Evidence map›Paper›PMID 24753602›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load.

Yasuharu Takagi, Rachel E Farrow, Neil Billington, Attila Nagy, Christopher Batters, Yi Yang, James R Sellers, Justin E Molloy

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  3. Screening and identification of protein 29 ofFrontiers in cellular and infection microbiology · 2025
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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

8 authors at 3 institutions in 2 countries.

Yasuharu TakagiLaboratory of Molecular Physiology, National Heart, Lung and Blood, Institute, National Institutes of Health, Bethesda, MD 20892.
Rachel E Farrow
Neil Billington
Attila Nagy
Christopher Batters
Yi Yang
James R Sellers
Justin E Molloy
National Heart Lung and Blood Institute · USMedical Research Council · GBNational Institutes of Health · US

Funding

Expression Studies of Other Unconventional MyosinsZIAHL004232 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$11.7M
RISK FACTORS &BIOMARKERS OF OX STRESS IN GRAFT FAILUREK23HL004243 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI CHRISTIE, JASON D · 2000 to 2004
$652k
Intramural NIH HHSMedical Research Council MC_U117570592Medical Research Council U1175.70592NHLBI NIH HHS HL004243 12
6 · The paper itself

Abstract

Myosin-10 is an actin-based molecular motor that participates in essential intracellular processes such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance. To study this motor protein's mechano-chemical properties, we used a recombinant, truncated form of myosin-10 consisting of the first 936 amino acids, followed by a GCN4 leucine zipper motif, to force dimerization. Negative-stain electron microscopy reveals that the majority of molecules are dimeric with a head-to-head contour distance of ∼50 nm. In vitro motility assays show that myosin-10 moves actin filaments smoothly with a velocity of ∼310 nm/s. Steady-state and transient kinetic analysis of the ATPase cycle shows that the ADP release rate (∼13 s(-1)) is similar to the maximum ATPase activity (∼12-14 s(-1)) and therefore contributes to rate limitation of the enzymatic cycle. Single molecule optical tweezers experiments show that under intermediate load (∼0.5 pN), myosin-10 interacts intermittently with actin and produces a power stroke of ∼17 nm, composed of an initial 15-nm and subsequent 2-nm movement. At low optical trap loads, we observed staircase-like processive movements of myosin-10 interacting with the actin filament, consisting of up to six ∼35-nm steps per binding interaction. We discuss the implications of this load-dependent processivity of myosin-10 as a filopodial transport motor.

Indexed as

ActinsAdenosine DiphosphateAmino Acid SequenceAnimalsBiomechanical PhenomenaCattleIn Vitro TechniquesKineticsMicroscopy, ElectronMicroscopy, FluorescenceModels, BiologicalModels, MolecularMolecular Sequence DataMyosin Heavy ChainsMyosin SubfragmentsOptical TweezersActinsAdenosine DiphosphateMyosin Heavy ChainsMyosin SubfragmentsRecombinant Fusion Proteinsactomyosinmyosin-5amyosin Xoptical trappingstable single alpha-helix

Identifiers

PMID24753602
PMCPMC4020102
OpenAlexW2088622792

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.