Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control (Q24677354)

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published in

Journal of Cell Biology

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volume

165

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issue

1

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page(s)

41-52

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ImageQuant

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2172089/fullTextXML

inferred from PubMed Central ID database lookup

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28 September 2017

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28 September 2017

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Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD.

30 May 2018

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Crossref

https://api.crossref.org/works/10.1083%2FJCB.200309132

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

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1083%2FJCB.200309132

Quality Control in the Yeast Secretory Pathway

21 January 2018

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Crossref

https://api.crossref.org/works/10.1083%2FJCB.200309132

Targeting to the endoplasmic reticulum in yeast cells by determinants present in transmembrane domains

21 January 2018

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12 December 2020

The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct

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12 December 2020

Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi

1 reference

12 December 2020

Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast

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12 December 2020

Identifiers

DOI

10.1083/JCB.200309132

1 reference

release_yaefgyx6v5ghjos7yrlcew7hl4

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/yaefgyx6v5ghjos7yrlcew7hl4

24 November 2022

mapped directly with Wikidata item

1 reference

1 reference

PubMed publication ID

15078901

1 reference