Evidence map›Paper›PMID 18332143›Full record

ArticleThe Journal of biological chemistry2008

Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase.

Louise C Briggs, Geoff S Baldwin, Non Miyata, Hisao Kondo, Xiaodong Zhang, Paul S Freemont

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

58 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. A genome-scale drug discovery pipeline uncovers therapeutic targets and a unique p97 allosteric binding site inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024
    Article
  6. Systematic QM/MM Study for PredictingJournal of chemical theory and computation · 2024
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion.International journal of molecular sciences · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Interaction between the AAAThe Journal of biological chemistry · 2017
    Article
  20. The AAA+ ATPase p97, a cellular multitool.The Biochemical journal · 2017
    Review
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

6 authors at 2 institutions in 2 countries.

Louise C BriggsDivision of Molecular Biosciences, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
Geoff S Baldwin
Non Miyata
Hisao Kondo
Xiaodong Zhang
Paul S Freemont
Imperial College London · GBKyushu University · JP

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

p97, an essential chaperone in endoplasmic reticulum-associated degradation and organelle biogenesis, contains two AAA domains (D1 and D2) and assembles as a stable hexamer. We present a quantitative analysis of nucleotide binding to both D1 and D2 domains of p97, the first detailed study of nucleotide binding to both AAA domains for this type of AAA+ ATPase. We report that adenosine 5'-O-(thiotriphosphate) (ATPgammaS) binds with similar affinity to D1 and D2, but ADP binds with higher affinity to D1 than D2, offering an explanation for the higher ATPase activity in D2. Stoichiometric measurements suggest that although both ADP and ATPgammaS can saturate all 6 nucleotide binding sites in D1, only 3-4 of the 6 D2 sites can bind ATPgammaS simultaneously. ATPgammaS binding triggers a downstream cooperative conformational change of at least three monomers, which involves conserved arginine fingers and is necessary for ATP hydrolysis.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesDose-Response Relationship, DrugHydrolysisKineticsMiceMolecular ConformationNuclear ProteinsNucleotidesProtein BindingRatsadenosine 5'-O-(3-thiotriphosphate)Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateNuclear ProteinsNucleotidesp97 ATPase

Identifiers

PMID18332143
PMCPMC2376215
OpenAlexW2018753611

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.