Evidence map›Paper›PMID 30396883›Full record

ReviewCold Spring Harbor perspectives in biology2019

Early Events in the Endoplasmic Reticulum Unfolded Protein Response.

Steffen Preissler, David Ron

Erratum issuedOpen access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
–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

110 citing papers in PubMed, 202 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
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  11. Article
  12. Review
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  14. Review
  15. Article
  16. Review
  17. Article
  18. Oncotarget · 2025
    Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Steffen PreisslerCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
David RonCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
University of Cambridge · GB

Funding

Wellcome Trust 100140Wellcome Trust 200848/Z/16/Z
6 · The paper itself

Abstract

The physiological consequences of the unfolded protein response (UPR) are mediated by changes in gene expression. Underlying them are rapid processes involving preexisting components. We review recent insights gained into the regulation of the endoplasmic reticulum (ER) Hsp70 chaperone BiP, whose incorporation into inactive oligomers and reversible AMPylation and de-AMPylation present a first line of response to fluctuating levels of unfolded proteins. BiP activity is tied to the regulation of the UPR transducers by a recently discovered cycle of ER-localized, J protein-mediated formation of a repressive IRE1-BiP complex, whose working we contrast to an alternative model for UPR regulation that relies on direct recognition of unfolded proteins. We conclude with a discussion of mechanisms that repress messenger RNA (mRNA) translation to limit the flux of newly synthesized proteins into the ER, a rapid adaptation that does not rely on new macromolecule biosynthesis.

Indexed as

Unfolded Protein ResponseEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsProtein BiosynthesisProtein Processing, Post-TranslationalEndoplasmic Reticulum Chaperone BiPHeat-Shock Proteins

Identifiers

PMID30396883
PMCPMC6442202
OpenAlexW2900242960

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.