Evidence map›Paper›PMID 21518908›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structural mechanism of the ATP-induced dissociation of rigor myosin from actin.

Sebastian Kühner, Stefan Fischer

Open access · greenAbstract readValidation Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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
3.5field-weighted citation impact, top 7% 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, 43 citations in OpenAlex.

  1. Chemically-fueled phase transition of a redox-responsive polymer.Science and technology of advanced materials · 2025
    Article
  2. Article
  3. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
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  6. Review
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  8. Review
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  11. Catalytic strategy used by the myosin motor to hydrolyze ATP.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
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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

2 authors at 1 institution in 1 country.

Sebastian KühnerComputational Biochemistry Group, Interdisciplinary Center for Scientific Computing, University of Heidelberg, D-69115 Heidelberg, Germany.
Stefan Fischer
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin is a true nanomachine, which produces mechanical force from ATP hydrolysis by cyclically interacting with actin filaments in a four-step cycle. The principle underlying each step is that structural changes in separate regions of the protein must be mechanically coupled. The step in which myosin dissociates from tightly bound actin (the rigor state) is triggered by the 30 Å distant binding of ATP. Large conformational differences between the crystal structures make it difficult to perceive the coupling mechanism. Energetically accessible transition pathways computed at atomic detail reveal a simple coupling mechanism for the reciprocal binding of ATP and actin.

Indexed as

ActinsAdenosine TriphosphateAnimalsAvian ProteinsBinding SitesChickensModels, BiologicalModels, MolecularMolecular Dynamics SimulationMolecular Motor ProteinsMyosinsProtein ConformationProtein Structure, TertiaryActinsAdenosine TriphosphateAvian ProteinsMolecular Motor ProteinsMyosins

Identifiers

PMID21518908
PMCPMC3093495
OpenAlexW2018365501

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.