Evidence map›Paper›PMID 23769672›Full record

ArticleMolecular cell2013

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor.

Ojore Benedict Valentine Oka, Marie Anne Pringle, Isabel Myriam Schopp, Ineke Braakman, Neil John Bulleid

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

72 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
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  15. Review
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  17. Activation of the UPR sensor ATF6α is regulated by its redox-dependent dimerization and ER retention by ERp18.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Ojore Benedict Valentine OkaInstitute of Molecular, Cellular and Systems Biology, College of Medical Veterinary and Life Sciences, Davidson Building, University of Glasgow, Glasgow G12 8QQ, UK.
Marie Anne Pringle
Isabel Myriam Schopp
Ineke Braakman
Neil John Bulleid
University of Glasgow · GBUtrecht University · NL

Funding

Wellcome Trust 088053
6 · The paper itself

Abstract

ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known. Here we identify a number of endogenous substrates that form mixed disulfides with ERdj5, greatly expanding its client repertoire. ERdj5 previously had been thought to exclusively reduce disulfides in proteins destined for dislocation to the cytosol for degradation. However, we demonstrate here that for one of the identified substrates, the low-density lipoprotein receptor (LDLR), ERdj5 is required not for degradation, but rather for efficient folding. Our results demonstrate that the crucial role of ERdj5 is to reduce non-native disulfides formed during productive folding and that this requirement is dependent on its interaction with BiP. Hence, ERdj5 acts as the ER reductase, both preparing misfolded proteins for degradation and catalyzing the folding of proteins that form obligatory non-native disulfides.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceCatalytic DomainCell Line, TumorCystineEndoplasmic ReticulumGene Knockdown TechniquesHSP40 Heat-Shock ProteinsHumansMolecular ChaperonesProteasome Endopeptidase ComplexProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein TransportProteolysisCystineDNAJC10 protein, humanHSP40 Heat-Shock ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexReceptors, LDLRNA, Small Interfering

Identifiers

PMID23769672
PMCPMC3906653
OpenAlexW2088167857

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.