PDI1/YCL043C Literature Guide Help

Other names published for PDI1: MFP1, TRG1, protein disulfide isomerase PDI1, YCL043C

PDI1 - Function/Process (31)

Results: 1 - 30 of 31 records
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ReferenceOther Genes Addressed
Grubb S, et al.  (2012) Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Mol Biol Cell 23(4):520-32
Gauss R, et al.  (2011) A complex of pdi1p and the mannosidase htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum. Mol Cell 42(6):782-93
Hacioglu E, et al.  (2010) The roles of thiol oxidoreductases in yeast replicative aging. Mech Ageing Dev 131(11-12):692-9
Tian G, et al.  (2008) The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule. J Biol Chem 283(48):33630-40
Powers SL and Robinson AS  (2007) PDI improves secretion of redox-inactive beta-glucosidase. Biotechnol Prog 23(2):364-9
Gasser B, et al.  (2006) Engineering of Pichia pastoris for improved production of antibody fragments. Biotechnol Bioeng 94(2):353-61
Heiligenstein S, et al.  (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25(20):4717-27
Tian G, et al.  (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124(1):61-73
Wilkinson B, et al.  (2005) A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain. J Biol Chem 280(12):11483-7
Kimura T, et al.  (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65
Solovyov A, et al.  (2004) Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. J Biol Chem 279(33):34095-100
Fetrow JS, et al.  (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14
Katiyar S, et al.  (2001) Studies on the function of yeast protein disulfide isomerase in renaturation of proteins. Biochim Biophys Acta 1548(1):47-56
Norgaard P and Winther JR  (2001) Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem J 358(Pt 1):269-74
Norgaard P, et al.  (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62
Sevier CS, et al.  (2001) A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3(10):874-82
Song Y, et al.  (2001) Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J Biochem 130(6):757-64
Frand AR and Kaiser CA  (2000) Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol Biol Cell 11(9):2833-43
Tu BP, et al.  (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290(5496):1571-4
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
Gillece P, et al.  (1999) Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol 147(7):1443-56
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
Luz JM and Lennarz WJ  (1998) The nonactive site cysteine residues of yeast protein disulfide isomerase are not required for cell viability. Biochem Biophys Res Commun 248(3):621-7
Dunn A, et al.  (1995) Protein disulphide isomerase (PDI) is required for the secretion of a native disulphide-bonded protein from Saccharomyces cerevisiae. Biochem Soc Trans 23(1):78S
Hayano T, et al.  (1995) Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett 377(3):505-11
Laboissiere MC, et al.  (1995) The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 270(47):28006-9
LaMantia ML and Lennarz WJ  (1993) The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74(5):899-908
Gunther R, et al.  (1991) The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase. J Biol Chem 266(36):24557-63
LaMantia M, et al.  (1991) Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc Natl Acad Sci U S A 88(10):4453-7
Scherens B, et al.  (1991) Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms. Yeast 7(2):185-93
Results: 1 - 30 of 31 records
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