Relevant bibliographies by topics / Cardiac Myosin ATPase Inhibition

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Cardiac Myosin ATPase Inhibition'

Author: Grafiati
Published: 7 June 2025
Last updated: 2 August 2025

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Journal articles on the topic "Cardiac Myosin ATPase Inhibition"

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Tang, Wanjian, William C. Unrath, Rohini Desetty, and Christopher M. Yengo. "Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil." Journal of Biological Chemistry 294, no. 46 (2019): 17314–25. http://dx.doi.org/10.1074/jbc.ra119.010217.

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We investigated a dilated cardiomyopathy (DCM) mutation (F764L) in human β-cardiac myosin by determining its motor properties in the presence and absence of the heart failure drug omecamtive mecarbil (OM). The mutation is located in the converter domain, a key region of communication between the catalytic motor and lever arm in myosins, and is nearby but not directly in the OM-binding site. We expressed and purified human β-cardiac myosin subfragment 1 (M2β-S1) containing the F764L mutation, and compared it to WT with in vitro motility as well as steady-state and transient kinetics measurement
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Hartmund, T., and H. Gesser. "Cardiac force and high-energy phosphates under metabolic inhibition in four ectothermic vertebrates." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 271, no. 4 (1996): R946—R954. http://dx.doi.org/10.1152/ajpregu.1996.271.4.r946.

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Isometric twitch tension of ventricular preparations stimulated at 0.2 Hz fell over 30 min of anoxia by a fraction decreasing in the order rainbow trout, cod, eel, and freshwater turtle. Drops in the estimated cytoplasmic energy state were related to larger tension losses for trout than for the other species, possibly due to larger changes in free phosphate. Anoxic energy degradation was slower for turtle than for the other species. Anoxia combined with glycolytic inhibition (1 mmol/l iodoacetate) enhanced the decrease in twitch tension for a drop in energy state and enlarged the increase in A
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Vander Roest, Alison Schroer, Chao Liu, Makenna M. Morck та ін. "Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state". Proceedings of the National Academy of Sciences 118, № 24 (2021): e2025030118. http://dx.doi.org/10.1073/pnas.2025030118.

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Hypertrophic cardiomyopathy (HCM) is the most common inherited form of heart disease, associated with over 1,000 mutations, many in β-cardiac myosin (MYH7). Molecular studies of myosin with different HCM mutations have revealed a diversity of effects on ATPase and load-sensitive rate of detachment from actin. It has been difficult to predict how such diverse molecular effects combine to influence forces at the cellular level and further influence cellular phenotypes. This study focused on the P710R mutation that dramatically decreased in vitro motility velocity and actin-activated ATPase, in c
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Lim, Megan S., and Michael P. Walsh. "Phosphorylation of skeletal and cardiac muscle C-proteins by the catalytic subunit of cAMP-dependent protein kinase." Biochemistry and Cell Biology 64, no. 7 (1986): 622–30. http://dx.doi.org/10.1139/o86-086.

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Catecholamines are known to influence the contractility of cardiac and skeletal muscles, presumably via cAMP-dependent phosphorylation of specific proteins. We have investigated the in vitro phosphorylation of myofibrillar proteins by the catalytic subunit of cAMP-dependent protein kinase of fast- and slow-twitch skeletal muscles and cardiac muscle with a view to gaining a better understanding of the biochemical basis of catecholamine effects on striated muscles. Incubation of canine red skeletal myofibrils with the isolated catalytic subunit of cAMP-dependent protein kinase and Mg-[γ-32P]ATP
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Toepfer, Christopher N., Hiroko Wakimoto, Amanda C. Garfinkel, et al. "Hypertrophic cardiomyopathy mutations in MYBPC3 dysregulate myosin." Science Translational Medicine 11, no. 476 (2019): eaat1199. http://dx.doi.org/10.1126/scitranslmed.aat1199.

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The mechanisms by which truncating mutations in MYBPC3 (encoding cardiac myosin-binding protein C; cMyBPC) or myosin missense mutations cause hypercontractility and poor relaxation in hypertrophic cardiomyopathy (HCM) are incompletely understood. Using genetic and biochemical approaches, we explored how depletion of cMyBPC altered sarcomere function. We demonstrated that stepwise loss of cMyBPC resulted in reciprocal augmentation of myosin contractility. Direct attenuation of myosin function, via a damaging missense variant (F764L) that causes dilated cardiomyopathy (DCM), normalized the incre
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SMITH, Gerry A., Jamie I. VANDENBERG, Nicholas S. FREESTONE, and Henry B. F. DIXON. "The effect of Mg2+ on cardiac muscle function: is CaATP the substrate for priming myofibril cross-bridge formation and Ca2+ reuptake by the sarcoplasmic reticulum?" Biochemical Journal 354, no. 3 (2001): 539–51. http://dx.doi.org/10.1042/bj3540539.

