SOD1/YJR104C Literature Guide Help

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

SOD1 - Protein Sequence Features (20)

ReferenceOther Genes Addressed
Huppke P, et al.  (2012) Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase. Hum Mutat 33(8):1207-15
Brandes N, et al.  (2011) Using quantitative redox proteomics to dissect the yeast redoxome. J Biol Chem 286(48):41893-903
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
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
Wu CY, et al.  (2009) Cytosolic superoxide dismutase (SOD1) is critical for tolerating the oxidative stress of zinc deficiency in yeast. PLoS One 4(9):e7061
Xie H, et al.  (2009) Characterization of protein impurities and site-specific modifications using peptide mapping with liquid chromatography and data independent acquisition mass spectrometry. Anal Chem 81(14):5699-708
Jensen LT and Culotta VC  (2005) Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS. J Biol Chem 280(50):41373-9
Furukawa Y, et al.  (2004) Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. EMBO J 23(14):2872-81
Field LS, et al.  (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J Biol Chem 278(30):28052-9
Zielinski R, et al.  (2002) Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase. Biochem Biophys Res Commun 296(5):1310-6
Sturtz LA, et al.  (2001) A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 276(41):38084-9
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
Schmidt PJ, et al.  (1999) A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1. J Biol Chem 274(52):36952-6
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
Scheibel T, et al.  (1997) S. cerevisiae and sulfur: a unique way to deal with the environment. FASEB J 11(11):917-21
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
Borders CL Jr, et al.  (1991) The positive charge at position 189 is essential for the catalytic activity of iron- and manganese-containing superoxide dismutases. Free Radic Res Commun 12-13 Pt 1:279-85
Bermingham-McDonogh O, et al.  (1988) The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity. Proc Natl Acad Sci U S A 85(13):4789-93
Phillips JC, et al.  (1984) A proposal for the metal geometry in yeast superoxide dismutase based on results from EXAFS spectroscopy. J Inorg Biochem 22(3):179-86
Steinman HM  (1980) The amino acid sequence of copper-zinc superoxide dismutase from bakers' yeast. J Biol Chem 255(14):6758-65