TY - JOUR
T1 - Evidence of native α-synuclein conformers in the human brain
AU - Gould, Neal
AU - Mor, Danielle E.
AU - Lightfoot, Richard
AU - Malkus, Kristen
AU - Giasson, Benoit
AU - Ischiropoulos, Harry
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 2014/3/14
Y1 - 2014/3/14
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.c113.538249
DO - 10.1074/jbc.c113.538249
M3 - Article
C2 - 24474688
SN - 0021-9258
VL - 289
SP - 7929
EP - 7934
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 11
ER -