PDI1/YCL043C Literature Guide Help

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

PDI1 - Strains/Constructs (40)

Results: 1 - 30 of 40 records
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ReferenceOther Genes Addressed
Geitner AJ and Schmid FX  (2012) Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activity. J Mol Biol 420(4-5):335-49
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
Izawa T, et al.  (2012) Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation. Mol Biol Cell 23(7):1283-93
Kim S, et al.  (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196(6):713-25
Park YK, et al.  (2012) Effects of Trx2p and Sec23p expression on stable production of hepatitis B surface antigen S domain in recombinant Saccharomyces cerevisiae. J Biotechnol 160(3-4):151-60
Lappi AK and Ruddock LW  (2011) Reexamination of the role of interplay between glutathione and protein disulfide isomerase. J Mol Biol 409(2):238-49
Hacioglu E, et al.  (2010) The roles of thiol oxidoreductases in yeast replicative aging. Mech Ageing Dev 131(11-12):692-9
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
Clerc S, et al.  (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184(1):159-72
Sakoh-Nakatogawa M, et al.  (2009) Roles of Protein-disulfide Isomerase-mediated Disulfide Bond Formation of Yeast Mnl1p in Endoplasmic Reticulum-associated Degradation. J Biol Chem 284(18):11815-25
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Merksamer PI, et al.  (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135(5):933-47
Tian G, et al.  (2008) The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule. J Biol Chem 283(48):33630-40
Gasser B, et al.  (2007) Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl Environ Microbiol 73(20):6499-507
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
Rakestraw A and Wittrup KD  (2006) Contrasting secretory processing of simultaneously expressed heterologous proteins in Saccharomyces cerevisiae. Biotechnol Bioeng 93(5):896-905
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
Vala A, et al.  (2005) Structural determinants of substrate access to the disulfide oxidase Erv2p. J Mol Biol 354(4):952-66
Xu P, et al.  (2005) Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding. Metab Eng 7(4):269-79
Kimura T, et al.  (2004) Functional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins. Biochem J 382(Pt 1):169-76
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
Xiao R, et al.  (2004) The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem 279(48):49780-6
Kramer B, et al.  (2001) Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding. Biochem J 357(Pt 1):83-95
Nakanishi H, et al.  (2001) Hut1 proteins identified in Saccharomyces cerevisiae and Schizosaccharomyces pombe are functional homologues involved in the protein-folding process at the endoplasmic reticulum. Yeast 18(6):543-54
Norgaard P, et al.  (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62
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
Westphal V, et al.  (1999) Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo. J Mol Biol 286(4):1229-39
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
Results: 1 - 30 of 40 records
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