1-5 of 5
Keywords: thioredoxin
Follow your search
Access your saved searches in your account

Would you like to receive an alert when new items match your search?
Close Modal
Sort by
Biochem Soc Trans (2015) 43 (4): 632–638.
Published: 03 August 2015
...Edward E. Schmidt NADPH transfers reducing power from bioenergetic pathways to thioredoxin reductase-1 (TrxR1) and glutathione reductase (GR) to support essential reductive systems. Surprisingly, it was recently shown that mouse livers lacking both TrxR1 and GR (‘TR/GR-null’) can sustain redox...
Biochem Soc Trans (2014) 42 (4): 905–908.
Published: 11 August 2014
... 124 2349 2356 10.1242/jcs.085530 21693587 Both of these hypotheses suggest the presence of a reductive pathway that channels reducing equivalents through a disulfide–exchange protein that is usually a member of the thioredoxin superfamily. We now know that some members of the PDI (protein...
Biochem Soc Trans (2014) 42 (4): 922–927.
Published: 11 August 2014
...Helen R. Griffiths; Stuart J. Bennett; Peter Olofsson; Christopher R. Dunston The oxidoreductase Trx-1 (thioredoxin 1) is highly conserved and found intra- and extra-cellularly in mammalian systems. There is increasing interest in its capacity to regulate immune function based on observations...
Biochem Soc Trans (2011) 39 (5): 1268–1272.
Published: 21 September 2011
... enzyme players such as Trx (thioredoxin) or Grx (glutaredoxin). 1 To whom correspondence should be addressed (email p.ghezzi@bsms.ac.uk ). 28 6 2011 © The Authors Journal compilation © 2011 Biochemical Society 2011 cytokine glutathione immunity inflammation redox regulation...
Biochem Soc Trans (2008) 36 (6): 1124–1128.
Published: 19 November 2008
... converted the active-site CXXCK motif of a thioredoxin-like protein into CXXCH, the C-terminal domain of the transmembrane oxidoreductase DsbD (cDsbD). The E. coli Ccm system was found to catalyse haem attachment to a very small percentage of the resultant protein (∼0.2%). We argue that cDsbD folds...