...T.R. Hurd; A. Filipovska; N.J. Costa; C.C. Dahm; M.P. Murphy A large number of proteins contain free thiols that can be modified by the formation of internal disulphides or by mixed disulphides with low-molecular-mass thiols. The majority of these latter modifications result from the interaction...

...P. Ghezzi Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide formation, glutathionylation and S-nitrosylation). While in the past these were viewed as protein damage in the context of oxidative stress, there is growing interest in oxidoreduction of protein...

... Arne.Holmgren@mbb.ki.se ). 11 7 2005 © 2005 The Biochemical Society 2005 disulphide glutaredoxin (Grx) GSH thiol redox control thioredoxin (Trx) thioredoxin reductase (TrxR) The cellular redox state is a crucial mediator of multiple metabolic, signalling and transcriptional...

... cytochrome c maturation in Bacillus subtilis with particular emphasis on the crystal structures of ResA. Because of the intimate nature of the thiol–disulphide redox chemistry (which involves the formation of a transient disulphide bond between redox partners) and short distance between the cleft...