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Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis.

Abstract:

Regulation of protein function by reversible cysteine-targeted oxidation can be achieved by multiple mechanisms, such as S-glutathiolation, S-nitrosylation, sulfenic acid, sulfinic acid, and sulfenyl amide formation, as well as intramolecular disulfide bonding of vicinal thiols. Another cysteine oxidation state with regulatory potential involves the formation of intermolecular protein disulfides. We utilized two-dimensional sequential non-reducing/reducing SDS-PAGE (diagonal electrophoresis) ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m403827200

Authors


Brennan, JP More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
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Journal:
The Journal of biological chemistry
Volume:
279
Issue:
40
Pages:
41352-41360
Publication date:
2004-10-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:cff70062-c87b-4b13-b39e-4459dbd9f428
Source identifiers:
230186
Local pid:
pubs:230186

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