Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1 (Q24674605)

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

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title

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

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2

Tom A Rapoport

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author name string

Billy Tsai

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1

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language of work or name

Englisch

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publication date

28 October 2002

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published in

Journal of Cell Biology

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volume

159

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issue

2

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page(s)

207-16

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cites work

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

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PubMed Central

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7 April 2017

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

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7 April 2017

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

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7 April 2017

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

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7 April 2017

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

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7 April 2017

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

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PubMed Central

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7 April 2017

Retro-translocation of proteins from the endoplasmic reticulum into the cytosol

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28 September 2017

Biochemical basis of oxidative protein folding in the endoplasmic reticulum

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

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PubMed Central

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28 September 2017

Membrane traffic and the cellular uptake of cholera toxin

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PubMed Central

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28 September 2017

Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion

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Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

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Cholera toxin is exported from microsomes by the Sec61p complex

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30 May 2018

Protein translocation: tunnel vision

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30 May 2018

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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30 May 2018

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

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Crossref

reference URL

https://api.crossref.org/works/10.1083%2FJCB.200207120

retrieved

21 January 2018

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

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1083%2FJCB.200207120

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21 January 2018

Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1083%2FJCB.200207120

retrieved

21 January 2018

Identifiers

DOI

10.1083/JCB.200207120

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PMC publication ID

2173060

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PubMed publication ID

12403808

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ResearchGate publication ID

11059871

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Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1 (Q24674605)

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Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1 (Q24674605)

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