Evidence map›Paper›PMID 37503193›Full record

ArticlebioRxiv : the preprint server for biology2023

Myosin-5 varies its steps along the irregular F-actin track.

Adam Fineberg, Yasuharu Takagi, Kavitha Thirumurugan, Joanna Andrecka, Neil Billington, Gavin Young, Daniel Cole, Stan A Burgess, Alistair P Curd, John A Hammer and 3 more

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. AI in neurocritical care: what to expect.Intensive care medicine · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 4 institutions in 4 countries.

Adam FinebergPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, U.K.
Yasuharu TakagiLaboratory of Molecular Physiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, U.S.A.
Kavitha ThirumuruganAstbury Centre for Structural Molecular Biology, and Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, U.K.
Joanna AndreckaPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, U.K.
Neil BillingtonLaboratory of Molecular Physiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, U.S.A.
Gavin YoungPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, U.K.
Daniel ColePhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, U.K.
Stan A BurgessAstbury Centre for Structural Molecular Biology, and Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, U.K.
Alistair P CurdAstbury Centre for Structural Molecular Biology, and Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, U.K.
John A HammerCell and Developmental Biology Center, NHLBI, National Institutes of Health, Bethesda, MD 20892, U.S.A.
James R SellersLaboratory of Molecular Physiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, U.S.A.
Philipp KukuraPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, U.K.
Peter J KnightAstbury Centre for Structural Molecular Biology, and Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, U.K.
National Institutes of Health · USUniversity of Leeds · GBUniversity of Oxford · GBWest Virginia University · US

Funding

Studies Of Myosin VZIAHL004229 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$2.3M
MAKAP FUNCTIONS OF A PKA ANCHORING PROTEINK08HL004229 · NHLBI · OREGON HEALTH AND SCIENCE UNIVERSITY · PI KAPILOFF, MICHAEL SETH · 2000 to 2004
$635k
Intramural NIH HHS ZIA HL004229Wellcome Trust
6 · The paper itself

Abstract

Molecular motors employ chemical energy to generate unidirectional mechanical output against a track. By contrast to the majority of macroscopic machines, they need to navigate a chaotic cellular environment, potential disorder in the track and Brownian motion. Nevertheless, decades of nanometer-precise optical studies suggest that myosin-5a, one of the prototypical molecular motors, takes uniform steps spanning 13 subunits (36 nm) along its F-actin track. Here, we use high-resolution interferometric scattering (iSCAT) microscopy to reveal that myosin takes strides spanning 22 to 34 actin subunits, despite walking straight along the helical actin filament. We show that cumulative angular disorder in F-actin accounts for the observed proportion of each stride length, akin to crossing a river on variably-spaced stepping stones. Electron microscopy revealed the structure of the stepping molecule. Our results indicate that both motor and track are soft materials that can adapt to function in complex cellular conditions.

Indexed as

Actin FilamentCryogenic Electron Microscopy (cryoEM)Cumulative Angular Disorder (CAD)Interferometric Scattering (iSCAT) MicroscopyMyosin-5Negative-stain Electron Microscopy (nsEM)Single Molecule Biophysics

Identifiers

PMID37503193
PMCPMC10370000
OpenAlexW4384461085

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.