Evidence map›Paper›PMID 20448033›Full record

ArticleThe Journal of biological chemistry2010

The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.

B Erin Horne, Tingfeng Li, Pierre Genevaux, Costa Georgopoulos, Samuel J Landry

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

16 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. A History of Molecular Chaperone Structures in the Protein Data Bank.International journal of molecular sciences · 2019
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Allostery in the Hsp70 chaperone proteins.Topics in current chemistry · 2013
    Review
  16. Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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

5 authors at 3 institutions in 2 countries.

B Erin HorneDepartment of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112, USA.
Tingfeng Li
Pierre Genevaux
Costa Georgopoulos
Samuel J Landry
Tulane University · USUniversité Toulouse III - Paul Sabatier · FRUniversity of Utah · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Escherichia coli Hsp40 DnaJ uses its J-domain (Jd) to couple ATP hydrolysis and client protein capture in Hsp70 DnaK. Fusion of the Jd to peptide p5 (as in Jdp5) dramatically increases the apparent affinity of the p5 moiety for DnaK in the presence of ATP, and Jdp5 stimulates ATP hydrolysis in DnaK by several orders of magnitude. NMR experiments with [(15)N]Jdp5 demonstrated that the peptide tethers the Jd to the ATPase domain. Thus, ATP hydrolysis and client protein binding in DnaK are coupled principally through the association of the client with DnaJ. Overexpression of a recombinant Jd was specifically toxic to cells that simultaneously expressed DnaK. No toxicity was observed when overexpressing Jdp5 or mutant Jd or when co-overexpressing the Jd and the nucleotide exchange factor GrpE. The results suggest that the Jd shifts DnaK to a client-bound form by stimulating the DnaK ATPase but only when the Jd is brought to DnaK by a client-Hsp40 complex.

Indexed as

Adenosine TriphosphatasesChaperoninsEscherichia coliEscherichia coli ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHydrolysisMagnetic Resonance SpectroscopyMolecular ChaperonesMutationProtein BindingProtein Structure, TertiaryRecombinant ProteinsAdenosine TriphosphatasesChaperoninsdnaK protein, E coliEscherichia coli ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesRecombinant Proteins

Identifiers

PMID20448033
PMCPMC2898438
OpenAlexW1983287219

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.