ArticleScience advances2026
Mavacamten inhibits myosin activity by stabilizing the myosin interacting-heads motif and stalling motor force generation.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed.
- Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy.Nature communications · 2026Article
- Cryo-EM reveals how cardiomyopathy therapeutic drugs modulate the myosin motors of the heart.Science advances · 2026Article
- Cryo-EM structure of shutdown human nonmuscle myosin 2A.Science advances · 2026Article
- Comparing cryo-EM structures of the vertebrate cardiac muscle thick filament.Biophysical reviews · 2026Article
- S2Tag, a novel affinity tag for the capture and immobilization of coiled-coil proteins: Application to the study of human β-cardiac myosin.The Journal of biological chemistry · 2025Article
- Cryo-EM Reveals How Cardiomyopathy Therapeutic Drugs Modulate the Myosin Motors of the Heart.bioRxiv : the preprint server for biology · 2025Article
- Review
- Mechanistic insights into effects of the cardiac myosin activator omecamtiv mecarbil from mechanokinetic modelling.Frontiers in physiology · 2025Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Most sudden cardiac deaths in young people arise from hypertrophic cardiomyopathy, a genetic heart muscle disease. Treatment has until recently been limited to symptomatic relief or invasive procedures. Small-molecule modulators of cardiac myosin are promising therapeutic options to target disease progression. Mavacamten, the first Food and Drug Administration-approved example, has an unclear mechanism. To address this, we solved cryo-electron microscopy (cryo-EM) structures of beta-cardiac heavy meromyosin in three adenosine 5'-diphosphate and inorganic phosphate (ADP.P
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