Evidence map›Paper›PMID 26929436›Full record

ReviewTraffic (Copenhagen, Denmark)2016

Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.

Sarah M Heissler, James R Sellers

Open access · bronzeAbstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
7.4field-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

67 citing papers in PubMed, 107 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  15. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Non-muscle myosin 2 at a glance.Journal of cell science · 2023
    Review

7 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

2 authors at 2 institutions in 1 country.

Sarah M HeisslerLaboratory of Molecular Physiology, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, B50/3523, Bethesda, MD 20892-8015, USA.
James R SellersLaboratory of Molecular Physiology, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, B50/3523, Bethesda, MD 20892-8015, USA.
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Regulation Of Smooth and Nonmuscle MyosinZIAHL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$17.4M
Expression Studies of Other Unconventional MyosinsZIAHL004232 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$11.7M
Intramural NIH HHS ZIA HL001786
6 · The paper itself

Abstract

Members of the myosin superfamily are involved in all aspects of eukaryotic life. Their function ranges from the transport of organelles and cargos to the generation of membrane tension, and the contraction of muscle. The diversity of physiological functions is remarkable, given that all enzymatically active myosins follow a conserved mechanoenzymatic cycle in which the hydrolysis of ATP to ADP and inorganic phosphate is coupled to either actin-based transport or tethering of actin to defined cellular compartments. Kinetic capacities and limitations of a myosin are determined by the extent to which actin can accelerate the hydrolysis of ATP and the release of the hydrolysis products and are indispensably linked to its physiological tasks. This review focuses on kinetic competencies that - together with structural adaptations - result in myosins with unique mechanoenzymatic properties targeted to their diverse cellular functions.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsHumansKineticsMyosinsOrganellesActinsAdenosine DiphosphateAdenosine TriphosphateMyosinsactinallosterycationcytoskeletonmechanoenzymologymolecular motormusclemyosintransporter

Identifiers

PMID26929436
PMCPMC5067728
OpenAlexW2289101558

What OpenQuestion holds

Textmetadata
LicenceTDM
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.