ArticleBiophysical journal2009
Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.
- Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation.Frontiers in physiology · 2022Pooled it
- Troponin I - a comprehensive review of its function, structure, evolution, and role in muscle diseases.Animal cells and systems · 2025Review
- Basic residues within the cardiac troponin T C terminus are required for full inhibition of muscle contraction and limit activation by calcium.The Journal of biological chemistry · 2019Article
- Stepwise C-Terminal Truncation of Cardiac Troponin T Alters Function at Low and Saturating CaBiophysical journal · 2018Article
- Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Biochemistry · 2017Article
- Order-Disorder Transitions in the Cardiac Troponin Complex.Journal of molecular biology · 2016Review
- The functional significance of the last 5 residues of the C-terminus of cardiac troponin I.Archives of biochemistry and biophysics · 2016Article
- Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin.Frontiers in physiology · 2016Article
- Disease causing mutations of troponin alter regulated actin state distributions.Journal of muscle research and cell motility · 2012Review
- The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin.Biophysical journal · 2012Article
- Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.Journal of molecular and cellular cardiology · 2011Article
- A computational and experimental approach to investigate bepridil binding with cardiac troponin.The journal of physical chemistry. B · 2011Article
- Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin.Biochemical and biophysical research communications · 2011Article
- Low temperature dynamic mapping reveals unexpected order and disorder in troponin.The Journal of biological chemistry · 2010Article
- Dual regulatory functions of the thin filament revealed by replacement of the troponin I inhibitory peptide with a linker.The Journal of biological chemistry · 2010Article
- Molecular dynamics studies on troponin (TnI-TnT-TnC) complexes: insight into the regulation of muscle contraction.Journal of biomolecular structure & dynamics · 2010Article
- Kinetics of regulated actin transitions measured by probes on tropomyosin.Biophysical journal · 2010Article
- The C terminus of cardiac troponin I stabilizes the Ca2+-activated state of tropomyosin on actin filaments.Circulation research · 2010Article
- Ala scanning of the inhibitory region of cardiac troponin I.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We examined four cardiomyopathy-causing mutations of troponin I that appear to disturb function by altering the distribution of thin filament states. The R193H (mouse) troponin I mutant had greater than normal actin-activated myosin-S1 ATPase activity in both the presence and absence of calcium. The rate of ATPase activity was the same as that of the wild-type at near-saturating concentrations of the activator, N-ethylmaleimide-S1. This mutant appeared to function by stabilizing the active state of thin filaments. Mutations D191H, R146G, and R146W had lower ATPase activities in the presence of calcium, but higher activities in the absence of calcium. These effects were most pronounced with mutations at position 146. For all three mutants the rates were similar to those of the wild-type at near-saturating concentrations of N-ethylmaleimide-S1. These results, combined with previous results, show that any alteration in the normal distribution of actomyosin states is capable of producing cardiomyopathy. The results of the D191H, R146G, and R146W mutations are most readily explained if the intermediate state of regulated actin has a unique function. The intermediate state appears to have an ability to accelerate the rate of ATP hydrolysis by myosin that exceeds that of the inactive state.
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Registered trials
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