Evidence map›Paper›PMID 23209157›Full record

ReviewCold Spring Harbor perspectives in biology2012

Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation.

David Ron, Heather P Harding

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed, 112 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Multi-omic analysis reveals that theAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Unraveling the Connection: Pain and Endoplasmic Reticulum Stress.International journal of molecular sciences · 2024
    Review
  12. Wogonin, a Compound inNutrients · 2022
    Article
  13. Article
  14. 4-PBA Treatment Improves Bone Phenotypes in the Aga2 Mouse Model of Osteogenesis Imperfecta.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

2 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

2 authors at 2 institutions in 1 country.

David RonMetabolic Research Laboratories, University of Cambridge, and NIHR Cambridge Biomedical Research Centre, Addenbrookes Hospital, Cambridge CB2 0QQ, United Kingdom. dr360@medschl.cam.ac.uk
Heather P Harding
NIHR Cambridge Biomedical Research CentreUniversity of Cambridge · GB

Funding

Metabolic Regulation in the Acute PhaseR37DK047119 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RON, DAVID · 2003 to 2009
$3.0M
METABOLIC REGULATION IN THE ACUTE PHASER01DK047119 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RYOO, HYUNG D · 1999 to 2010
$1.5M
METABOLIC REGULATION IN THE ACUTE-PHASE RESPONSER29DK047119 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RON, DAVID · 1993 to 1997
–
Medical Research Council G0600717NIDDK NIH HHS DK47119NIDDK NIH HHS R01 DK047119NIDDK NIH HHS R37 DK047119Wellcome Trust
6 · The paper itself

Abstract

The flux of newly synthesized proteins entering the endoplasmic reticulum (ER) is under negative regulation by the ER-localized PKR-like ER kinase (PERK). PERK is activated by unfolded protein stress in the ER lumen and inhibits new protein synthesis by the phosphorylation of translation initiation factor eIF2α. This homeostatic mechanism, shared by all animal cells, has proven to be especially important to the well-being of professional secretory cells, notably the endocrine pancreas. PERK, its downstream effectors, and the allied branches of the unfolded protein response intersect broadly with signaling pathways that regulate nutrient assimilation, and ER stress and the response to it have been implicated in the development of the metabolic syndrome accompanying obesity in mammals. Here we review our current understanding of the cell biology underlying these relationships.

Indexed as

Protein FoldingAnimalseIF-2 KinaseEndoplasmic ReticulumEukaryotic Initiation Factor-2Gene Expression RegulationHomeostasisHumansInsulin ResistanceInsulin-Secreting CellsPhosphorylationSignal TransductionUnfolded Protein ResponseeIF-2 KinaseEukaryotic Initiation Factor-2

Identifiers

PMID23209157
PMCPMC3504434
OpenAlexW2155086326

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.