Evidence map›Paper›PMID 24101499›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Design principles governing the motility of myosin V.

Michael Hinczewski, Riina Tehver, D Thirumalai

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Robust mechanobiological behavior emerges in heterogeneous myosin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. Article
  15. Protein folding guides disulfide bond formation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Article
  17. Article
  18. Electrostatic origin of the unidirectionality of walking myosin V motors.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

Michael HinczewskiBiophysics Program, Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742.
Riina Tehver
D Thirumalai

Funding

Computational Approaches to Single Molecule Force SpectroscopyR01GM089685 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI THIRUMALAI, DEVARAJAN · 2010 to 2020
$2.9M
Extraction of protein and RNA folding landscapes from force clamp experimentsF32GM097756 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI HINCZEWSKI, MICHAEL · 2011 to 2011
$59k
NIGMS NIH HHS 1 F32 GM 97756-1NIGMS NIH HHS F32 GM097756NIGMS NIH HHS GM 089685NIGMS NIH HHS R01 GM089685
6 · The paper itself

Abstract

The molecular motor myosin V (MyoV) exhibits a wide repertoire of pathways during the stepping process, which is intimately connected to its biological function. The best understood of these is the hand-over-hand stepping by a swinging lever arm movement toward the plus end of actin filaments. Single-molecule experiments have also shown that the motor "foot stomps," with one hand detaching and rebinding to the same site, and back-steps under sufficient load. The complete taxonomy of MyoV's load-dependent stepping pathways, and the extent to which these are constrained by motor structure and mechanochemistry, are not understood. Using a polymer model, we develop an analytical theory to describe the minimal physical properties that govern motor dynamics. We solve the first-passage problem of the head reaching the target-binding site, investigating the competing effects of backward load, strain in the leading head biasing the diffusion in the direction of the target, and the possibility of preferential binding to the forward site due to the recovery stroke. The theory reproduces a variety of experimental data, including the power stroke and slow diffusive search regimes in the mean trajectory of the detached head, and the force dependence of the forward-to-backward step ratio, run length, and velocity. We derive a stall force formula, determined by lever arm compliance and chemical cycle rates. By exploring the MyoV design space, we predict that it is a robust motor whose dynamical behavior is not compromised by reasonable perturbations to the reaction cycle and changes in the architecture of the lever arm.

Indexed as

Models, ChemicalModels, MolecularActin CytoskeletonActinsAdenosine DiphosphateAdenosine TriphosphateAlgorithmsKineticsMolecular Motor ProteinsMyosin Type VProtein BindingThermodynamicsActinsAdenosine DiphosphateAdenosine TriphosphateMolecular Motor ProteinsMyosin Type Varchitectural basisfunctional robustnesspolymer physicsstall force expression

Identifiers

PMID24101499
PMCPMC3808654

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.