ERO1/YML130C Literature Guide Help

Other names published for ERO1: YML130C

ERO1 - Mutants/Phenotypes (28)

ReferenceOther Genes Addressed
Kim S, et al.  (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196(6):713-25
Kumar C, et al.  (2011) Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol-redox control. EMBO J 30(10):2044-56
Babour A, et al.  (2010) A Surveillance Pathway Monitors the Fitness of the Endoplasmic Reticulum to Control Its Inheritance. Cell 142(2):256-269
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
Vitu E, et al.  (2010) Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum. J Biol Chem 285(24):18155-65
Tan SX, et al.  (2009) Cu, Zn superoxide dismutase and NADP(H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae. Mol Biol Cell 20(5):1493-508
Merksamer PI, et al.  (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135(5):933-47
Bicknell AA, et al.  (2007) A novel role in cytokinesis reveals a housekeeping function for the unfolded protein response. J Cell Biol 177(6):1017-27
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
Lopez-Mirabal HR, et al.  (2007) Genetic interaction between the ero1-1 and leu2 mutations in Saccharomyces cerevisiae. Biosci Biotechnol Biochem 71(12):2934-42
Sevier CS, et al.  (2007) Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129(2):333-44
Wentz AE and Shusta EV  (2007) A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteins. Appl Environ Microbiol 73(4):1189-98
Kulp MS, et al.  (2006) Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J Biol Chem 281(2):876-84
Rand JD and Grant CM  (2006) The thioredoxin system protects ribosomes against stress-induced aggregation. Mol Biol Cell 17(1):387-401
Sevier CS and Kaiser CA  (2006) Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1. Mol Biol Cell 17(5):2256-66
Takemori Y, et al.  (2006) Stress-induced transcription of the endoplasmic reticulum oxidoreductin gene ERO1 in the yeast Saccharomyces cerevisiae. Mol Genet Genomics 275(1):89-96
Davierwala AP, et al.  (2005) The synthetic genetic interaction spectrum of essential genes. Nat Genet 37(10):1147-52
Lodi T, et al.  (2005) Secretion of human serum albumin by Kluyveromyces lactis overexpressing KlPDI1 and KlERO1. Appl Environ Microbiol 71(8):4359-63
Schuldiner M, et al.  (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123(3):507-19
Haynes CM, et al.  (2004) Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol Cell 15(5):767-76
Kettner K, et al.  (2004) Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p. Yeast 21(12):1035-44
Kadokura H and Beckwith J  (2001) The expanding world of oxidative protein folding. Nat Cell Biol 3(11):E247-9
Pagani M, et al.  (2001) The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. FEBS Lett 508(1):117-20
Frand AR and Kaiser CA  (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77
Frand AR and Kaiser CA  (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1(2):161-70
Pollard MG, et al.  (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1(2):171-82