Evidence map›Paper›PMID 15160485›Full record

ArticleJournal of muscle research and cell motility2004

Does the myosin V neck region act as a lever?

Jeffrey R Moore, Elena B Krementsova, Kathleen M Trybus, David M Warshaw

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Robust mechanobiological behavior emerges in heterogeneous myosin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  3. Article
  4. Article
  5. Flexural Stiffness of Myosin Va Subdomains as Measured from Tethered Particle Motion.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2015
    Article
  6. Article
  7. Article
  8. Article
  9. Design principles governing the motility of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Review
  11. Review
  12. Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  13. Article
  14. Article
  15. Removal of the cardiac myosin regulatory light chain increases isometric force production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  16. Article
  17. Article
  18. Article
  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

4 authors at 1 institution in 1 country.

Jeffrey R MooreDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.
Elena B Krementsova
Kathleen M Trybus
David 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
SINGLE MOLECULAR MECHANICS OF MYOSIN VF32GM020384 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MOORE, JEFFREY R · 2000 to 2003
$101k
NHLBI NIH HHS HL38119NIAMS NIH HHS AR47906NIGMS NIH HHS F32 GM020384
6 · The paper itself

Abstract

Recent research efforts from several groups have addressed the question of whether the amplitude of myosin's unitary step size is proportional to the length of the neck region. Unconventional myosin V, which has an extended neck region with 6IQ motifs, provides a natural template by which to test the lever arm model via mutational analysis. The most stringent test requires that a series of single-headed molecules from the same myosin class be analyzed. Here we characterized the unitary mechanics of three single-headed fragments of myosin V expressed in the baculovirus/insect cell system. Each construct consisted of the motor domain (MD) and a variable number of IQ motifs (MD2IQ, MD4IQ and MD6IQ) that bind calmodulin, followed by an epitope tag so that the molecule can be attached to the nitrocellulose surface via an antibody. The results show a correlation between the unitary step size and the number of IQ motifs, confirming that the myosin neck region acts as a lever. The step size of MD2IQ is twice that observed from single-headed subfragments of class II myosins with the same neck length. Our results are discussed in relation to data obtained concurrently from other laboratories with similar constructs.

Indexed as

ActinsAnimalsGene ExpressionLasersMuscle ContractionMutationMyosin Type VProtein TransportRecombinant ProteinsTime FactorsActinsMyosin Type VRecombinant Proteins

Identifiers

PMID15160485
OpenAlexW2062262183

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.