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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Authors
Bibliographic Details
- Journal:
- Open biology
- Volume:
- 1
- Issue:
- 3
- Pages:
- 110010
- Publication date:
- 2011-11-01
- DOI:
- EISSN:
-
2046-2441
- ISSN:
-
2046-2441
- Source identifiers:
-
228586
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:228586
- UUID:
-
uuid:31626448-8b2c-456c-bd05-637c9d6d8221
- Local pid:
- pubs:228586
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2011
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