Evidence map›Paper›PMID 23388626›Full record

ReviewCold Spring Harbor perspectives in biology2013

Endoplasmic reticulum stress sensing in the unfolded protein response.

Brooke M Gardner, David Pincus, Katja Gotthardt, Ciara M Gallagher, Peter Walter

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 437 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
437citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

437 citing papers in PubMed, 1 synthesis or guideline pooled it, 726 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
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  6. Article
  7. Article
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  9. Article
  10. Review
  11. Review
  12. Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Article
  14. Tumor necrosis factor α-induced endoplasmic reticulum stress promotes airway smooth muscle cell proliferation.American journal of physiology. Lung cellular and molecular physiology · 2026
    Article
  15. Article
  16. Article
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  18. Article
  19. Journal of microbiology and biotechnology · 2025
    Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Brooke M GardnerDepartment of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158, USA.
David Pincus
Katja Gotthardt
Ciara M Gallagher
Peter Walter
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BABBITT, PATRICIA CLEMENT · 1985 to 2011
$17.6M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
NCRR NIH HHS 2P41RR001081NCRR NIH HHS P41 RR001081NIGMS NIH HHS 9P41GM103311NIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded proteins and exit as either folded proteins in transit to their target organelles or as misfolded proteins targeted for degradation. The unfolded protein response (UPR) maintains the protein-folding homeostasis within the ER, ensuring that the protein-folding capacity of the ER meets the load of client proteins. Activation of the UPR depends on three ER stress sensor proteins, Ire1, PERK, and ATF6. Although the consequences of activation are well understood, how these sensors detect ER stress remains unclear. Recent evidence suggests that yeast Ire1 directly binds to unfolded proteins, which induces its oligomerization and activation. BiP dissociation from Ire1 regulates this oligomeric equilibrium, ultimately modulating Ire1's sensitivity and duration of activation. The mechanistic principles of ER stress sensing are the focus of this review.

Indexed as

Models, BiologicalActivating Transcription Factor 6eIF-2 KinaseEndoplasmic Reticulum StressEndoribonucleasesFungal ProteinsHSP70 Heat-Shock ProteinsHumansMembrane ProteinsPolymerizationProtein Serine-Threonine KinasesSignal TransductionUnfolded Protein ResponseYeastsActivating Transcription Factor 6ATF6 protein, humanEIF2AK3 protein, humaneIF-2 KinaseEndoribonucleasesERN2 protein, humanFungal ProteinsHSP70 Heat-Shock ProteinsKAR2 protein, yeastMembrane ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID23388626
PMCPMC3578356
OpenAlexW2153074213

What OpenQuestion holds

Textmetadata
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.