Evidence map›Paper›PMID 22079671›Full record

ReviewBiochimica et biophysica acta2012

GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.

Michal Marzec, Davide Eletto, Yair Argon

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 233 papers.

0numbers the graph read from it
0cells of the map it votes in
233citing papers in PubMed
7.4field-weighted citation impact, top 2% of its field
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

233 citing papers in PubMed, 415 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Exosomal NEAT1 from tumor stem cells induces SIRPAJournal of experimental & clinical cancer research : CR · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Evaluating the Effect of RNA Interference of Two Heat Shock Proteins (Biochemistry & molecular biology journal · 2026
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Molecular mechanisms attributed to colistin renal proximal tubular epithelial cytotoxicity.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2025
    Review
  17. Article
  18. Review
  19. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  20. Article

173 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 1 institution in 1 country.

Michal MarzecDepartment of Pathology and Lab Medicine, The Children's Hospital of Philadelphia, Philadelphia, PA, USA.
Davide Eletto
Yair Argon
Children's Hospital of Philadelphia · US

Funding

TRAINING GRANT IN GENETICST32GM007748 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Anne O'Donnell-Luria, Louise Wilkins-Haug · 1985 to 2026
$12.0M
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
Regulation of IGF-1 by Human GRP94K01AG040153 · NIA · CHILDREN'S HOSP OF PHILADELPHIA · PI MARZEC, MICHAL TOMASZ · 2011 to 2014
$454k
NIA NIH HHS AG040153NIA NIH HHS AG18001NIA NIH HHS K01 AG040153NIA NIH HHS R01 AG018001NIGMS NIH HHS GM07748NIGMS NIH HHS R01 GM077480NIGMS NIH HHS T32 GM007748
6 · The paper itself

Abstract

Glucose-regulated protein 94 is the HSP90-like protein in the lumen of the endoplasmic reticulum and therefore it chaperones secreted and membrane proteins. It has essential functions in development and physiology of multicellular organisms, at least in part because of this unique clientele. GRP94 shares many biochemical features with other HSP90 proteins, in particular its domain structure and ATPase activity, but also displays distinct activities, such as calcium binding, necessitated by the conditions in the endoplasmic reticulum. GRP94's mode of action varies from the general HSP90 theme in the conformational changes induced by nucleotide binding, and in its interactions with co-chaperones, which are very different from known cytosolic co-chaperones. GRP94 is more selective than many of the ER chaperones and the basis for this selectivity remains obscure. Recent development of molecular tools and functional assays has expanded the spectrum of clients that rely on GRP94 activity, but it is still not clear how the chaperone binds them, or what aspect of folding it impacts. These mechanistic questions and the regulation of GRP94 activity by other proteins and by post-translational modification differences pose new questions and present future research avenues. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).

Indexed as

Amino Acid SequenceAnimalsEndoplasmic ReticulumHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMembrane ProteinsMolecular Sequence DataProtein Foldingglucose-regulated proteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMembrane Proteins

Identifiers

PMID22079671
PMCPMC3443595
OpenAlexW2003801319

What OpenQuestion holds

Textmetadata
LicenceTDM
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.