Evidence map›Paper›PMID 29198525›Full record

ArticleCell2017

A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response.

Niko Amin-Wetzel, Reuben A Saunders, Maarten J Kamphuis, Claudia Rato, Steffen Preissler, Heather P Harding, David Ron

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed, 1 pooled it
13.2field-weighted citation impact, top 1% 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

153 citing papers in PubMed, 1 synthesis or guideline pooled it, 251 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Functional Characterization ofInternational journal of molecular sciences · 2026
    Article
  10. Article
  11. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

93 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

7 authors at 1 institution in 1 country.

Niko Amin-WetzelCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Reuben A SaundersCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Maarten J KamphuisCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Claudia RatoCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Steffen PreisslerCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Heather P HardingCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
David RonCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: dr360@medschl.cam.ac.uk.
University of Cambridge · GB

Funding

Wellcome Trust 200848/Z/16/Z
6 · The paper itself

Abstract

When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER-protein-folding capacity to restore protein-folding homeostasis. Unfolded proteins activate UPR signaling across the ER membrane to the nucleus by promoting oligomerization of IRE1, a conserved transmembrane ER stress receptor. However, the coupling of ER stress to IRE1 oligomerization and activation has remained obscure. Here, we report that the ER luminal co-chaperone ERdj4/DNAJB9 is a selective IRE1 repressor that promotes a complex between the luminal Hsp70 BiP and the luminal stress-sensing domain of IRE1α (IRE1

Indexed as

Unfolded Protein ResponseAnimalsCricetinaeEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPEndoribonucleasesHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHumansMembrane ProteinsMolecular ChaperonesProtein FoldingProtein Serine-Threonine KinasesDNAJB9 protein, humanEndoplasmic Reticulum Chaperone BiPEndoribonucleasesERN1 protein, humanHeat-Shock ProteinsHSP40 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesProtein Serine-Threonine KinasesAllosteric RegulationBiological FeedbackEndoplasmic ReticulumFluorescence Resonance Energy TransferHSP70 Heat-Shock ProteinsProtein DimerizationProtein FoldingRepressor ProteinStressUnfolded Protein Response

Identifiers

PMID29198525
PMCPMC5733394
OpenAlexW2774090632

What OpenQuestion holds

Textmetadata
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.