Evidence map›Paper›PMID 30670466›Full record

ReviewCold Spring Harbor perspectives in biology2019

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum.

G Elif Karagöz, Diego Acosta-Alvear, Peter Walter

Open 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. Cited by 168 papers.

0numbers the graph read from it
0cells of the map it votes in
168citing 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

168 citing papers in PubMed, 311 citations in OpenAlex.

  1. Systematic optimization ofEngineering microbiology · 2026
    Review
  2. Review
  3. Biomedicines · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Disruption of thePathogens (Basel, Switzerland) · 2026
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026
    Review
  13. Article
  14. Cnpy1 is a candidate endoplasmic reticulum chaperone of vomeronasal type 2 GPCRs.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

108 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

3 authors at 2 institutions in 1 country.

G Elif KaragözHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94143.
Diego Acosta-AlvearDepartment of Molecular, Cellular, and Developmental Biology, University of California at Santa Barbara, Santa Barbara, California 93106.
Peter WalterHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94143.
Howard Hughes Medical Institute · USUniversity of California, Santa Barbara · US

Funding

MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR01GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2023
$7.6M
NIGMS NIH HHS R01 GM032384
6 · The paper itself

Abstract

Most of the secreted and plasma membrane proteins are synthesized on membrane-bound ribosomes on the endoplasmic reticulum (ER). They require engagement of ER-resident chaperones and foldases that assist in their folding and maturation. Since protein homeostasis in the ER is crucial for cellular function, the protein-folding status in the organelle's lumen is continually surveyed by a network of signaling pathways, collectively called the unfolded protein response (UPR). Protein-folding imbalances, or "ER stress," are detected by highly conserved sensors that adjust the ER's protein-folding capacity according to the physiological needs of the cell. We review recent developments in the field that have provided new insights into the ER stress-sensing mechanisms used by UPR sensors and the mechanisms by which they integrate various cellular inputs to adjust the folding capacity of the organelle to accommodate to fluctuations in ER protein-folding demands.

Indexed as

Unfolded Protein ResponseAnimalsCell MembraneEndoplasmic ReticulumEndoplasmic Reticulum StressEndoribonucleasesHomeostasisHumansMembrane ProteinsMolecular ChaperonesProtein BindingProtein FoldingProtein Serine-Threonine KinasesProteomeRibosomesSaccharomyces cerevisiaeEndoribonucleasesERN1 protein, humanMembrane ProteinsMolecular ChaperonesProtein Serine-Threonine KinasesProteome

Identifiers

PMID30670466
PMCPMC6719602
OpenAlexW2913687928

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.