...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...

...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...

... 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 disulfide-isomerase) family are capable of reducing non-native disulfides during protein folding...

... enzyme players such as Trx (thioredoxin) or Grx (glutaredoxin). 1 To whom correspondence should be addressed (email [email protected] ). 28 6 2011 © The Authors Journal compilation © 2011 Biochemical Society 2011 cytokine glutathione immunity inflammation redox regulation...

... 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...