Evidence map›Paper›PMID 30563838›Full record

ReviewThe Journal of biological chemistry2019

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.

Kristine Faye R Pobre, Greg J Poet, Linda M Hendershot

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 256 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
256citing papers in PubMed, 1 pooled it
17.5field-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

256 citing papers in PubMed, 1 synthesis or guideline pooled it, 418 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Toxoplasma gondii SIR2A Promotes Tachyzoite Invasion via Lysine Deacetylase Activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026
    Article
  12. Article
  13. Article
  14. Coordinated expression and assembly of BiP, p58Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article

196 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.

Kristine Faye R PobreFrom the Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
Greg J PoetFrom the Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.ORCID 0000-0002-9923-5218
Linda M HendershotFrom the Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105 linda.hendershot@stjude.org.ORCID 0000-0002-5473-0274
St. Jude Children's Research Hospital · US

Funding

Role of Molecular Chaperones in Ig Biosynthesis 11-2008R01GM054068 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI HENDERSHOT, LINDA M · 1996 to 2018
$5.7M
NIGMS NIH HHS R01 GM054068
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) represents the entry point into the secretory pathway where nascent proteins encounter a specialized environment for their folding and maturation. Inherent to these processes is a dedicated quality-control system that detects proteins that fail to mature properly and targets them for cytosolic degradation. An imbalance in protein folding and degradation can result in the accumulation of unfolded proteins in the ER, resulting in the activation of a signaling cascade that restores proper homeostasis in this organelle. The ER heat shock protein 70 (Hsp70) family member BiP is an ATP-dependent chaperone that plays a critical role in these processes. BiP interacts with specific ER-localized DnaJ family members (ERdjs), which stimulate BiP's ATP-dependent substrate interactions, with several ERdjs also binding directly to unfolded protein clients. Recent structural and biochemical studies have provided detailed insights into the allosteric regulation of client binding by BiP and have enhanced our understanding of how specific ERdjs enable BiP to perform its many functions in the ER. In this review, we discuss how BiP's functional cycle and interactions with ERdjs enable it to regulate protein homeostasis in the ER and ensure protein quality control.

Indexed as

Unfolded Protein ResponseAnimalsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPFetal ProteinsHeat-Shock ProteinsHumansMolecular ChaperonesDNAJC14 protein, humanEndoplasmic Reticulum Chaperone BiPFetal ProteinsHeat-Shock ProteinsHSPA5 protein, humanMolecular ChaperonesATPaseBiPendoplasmic reticulum–associated protein degradation (ERAD)endoplasmic reticulum (ER)ER-localized DnaJ proteinsGRP78heat shock protein (HSP)molecular chaperoneprotein foldingprotein misfoldingstress responseunfolded protein response (UPR)

Identifiers

PMID30563838
PMCPMC6369273
OpenAlexW2904223696

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.