PDI1/YCL043C Literature Guide Help

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

PDI1 - Genetic Interactions (16)

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
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
Kim JH, et al.  (2009) The unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization. J Biol Chem 284(16):10400-8
Mesecke N, et al.  (2008) A Novel Group of Glutaredoxins in the cis-Golgi Critical for Oxidative Stress Resistance. Mol Biol Cell 19(6):2673-80
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
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
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  (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1(2):161-70
Holst B, et al.  (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38
Tachikawa H, et al.  (1997) Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem Biophys Res Commun 239(3):710-4
Tachikawa H, et al.  (1995) Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett 369(2-3):212-6
Tachibana C and Stevens TH  (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11