ArticleThe Journal of physiology1999
Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.
Article in The Journal of physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
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Who cites it
66 citing papers in PubMed, 126 citations in OpenAlex.
- Human atrial skinned muscle fibers exhibit reduced length-dependent activation but show faster force development kinetics than ventricular muscle.Journal of molecular and cellular cardiology · 2026Article
- Reduction in myofilament CaFrontiers in physiology · 2025Article
- Tail length and E525K dilated cardiomyopathy mutant alter human β-cardiac myosin super-relaxed state.The Journal of general physiology · 2024Article
- Assessing Cardiac Contractility From Single Molecules to Whole Hearts.JACC. Basic to translational science · 2024Review
- Tail Length and E525K Dilated Cardiomyopathy Mutant Alter Human β-Cardiac Myosin Super-Relaxed State.bioRxiv : the preprint server for biology · 2023Article
- Myosin expression and contractile function are altered by replating stem cell-derived cardiomyocytes.The Journal of general physiology · 2023Article
- Proteomic profiling of sudden cardiac death with acquired cardiac hypertrophy.International journal of legal medicine · 2023Article
- Single-molecule mechanics and kinetics of cardiac myosin interacting with regulated thin filaments.Biophysical journal · 2023Article
- Effect of Myosin Isoforms on Cardiac Muscle Twitch of Mice, Rats and Humans.International journal of molecular sciences · 2022Article
- Cardiac myosin contraction and mechanotransduction in health and disease.The Journal of biological chemistry · 2021Review
- STZ-diabetic rat heart maintains developed tension amplitude by increasing sarcomere length and crossbridge density.Experimental physiology · 2021Article
- Chronic Red Bull Consumption during Adolescence: Effect on Mesocortical and Mesolimbic Dopamine Transmission and Cardiovascular System in Adult Rats.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Electrostatic interactions in the SH1-SH2 helix of human cardiac myosin modulate the time of strong actomyosin binding.Journal of muscle research and cell motility · 2021Article
- Positional Isomers of a Non-Nucleoside Substrate Differentially Affect Myosin Function.Biophysical journal · 2020Article
- Sildenafil reverses the hypertrophy of mice right ventricle caused by hypoxia but does not reverse the changes in the myosin heavy chain isoforms.International journal of physiology, pathophysiology and pharmacology · 2020Article
- Cardiomyopathy-associated mutations in tropomyosin differently affect actin-myosin interaction at single-molecule and ensemble levels.Journal of muscle research and cell motility · 2019Review
- Cardiac and skeletal actin substrates uniquely tune cardiac myosin strain-dependent mechanics.Open biology · 2018Article
- Single cardiac ventricular myosins are autonomous motors.Open biology · 2018Article
- A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Science advances · 2017Article
- In vitro actin motility velocity varies linearly with the number of myosin impellers.Archives of biochemistry and biophysics · 2017Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
1. Cardiac V3 myosin generates slower actin filament velocities and higher average isometric forces (in an in vitro motility assay) when compared with the V1 isoform. 2. To account for differences in V1 and V3 force and motion generation at the molecular level, we characterized the mechanics and kinetics of single V1 and V3 myosin molecules using a dual laser trap setup. 3. No differences in either unitary displacement (approximately 7 nm) or force (approximately 0.8 pN) were observed between isoforms; however, the duration of unitary displacement events was significantly longer for the V3 isoform at MgATP concentrations > 10 microM. 4. Our results were interpreted on the basis of a cross-bridge model in which displacement event durations were determined by the rates of MgADP release from, and MgATP binding to, myosin. 5. We propose that the release rate of MgADP from V3 myosin is half that of V1 myosin without any difference in their rates of MgATP binding; thus, kinetic differences between the two cardiac myosin isoforms are sufficient to account for their functional diversity.
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Registered trials
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.