SOD1/YJR104C Literature Guide Help

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

SOD1 - Non-Fungal Related Genes/Proteins (36)

Results: 1 - 30 of 36 records
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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
Leitch JM, et al.  (2012) Post-translational modification of Cu/Zn superoxide dismutase under anaerobic conditions. Biochemistry 51(2):677-85
Anderson DM, et al.  (2011) Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU. Mol Microbiol 82(6):1454-67
Dias PJ, et al.  (2010) Insights into the mechanisms of toxicity and tolerance to the agricultural fungicide mancozeb in yeast, as suggested by a chemogenomic approach. OMICS 14(2):211-27
Seetharaman SV, et al.  (2010) Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R. Biochemistry 49(27):5714-25
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
Szklarczyk R and Huynen MA  (2009) Expansion of the human mitochondrial proteome by intra- and inter-compartmental protein duplication. Genome Biol 10(11):R135
Thorsen M, et al.  (2009) Genetic basis of arsenite and cadmium tolerance in Saccharomyces cerevisiae. BMC Genomics 10:105
Wood LK and Thiele DJ  (2009) Transcriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutase. J Biol Chem 284(1):404-13
Kawamata H and Manfredi G  (2008) Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria. Hum Mol Genet 17(21):3303-17
Kawamata H, et al.  (2008) Lysyl-tRNA Synthetase Is a Target for Mutant SOD1 Toxicity in Mitochondria. J Biol Chem 283(42):28321-8
Kirby K, et al.  (2008) Instability of superoxide dismutase 1 of Drosophila in mutants deficient for its cognate copper chaperone. J Biol Chem 283(51):35393-401
Watanabe S, et al.  (2007) Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis. Free Radic Biol Med 42(10):1534-42
Banci L, et al.  (2006) Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. J Biol Chem 281(4):2333-7
Cobine PA, et al.  (2006) Mitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutase. J Biol Chem 281(48):36552-9
Danzeisen R, et al.  (2006) Superoxide dismutase 1 modulates expression of transferrin receptor. J Biol Inorg Chem 11(4):489-98
Tischler J, et al.  (2006) Combinatorial RNA interference in Caenorhabditis elegans reveals that redundancy between gene duplicates can be maintained for more than 80 million years of evolution. Genome Biol 7(8):R69
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
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
Carroll MC, et al.  (2004) Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone. Proc Natl Acad Sci U S A 101(16):5964-9
Cobine PA, et al.  (2004) Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix. J Biol Chem 279(14):14447-55
Gunther MR, et al.  (2004) Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport. Arch Biochem Biophys 431(2):207-14
Takahashi K, et al.  (2004) Cellular signaling mediated by calphoglin-induced activation of IPP and PGM. Biochem Biophys Res Commun 325(1):203-14
Akaza Y, et al.  (2002) Analysis of the gene encoding copper/zinc superoxide dismutase homolog in Dictyostelium discoideum. Biol Pharm Bull 25(12):1528-32
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
Srinivasan C, et al.  (2000) Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance. J Biol Chem 275(38):29187-92
Wong PC, et al.  (2000) Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc Natl Acad Sci U S A 97(6):2886-91
Yoo HY, et al.  (1999) Overexpression and simple purification of human superoxide dismutase (SOD1) in yeast and its resistance to oxidative stress. J Biotechnol 68(1):29-35
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
Results: 1 - 30 of 36 records
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