Evidence map›Paper›PMID 10570140›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

The kinetic mechanism of myosin V.

E M De La Cruz, A L Wells, S S Rosenfeld, E M Ostap, H L Sweeney

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 193 papers.

0numbers the graph read from it
0cells of the map it votes in
193citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

193 citing papers in PubMed, 423 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  8. Article
  9. Review
  10. Switch-2 determines MgFrontiers in physiology · 2024
    Article
  11. Article
  12. Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Article
  15. Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

133 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

E M De La CruzUniversity of Pennsylvania School of Medicine, Department of Physiology, Pennsylvania Muscle Institute, Philadelphia, PA 19104-6085, USA.
A L Wells
S S Rosenfeld
E M Ostap
H L Sweeney
University of Alabama · USUniversity of Pennsylvania · US

Funding

Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
PHYSIOLOGY AND MYOSIN ISOZYMES OF SKELETAL MUSCLE FIBERSR01AR035661 · NIAMS · UNIVERSITY OF TEXAS AUSTIN · PI SWEENEY, H LEE · 1986 to 2010
$3.7M
NIAMS NIH HHS AR35661NIAMS NIH HHS R01 AR035661NIGMS NIH HHS GM57247NIGMS NIH HHS R01 GM057247NIGMS NIH HHS R37 GM057247
6 · The paper itself

Abstract

Myosin V is an unconventional myosin proposed to be processive on actin filaments, analogous to kinesin on a microtubule [Mehta, A. D., et al. (1999) Nature (London) 400, 590-593]. To ascertain the unique properties of myosin V that permit processivity, we undertook a detailed kinetic analysis of the myosin V motor. We expressed a truncated, single-headed myosin V construct that bound a single light chain to study its innate kinetics, free from constraints imposed by other regions of the molecule. The data demonstrate that unlike any previously characterized myosin a single-headed myosin V spends most of its kinetic cycle (>70%) strongly bound to actin in the presence of ATP. This kinetic tuning is accomplished by increasing several of the rates preceding strong binding to actin and concomitantly prolonging the duration of the strongly bound state by slowing the rate of ADP release. The net result is a myosin unlike any previously characterized, in that ADP release is the rate-limiting step for the actin-activated ATPase cycle. Thus, because of a number of kinetic adaptations, myosin V is tuned for processive movement on actin and will be capable of transporting cargo at lower motor densities than any other characterized myosin.

Indexed as

Myosin Type VActin CytoskeletonActinsActomyosinAdenosine DiphosphateAnimalsCalmodulin-Binding ProteinsChickensFluorescenceKineticsMyosinsNerve Tissue ProteinsPhosphatesRabbitsTryptophanActinsActomyosinAdenosine DiphosphateCalmodulin-Binding Proteinschicken brain myosin-V p190MyosinsMyosin Type VNerve Tissue ProteinsPhosphatesTryptophan

Identifiers

PMID10570140
PMCPMC24132
OpenAlexW2001758775

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.