The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha

scientific article

The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1093/EMBOJ/19.17.4493
P932PMC publication ID302061
P698PubMed publication ID10970843
P5875ResearchGate publication ID12350953

P50authorAnna FassioQ30500571
Adam BenhamQ40634210
P2093author name stringR Sitia
A Cabibbo
I Braakman
N Bulleid
P2860cites workERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulumQ22253168
Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein responseQ22254117
ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assemblyQ24533211
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 BQ24568234
Structure of influenza haemagglutinin at the pH of membrane fusionQ27730888
Crystal structure of the DsbA protein required for disulphide bond formation in vivoQ27732066
Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformationQ27766025
Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymeraseQ27860943
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulumQ27936188
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulumQ27939552
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolutionQ28131812
Pathways for protein disulphide bond formationQ28141294
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I moleculesQ28577478
Thioredoxin--a fold for all reasonsQ29618984
Oxidized redox state of glutathione in the endoplasmic reticulumQ29619789
The thioredoxin superfamily: redundancy, specificity, and gray-area genomicsQ33537167
The protein disulphide-isomerase family: unravelling a string of foldsQ33543247
Fe-S proteins in sensing and regulatory functionsQ33606907
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzymeQ33937247
Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chainsQ35848909
Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomeraseQ36326158
Folding of influenza hemagglutinin in the endoplasmic reticulumQ36530148
Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coliQ37620314
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexinQ38612771
In vivo cross-linking of protein disulfide isomerase to immunoglobulinsQ41464197
Making and breaking disulfide bondsQ41620623
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 cellsQ41824074
Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of the P58 containing compartmentQ42135792
Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulumQ42151080
Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedureQ42286207
Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coliQ42685653
A novel tumour marker related to the c-myc oncogene productQ44045572
Preparation of semiintact cells for study of vesicular trafficking in vitroQ46143948
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 complexQ47934748
Identification of a protein required for disulfide bond formation in vivoQ48201805
Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomesQ50335732
Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulumQ59053405
Glycoproteins form mixed disulphides with oxidoreductases during folding in living cellsQ59098658
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulumQ73151253
Competition between glutathione and protein thiols for disulphide-bond formationQ73177752
The genetics of disulfide bond metabolismQ77936221
Oxidative protein folding is driven by the electron transport systemQ78066764
P433issue17
P407language of work or nameEnglishQ1860
P304page(s)4493-4502
P577publication date2000-09-01
P1433published inThe EMBO JournalQ1278554
P1476titleThe CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
P478volume19

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cites work (P2860)
Q43817419A critical step in the folding of influenza virus HA determined with a novel folding assay
Q35942438A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells
Q36978164A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells
Q39420582Biogenesis of Weibel-Palade bodies in von Willebrand's disease variants with impaired von Willebrand factor intrachain or interchain disulfide bond formation
Q28080871Cellular disulfide bond formation in bioactive peptides and proteins
Q34032642Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation
Q27664438Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI
Q34559609Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1
Q40204873Disulfide-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
Q24297912Disulphide production by Ero1α-PDI relay is rapid and effectively regulated
Q24292308ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
Q39175487Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
Q34991338Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases
Q36890086Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster
Q42423811Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3.
Q39734860Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).
Q44652130FAD Transport and FAD-dependent Protein Thiol Oxidation in Rat Liver Microsomes
Q28214904Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum
Q34157680Formation and transfer of disulphide bonds in living cells
Q36757973Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family
Q44978565Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway
Q34322869Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.
Q34153590Glycoprotein folding in the endoplasmic reticulum
Q57191226Homocysteine causes vascular endothelial dysfunction by disrupting endoplasmic reticulum redox homeostasis
Q43142090Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.
Q39167888Human endoplasmic reticulum oxidoreductin 1-α is a novel predictor for poor prognosis of breast cancer
Q36408006Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response
Q35883238Imexon induces an oxidative endoplasmic reticulum stress response in pancreatic cancer cells
Q41808379Intracellular storage and regulated secretion of von Willebrand factor in quantitative von Willebrand disease
Q33785769Large-scale discovery and characterization of protein regulatory motifs in eukaryotes
Q41864924Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.
Q24291898Manipulation of oxidative protein folding and PDI redox state in mammalian cells
Q93229413Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding
Q37489810Molecular characterization of a Bombyx mori protein disulfide isomerase (bPDI).
Q34545015Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.
Q36778877Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1
Q37367455Overexpression of Endoplasmic Reticulum Oxidoreductin 1-α (ERO1L) Is Associated with Poor Prognosis of Gastric Cancer
Q37771758Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?
Q34222636Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins
Q33941860Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase
Q34357696PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.
Q53122740Plasma cells require autophagy for sustainable immunoglobulin production.
Q37235421Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol
Q40752554Re-evaluation of primary structure, topology, and localization of Scamper, a putative intracellular Ca2+ channel activated by sphingosylphosphocholine
Q30977675Regulated increase in folding capacity prevents unfolded protein stress in the ER.
Q28263496Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
Q28512421Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes
Q37898056Sulfhydryl oxidases: sources, properties, production and applications.
Q34101630The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function
Q28571513The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1‐Lα
Q38054482The oxidative protein folding machinery in plant cells
Q37009261The subcellular distribution of multigene family 110 proteins of African swine fever virus is determined by differences in C-terminal KDEL endoplasmic reticulum retention motifs
Q34433364Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta
Q34319945Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum
Q37343919Two phases of disulfide bond formation have differing requirements for oxygen.
Q46864538Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment
Q36242585Versatility of the endoplasmic reticulum protein folding factory
Q42181768Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
Q34093937Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners
Q61799397Zinc regulates ERp44-dependent protein quality control in the early secretory pathway

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