GLR1/YPL091W Literature Guide Help

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

GLR1 - Primary Literature (71)

ReferenceOther Genes Addressed
Aksnes H, et al.  (2013) N-Terminal Acetylation by NatC Is Not a General Determinant for Substrate Subcellular Localization in Saccharomyces cerevisiae. PLoS One 8(4):e61012
Couto N, et al.  (2013) Partition and Turnover of Glutathione Reductase from Saccharomyces cerevisiae: a Proteomic Approach. J Proteome Res ()
Greetham D, et al.  (2013) Oxidation of the yeast mitochondrial thioredoxin promotes cell death. Antioxid Redox Signal 18(4):376-85
Li Y, et al.  (2013) Mechanism-oriented controllability of intracellular quantum dots formation: the role of glutathione metabolic pathway. ACS Nano 7(3):2240-8
Matsufuji Y, et al.  (2013) Novel physiological roles for glutathione in sequestering acetaldehyde to confer acetaldehyde tolerance in Saccharomyces cerevisiae. Appl Microbiol Biotechnol 97(1):297-303
Morgan B, et al.  (2013) Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat Chem Biol 9(2):119-25
Alex D, et al.  (2012) Amino acid-derived 1,2-benzisothiazolinone derivatives as novel small-molecule antifungal inhibitors: identification of potential genetic targets. Antimicrob Agents Chemother 56(9):4630-9
Harigaya Y and Parker R  (2012) Global analysis of mRNA decay intermediates in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 109(29):11764-9
Kim JH, et al.  (2012) Targeting the oxidative stress response system of fungi with redox-potent chemosensitizing agents. Front Microbiol 3():88
Kojer K, et al.  (2012) Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state. EMBO J 31(14):3169-82
Lis P, et al.  (2012) Transport and cytotoxicity of the anticancer drug 3-bromopyruvate in the yeast Saccharomyces cerevisiae. J Bioenerg Biomembr 44(1):155-61
Manikova D, et al.  (2012) Selenium toxicity toward yeast as assessed by microarray analysis and deletion mutant library screen: a role for DNA repair. Chem Res Toxicol 25(8):1598-608
Mapelli V, et al.  (2012) The interplay between sulphur and selenium metabolism influences the intracellular redox balance in Saccharomyces cerevisiae. FEMS Yeast Res 12(1):20-32
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
Yoboue ED, et al.  (2012) cAMP-induced mitochondrial compartment biogenesis: role of glutathione redox state. J Biol Chem 287(18):14569-78
Yoon HS, et al.  (2012) Glutathione reductase from Brassica rapa affects tolerance and the redox state but not fermentation ability in response to oxidative stress in genetically modified Saccharomyces cerevisiae. World J Microbiol Biotechnol 28(5):1901-15
Kim JH, et al.  (2011) Antifungal activity of redox-active benzaldehydes that target cellular antioxidation. Ann Clin Microbiol Antimicrob 10(1):23
Kim JH, et al.  (2011) Chemosensitization of aflatoxigenic fungi to antimycin a and strobilurin using salicylaldehyde, a volatile natural compound targeting cellular antioxidation system. Mycopathologia 171(4):291-8
Sato I, et al.  (2011) Glutathione reductase/glutathione is responsible for cytotoxic elemental sulfur tolerance via polysulfide shuttle in fungi. J Biol Chem 286(23):20283-91
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
Greetham D, et al.  (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem 11():3
Rousar T, et al.  (2010) Glutathione reductase is inhibited by acetaminophen-glutathione conjugate in vitro. Physiol Res 59(2):225-32
Tan SX, et al.  (2010) The Thioredoxin-Thioredoxin Reductase System Can Function in Vivo as an Alternative System to Reduce Oxidized Glutathione in Saccharomyces cerevisiae. J Biol Chem 285(9):6118-26
Greetham D and Grant CM  (2009) Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol Cell Biol 29(11):3229-40
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
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
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
Gales G, et al.  (2008) Role of glutathione metabolism status in the definition of some cellular parameters and oxidative stress tolerance of Saccharomyces cerevisiae cells growing as biofilms. FEMS Yeast Res 8(5):667-75
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
Seitomer E, et al.  (2008) Analysis of Saccharomyces cerevisiae null allele strains identifies a larger role for DNA damage versus oxidative stress pathways in growth inhibition by selenium. Mol Nutr Food Res 52(11):1305-15