Evidence map›Paper›PMID 25655283›Full record

ReviewExperimental cell research2015

Myosin II isoform co-assembly and differential regulation in mammalian systems.

Jordan R Beach, John A Hammer

Open access · greenAbstract readReview
In one paragraph

Review in Experimental cell research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.5field-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

38 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Myosin 18Aα targets the guanine nucleotide exchange factor β-Pix to the dendritic spines of cerebellar Purkinje neurons and promotes spine maturation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The role of actin and myosin in antigen extraction by B lymphocytes.Seminars in cell & developmental biology · 2020
    Review
  19. Article
  20. 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 1 institution in 1 country.

Jordan R BeachCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: jordan.beach@nih.gov.
John A HammerCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: hammer@nhlbi.nih.gov.
National Heart Lung and Blood Institute · US

Funding

Structure And Function Of Unconventional Myosins and CARMIL ProteinsZIAHL000514 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI HAMMER, JOHN A · 2009 to 2018
$9.6M
Intramural NIH HHS Z99 HL999999Intramural NIH HHS ZIA HL000514PHS HHS ZIAHL000514-31
6 · The paper itself

Abstract

Non-muscle myosin 2 (NM2) is a major force-producing, actin-based motor in mammalian non-muscle cells, where it plays important roles in a broad range of fundamental biological processes, including cytokinesis, cell migration, and epithelial barrier function. This breadth of function at the tissue and cellular levels suggests extensive diversity and differential regulation of NM2 bipolar filaments, the major, if not sole, functional form of NM2s in vivo. Previous in vitro, cellular and animal studies indicate that some of this diversity is supported by the existence of multiple NM2 isoforms. Moreover, two recent studies have shown that these isoforms can co-assemble to form heterotypic filaments, further expanding functional diversity. In addition to isoform co-assembly, cells may differentially regulate NM2 function via isoform-specific expression, RLC phosphorylation, MHC phosphorylation or regulation via binding partners. Here, we provide a brief summary of NM2 filament assembly, summarize the recent findings regarding NM2 isoform co-assembly, consider the mechanisms cells might utilize to differentially regulate NM2 isoforms, and review the data available to support these mechanisms.

Indexed as

AnimalsHumansMyosin Type IIProtein IsoformsMyosin Type IIProtein IsoformsFilament assemblyIsoformNonmuscle myosin II

Identifiers

PMID25655283
PMCPMC4433797
OpenAlexW2023417132

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.