ERV2/YPR037C Literature Guide Help

Other names published for ERV2: YPR037C

ERV2 Literature Curation Summary

Curated References for ERV2: 35

Date of last curation: 2013-03-07

ReferenceOther 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