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Keywords: disulphide
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Articles
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...
Articles
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...
Articles
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...
Articles
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...