Evidence map›Paper›PMID 17481612›Full record

ReviewFEBS letters2007

ER chaperones in mammalian development and human diseases.

Min Ni, Amy S Lee

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 350 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
350citing papers in PubMed, 1 pooled it
22.4field-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

350 citing papers in PubMed, 1 synthesis or guideline pooled it, 729 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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
  13. Article
  14. Article
  15. Article
  16. Review
  17. Screening and identification of protein interacting with goose astrovirus.Frontiers in cellular and infection microbiology · 2025
    Article
  18. Review
  19. Article
  20. Article

290 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 1 institution in 1 country.

Min NiDepartment of Biochemistry and Molecular Biology, USC/Norris Comprehensive Cancer Center, Keck School of Medicine of the University of Southern California, 1441 Eastlake Ave., Los Angeles, CA 90089-9176, United States.
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
COORDINATED GENE EXPRESSION IN MAMMALIAN CELLSR37CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1988 to 1995
–
NCI NIH HHS CA111700NCI NIH HHS CA27607NCI NIH HHS R01 CA027607NCI NIH HHS R01 CA111700
6 · The paper itself

Abstract

The field of endoplasmic reticulum (ER) stress in mammalian cells has expanded rapidly during the past decade, contributing to understanding of the molecular pathways that allow cells to adapt to perturbations in ER homeostasis. One major mechanism is mediated by molecular ER chaperones which are critical not only for quality control of proteins processed in the ER, but also for regulation of ER signaling in response to ER stress. Here, we summarized the properties and functions of GRP78/BiP, GRP94/gp96, GRP170/ORP150, GRP58/ERp57, PDI, ERp72, calnexin, calreticulin, EDEM, Herp and co-chaperones SIL1 and P58(IPK) and their role in development and diseases. Many of the new insights are derived from recently constructed mouse models where the genes encoding the chaperones are genetically altered, providing invaluable tools for examining the physiological involvement of the ER chaperones in vivo.

Indexed as

DiseaseGrowth and DevelopmentAnimalsBacterial ToxinsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHumansMiceMolecular ChaperonesProtein FoldingBacterial ToxinsEndoplasmic Reticulum Chaperone BiPHSPA5 protein, humanHspa5 protein, mouseMolecular Chaperones

Identifiers

PMID17481612
PMCPMC2040386
OpenAlexW2139396663

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.