Evidence map›Paper›PMID 21454554›Full record

ArticleThe Journal of biological chemistry2011

Positive cooperativity of the p97 AAA ATPase is critical for essential functions.

Shingo Nishikori, Masatoshi Esaki, Kunitoshi Yamanaka, Shinya Sugimoto, Teru Ogura

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Article
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  4. Article
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  9. Article
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  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Mutations in the Human AAAFrontiers in molecular biosciences · 2016
    Review
  17. Article
  18. Altered cofactor regulation with disease-associated p97/VCP mutations.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
  20. 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.

Shingo NishikoriDepartment of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan.
Masatoshi Esaki
Kunitoshi Yamanaka
Shinya Sugimoto
Teru Ogura

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p97 is composed of two conserved AAA (ATPases associated with diverse cellular activities) domains, which form a tandem hexameric ring. We characterized the ATP hydrolysis mechanism of CDC-48.1, a p97 homolog of Caenorhabditis elegans. The ATPase activity of the N-terminal AAA domain was very low at physiological temperature, whereas the C-terminal AAA domain showed high ATPase activity in a coordinated fashion with positive cooperativity. The cooperativity and coordination are generated by different mechanisms because a noncooperative mutant still showed the coordination. Interestingly, the growth speed of yeast cells strongly related to the positive cooperativity rather than the ATPase activity itself, suggesting that the positive cooperativity is critical for the essential functions of p97.

Indexed as

Adenosine TriphosphatasesAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell Cycle ProteinsProtein Structure, TertiarySaccharomyces cerevisiaeSequence Homology, Amino AcidAdenosine TriphosphatasesCaenorhabditis elegans ProteinsCell Cycle Proteins

Identifiers

PMID21454554
PMCPMC3091191

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.