Evidence map›Paper›PMID 30189615›Full record

ReviewInternational journal of molecular sciences2018

Actin-Myosin Interaction: Structure, Function and Drug Discovery.

Piyali Guhathakurta, Ewa Prochniewicz, David D Thomas

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Reduced Dietary Protein Induces Changes in the Dental Proteome.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. E3 Ubiquitin LigaseInternational journal of molecular sciences · 2024
    Article
  11. [Latest Findings on Phase Separation of Cytomechanical Proteins].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. A Novel Missense Variant in Actin Binding Domain ofFrontiers in cardiovascular medicine · 2022
    Article
  18. 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

3 authors.

Piyali GuhathakurtaDepartment of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, MN 55455, USA. pgt@ddt.umn.edu.
Ewa ProchniewiczDepartment of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, MN 55455, USA. ewa@ddt.umn.edu.
David D ThomasDepartment of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, MN 55455, USA. ddt@umn.edu.ORCID 0000-0002-8822-2040

Funding

Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
Site-Directed Oxidative Modification of Muscle Protein Structural DynamicsR37AG026160 · NIA · UNIVERSITY OF MINNESOTA · PI THOMAS, DAVID D · 2011 to 2020
$4.5M
Calcium Pump Activators for Heart Failure TherapyR01HL129814 · NHLBI · UNIVERSITY OF MINNESOTA · PI THOMAS, DAVID D · 2015 to 2018
$3.2M
Protein Oxidation, Structure, &Function in Aging MuscleR01AG026160 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 2004 to 2008
$2.2M
Live-Cell Fluorescence Lifetime FRET Assays for HTSR42DA037622 · NIDA · FLUORESCENCE INNOVATIONS, INC. · PI GILLISPIE, GREGORY DAVID · 2015 to 2016
$1.5M
NIAMS NIH HHS R01 AR032961NIA NIH HHS R01 AG026160NIA NIH HHS R37 AG026160NIH HHS R01 AR32961NIH HHS R01 HL129814NIH HHS R37 AG26160NIH HHS R42 DA037622
6 · The paper itself

Abstract

Actin-myosin interactions play crucial roles in the generation of cellular force and movement. The molecular mechanism involves structural transitions at the interface between actin and myosin's catalytic domain, and within myosin's light chain domain, which contains binding sites for essential (ELC) and regulatory light chains (RLC). High-resolution crystal structures of isolated actin and myosin, along with cryo-electron micrographs of actin-myosin complexes, have been used to construct detailed structural models for actin-myosin interactions. However, these methods are limited by disorder, particularly within the light chain domain, and they do not capture the dynamics within this complex under physiological conditions in solution. Here we highlight the contributions of site-directed fluorescent probes and time-resolved fluorescence resonance energy transfer (TR-FRET) in understanding the structural dynamics of the actin-myosin complex in solution. A donor fluorescent probe on actin and an acceptor fluorescent probe on myosin, together with high performance TR-FRET, directly resolves structural states in the bound actin-myosin complex during its interaction with adenosine triphosphate (ATP). Results from these studies have profound implications for understanding the contractile function of actomyosin and establish the feasibility for the discovery of allosteric modulators of the actin-myosin interaction, with the ultimate goal of developing therapies for muscle disorders.

Indexed as

ActinsAdenosine TriphosphateAnimalsDisease SusceptibilityDrug DiscoveryHumansMuscle, SkeletalMutationMyocardiumMyosin Light ChainsMyosinsProtein BindingProtein IsoformsStructure-Activity RelationshipActinsAdenosine TriphosphateMyosin Light ChainsMyosinsProtein IsoformsactinATPdrug discoveryfluorescenceFRETheart failuremyosin

Identifiers

PMID30189615
PMCPMC6163256

What OpenQuestion holds

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Registered trials

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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.