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Disulfide bond reshuffling

The mammalian ER luminal chaperone PDI is an oxidoreductase involved in the formation and reshuffling of disulfide bonds, although it is also capable of interactions with proteins that do not form disulfides (Gilbert 1997 Noiva 1999 Ferrari and Soling 1999). Because disulfides of dislocating MHC class I heavy chains are reduced just before the proteins are deglycosylated, it has been hypothesized that PDI may play a role in breaking up disulfide bonds in an early phase of dislocation (Tortorella et al. 1998). In addition to PDI, other disulfide... [Pg.46]

Fig. 15 Self-healing via covalent bond reformation using chain exchange reactions (a) acylhydrazone equilibrium (b) reshuffling reaction of trithiocarbonates (TTC) (c) disulfide chain exchange (d) siloxane chain exchange. Reproduced with permission from [62]... Fig. 15 Self-healing via covalent bond reformation using chain exchange reactions (a) acylhydrazone equilibrium (b) reshuffling reaction of trithiocarbonates (TTC) (c) disulfide chain exchange (d) siloxane chain exchange. Reproduced with permission from [62]...
See other pages where Disulfide bond reshuffling is mentioned: [Pg.170]    [Pg.170]    [Pg.161]    [Pg.508]    [Pg.503]    [Pg.142]    [Pg.154]    [Pg.54]    [Pg.230]    [Pg.15]    [Pg.404]    [Pg.2089]    [Pg.275]    [Pg.276]    [Pg.285]    [Pg.328]   
See also in sourсe #XX -- [ Pg.170 ]



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