Pathways for protein disulphide bond formation (Q28141294)

Principles that govern the folding of protein chains

Europe PubMed Central

title

Pathways for protein disulphide bond formation (English)

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author name string

A R Frand

series ordinal

1

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J W Cuozzo

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2

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C A Kaiser

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3

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language of work or name

English

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publication date

May 2000

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published in

Trends in Cell Biology

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volume

10

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issue

5

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page(s)

203-10

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cites work

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Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

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Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase

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The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity

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Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms

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Folding of influenza hemagglutinin in the endoplasmic reticulum

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Oxidized redox state of glutathione in the endoplasmic reticulum

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The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

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Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

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Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum

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Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum

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Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

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The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds.

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Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion.

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Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner.

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Eps1, a novel PDI-related protein involved in ER quality control in yeast

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Molecular cloning of the gamma-glutamylcysteine synthetase gene of Saccharomyces cerevisiae

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Competition between glutathione and protein thiols for disulphide-bond formation

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Preferential transport of glutathione versus glutathione disulfide in rat liver microsomal vesicles

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Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.

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Kinetic analysis of the mechanism and specificity of protein-disulfide isomerase using fluorescence-quenched peptides

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Protein folding in the bacterial periplasm

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Electron avenue: pathways of disulfide bond formation and isomerization

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Identification of a protein required for disulfide bond formation in vivo.

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Oxidative protein folding is driven by the electron transport system

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DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA

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Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA

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Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli.

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A pathway for disulfide bond formation in vivo

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An in vivo pathway for disulfide bond isomerization in Escherichia coli

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The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase

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Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

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Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57

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The unfolded protein response: an intracellular signalling pathway with many surprising features

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Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells

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Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway

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Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

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The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

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Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase.

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Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp

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