Evidence map›Paper›PMID 12499355›Full record

ArticleThe Journal of cell biology2002

The prepower stroke conformation of myosin V.

Stan Burgess, Matt Walker, Fei Wang, James R Sellers, Howard D White, Peter J Knight, John Trinick

Abstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. Article
  2. Myosin-5 varies its step length to carry cargo straight along the irregular F-actin track.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Article
  9. Calcium can mobilize and activate myosin-VI.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. 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
  12. Review
  13. Article
  14. Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. To understand muscle you must take it apart.Frontiers in physiology · 2014
    Review
  16. Visualization of human Bloom's syndrome helicase molecules bound to homologous recombination intermediates.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  17. Mammalian myosin-18A, a highly divergent myosin.The Journal of biological chemistry · 2013
    Article
  18. Article
  19. Article
  20. The kinetic mechanism of mouse myosin VIIA.The Journal of biological chemistry · 2011
    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

7 authors.

Stan BurgessAstbury Centre for Structural Molecular Biology and School of Biomedical Sciences, University of Leeds, Leeds, UK.
Matt Walker
Fei Wang
James R Sellers
Howard D White
Peter J Knight
John Trinick

Funding

Studies Of Myosin VZ01HL004229 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES R. · 1997 to 2008
$1.1M
CRYOELECTRONMICROSCOPY OF ACTOS1 ATPASE INTERMEDIATESR01AR040964 · NIAMS · EASTERN VIRGINIA MEDICAL SCHOOL · PI WHITE, HOWARD D. · 1995 to 2001
$642k
NIAMS NIH HHS AR40964NIAMS NIH HHS R01 AR040964
6 · The paper itself

Abstract

We have used electron microscopy and single-particle image processing to study head conformation in myosin V molecules. We find that in the presence of ATP, many heads have a sharply angled conformation that is rare in its absence. The sharply angled conformation is similar to a myosin II atomic structure proposed to mimic the prepower stroke state. The leading head in molecules attached to actin by both heads has a similar conformation, but is also sharply angled in a second plane by tethering through the trail head. The lead head lever joins the motor domain approximately 5 nm axially from where it joins the trail motor. These positions locate the converter subdomain and show the lead motor is in the prepower stroke conformation. Tethering by the trail head places the lead head motor domain at the correct axial position along the actin for binding, but at the wrong orientation. Attachment is achieved either by bending the lead head lever throughout its length or at the pliant point. The microscopy shows that most of the walking stride is produced by changes in lever angle brought about by converter movement, but is augmented by distortion produced by thermal energy.

Indexed as

ActinsAdenosine TriphosphateAnimalsCell LineCrystallography, X-RayHot TemperatureHydrolysisInsectaMiceMicroscopy, ElectronModels, MolecularMyosin Type IIMyosin Type VProtein BindingProtein ConformationProtein Structure, TertiaryActinsAdenosine TriphosphateMyosin Type IIMyosin Type V

Identifiers

PMID12499355
PMCPMC2173995

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.