GRX1/YCL035C Literature Guide Help

Other names published for GRX1: YCL035C

GRX1 - Function/Process (22)

ReferenceOther Genes Addressed
Ding MZ, et al.  (2012) Proteomic research reveals the stress response and detoxification of yeast to combined inhibitors. PLoS One 7(8):e43474
Greetham D, et al.  (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem 11():3
Hacioglu E, et al.  (2010) The roles of thiol oxidoreductases in yeast replicative aging. Mech Ageing Dev 131(11-12):692-9
Iversen R, et al.  (2010) Thiol-disulfide exchange between glutaredoxin and glutathione. Biochemistry 49(4):810-20
Izquierdo A, et al.  (2010) Selenite-induced cell death in Saccharomyces cerevisiae: protective role of glutaredoxins. Microbiology 156(Pt 9):2608-20
Li WF, et al.  (2010) Structural basis for the different activities of yeast Grx1 and Grx2. Biochim Biophys Acta 1804(7):1542-1547
Luo M, et al.  (2010) Structural and biochemical characterization of yeast monothiol glutaredoxin Grx6. J Mol Biol 398(4):614-22
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
Discola KF, et al.  (2009) Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae. J Mol Biol 385(3):889-901
Jun KO, et al.  (2009) Activation of translation via reduction by thioredoxin-thioredoxin reductase in Saccharomyces cerevisiae. FEBS Lett 583(17):2804-10
Carroll MC, et al.  (2006) The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase. J Biol Chem 281(39):28648-56
Teixeira MC, et al.  (2004) The herbicide 2,4-dichlorophenoxyacetic acid induces the generation of free-radicals and associated oxidative stress responses in yeast. Biochem Biophys Res Commun 324(3):1101-7
Collinson EJ and Grant CM  (2003) Role of yeast glutaredoxins as glutathione S-transferases. J Biol Chem 278(25):22492-7
Collinson EJ, et al.  (2002) The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem 277(19):16712-7
Fetrow JS, et al.  (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14
Delaunay A, et al.  (2000) H2O2 sensing through oxidation of the Yap1 transcription factor. EMBO J 19(19):5157-66
Draculic T, et al.  (2000) A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Mol Microbiol 36(5):1167-74
Grant CM, et al.  (2000) Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1490(1-2):33-42
Mukhopadhyay R, et al.  (2000) Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase. J Biol Chem 275(28):21149-57
Izawa S, et al.  (1999) Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae. J Biol Chem 274(40):28459-65
Rodriguez-Manzaneque MT, et al.  (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19(12):8180-90
Luikenhuis S, et al.  (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell 9(5):1081-91