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Keywords: disulphide
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Biochem Soc Trans (2005) 33 (6): 1390–1393.
Published: 26 October 2005
...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...
Biochem Soc Trans (2005) 33 (6): 1378–1381.
Published: 26 October 2005
...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...
Biochem Soc Trans (2005) 33 (6): 1375–1377.
Published: 26 October 2005
... 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...
Biochem Soc Trans (2005) 33 (1): 149–151.
Published: 01 February 2005
... cytochrome c maturation in Bacillus subtilis with particular emphasis on the crystal structures of ResA. The active site of ResA comprises a redox-active CXXC motif (C 73 GPC 76 ) located at the N-terminus of a long α-helix (α1). The motif alternates between disulphide (oxidized) and dithiol (reduced...