Evidence map›Paper›PMID 8421702›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

Molecular evolution of the myosin family: relationships derived from comparisons of amino acid sequences.

H V Goodson, J A Spudich

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
19.4field-weighted citation impact, top 1% 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

46 citing papers in PubMed, 169 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Smooth muscle-like CaScientific reports · 2018
    Article
  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. Article
  11. An invertebrate smooth muscle with striated muscle myosin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  12. Article
  13. Article
  14. Article
  15. Structural and functional insights on the Myosin superfamily.Bioinformatics and biology insights · 2012
    Article
  16. How are the cellular functions of myosin VI regulated within the cell?Biochemical and biophysical research communications · 2008
    Review
  17. Article
  18. Multiplying myosins.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  19. A standardized kinesin nomenclature.The Journal of cell biology · 2004
    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.

H V GoodsonDepartment of Biochemistry, Beckman Center for Molecular and Genetic Medicine, Stanford University Medical School, CA 94305.
J A Spudich
Stanford University · US

Funding

Myosin-II Dynamics and CytokinesisR01GM046551 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES A · 2002 to 2005
$1.6M
REGULATION OF DICTYOSTELIUM MYOSIN BY PHOSPHORYLATIONR37GM046551 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES A · 1991 to 2000
$272k
NIGMS NIH HHS GM46551
6 · The paper itself

Abstract

To examine the evolutionary relationships between members of the myosin family, we have used two different phylogenetic methods, distance matrix and maximum parsimony, to analyze all available myosin head sequences. We find that there are at least three equally divergent classes of myosin, demonstrating that the current classification of myosin into only two classes needs to be reexamined. In the myosin II class, smooth muscle myosin is more closely related to nonmuscle myosin than to striated muscle myosin, implying that smooth muscle and skeletal muscle myosins were independently derived from nonmuscle myosin and suggesting that similarities between these types of muscle are the result of convergent evolution. The grouping of head sequences produced by phylogenetic analysis is consistent with classifications based on enzymology and structural localization and is generally consistent with grouping based on common tail structure elements. This result demonstrates that specific head sequences are tightly coupled to specific tail sequences throughout evolution and challenges the idea that myosin heads are freely interchangeable units whose unique function is determined only by the tail structure to which it is attached.

Indexed as

Biological EvolutionAnimalsMultigene FamilyMusclesMyosinsProtein ConformationSequence AlignmentSequence Homology, Amino AcidSoftwareMyosins

Identifiers

PMID8421702
PMCPMC45723
OpenAlexW1994728394

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.