(Q53059457)

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Different redox sensitivity of endoplasmic reticulum associated degradation clients suggests a novel role for disulphide bonds in secretory proteins.

scientific article published on 4 February 2014

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24697695%20AND%20SRC:MED&resulttype=core&format=json

12 March 2020

Different redox sensitivity of endoplasmic reticulum associated degradation clients suggests a novel role for disulphide bonds in secretory proteins (English)

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24697695%20AND%20SRC:MED&resulttype=core&format=json

12 March 2020

endoplasmic reticulum

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5

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12 March 2020

Iria Medraño-Fernández

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24697695%20AND%20SRC:MED&resulttype=core&format=json

12 March 2020

author name string

Claudio Fagioli

2

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12 March 2020

Alexandre Mezghrani

3

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12 March 2020

Mieko Otsu

4

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12 March 2020

publication date

4 February 2014

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12 March 2020

Biochemistry and Cell Biology

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12 March 2020

92

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12 March 2020

2

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12 March 2020

113-118

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12 March 2020

ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Quality control in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase I times the proteasomal degradation of unassembled immunoglobulin subunits

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Reduction of interchain disulfide bonds precedes the dislocation of Ig-mu chains from the endoplasmic reticulum to the cytosol for proteasomal degradation

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

The action of molecular chaperones in the early secretory pathway

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

ER quality control: the cytoplasmic connection

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Ca2+-dependent redox modulation of SERCA 2b by ERp57.

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER.

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Quality control in the endoplasmic reticulum protein factory

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

One step at a time: endoplasmic reticulum-associated degradation

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

1 reference

https://api.crossref.org/works/10.1139%2FBCB-2013-0090

21 January 2018

Identifiers

10.1139/BCB-2013-0090

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24697695%20AND%20SRC:MED&resulttype=core&format=json

12 March 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24697695%20AND%20SRC:MED&resulttype=core&format=json

12 March 2020

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