ERV1/YGR029W Literature Guide Help

Other names published for ERV1: YGR029W

ERV1 - Non-Fungal Related Genes/Proteins (23)

ReferenceOther Genes Addressed
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
Guo PC, et al.  (2012) Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space. J Biol Chem 287(42):34961-9
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
Carrie C, et al.  (2010) Conserved and Novel Functions for Arabidopsis thaliana MIA40 in Assembly of Proteins in Mitochondria and Peroxisomes. J Biol Chem 285(46):36138-48
Sharma AK, et al.  (2010) Cytosolic Iron-Sulfur Cluster Assembly (CIA) System: Factors, Mechanism, and Relevance to Cellular Iron Regulation. J Biol Chem 285(35):26745-51
Ang SK and Lu H  (2009) Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p. J Biol Chem 284(42):28754-61
Daithankar VN, et al.  (2009) Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space. Biochemistry 48(22):4828-37
Di Fonzo A, et al.  (2009) The mitochondrial disulfide relay system protein GFER is mutated in autosomal-recessive myopathy with cataract and combined respiratory-chain deficiency. Am J Hum Genet 84(5):594-604
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
Szklarczyk R and Huynen MA  (2009) Expansion of the human mitochondrial proteome by intra- and inter-compartmental protein duplication. Genome Biol 10(11):R135
Figueroa-Martinez F, et al.  (2008) Reconstructing the Mitochondrial Protein Import Machinery of Chlamydomonas reinhardtii. Genetics 179(1):149-55
Kawamata H and Manfredi G  (2008) Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria. Hum Mol Genet 17(21):3303-17
Coppock DL and Thorpe C  (2006) Multidomain flavin-dependent sulfhydryl oxidases. Antioxid Redox Signal 8(3-4):300-11
Levitan A, et al.  (2004) Unique features of plant mitochondrial sulfhydryl oxidase. J Biol Chem 279(19):20002-8
Vilella F, et al.  (2004) Evolution and cellular function of monothiol glutaredoxins: involvement in iron-sulphur cluster assembly. Comp Funct Genomics 5(4):328-41
Lange H, et al.  (2001) An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep 2(8):715-20
Lee J, et al.  (2000) Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett 477(1-2):62-6
Hofhaus G, et al.  (1999) Highly divergent amino termini of the homologous human ALR and yeast scERV1 gene products define species specific differences in cellular localization. Eur J Cell Biol 78(5):349-56
Wang G, et al.  (1999) Identification and characterization of receptor for mammalian hepatopoietin that is homologous to yeast ERV1. J Biol Chem 274(17):11469-72
Coppock DL, et al.  (1998) The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Genomics 54(3):460-8
Stein G and Lisowsky T  (1998) Functional comparison of the yeast scERV1 and scERV2 genes. Yeast 14(2):171-80
Lisowsky T  (1996) Removal of an intron with unique 3' branch site creates an amino-terminal protein sequence directing the scERV1 gene product to mitochondria. Yeast 12(15):1501-10
Lisowsky T, et al.  (1995) A new human gene located in the PKD1 region of chromosome 16 is a functional homologue to ERV1 of yeast. Genomics 29(3):690-7