- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/eji.201242849
-
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- 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
- Copyright date:
- 2013
Journal article
Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.
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