GLR1/YPL091W Literature Guide Help

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

GLR1 - Protein Processing/Modification/Regulation (15)

ReferenceOther Genes Addressed
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
Bayliak M, et al.  (2008) Inhibition of Catalase by Aminotriazole in vivo Results in Reduction of Glucose-6-phosphate Dehydrogenase Activity in Saccharomyces cerevisiae Cells. Biochemistry (Mosc) 73(4):420-6
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
Grzelak A, et al.  (2006) Accumulation of oxidative damage during replicative aging of the yeast Saccharomyces cerevisiae. Exp Gerontol 41(9):813-8
Lushchak VI and Gospodaryov DV  (2005) Catalases protect cellular proteins from oxidative modification in Saccharomyces cerevisiae. Cell Biol Int 29(3):187-92
Sohn HY, et al.  (2005) GLR1 plays an essential role in the homeodynamics of glutathione and the regulation of H2S production during respiratory oscillation of Saccharomyces cerevisiae. Biosci Biotechnol Biochem 69(12):2450-4
Outten CE and Culotta VC  (2004) Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase. J Biol Chem 279(9):7785-91
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
Pinto MC, et al.  (1984) Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions. Arch Biochem Biophys 228(1):1-12
Tsai CS  (1984) Recognition site of yeast glutathione reductase for 2'-phosphate of NADP+. Biochem Biophys Res Commun 124(2):572-7
Rafter GW  (1982) Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds. Biochem Med 27(3):381-91
Hati RN and Ingbar SH  (1981) Inhibition of yeast, & rat thyroidal, glutathione reductase activity by iodine. Indian J Biochem Biophys 18(5):342-5
Babson JR and Reed DJ  (1978) Inactivation of glutathione reductase by 2-chloroethyl nitrosourea-derived isocyanates. Biochem Biophys Res Commun 83(2):754-62