human brain are not precisely known. The native state of α-synuclein was probed by gel filtration coupled with native gradient gel separation, an array of antibodies with non-overlapping epitopes, and mass spectrometry. The existence of metastable conformers and stable monomer was revealed in the human brain.Entities:
Keywords: Alpha-Synuclein; Human Brain; Native State; Neurodegenerative Diseases; Parkinson Disease; Protein Conformation; Protein Folding
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Year: 2014 PMID: 24474688 PMCID: PMC3953303 DOI: 10.1074/jbc.C113.538249
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157