Evidence map›Paper›PMID 26976594›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Force-producing ADP state of myosin bound to actin.

Sarah F Wulf, Virginie Ropars, Setsuko Fujita-Becker, Marco Oster, Goetz Hofhaus, Leonardo G Trabuco, Olena Pylypenko, H Lee Sweeney, Anne M Houdusse, Rasmus R Schröder

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
9.9field-weighted citation impact, top 1% 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

50 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  14. Article
  15. A Novel Missense Variant in Actin Binding Domain ofFrontiers in cardiovascular medicine · 2022
    Article
  16. Article
  17. Review
  18. Review
  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

10 authors at 3 institutions in 3 countries.

Sarah F WulfCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany;
Virginie RoparsStructural Motility, Institut Curie, Paris Sciences et Lettres Research University, CNRS, UMR 144, F-75005, Paris, France;
Setsuko Fujita-BeckerCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany;
Marco OsterCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany;
Goetz HofhausCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany;
Leonardo G TrabucoProtein Evolution, CellNetworks, BioQuant, Universität Heidelberg, 69120 Heidelberg, Germany;
Olena PylypenkoStructural Motility, Institut Curie, Paris Sciences et Lettres Research University, CNRS, UMR 144, F-75005, Paris, France;
H Lee SweeneyDepartment of Pharmacology & Therapeutics, University of Florida College of Medicine, Gainesville, FL 32610 anne.houdusse@curie.fr Lsweeney@ufl.edu rasmus.schroeder@bioquant.uni-heidelberg.de.
Anne M HoudusseStructural Motility, Institut Curie, Paris Sciences et Lettres Research University, CNRS, UMR 144, F-75005, Paris, France; anne.houdusse@curie.fr Lsweeney@ufl.edu rasmus.schroeder@bioquant.uni-heidelberg.de.
Rasmus R SchröderCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany; anne.houdusse@curie.fr Lsweeney@ufl.edu rasmus.schroeder@bioquant.uni-heidelberg.de.
Heidelberg University · DECentre National de la Recherche Scientifique · FRUniversity of Florida · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Structure and Function of Myosin VIR01DC009100 · NIDCD · UNIVERSITY OF PENNSYLVANIA · PI SWEENEY, H LEE · 2007 to 2022
$6.0M
NIDCD NIH HHS DC009100NIDCD NIH HHS R01 DC009100NIGMS NIH HHS P41 GM103311NIGMS NIH HHS P41-GM103311
6 · The paper itself

Abstract

Molecular motors produce force when they interact with their cellular tracks. For myosin motors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to actin. We have generated an 8-Å cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for model building. We compare this state to the subsequent state on actin (Rigor). The ADP-bound structure reveals that the actin-binding cleft is closed, even though MgADP is tightly bound. This state is accomplished by a previously unseen conformation of the β-sheet underlying the nucleotide pocket. The transition from the force-generating ADP state to Rigor requires a 9.5° rotation of the myosin lever arm, coupled to a β-sheet rearrangement. Thus, the structure reveals the detailed rearrangements underlying myosin force generation as well as the basis of strain-dependent ADP release that is essential for processive myosins, such as myosin V.

Indexed as

ActinsAdenosine DiphosphateBinding SitesCryoelectron MicroscopyCrystallography, X-RayHumansModels, MolecularMolecular Dynamics SimulationMyosin Type VProtein ConformationActinsAdenosine DiphosphateMyosin Type Vforce generationmolecular motormyosin Vtransducer

Identifiers

PMID26976594
PMCPMC4822626
OpenAlexW2273975555

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.