scholarly article | Q13442814 |
P50 | author | Anna Fassio | Q30500571 |
Adam Benham | Q40634210 | ||
P2093 | author name string | R Sitia | |
A Cabibbo | |||
I Braakman | |||
N Bulleid | |||
P2860 | cites work | ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum | Q22253168 |
Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response | Q22254117 | ||
ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly | Q24533211 | ||
A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B | Q24568234 | ||
Structure of influenza haemagglutinin at the pH of membrane fusion | Q27730888 | ||
Crystal structure of the DsbA protein required for disulphide bond formation in vivo | Q27732066 | ||
Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation | Q27766025 | ||
Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase | Q27860943 | ||
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum | Q27936188 | ||
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum | Q27939552 | ||
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution | Q28131812 | ||
Pathways for protein disulphide bond formation | Q28141294 | ||
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules | Q28577478 | ||
Thioredoxin--a fold for all reasons | Q29618984 | ||
Oxidized redox state of glutathione in the endoplasmic reticulum | Q29619789 | ||
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics | Q33537167 | ||
The protein disulphide-isomerase family: unravelling a string of folds | Q33543247 | ||
Fe-S proteins in sensing and regulatory functions | Q33606907 | ||
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme | Q33937247 | ||
Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains | Q35848909 | ||
Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase | Q36326158 | ||
Folding of influenza hemagglutinin in the endoplasmic reticulum | Q36530148 | ||
Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli | Q37620314 | ||
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin | Q38612771 | ||
In vivo cross-linking of protein disulfide isomerase to immunoglobulins | Q41464197 | ||
Making and breaking disulfide bonds | Q41620623 | ||
A new cationic liposome reagent mediating nearly quantitative transfection of animal cells. | Q41689368 | ||
The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion. | Q41710374 | ||
The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells | Q41824074 | ||
Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of the P58 containing compartment | Q42135792 | ||
Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum | Q42151080 | ||
Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure | Q42286207 | ||
Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli | Q42685653 | ||
A novel tumour marker related to the c-myc oncogene product | Q44045572 | ||
Preparation of semiintact cells for study of vesicular trafficking in vitro | Q46143948 | ||
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. | Q46203577 | ||
The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex | Q47934748 | ||
Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes | Q50335732 | ||
Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum | Q59053405 | ||
Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells | Q59098658 | ||
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum | Q73151253 | ||
Competition between glutathione and protein thiols for disulphide-bond formation | Q73177752 | ||
The genetics of disulfide bond metabolism | Q77936221 | ||
Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
P433 | issue | 17 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 4493-4502 | |
P577 | publication date | 2000-09-01 | |
P1433 | published in | The EMBO Journal | Q1278554 |
P1476 | title | The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha | |
P478 | volume | 19 |
Q43817419 | A critical step in the folding of influenza virus HA determined with a novel folding assay |
Q35942438 | A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells |
Q36978164 | A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells |
Q39420582 | Biogenesis of Weibel-Palade bodies in von Willebrand's disease variants with impaired von Willebrand factor intrachain or interchain disulfide bond formation |
Q28080871 | Cellular disulfide bond formation in bioactive peptides and proteins |
Q34032642 | Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation |
Q27664438 | Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI |
Q34559609 | Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 |
Q40204873 | Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction |
Q24297912 | Disulphide production by Ero1α-PDI relay is rapid and effectively regulated |
Q24292308 | ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family |
Q39175487 | Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum |
Q34991338 | Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases |
Q36890086 | Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster |
Q42423811 | Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3. |
Q39734860 | Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). |
Q44652130 | FAD Transport and FAD-dependent Protein Thiol Oxidation in Rat Liver Microsomes |
Q28214904 | Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum |
Q34157680 | Formation and transfer of disulphide bonds in living cells |
Q36757973 | Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family |
Q44978565 | Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway |
Q34322869 | Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum. |
Q34153590 | Glycoprotein folding in the endoplasmic reticulum |
Q57191226 | Homocysteine causes vascular endothelial dysfunction by disrupting endoplasmic reticulum redox homeostasis |
Q43142090 | Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase. |
Q39167888 | Human endoplasmic reticulum oxidoreductin 1-α is a novel predictor for poor prognosis of breast cancer |
Q36408006 | Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response |
Q35883238 | Imexon induces an oxidative endoplasmic reticulum stress response in pancreatic cancer cells |
Q41808379 | Intracellular storage and regulated secretion of von Willebrand factor in quantitative von Willebrand disease |
Q33785769 | Large-scale discovery and characterization of protein regulatory motifs in eukaryotes |
Q41864924 | Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. |
Q24291898 | Manipulation of oxidative protein folding and PDI redox state in mammalian cells |
Q93229413 | Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding |
Q37489810 | Molecular characterization of a Bombyx mori protein disulfide isomerase (bPDI). |
Q34545015 | Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta. |
Q36778877 | Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1 |
Q37367455 | Overexpression of Endoplasmic Reticulum Oxidoreductin 1-α (ERO1L) Is Associated with Poor Prognosis of Gastric Cancer |
Q37771758 | Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis? |
Q34222636 | Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins |
Q33941860 | Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase |
Q34357696 | PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. |
Q53122740 | Plasma cells require autophagy for sustainable immunoglobulin production. |
Q37235421 | Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol |
Q40752554 | Re-evaluation of primary structure, topology, and localization of Scamper, a putative intracellular Ca2+ channel activated by sphingosylphosphocholine |
Q30977675 | Regulated increase in folding capacity prevents unfolded protein stress in the ER. |
Q28263496 | Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell |
Q28512421 | Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes |
Q37898056 | Sulfhydryl oxidases: sources, properties, production and applications. |
Q34101630 | The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function |
Q28571513 | The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1‐Lα |
Q38054482 | The oxidative protein folding machinery in plant cells |
Q37009261 | The subcellular distribution of multigene family 110 proteins of African swine fever virus is determined by differences in C-terminal KDEL endoplasmic reticulum retention motifs |
Q34433364 | Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta |
Q34319945 | Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum |
Q37343919 | Two phases of disulfide bond formation have differing requirements for oxygen. |
Q46864538 | Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment |
Q36242585 | Versatility of the endoplasmic reticulum protein folding factory |
Q42181768 | Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum |
Q34093937 | Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners |
Q61799397 | Zinc regulates ERp44-dependent protein quality control in the early secretory pathway |
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