Evidence map›Paper›PMID 26792327›Full record

ReviewThe Journal of experimental biology2016

Myosin isoforms and the mechanochemical cross-bridge cycle.

Jonathan Walklate, Zoltan Ujfalusi, Michael A Geeves

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of experimental biology, 2016. 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
4.9field-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, 65 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  12. Article
  13. The twoFrontiers in physiology · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. The interplay of inflammation, exosomes and CaCardiovascular diabetology · 2023
    Review
  19. Article
  20. Discovery of ultrafast myosin, its amino acid sequence, and structural features.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

3 authors at 1 institution in 1 country.

Jonathan WalklateSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, UK.
Zoltan UjfalusiSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, UK.
Michael A GeevesSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, UK m.a.geeves@kent.ac.uk.
University of Kent · GB

Funding

MYOSIN GENE DIVERSITY AND FUNCTIONR01GM029090 · NIGMS · YESHIVA UNIVERSITY · PI Leslie Anne Leinwand · 1985 to 2026
$12.3M
British Heart Foundation PG/13/75/30200British Heart Foundation PG 30200NIGMS NIH HHS R01 GM029090NIGMS NIH HHS R01 GM29090
6 · The paper itself

Abstract

At the latest count the myosin family includes 35 distinct groups, all of which have the conserved myosin motor domain attached to a neck or lever arm, followed by a highly variable tail or cargo binding region. The motor domain has an ATPase activity that is activated by the presence of actin. One feature of the myosin ATPase cycle is that it involves an association/dissociation with actin for each ATP hydrolysed. The cycle has been described in detail for a large number of myosins from different classes. In each case the cycle is similar, but the balance between the different molecular events in the cycle has been altered to produce a range of very different mechanical activities. Myosin may spend most of the ATPase cycle attached to actin (high duty ratio), as in the processive myosin (e.g. myosin V) or the strain-sensing myosins (e.g. myosin 1c). In contrast, most muscle myosins spend 80% of their ATPase cycle detached from actin. Within the myosin IIs found in human muscle, there are 11 different sarcomeric myosin isoforms, two smooth muscle isoforms as well as three non-muscle isoforms. We have been exploring how the different myosin isoforms have adapted the cross-bridge cycle to generate different types of mechanical activity and how this goes wrong in inherited myopathies. The ideas are outlined here.

Indexed as

Adenosine DiphosphateAnimalsBiomechanical PhenomenaHumansModels, BiologicalMyosinsProtein IsoformsSarcomeresAdenosine DiphosphateMyosinsProtein IsoformsCardiacContractionHumanMuscleSkeletal

Identifiers

PMID26792327
PMCPMC6514470
OpenAlexW2468128326

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.