Other names published for SCO1: PET161, YBR037C
SCO1 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
SCO1 - Primary Literature (33)
| Reference | Other Genes Addressed |
|---|---|
| Ask M, et al. (2013) The influence of HMF and furfural on redox-balance and energy-state of xylose-utilizing Saccharomyces cerevisiae. Biotechnol Biofuels 6(1):22 | |
| Gamberi T, et al. (2012) Evaluation of SCO1 deletion on Saccharomyces cerevisiae metabolism through a proteomic approach. Proteomics 12(11):1767-80 | |
| Steinebrunner I, et al. (2011) HCC1, the Arabidopsis homologue of the yeast mitochondrial copper chaperone SCO1, is essential for embryonic development. J Exp Bot 62(1):319-30 | |
| Veniamin S, et al. (2011) Characterization of the peroxide sensitivity of COX-deficient yeast strains reveals unexpected relationships between COX assembly proteins. Free Radic Biol Med 51(8):1589-600 | |
| Stoycheva T, et al. (2010) The role of reactive oxygen species in the induction of Ty1 retrotransposition in Saccharomyces cerevisiae. Yeast 27(5):259-67 | |
| Gamberi T, et al. (2009) Novel insights into phenotype and mitochondrial proteome of yeast mutants lacking proteins Sco1p or Sco2p. Mitochondrion 9(2):103-114 | |
| Marchi E and Cavalieri D (2008) Yeast as a model to investigate the mitochondrial role in adaptation to dietary fat and calorie surplus. Genes Nutr 3(3-4):159-66 | |
| Rigby K, et al. (2008) Mapping the functional interaction of sco1 and cox2 in cytochrome oxidase biogenesis. J Biol Chem 283(22):15015-22 | |
| Stamenova R, et al. (2008) Transposition of Saccharomyces cerevisiae Ty1 retrotransposon is activated by improper cryopreservation. Cryobiology 56(3):241-7 | |
| Khalimonchuk O, et al. (2007) Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase. J Biol Chem 282(24):17442-9 | |
| Abajian C and Rosenzweig AC (2006) Crystal structure of yeast Sco1. J Biol Inorg Chem 11(4):459-66 | |
| Cobine PA, et al. (2006) The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding. J Biol Chem 281(18):12270-6 | |
| Viau C, et al. (2006) Sensitivity to Sn(2+) of the Yeast Saccharomyces cerevisiae Depends on General Energy Metabolism, Metal Transport, Anti-Oxidative Defences, and DNA Repair. Biometals 19(6):705-14 | |
| Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 | |
| Horng YC, et al. (2005) Human Sco1 and Sco2 function as copper-binding proteins. J Biol Chem 280(40):34113-22 | |
| Khalimonchuk O, et al. (2005) Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the Cu(B) site formation of cytochrome c oxidase. Curr Genet 47(4):223-33 | |
| Williams JC, et al. (2005) Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. J Biol Chem 280(15):15202-11 | |
| Balatri E, et al. (2003) Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly. Structure 11(11):1431-43 | |
| Beers J, et al. (2002) Purification and characterization of yeast Sco1p, a mitochondrial copper protein. J Biol Chem 277(25):22185-90 | |
| Lode A, et al. (2002) Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p. Yeast 19(11):909-22 | |
| Nittis T, et al. (2001) Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J Biol Chem 276(45):42520-6 | |
| Chinenov YV (2000) Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes. J Mol Med (Berl) 78(5):239-42 | |
| Dickinson EK, et al. (2000) A human SCO2 mutation helps define the role of Sco1p in the cytochrome oxidase assembly pathway. J Biol Chem 275(35):26780-5 | |
| Lode A, et al. (2000) Mitochondrial copper metabolism in yeast: interaction between Sco1p and Cox2p. FEBS Lett 485(1):19-24 | |
| Paret C, et al. (2000) The P(174)L mutation in the human hSCO1 gene affects the assembly of cytochrome c oxidase. Biochem Biophys Res Commun 279(2):341-7 | |
| Rentzsch A, et al. (1999) Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase. Curr Genet 35(2):103-8 | |
| Glerum DM, et al. (1996) Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J Biol Chem 271(24):14504-9 | |
| Glerum DM, et al. (1996) SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J Biol Chem 271(34):20531-5 | |
| Buchwald P, et al. (1991) Immunological identification of yeast SCO1 protein as a component of the inner mitochondrial membrane. Mol Gen Genet 229(3):413-20 | |
| Krummeck G, et al. (1991) AUG codons in the RNA leader sequences of the yeast PET genes CBS1 and SCO1 have no influence on translation efficiency. Curr Genet 20(6):465-9 |



