Evidence map›Paper›PMID 20223290›Full record

ReviewSeminars in cell & developmental biology2010

GRP94 in ER quality control and stress responses.

Davide Eletto, Devin Dersh, Yair Argon

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing 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

128 citing papers in PubMed.

  1. Article
  2. The Pathogenesis of Preeclampsia: Hypoxia and the Unfolded Protein Response.Reproductive sciences (Thousand Oaks, Calif.) · 2026
    Review
  3. Article
  4. Review
  5. Evaluating the Effect of RNA Interference of Two Heat Shock Proteins (Biochemistry & molecular biology journal · 2026
    Article
  6. Review
  7. ATM interaction with GRP94 modulates oncogenic receptor expression and signaling and microglial activation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  9. Article
  10. Review
  11. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Dysregulation of N-glycosylation byInternational journal of biological sciences · 2025
    Article
  19. Article
  20. Review

68 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.

Davide ElettoDivision of Cell Pathology, Department of Pathology and Lab Medicine, The Children's Hospital of Philadelphia and the University of Pennsylvania, 3615 Civic Center Blvd., Philadelphia, PA 19104, USA.
Devin Dersh
Yair Argon

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Regulation of IGF Levels in Development and in AgingR01AG018001 · NIA · UNIVERSITY OF CHICAGO · PI ARGON, YAIR · 2000 to 2016
$5.9M
Regulation of insulin-like growth factors by the ER chaperone GRP94R01GM077480 · NIGMS · CHILDREN'S HOSP OF PHILADELPHIA · PI ARGON, YAIR · 2010 to 2013
$1.3M
NIA NIH HHS R01 AG018001NIGMS NIH HHS R01 GM077480NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

A system of endoplasmic reticulum (ER) chaperones has evolved to optimize the output of properly folded secretory and membrane proteins. An important player in this network is Glucose Regulated Protein 94 (GRP94). Over the last decade, new structural and functional data have begun to delineate the unique characteristics of GRP94 and have solidified its importance in ER quality control pathways. This review describes our current understanding of GRP94 and the four ways in which it contributes to the ER quality control: (1) chaperoning the folding of proteins; (2) interacting with other components of the ER protein folding machinery; (3) storing calcium; and (4) assisting in the targeting of malfolded proteins to ER-associated degradation (ERAD).

Indexed as

AnimalsEndoplasmic ReticulumHSP70 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesProtein FoldingProtein Processing, Post-TranslationalProteinsglucose-regulated proteinsHSP70 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesProteins

Identifiers

PMID20223290
PMCPMC3676867

What OpenQuestion holds

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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.