Primary Literature
TEXT HERE
- Banerjee V, et al. (2017) A computational combinatorial approach identifies a protein inhibitor of superoxide dismutase 1 misfolding, aggregation, and cytotoxicity. J Biol Chem 292(38):15777-15788 PMID: 28768772
- Sea K, et al. (2015) Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase. J Biol Chem 290(4):2405-18 PMID: 25433341
- Wang Z, et al. (2014) Secretion expression of SOD1 and its overlapping function with GSH in brewing yeast strain for better flavor and anti-aging ability. J Ind Microbiol Biotechnol 41(9):1415-24 PMID: 25037722
- Kim Y, et al. (2013) Characterization and Hsp104-induced artificial clearance of familial ALS-related SOD1 aggregates. Biochem Biophys Res Commun 434(3):521-6 PMID: 23583391
- Sea KW, et al. (2013) Yeast copper-zinc superoxide dismutase can be activated in the absence of its copper chaperone. J Biol Inorg Chem 18(8):985-92 PMID: 24061560
- Bastow EL, et al. (2011) Using yeast models to probe the molecular basis of amyotrophic lateral sclerosis. Biochem Soc Trans 39(5):1482-7 PMID: 21936838
- 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 PMID: 15215895
- Field LS, et al. (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J Biol Chem 278(30):28052-9 PMID: 12748182
- Lamb AL, et al. (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol 8(9):751-5 PMID: 11524675
- 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 PMID: 11473116
- Lamb AL, et al. (2000) Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry 39(7):1589-95 PMID: 10677207
- Lamb AL, et al. (2000) Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry 39(48):14720-7 PMID: 11101286
- 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 PMID: 10944535
- Hart PJ, et al. (1999) A structure-based mechanism for copper-zinc superoxide dismutase. Biochemistry 38(7):2167-78 PMID: 10026301
- Lamb AL, et al. (1999) Crystal structure of the copper chaperone for superoxide dismutase. Nat Struct Biol 6(8):724-9 PMID: 10426947
- 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 PMID: 10446130
- Chang EC, et al. (1991) Genetic and biochemical characterization of Cu,Zn superoxide dismutase mutants in Saccharomyces cerevisiae. J Biol Chem 266(7):4417-24 PMID: 1999425
- 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 PMID: 3290902