Evidence map›Paper›PMID 20651708›Full record

ReviewNature reviews. Molecular cell biology2010

The HSP70 chaperone machinery: J proteins as drivers of functional specificity.

Harm H Kampinga, Elizabeth A Craig

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1,000 papers.

0numbers the graph read from it
0cells of the map it votes in
1,000citing papers in PubMed
36.0field-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

1,000 citing papers in PubMed, 1,722 citations in OpenAlex.

  1. Article
  2. Chaperone-mediated remodelling of mutant huntingtin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Molecular genetics and metabolism reports · 2026
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Human Hsp70 paralogs display selective J-domain interactions tuning proteostasis under stress.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Article
  16. Article
  17. Review
  18. DNAJC12 Stabilizes Phenylalanine Hydroxylase and Facilitates Its Substrate-Dependent Activation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  19. Article
  20. Article

940 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Harm H KampingaDepartment of Cell Biology, University of Groningen, University Medical Center, 713 AV Groningen, The Netherlands. h.h.kampinga@med.umcg.nl
Elizabeth A Craig
University Medical Center Groningen · NLUniversity of Wisconsin–Madison · US

Funding

TRANSCRIPTIONALLY REGULATED GENESR01GM027870 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2017
$5.8M
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER37GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1999 to 2008
$3.3M
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER01GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2012
$1.9M
NIGMS NIH HHS GM27870NIGMS NIH HHS GM31107NIGMS NIH HHS R01 GM027870NIGMS NIH HHS R01 GM031107NIGMS NIH HHS R37 GM031107
6 · The paper itself

Abstract

Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across membranes, and protein-protein interactions. This multitude of roles is not easily reconciled with the universality of the activity of HSP70s in ATP-dependent client protein-binding and release cycles. Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70. Some target HSP70 activity to clients at precise locations in cells and others bind client proteins directly, thereby delivering specific clients to HSP70 and directly determining their fate.

Indexed as

Adenosine TriphosphateGuanine Nucleotide Exchange FactorsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansModels, BiologicalModels, MolecularProtein BindingProtein FoldingProtein Interaction Domains and MotifsSaccharomyces cerevisiae ProteinsAdenosine TriphosphateGuanine Nucleotide Exchange FactorsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID20651708
PMCPMC3003299
OpenAlexW1972121275

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.