Evidence map›Paper›PMID 28461478›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis.

Ranit Gruber, Michael Levitt, Amnon Horovitz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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
1.7field-weighted citation impact, top 16% 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, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Allostery in Its Many Disguises: From Theory to Applications.Structure (London, England : 1993) · 2019
    Review
  12. Review
  13. The substrate specificity of eukaryotic cytosolic chaperonin CCT.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. Molecular switch-like regulation in motor proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  15. Unpicking allosteric mechanisms of homo-oligomeric proteins by determining their successive ligand binding constants.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  16. Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    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

3 authors at 2 institutions in 2 countries.

Ranit GruberDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Michael LevittDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.
Amnon HorovitzDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel; Amnon.Horovitz@weizmann.ac.il.
Weizmann Institute of Science · ILStanford University · US

Funding

Emergent Properties of Complex Systems: From Atoms to Macromolecules; from Humans to SocietiesR35GM122543 · NIGMS · STANFORD UNIVERSITY · PI MICHAEL LEVITT · 2017 to 2026
$5.1M
NIGMS NIH HHS R35 GM122543
6 · The paper itself

Abstract

Knowing the mechanism of allosteric switching is important for understanding how molecular machines work. The CCT/TRiC chaperonin nanomachine undergoes ATP-driven conformational changes that are crucial for its folding function. Here, we demonstrate that insight into its allosteric mechanism of ATP hydrolysis can be achieved by Arrhenius analysis. Our results show that ATP hydrolysis triggers sequential ‟conformational waves." They also suggest that these waves start from subunits CCT6 and CCT8 (or CCT3 and CCT6) and proceed clockwise and counterclockwise, respectively.

Indexed as

Adenosine TriphosphateAllosteric RegulationChaperonin Containing TCP-1ChaperoninsHydrolysisModels, MolecularProtein ConformationProtein FoldingProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateChaperonin Containing TCP-1ChaperoninsProtein SubunitsSaccharomyces cerevisiae Proteinsallosterychaperoninsconformational changesmolecular machines

Identifiers

PMID28461478
PMCPMC5441784
OpenAlexW2610194091

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.