Evidence map›Paper›PMID 11058170›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Coevolution of head, neck, and tail domains of myosin heavy chains.

E D Korn

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  4. Article
  5. Article
  6. Review
  7. Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Article
  10. Loop 2 of myosin is a force-dependent inhibitor of the rigor bond.Journal of muscle research and cell motility · 2014
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. New insights into myosin evolution and classification.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  18. Article
  19. Article
  20. Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2004
    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

1 author at 1 institution in 1 country.

E D KornLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. edk@nih.gov
National Heart Lung and Blood Institute · US

Funding

Biochemical and Biological Properties of Actins and MyosinsZIAHL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 2009 to 2014
$4.4M
REGULATION OF MYOSINS AND MYOSIN KINASES (PAKs)Z01HL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 1985 to 2008
$3.7M
THERMAL UNFOLDING OF THE ACANTHAMOEBA MYOSIN II RODZ01HL000312 · NHLBI · HEART, LUNG, AND BLOOD INSTITUTE · PI GINSBURG, ANN · 1996 to 2000
–
6 · The paper itself

Abstract

Myosins, a large family of actin-based motors, have one or two heavy chains with one or more light chains associated with each heavy chain. The heavy chains have a (generally) N-terminal head domain with an ATPase and actin-binding site, followed by a neck domain to which the light chains bind, and a C-terminal tail domain through which the heavy chains self-associate and/or bind the myosin to its cargo. Approximately 140 members of the myosin superfamily have been grouped into 17 classes based on the sequences of their head domains. I now show that a phylogenetic tree based on the sequences of the combined neck and tail domains groups 144 myosins, with a few exceptions, into the same 17 classes. For the nine myosin classes that have multiple members, phylogenetic trees based on the head domain or the combined neck/tail domains are either identical or very similar. For class II myosins, very similar phylogenetic trees are obtained for the head, neck, and tail domains of 47 heavy chains and for 29 essential light chains and 19 regulatory light chains. These data strongly suggest that the head, neck, and tail domains of all myosin heavy chains, and light chains at least of class II myosins, have coevolved and are likely to be functionally interdependent, consistent with biochemical evidence showing that regulated actin-dependent MgATPase activity of Dictyostelium myosin II requires isoform specific interactions between the heavy chain head and tail and light chains.

Indexed as

Evolution, MolecularAnimalsDictyosteliumHumansMyosin Heavy ChainsPhylogenyProtein Structure, TertiaryMyosin Heavy Chains

Identifiers

PMID11058170
PMCPMC18803
OpenAlexW2089718116

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.