Other names published for ERV2: YPR037C
ERV2 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
- Literature Curation Summary
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- All genome-wide analysis papers
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| Reference | Other Genes Addressed |
|---|---|
| Liu Z, et al. (2013) Anaerobic a-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae. Appl Environ Microbiol 79(9):2962-7 | |
| Daithankar VN, et al. (2012) Flavin-linked Erv-family sulfhydryl oxidases release superoxide anion during catalytic turnover. Biochemistry 51(1):265-72 | |
| Davey HM, et al. (2012) Genome-wide analysis of longevity in nutrient-deprived Saccharomyces cerevisiae reveals importance of recycling in maintaining cell viability. Environ Microbiol 14(5):1249-60 | |
| Fomenko DE and Gladyshev VN (2012) Comparative genomics of thiol oxidoreductases reveals widespread and essential functions of thiol-based redox control of cellular processes. Antioxid Redox Signal 16(3):193-201 | |
| Sevier C (2012) Erv2 and quiescin sulfhydryl oxidases: Erv-domain enzymes associated with the secretory pathway. Antioxid Redox Signal 16(8):800-8 | |
| Bien M, et al. (2010) Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Mol Cell 37(4):516-28 | |
| Endo T, et al. (2010) Structural basis for the disulfide relay system in the mitochondrial intermembrane space. Antioxid Redox Signal 13(9):1359-73 | |
| Hacioglu E, et al. (2010) The roles of thiol oxidoreductases in yeast replicative aging. Mech Ageing Dev 131(11-12):692-9 | |
| Harvey AR, et al. (2010) Identification and characterisation of eroA and ervA, encoding two putative thiol oxidases from Aspergillus niger. Gene 461(1-2):32-41 | |
| Kodali VK and Thorpe C (2010) Oxidative protein folding and the quiescin-sulfhydryl oxidase family of flavoproteins. Antioxid Redox Signal 13(8):1217-30 | |
| Marino SM and Gladyshev VN (2009) A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. PLoS Comput Biol 5(5):e1000383 | |
| Christis C, et al. (2008) Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol. FEBS J 275(19):4700-27 | |
| Fass D (2008) The Erv family of sulfhydryl oxidases. Biochim Biophys Acta 1783(4):557-66 | |
| Chakravarthi S, et al. (2007) Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Biochem J 404(3):403-11 | |
| Lopez-Mirabal HR and Winther JR (2007) The thiol oxidant dipyridyl disulfide can supply the PDI-Ero1p pathway with additional oxidative equivalents. Antonie Van Leeuwenhoek 92(4):463-72 | |
| Wang W, et al. (2007) Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase. Biochemistry 46(11):3246-54 | |
| Cliften PF, et al. (2006) After the duplication: gene loss and adaptation in Saccharomyces genomes. Genetics 172(2):863-72 | |
| Coppock DL and Thorpe C (2006) Multidomain flavin-dependent sulfhydryl oxidases. Antioxid Redox Signal 8(3-4):300-11 | |
| Gatzidou E, et al. (2006) Insights on augmenter of liver regeneration cloning and function. World J Gastroenterol 12(31):4951-8 | |
| Gruber CW, et al. (2006) Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci 31(8):455-64 | |
| Sevier CS and Kaiser CA (2006) Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid Redox Signal 8(5-6):797-811 | |
| Vala A, et al. (2005) Structural determinants of substrate access to the disulfide oxidase Erv2p. J Mol Biol 354(4):952-66 | |
| Gross E, et al. (2004) Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117(5):601-10 | |
| Hiniker A and Bardwell JC (2004) Disulfide relays between and within proteins: the Ero1p structure. Trends Biochem Sci 29(10):516-9 | |
| Levitan A, et al. (2004) Unique features of plant mitochondrial sulfhydryl oxidase. J Biol Chem 279(19):20002-8 | |
| Raje S and Thorpe C (2003) Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation. Biochemistry 42(15):4560-8 | |
| Collet JF and Bardwell JC (2002) Disulfides out of thin air. Nat Struct Biol 9(1):2-3 | |
| Gross E, et al. (2002) A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Biol 9(1):61-7 | |
| Marc P, et al. (2002) Genome-wide analysis of mRNAs targeted to yeast mitochondria. EMBO Rep 3(2):159-64 | |
| Sevier CS and Kaiser CA (2002) Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol 3(11):836-47 |





