(Q27936575)

GOA release 2020-03-11

author name string

Ruoyu Xiao

1

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Bonney Wilkinson

2

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Anton Solovyov

3

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Jakob R Winther

4

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Arne Holmgren

5

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Johanna Lundström-Ljung

6

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Hiram F Gilbert

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

26 November 2004

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published in

1 reference

1 December 2016

279

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page(s)

49780-6

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issue

48

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cites work

Protein disulfide isomerase and assisted protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Oxidative protein folding in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Protein disulfide bond formation in prokaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Functional differences in yeast protein disulfide isomerases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Folding of influenza hemagglutinin in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200

Structural features in a brittle–ductile wax model of continental extension

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M409210200