Evidence map›Paper›PMID 30931312›Full record

ReviewFrontiers in molecular biosciences2019

Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1.

Christopher J Adams, Megan C Kopp, Natacha Larburu, Piotr R Nowak, Maruf M U Ali

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 304 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
304citing 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

304 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Trial
  3. The Effects of Disrupting CaMarine biotechnology (New York, N.Y.) · 2026
    Article
  4. Review
  5. Article
  6. The influence of exercise duration on inhibiting endoplasmic reticulum stress in ischemic stroke rats.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Cerebral Accumulation of Gadolinium (GdTomography (Ann Arbor, Mich.) · 2026
    Article
  13. 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
  14. Article
  15. Chemo-/radiotherapy-induced cardiomyopathy: roles of mitochondria and endoplasmic reticulum.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2026
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

244 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.

Christopher J AdamsDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Megan C KoppDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Natacha LarburuDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Piotr R NowakDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Maruf M U AliDepartment of Life Sciences, Imperial College London, London, United Kingdom.

Funding

Cancer Research UK 20752
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is an important site for protein folding and maturation in eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its folding capacity. However, the physiological demands or aberrations in folding may result in an imbalance which can lead to the accumulation of misfolded protein, also known as "ER stress." The unfolded protein response (UPR) is a cell-signaling system that readjusts ER folding capacity to restore protein homeostasis. The key UPR signal activator, IRE1, responds to stress by propagating the UPR signal from the ER to the cytosol. Here, we discuss the structural and molecular basis of IRE1 stress signaling, with particular focus on novel mechanistic advances. We draw a comparison between the recently proposed allosteric model for UPR induction and the role of Hsp70 during polypeptide import to the mitochondrial matrix.

Indexed as

BiPcrystal structuresER stressHsp70IRE1 inositol-requiring enzyme 1unfolded protein response (UPR)

Identifiers

PMID30931312
PMCPMC6423427

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.