Evidence of native α-synuclein conformers in the human brain
- Neal Gould,
- ,
- Richard Lightfoot,
- Kristen Malkus,
- Benoit Giasson,
- Harry Ischiropoulos(corresponding author)
- University of Pennsylvania
Scholary Output:
Contribution to journal
Article
Peer-reviewAbstract
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.
Publication Information
Output type
Scholary Output:
Contribution to journal
Article
Peer-reviewOriginal language
English (US)Pages from-to (Number of pages)
Pages 7929-7934 (6 pages)Journal (Volume, Issue Number)
Journal of Biological Chemistry (Volume 289, Issue 11)Publication milestones
- Published - 03/14/2014
Publication status
Published - 03/14/2014
ISSN
0021-9258Publication IDs
- ORCID: /0000-0003-3851-5010/work/84895559
- PubMed: 24474688
- Scopus: 84896267689
Publication metrics
Metrics
SciVal
FWCI
1.65
SciVal
Author count
6
SciVal
Paper percentile
93
SciVal
Top percentile
10
SciVal
citations
48
Fractional count
1
Fractional count
0.17
Fractional count
5
Fractional count
0.83
Fractional count
1
Fractional count
1
PlumX, opens in new tab
Captures
125
Citation count
60
