Evidence map›Paper›PMID 21309747›Full record

ReviewThe Biochemical journal2011

Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting.

Min Ni, Yi Zhang, Amy S Lee

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 318 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
318citing papers in PubMed, 1 pooled it
18.0field-weighted citation impact, top 1% 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

318 citing papers in PubMed, 1 synthesis or guideline pooled it, 530 citations in OpenAlex.

  1. Guideline
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. How Do Cancer Cells Fuse and Why?Advances in experimental medicine and biology · 2026
    Review
  11. Article
  12. Targeted Degradation of sGRP78 Alleviates the Immunosuppressive Tumor Microenvironment.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  13. Journal of microbiology and biotechnology · 2025
    Article
  14. Article
  15. Article
  16. Review
  17. Stress-induced translocation of the endoplasmic reticulum chaperone GRP78/BiP and its impact on human disease and therapy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Review
  20. Review

258 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.

Min NiDepartment of Biochemistry and Molecular Biology, University of Southern California Keck School of Medicine, USC Norris Comprehensive Cancer Center, 1441 Eastlake Avenue, Los Angeles, CA 90089-9176, USA.
Yi Zhang
Amy S Lee
University of Southern California · US

Funding

STRESS INDUCTION OF THE GLUCOSE REGULATED PROTEINSR01CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1985 to 2021
$11.1M
MECHANISM OF ANTI-APOPTOTIC FUNCTION OF GRP78/BiPR01CA111700 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 2005 to 2008
$1.1M
Endoplasmic Reticulum Chaperone as a Regulator of Obesity and DiabetesR01DK079999 · NIDDK · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 2009 to 2010
$776k
COORDINATED GENE EXPRESSION IN MAMMALIAN CELLSR37CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1988 to 1995
–
NCI NIH HHS CA027607NCI NIH HHS CA111700NCI NIH HHS R01 CA027607NCI NIH HHS R01 CA111700NIDDK NIH HHS DK079999NIDDK NIH HHS R01 DK079999
6 · The paper itself

Abstract

GRP78 (glucose-regulated protein of 78 kDa) is traditionally regarded as a major ER (endoplasmic reticulum) chaperone facilitating protein folding and assembly, protein quality control, Ca(2+) binding and regulating ER stress signalling. It is a potent anti-apoptotic protein and plays a critical role in tumour cell survival, tumour progression and angiogenesis, metastasis and resistance to therapy. Recent evidence shows that GRP78 can also exist outside the ER. The finding that GRP78 is present on the surface of cancer but not normal cells in vivo represents a paradigm shift on how GRP78 controls cell homoeostasis and provides an opportunity for cancer-specific targeting. Cell-surface GRP78 has emerged as an important regulator of tumour cell signalling and viability as it forms complexes with a rapidly expanding repertoire of cell-surface protein partners, regulating proliferation, PI3K (phosphoinositide 3-kinase)/Akt signalling and cell viability. Evidence is also emerging that GRP78 serves as a receptor for viral entry into host cells. Additionally, a novel cytosolic form of GRP78 has been discovered prominently in leukaemia cells. These, coupled with reports of nucleus- and mitochondria-localized forms of GRP78, point to the previously unanticipated role of GRP78 beyond the ER that may be critical for cell viability and therapeutic targeting.

Indexed as

Signal TransductionAnimalsCell MembraneCell NucleusCell SurvivalCytosolEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHumansModels, BiologicalNeoplasmsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, human

Identifiers

PMID21309747
PMCPMC3353658
OpenAlexW2142282255

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.