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Keywords: disulphide
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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): 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): 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
..., required for translocation of the unfolded apo-cytochrome across the cytoplasmic membrane, and the general disulphide bond formation and isomerization machinery that generates a disulphide bond between the cysteine residues of the haem-binding motif upon arrival of the apo-cytochrome in the extra...