Evidence map›Paper›PMID 32958886›Full record

ArticleNature chemistry2020

The catalytic dwell in ATPases is not crucial for movement against applied torque.

Chen Bai, Mojgan Asadi, Arieh Warshel

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  5. Exploring the Activation Process of the Glycine Receptor.Journal of the American Chemical Society · 2024
    Article
  6. Article
  7. Article
  8. Exploring the activation mechanism of metabotropic glutamate receptor 2.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. FBiophysical journal · 2023
    Article
  10. Article
  11. Molecular mechanism and energetics of coupling between substrate binding and product release in the FProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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 1 institution in 1 country.

Chen BaiDepartment of Chemistry, University of Southern California, Los Angeles, CA, USA.
Mojgan AsadiDepartment of Chemistry, University of Southern California, Los Angeles, CA, USA.
Arieh WarshelDepartment of Chemistry, University of Southern California, Los Angeles, CA, USA. warshel@usc.edu.ORCID http://orcid.org/0000-0001-7971-5401
University of Southern California · US

Funding

SV40 T Antigen Structure and Helicase MechanismsR01AI055926 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2004 to 2013
$4.0M
NIAID NIH HHS R01 AI055926
6 · The paper itself

Abstract

The ATPase-catalysed conversion of ATP to ADP is a fundamental process in biology. During the hydrolysis of ATP, the α

Indexed as

TorqueAdenosine TriphosphateBiocatalysisChlorophytaProtein ConformationRotationSpinacia oleraceaThermodynamicsThermus thermophilusVacuolar Proton-Translocating ATPasesAdenosine TriphosphateVacuolar Proton-Translocating ATPases

Identifiers

PMID32958886
OpenAlexW3087404198

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.