ArticleThe Journal of biological chemistry2019
Converter domain mutations in myosin alter structural kinetics and motor function.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Multi-omics Insight into Cardiac Myofibril Remodeling in Post-Prandial Burmese Pythons.bioRxiv : the preprint server for biology · 2026Article
- Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin.The Journal of general physiology · 2023Article
- Article
- Muscle LIM Protein Force-Sensing Mediates Sarcomeric Biomechanical Signaling in Human Familial Hypertrophic Cardiomyopathy.Circulation · 2022Article
- Cardiac myosin contraction and mechanotransduction in health and disease.The Journal of biological chemistry · 2021Review
- Impact of regulatory light chain mutation K104E on the ATPase and motor properties of cardiac myosin.The Journal of general physiology · 2021Article
- Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin.Biophysical journal · 2021Article
- Complexity in genetic cardiomyopathies and new approaches for mechanism-based precision medicine.The Journal of general physiology · 2021Article
- FRET and optical trapping reveal mechanisms of actin activation of the power stroke and phosphate release in myosin V.The Journal of biological chemistry · 2020Article
- Structural and Computational Insights into a Blebbistatin-Bound Myosin•ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke.International journal of molecular sciences · 2020Article
- Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil.The Journal of biological chemistry · 2019Article
- Mechanistic analysis of actin-binding compounds that affect the kinetics of cardiac myosin-actin interaction.The Journal of biological chemistryArticle
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Authors and funding
9 authors.
Funding
Abstract
Myosins are molecular motors that use a conserved ATPase cycle to generate force. We investigated two mutations in the converter domain of myosin V (R712G and F750L) to examine how altering specific structural transitions in the motor ATPase cycle can impair myosin mechanochemistry. The corresponding mutations in the human β-cardiac myosin gene are associated with hypertrophic and dilated cardiomyopathy, respectively. Despite similar steady-state actin-activated ATPase and unloaded
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