Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast.
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Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulumProtein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applicationsThe protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membraneThe Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible MoleculeCoordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein.A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursorsThe Ost1p subunit of yeast oligosaccharyl transferase recognizes the peptide glycosylation site sequence, -Asn-X-Ser/Thr-.The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system.The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation.ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteinsCole-Carpenter syndrome is caused by a heterozygous missense mutation in P4HBEndoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunitThe complete general secretory pathway in gram-negative bacteriaCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsExtracellular protein disulfide isomerase regulates ligand-binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammationPlatelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in miceDifferent contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding.Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome.Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C.The protein disulphide-isomerase family: unravelling a string of folds.Protein disulfide isomerase in thrombosis and vascular inflammationIdentification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitopeNovel roles for protein disulphide isomerase in disease states: a double edged sword?The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection.Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5pSignal-mediated retrieval of a membrane protein from the Golgi to the ER in yeastSignal sequences specify the targeting route to the endoplasmic reticulum membraneExport of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control.Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein responseA deletion polymorphism in the human alpha-2-macroglobulin (A2M) geneBrefeldin A reversibly blocks early but not late protein transport steps in the yeast secretory pathwayCatalysis of protein disulfide bond isomerization in a homogeneous substrateThe yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.Retrieval of HDEL proteins is required for growth of yeast cells.Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum.Interaction of transcription factor Sp1 with the promoter of the gene for the multifunctional protein disulphide isomerase polypeptide.Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum.Replacement of domain b of human protein disulfide isomerase-related protein with domain b' of human protein disulfide isomerase dramatically increases its chaperone activity.
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P2860
Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Glycosylation site binding pro ...... l for cell viability in yeast.
@en
Glycosylation site binding pro ...... l for cell viability in yeast.
@nl
type
label
Glycosylation site binding pro ...... l for cell viability in yeast.
@en
Glycosylation site binding pro ...... l for cell viability in yeast.
@nl
prefLabel
Glycosylation site binding pro ...... l for cell viability in yeast.
@en
Glycosylation site binding pro ...... l for cell viability in yeast.
@nl
P2093
P2860
P356
P1476
Glycosylation site binding pro ...... l for cell viability in yeast.
@en
P2093
H A Kaplan
H Tachikawa
M LaMantia
T Mizunaga
W J Lennarz
P2860
P304
P356
10.1073/PNAS.88.10.4453
P407
P577
1991-05-01T00:00:00Z