SOD1/YJR104C Literature Guide Help

Other names published for SOD1: CRS4, superoxide dismutase SOD1, YJR104C

SOD1 - Substrates/Ligands/Cofactors (32)

Results: 1 - 30 of 32 records
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ReferenceOther Genes Addressed
Tran DT, et al.  (2012) Slow histidine H/D exchange protocol for thermodynamic analysis of protein folding and stability using mass spectrometry. Anal Chem 84(3):1653-60
Reeder NL, et al.  (2011) Zinc pyrithione inhibits yeast growth through copper influx and inactivation of iron-sulfur proteins. Antimicrob Agents Chemother 55(12):5753-60
Sharma PK, et al.  (2011) Mitochondria-mediated hormetic response in life span extension of calorie-restricted Saccharomyces cerevisiae. Age (Dordr) 33(2):143-54
Horn D, et al.  (2010) The conserved mitochondrial twin Cx9C protein Cmc2 Is a Cmc1 homologue essential for cytochrome c oxidase biogenesis. J Biol Chem 285(20):15088-99
Irazusta V, et al.  (2010) Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage. Free Radic Biol Med 48(3):411-420
Leitch JM, et al.  (2009) Activation of Cu,Zn-Superoxide Dismutase in the Absence of Oxygen and the Copper Chaperone CCS. J Biol Chem 284(33):21863-71
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
Horn D, et al.  (2008) Cmc1p is a conserved mitochondrial twin CX9C protein involved in cytochrome c oxidase biogenesis. Mol Cell Biol 28(13):4354-64
Lushchak OV and Lushchak VI  (2008) Sodium nitroprusside induces mild oxidative stress in Saccharomyces cerevisiae. Redox Rep 13(4):144-52
Giannattasio S, et al.  (2005) Acid stress adaptation protects Saccharomyces cerevisiae from acetic acid-induced programmed cell death. Gene 354:93-8
Harris N, et al.  (2005) Overexpressed Sod1p acts either to reduce or to increase the lifespans and stress resistance of yeast, depending on whether it is Cu(2+)-deficient or an active Cu,Zn-superoxide dismutase. Aging Cell 4(1):41-52
John L, et al.  (2005) Cigarette smoke extract induces changes in growth and gene expression of Saccharomyces cerevisiae. Biochem Biophys Res Commun 338(3):1578-86
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
Nedeva TS, et al.  (2004) Cu/Zn superoxide dismutase in yeast mitochondria - a general phenomenon. FEMS Microbiol Lett 230(1):19-25
Field LS, et al.  (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J Biol Chem 278(30):28052-9
Gonzalez-Alvarez M, et al.  (2003) Development of novel copper(II) complexes of benzothiazole- N-sulfonamides as protective agents against superoxide anion. Crystal structures of [Cu( N-2-(4-methylbenzothiazole)benzenesulfonamidate)(2)(py)(2)] and [Cu( N-2-(6-nitrobenzothiazole)naphthalenesulfonamidate)(2)(py)(2)]. J Biol Inorg Chem 8(1-2):112-20
Torres AS, et al.  (2001) Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase. J Biol Chem 276(42):38410-6
Endo T, et al.  (2000) A pivotal role of Zn-binding residues in the function of the copper chaperone for SOD1. Biochem Biophys Res Commun 276(3):999-1004
Lamb AL, et al.  (2000) Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry 39(48):14720-7
Lyons TJ, et al.  (2000) The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis. J Biol Inorg Chem 5(2):189-203
Schmidt PJ, et al.  (2000) Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1. J Biol Chem 275(43):33771-6
Culotta VC, et al.  (1999) Intracellular pathways of copper trafficking in yeast and humans. Adv Exp Med Biol 448:247-54
Lamb AL, et al.  (1999) Crystal structure of the copper chaperone for superoxide dismutase. Nat Struct Biol 6(8):724-9
Piper PW  (1999) Yeast superoxide dismutase mutants reveal a pro-oxidant action of weak organic acid food preservatives. Free Radic Biol Med 27(11-12):1219-27
Rae TD, et al.  (1999) Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284(5415):805-8
Schmidt PJ, et al.  (1999) Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase. J Biol Chem 274(34):23719-25
Corson LB, et al.  (1998) Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants. Proc Natl Acad Sci U S A 95(11):6361-6
Gamonet F and Lauquin GJ  (1998) The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection. Eur J Biochem 251(3):716-23
Nishida CR, et al.  (1994) Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 91(21):9906-10
Results: 1 - 30 of 32 records
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