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Journal article

Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.

Abstract:

Selected disulfide bonds in membrane proteins are labile and are thus susceptible to changes in redox potential and/or the presence of thiol isomerase enzymes. Modification of these disulfide bonds can lead to conformational changes of the protein that in turn may alter protein activity and function. This occurs in the entry of several enveloped viruses into their host cells, e.g. HIV, hepatitis C virus and Newcastle disease virus. Labile disulfide bonds are also important in platelet activat...

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Publication status:
Published

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Publisher copy:
10.1002/eji.201242849

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Role:
Author
Journal:
European journal of immunology
Volume:
43
Issue:
1
Pages:
15-21
Publication date:
2013-01-05
DOI:
EISSN:
1521-4141
ISSN:
0014-2980
URN:
uuid:e5fcb6be-ed21-418a-ab5b-4a137abbc357
Source identifiers:
367669
Local pid:
pubs:367669

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