Evidence map›Paper›PMID 11706052›Full record

ArticleThe Journal of cell biology2001

Myosin V exhibits a high duty cycle and large unitary displacement.

J R Moore, E B Krementsova, K M Trybus, D M Warshaw

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Coarse-grained simulation of myosin-V movement.Computational and mathematical methods in medicine · 2012
    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

4 authors at 1 institution in 1 country.

J R MooreDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.
E B Krementsova
K M Trybus
D M Warshaw
University of Vermont · US

Funding

Structural/biochemical analysis of myosin based movementP01AR047906 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2001 to 2005
$6.5M
SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
SINGLE MOLECULAR MECHANICS OF MYOSIN VF32GM020384 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MOORE, JEFFREY R · 2000 to 2003
$101k
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
NHLBI NIH HHS HL38113NHLBI NIH HHS R01 HL038113NIAMS NIH HHS AR47906NIAMS NIH HHS P01 AR047906NIGMS NIH HHS F32 GM020384NIGMS NIH HHS GM208343
6 · The paper itself

Abstract

Myosin V is a double-headed unconventional myosin that has been implicated in organelle transport. To perform this role, myosin V may have a high duty cycle. To test this hypothesis and understand the properties of this molecule at the molecular level, we used the laser trap and in vitro motility assay to characterize the mechanics of heavy meromyosin-like fragments of myosin V (M5(HMM)) expressed in the Baculovirus system. The relationship between actin filament velocity and the number of interacting M5(HMM) molecules indicates a duty cycle of > or =50%. This high duty cycle would allow actin filament translocation and thus organelle transport by a few M5(HMM) molecules. Single molecule displacement data showed predominantly single step events of 20 nm and an occasional second step to 37 nm. The 20-nm unitary step represents the myosin V working stroke and is independent of the mode of M5(HMM) attachment to the motility surface or light chain content. The large M5(HMM) working stroke is consistent with the myosin V neck acting as a mechanical lever. The second step is characterized by an increased displacement variance, suggesting a model for how the two heads of myosin V function in processive motion.

Indexed as

AnimalsGene ExpressionMiceMyosin SubfragmentsMyosin Type VProtein TransportMyosin SubfragmentsMyosin Type V

Identifiers

PMID11706052
PMCPMC2198872
OpenAlexW2025039463

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.