GLR1/YPL091W Literature Guide Help

Other names published for GLR1: LPG17, glutathione-disulfide reductase GLR1, YPL091W

GLR1 - Protein Physical Properties (33)

Results: 1 - 30 of 33 records
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ReferenceOther Genes Addressed
Rigobello MP, et al.  (2011) Interaction of selenite and tellurite with thiol-dependent redox enzymes: Kinetics and mitochondrial implications. Free Radic Biol Med 50(11):1620-9
Tandogan B, et al.  (2011) In Vitro Effects of Imatinib on Glucose-6-phosphate Dehydrogenase and Glutathione Reductase. Folia Biol (Praha) 57(2):57-64
Melnikov D, et al.  (2010) Enzymatic AND logic gates operated under conditions characteristic of biomedical applications. J Phys Chem B 114(37):12166-74
Rousar T, et al.  (2010) Glutathione reductase is inhibited by acetaminophen-glutathione conjugate in vitro. Physiol Res 59(2):225-32
Seefeldt T, et al.  (2009) Characterization of a novel dithiocarbamate glutathione reductase inhibitor and its use as a tool to modulate intracellular glutathione. J Biol Chem 284(5):2729-37
Cardoso LA, et al.  (2008) Reductive inactivation of yeast glutathione reductase by Fe(II) and NADPH. Comp Biochem Physiol A Mol Integr Physiol 151(3):313-21
Galganska H, et al.  (2008) Redox regulation of protein expression in Saccharomyces cerevisiae mitochondria: Possible role of VDAC. Arch Biochem Biophys 479(1):39-45
Tandogan B and Ulusu NN  (2007) The inhibition kinetics of yeast glutathione reductase by some metal ions. J Enzyme Inhib Med Chem 22(4):489-95
Picaud T and Desbois A  (2006) Interaction of Glutathione Reductase with Heavy Metal: The Binding of Hg(II) or Cd(II) to the Reduced Enzyme Affects Both the Redox Dithiol Pair and the Flavin. Biochemistry 45(51):15829-15837
Lushchak V, et al.  (2005) Diethyldithiocarbamate inhibits in vivo Cu,Zn-superoxide dismutase and perturbs free radical processes in the yeast Saccharomyces cerevisiae cells. Biochem Biophys Res Commun 338(4):1739-44
Lushchak V, et al.  (2005) Possible role of superoxide dismutases in the yeast Saccharomyces cerevisiae under respiratory conditions. Arch Biochem Biophys 441(1):35-40
Morais AC, et al.  (2005) Acid- and pressure-induced (un)folding of yeast glutathione reductase: competition between protein oligomerization and aggregation. Int J Biochem Cell Biol 37(9):1890-9
Paulikova H and Berczeliova E  (2005) The effect of quercetin and galangin on glutathione reductase. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub 149(2):497-500
Picaud T and Desbois A  (2002) Electrostatic control of the isoalloxazine environment in the two-electron reduced states of yeast glutathione reductase. J Biol Chem 277(35):31715-21
Arscott LD, et al.  (2000) Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell. Biochemistry 39(16):4711-21
Levron B, et al.  (2000) On the reduction of dithiolethiones and dithiolylium ions by NADPH and glutathione reductase. Arch Biochem Biophys 382(2):189-94
Baylor KJ and Heffron JJ  (1996) Isocyanate inactivation of yeast glutathione reductase & its modulation by oxidised glutathione and NADPH. Biochem Soc Trans 24(2):325S
Collinson LP and Dawes IW  (1995) Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase. Gene 156(1):123-7
Pick U, et al.  (1995) Glutathione reductase and lipoamide dehydrogenase have opposite stereospecificities for alpha-lipoic acid enantiomers. Biochem Biophys Res Commun 206(2):724-30
Alhama J, et al.  (1991) High-performance affinity chromatography of NADP+ dehydrogenases from cell-free extracts using a nucleotide analogue as general ligand. J Chromatogr 586(1):51-9
Sahlman L and Williams CH Jr  (1989) Titration studies on the active sites of pig heart lipoamide dehydrogenase and yeast glutathione reductase as monitored by the charge transfer absorbance. J Biol Chem 264(14):8033-8
Llobell A, et al.  (1986) Electron transfer between reduced methyl viologen and oxidized glutathione: a new assay of Saccharomyces cerevisiae glutathione reductase. Arch Biochem Biophys 250(2):373-81
Huber PW and Brandt KG  (1985) Kinetic studies of the reduction of yeast glutathione reductase by reduced nicotinamide hypoxanthine dinucleotide phosphate. Arch Biochem Biophys 238(1):213-8
Pinto MC, et al.  (1985) The redox interconversion mechanism of Saccharomyces cerevisiae glutathione reductase. Eur J Biochem 151(2):275-81
Dubler RE and Anderson BM  (1981) Simultaneous inactivation of the catalytic activities of yeast glutathione reductase by N-alkylmaleimides. Biochim Biophys Acta 659(1):70-85
Carlberg I and Mannervik B  (1977) Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione. Biochim Biophys Acta 484(2):268-74
Moroff G, et al.  (1976) Yeast glutathione reductase. Steady-state kinetic studies of its transhydrogenase activity. Arch Biochem Biophys 173(1):42-9
Moroff G and Brandt KG  (1975) Yeast glutathione reductase. Studies of the kinetics and stability of the enzyme as a function of pH and salt concentration. Biochim Biophys Acta 410(1):21-31
Bulger JE and Brandt KG  (1971) Yeast glutathione reductase. I. Spectrophotometric and kinetic studies of its interaction with reduced nicotinamide adenine dinucleotide. J Biol Chem 246(18):5570-7
Bulger JE and Brandt KG  (1971) Yeast glutathione reductase. II. Interaction of oxidized and 2-electron reduced enzyme with reduced and oxidized nicotinamide adenine dinucleotide phosphate. J Biol Chem 246(18):5578-87
Results: 1 - 30 of 33 records
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