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Keywords: thioredoxin
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Articles
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...
Articles
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...
Articles
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...
Articles
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...
Articles
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...