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Evidence of native α-synuclein conformers in the human brain

  • Neal Gould
    ,
  • ,
  • Richard Lightfoot
    ,
  • Kristen Malkus
    ,
  • Benoit Giasson
    ,
  • Harry Ischiropoulos(corresponding author)
*Corresponding author for this work
  • University of Pennsylvania
Scholary Output:
Contribution to journal
Article
Peer-review

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.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original 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

0021-9258

Publication 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
Scopus
citations

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125
Citation count
60