Evidence map›Paper›PMID 23580641›Full record

ArticleThe Journal of biological chemistry2013

Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate.

Jorge Cuéllar, Judit Perales-Calvo, Arturo Muga, José María Valpuesta, Fernando Moro

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.2field-weighted citation impact, top 22% 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, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Design principles to tailor Hsp104 therapeutics.bioRxiv : the preprint server for biology · 2024
    Article
  4. Review
  5. Article
  6. Cereblon Regulates the Proteotoxicity of Tau by Tuning the Chaperone Activity of DNAJA1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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 2 institutions in 1 country.

Jorge CuéllarDepartamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología, CNB-CSIC, Darwin 3, 28049 Madrid, Spain.
Judit Perales-Calvo
Arturo Muga
José María Valpuesta
Fernando Moro
University of the Basque Country · ESCentro Nacional de Biotecnología · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp40 chaperones bind and transfer substrate proteins to Hsp70s and regulate their ATPase activity. The interaction of Hsp40s with native proteins modifies their structure and function. A good model for this function is DnaJ, the bacterial Hsp40 that interacts with RepE, the repressor/activator of plasmid F replication, and together with DnaK regulates its function. We characterize here the structure of the DnaJ-RepE complex by electron microscopy, the first described structure of a complex between an Hsp40 and a client protein. The comparison of the complexes of DnaJ with two RepE mutants reveals an intrinsic plasticity of the DnaJ dimer that allows the chaperone to adapt to different substrates. We also show that DnaJ induces conformational changes in dimeric RepE, which increase the intermonomeric distance and remodel both RepE domains enhancing its affinity for DNA.

Indexed as

Escherichia coliEscherichia coli ProteinsF FactorHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMultiprotein ComplexesRepressor ProteinsDnaJ protein, E colidnaK protein, E coliEscherichia coli ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMultiprotein ComplexesRepE protein, E coliRepressor ProteinsChaperonesDnaJElectron Microscopy (EM)Heat Shock ProteinHsp40Protein ComplexesProtein ConformationProtein FoldingProtein Structure

Identifiers

PMID23580641
PMCPMC3663527
OpenAlexW2049057605

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.