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Journal article

Labile disulfide bonds are common at the leucocyte cell surface.

Abstract:

Redox conditions change in events such as immune and platelet activation, and during viral infection, but the biochemical consequences are not well characterized. There is evidence that some disulfide bonds in membrane proteins are labile while others that are probably structurally important are not exposed at the protein surface. We have developed a proteomic/mass spectrometry method to screen for and identify non-structural, redox-labile disulfide bonds in leucocyte cell-surface proteins. T...

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Publication status:
Published

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Publisher copy:
10.1098/rsob.110010

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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Journal:
Open biology
Volume:
1
Issue:
3
Pages:
110010
Publication date:
2011-11-01
DOI:
EISSN:
2046-2441
ISSN:
2046-2441
Source identifiers:
228586
Language:
English
Keywords:
Pubs id:
pubs:228586
UUID:
uuid:31626448-8b2c-456c-bd05-637c9d6d8221
Local pid:
pubs:228586
Deposit date:
2012-12-19

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