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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 activation, cytokine signalling and in a variety of diseases including cancer and arthritis. In this review we will concentrate on recent advances in understanding the conditions that lead to disulfide bond reduction in membrane proteins and their effects in regulating immune function.

Original publication

DOI

10.1002/eji.201242849

Type

Journal article

Journal

Eur J Immunol

Publication Date

01/2013

Volume

43

Pages

15 - 21

Keywords

Animals, Arthritis, Cystine, Cytokines, HIV, Hepacivirus, Humans, Membrane Proteins, Neoplasms, Oxidation-Reduction, Platelet Activation, Protein Conformation, Protein Disulfide-Isomerases, Virus Internalization