Evidence map›Paper›PMID 32169021›Full record

ReviewAnnual review of biochemistry2020

The Myosin Family of Mechanoenzymes: From Mechanisms to Therapeutic Approaches.

Darshan V Trivedi, Suman Nag, Annamma Spudich, Kathleen M Ruppel, James A Spudich

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
6.6field-weighted citation impact, top 2% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.

  1. Pooled it
  2. Antimalarial cytoskeletal targeting with broad apicomplexan activity.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Small science · 2025
    Article
  12. Review
  13. Review
  14. Chemically-fueled phase transition of a redox-responsive polymer.Science and technology of advanced materials · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

5 authors at 3 institutions in 2 countries.

Darshan V TrivediDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA; email: darshandaasro@gmail.com, kathleen.ruppel@gmail.com, jaspudich@gmail.com.
Suman NagMyoKardia Inc., Brisbane, California 94005, USA; email: sumannag@gmail.com.
Annamma SpudichNational Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560-097, India; email: aspudich@gmail.com.
Kathleen M RuppelDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA; email: darshandaasro@gmail.com, kathleen.ruppel@gmail.com, jaspudich@gmail.com.
James A SpudichDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA; email: darshandaasro@gmail.com, kathleen.ruppel@gmail.com, jaspudich@gmail.com.
Cardiovascular Institute of the South · USSumitomo Chemical (United States) · USTata Institute of Fundamental Research · IN

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
Molecular Characterization of Cardiomyopathy Mutations in Human Cardiac MyosinR01HL117138 · NHLBI · UNIVERSITY OF COLORADO · PI LEINWAND, LESLIE ANNE, PERKINS, THOMAS TUPPER · 2013 to 2021
$4.2M
NHLBI NIH HHS R01 HL117138NIGMS NIH HHS R01 GM033289
6 · The paper itself

Abstract

Myosins are among the most fascinating enzymes in biology. As extremely allosteric chemomechanical molecular machines, myosins are involved in myriad pivotal cellular functions and are frequently sites of mutations leading to disease phenotypes. Human β-cardiac myosin has proved to be an excellent target for small-molecule therapeutics for heart muscle diseases, and, as we describe here, other myosin family members are likely to be potentially unique targets for treating other diseases as well. The first part of this review focuses on how myosins convert the chemical energy of ATP hydrolysis into mechanical movement, followed by a description of existing therapeutic approaches to target human β-cardiac myosin. The next section focuses on the possibility of targeting nonmuscle members of the human myosin family for several diseases. We end the review by describing the roles of myosin in parasites and the therapeutic potential of targeting them to block parasitic invasion of their hosts.

Indexed as

Adenosine TriphosphateAllosteric RegulationAnimalsBiomechanical PhenomenaCryptosporidiumEnzyme InhibitorsGene ExpressionHeart FailureHumansMultigene FamilyMutationMyosinsNeoplasmsNervous System DiseasesPlasmodiumProtozoan InfectionsAdenosine TriphosphateEnzyme InhibitorsMyosinscancerinteracting heads motifmyosinparasitestherapeutics

Identifiers

PMID32169021
PMCPMC8742983
OpenAlexW3012351975

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.