Evidence map›Paper›PMID 18427938›Full record

ReviewJournal of muscle research and cell motility2007

Folding and regulation in myosins II and V.

James R Sellers, Peter J Knight

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  3. Force transmission in epithelial tissues.Developmental dynamics : an official publication of the American Association of Anatomists · 2016
    Review
  4. Article
  5. Structure and Regulation of the Movement of Human Myosin VIIA.The Journal of biological chemistry · 2015
    Article
  6. Article
  7. Structural insights into the assembly of a monomeric class V myosin.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Multiple roles for the actin cytoskeleton during regulated exocytosis.Cellular and molecular life sciences : CMLS · 2013
    Review
  9. Article
  10. Article
  11. Structural dynamics of muscle protein phosphorylation.Journal of muscle research and cell motility · 2012
    Review
  12. Regulation of zipcode binding protein 1 transport dynamics in axons by myosin Va.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  13. Full-length myosin Va exhibits altered gating during processive movement on actin.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Review
  15. Multifunctional myosin VI has a multitude of cargoes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  18. Article
  19. Article
  20. A FERM domain autoregulates Drosophila myosin 7a activity.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

2 authors at 2 institutions in 2 countries.

James R SellersLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, Room 3523, Bethesda, MD 20892, USA. sellersj@nhlbi.nih.gov
Peter J Knight
National Institutes of Health · USUniversity of Leeds · GB

Funding

Regulation Of Smooth and Nonmuscle MyosinZIAHL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$17.4M
ROLE OF PHOSPHORYLATION AS A REGULATORY MECHANISM IN MUSCLE CONTRACTIONZ01HL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES R. · 1985 to 2008
$601k
Intramural NIH HHSWellcome Trust 076057
6 · The paper itself

Abstract

The enzymatic activity of many myosins is regulated by various means including calcium binding, phosphorylation or binding of receptor molecules. In this review we compare and contrast the regulation of smooth muscle myosin II and myosin Va with particular emphasis on the structural basis for the regulation. Both myosins adopt folded compact conformations in their off states, but the details of the conformations are markedly different. In the regulated smooth muscle myosin II, the key feature is an asymmetric interaction between the two heads of the molecule with contributions of specific tail-head interactions. In myosin V the key feature is an interaction between the heads and the globular tail domain.

Indexed as

Protein FoldingAnimalsCalciumHumansMyosin Type IIMyosin Type VPhosphorylationProtein BindingProtein Structure, TertiaryCalciumMyosin Type IIMyosin Type V

Identifiers

PMID18427938
OpenAlexW2082065486

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.