The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum (Q27936188)

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

GOA release 2020-03-11

author name string

A R Frand

series ordinal

1

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C A Kaiser

series ordinal

2

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language of work or name

English

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publication date

January 1998

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1 December 2016

1

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page(s)

161-70

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issue

2

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cites work

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7 January 2021

A pathway for disulfide bond formation in vivo

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Recent developments in the field of iron-sulfur proteins.

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Folding of influenza hemagglutinin in the endoplasmic reticulum

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7 January 2021

Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase

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7 January 2021

Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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7 January 2021

Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon

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Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations

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2.8-A structure of yeast serine carboxypeptidase

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7 January 2021

Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p

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7 January 2021

Protein disulphide isomerase: building bridges in protein folding

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10 Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast

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7 January 2021

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

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7 January 2021

A pathway for targeting soluble misfolded proteins to the yeast vacuole

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7 January 2021

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

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7 January 2021

Oxidized redox state of glutathione in the endoplasmic reticulum

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7 January 2021

Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent

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7 January 2021

In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.

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7 January 2021

Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers

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

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7 January 2021

The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum

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7 January 2021

Diamide: an oxidant probe for thiols

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

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

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7 January 2021

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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7 January 2021

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

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7 January 2021

Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.

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

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7 January 2021

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

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7 January 2021

A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector

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Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme

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The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi.

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7 January 2021

A microbiological assay for the quantitative determination of glutathione

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tRNA ligase is required for regulated mRNA splicing in the unfolded protein response

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7 January 2021

BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast

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7 January 2021

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

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7 January 2021

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

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7 January 2021

10.1016/S1097-2765(00)80017-9

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Consolidated OpenCitations Corpus – April 2017

release_ld6q4drdgzgajjmz3pzdwehzge

490261

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https://api.fatcat.wiki/v0/release/ld6q4drdgzgajjmz3pzdwehzge

24 November 2022

mapped directly with Wikidata item

490261

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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