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Kinetics are established for the activation of the myofibril from the relaxed state [Smith, Dixon, Kirschenlohr, Grace, Metcalfe and Vandenberg (2000) Biochem. J. 346, 393–402]. These require two troponin Ca2+-binding sites, one for each myosin head, to act as a single unit in initial cross-bridge formation. This defines the first, or activating, ATPase reaction, as distinct from the further activity of the enzyme that continues when a cross-bridge to actin is already established. The pairing of myosin heads to act as one unit suggests a possible alternating mechanism for muscle action. A larg
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Yutisha, Deshmukh* Tejashri Kadu Sachin Dighade. "Recent Therapy and Clinical Approaches for Hypertrophic Cardiomyopathy." International Journal of Pharmaceutical Sciences 3, no. 3 (2025): 728–38. https://doi.org/10.5281/zenodo.14998473.

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Hypertrophic cardiomyopathy (HCM) is a genetic cardiac condition characterized by abnormal thickening of the myocardium, often due to mutations in sarcomere protein genes. This leads to complications like arrhythmias, left ventricular outflow tract obstruction (LVOT), and sudden cardiac death (SCD). Recent advancements have highlighted the importance of early diagnosis using echocardiography, genetic testing, and advanced imaging. Among the therapeutic innovations, Mavacamten, an allosteric cardiac myosin ATPase inhibitor, offers a novel approach by reducing myocardial hypercontractility and i
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Makhija, Mahima, Alka Bansal, Punam Jakhar, Lokendra Sharma, Susheel Kumar, and Dharmendra Gupta. "Mavacamten: a novel avenue towards hypertrophic obstructive cardiomyopathy." International Journal of Basic & Clinical Pharmacology 13, no. 4 (2024): 568–72. http://dx.doi.org/10.18203/2319-2003.ijbcp20241661.

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Hypertrophic obstructive cardiomyopathy (HCM) is the most common heterogeneous genetic cardiovascular disorder. Its pathophysiology involves left ventricular hypertrophy, increased fibrosis, hypercontractility, and reduced compliance. The symptomatic obstructive HCM presents as dyspnoea, syncope, chest pain, palpitations, arrhythmias, or sudden death, usually after provocative manoeuvres like exercise. Until April 2022, treatment options were disease non-specific like Beta blockers, Cardio-selective Calcium Channel Blockers, Dipyridamole, and Ranolazine. Mavacamten is a first-in-class, FDA-app
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Tahiliani, Arun G., and John H. McNeill. "Prevention of diabetes-induced myocardial dysfunction in rats by methyl palmoxirate and triiodothyronine treatment." Canadian Journal of Physiology and Pharmacology 63, no. 8 (1985): 925–31. http://dx.doi.org/10.1139/y85-153.

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Diabetes results in myocardial functional alterations which are accompanied by a depression of biochemical parameters such as myosin ATPase and calcium uptake in the sarcoplasmic reticulum. Methyl palmoxirate, a fatty acid analog, is reported to decrease circulating glucose levels by inhibiting fatty acid metabolism, thus forcing carbohydrate utilization. In the present study, we attempted to prevent streptozotocin diabetes-induced myocardial alterations in the rat. Using the isolated working heart preparation, we observed a depression of myocardial function in rats 6 weeks after the induction
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Wu, Li-Ling, Chaoshu Tang, and Maw-Shung Liu. "Altered phosphorylation and calcium sensitivity of cardiac myofibrillar proteins during sepsis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 281, no. 2 (2001): R408—R416. http://dx.doi.org/10.1152/ajpregu.2001.281.2.r408.

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Altered phosphorylation and Ca2+ sensitivity of cardiac myofibrillar proteins during different phases of sepsis were investigated. Sepsis was induced by cecal ligation and puncture (CLP). The results show that phosphorylation of troponin I (TnI) was increased by 268% during the early phase (9 h after CLP) but decreased by 46% during the late phase (18 h after CLP) of sepsis. Phosphorylation of C protein was increased by 76% during the early phase but decreased by 41% during the late phase of sepsis. Phosphorylation of myosin light chain-2 (MLC-2) remained unaltered during the early phase but w
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Dissertations / Theses on the topic "Cardiac Myosin ATPase Inhibition"

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McNamara, James W., Amy Li, Nicola J. Smith, et al. "Ablation of cardiac myosin binding protein-C disrupts the super-relaxed state of myosin in murine cardiomyocytes." ELSEVIER SCI LTD, 2016. http://hdl.handle.net/10150/621325.

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Cardiac myosin binding protein-C (cMyBP-C) is a structural and regulatory component of cardiac thick filaments. It is observed in electron micrographs as seven to nine transverse stripes in the central portion of each half of the A band. Its C-terminus binds tightly to the myosin rod and contributes to thick filament structure, while the N-terminus can bind both myosin S2 and actin, influencing their structure and function. Mutations in the MYBPC3 gene (encoding cMyBP-C) are commonly associated with hypertrophic cardiomyopathy (HCM). In cardiac cells there exists a population of myosin heads i
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Book chapters on the topic "Cardiac Myosin ATPase Inhibition"

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Breier, Albert, Attila Ziegelhöffer, Tania Stankovičová, Peter Dočolomanský, Peter Gemeiner, and Alena Vrbanová. "Inhibition of (Na/K)-ATPase by electrophilic substances: Functional implications." In Cellular Interactions in Cardiac Pathophysiology. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2005-4_24.

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Shao, Qiming, Taku Matsubara, Sunil K. Bhatt, and Naranjan S. Dhalla. "Inhibition of cardiac sarcolemma Na+-K+ ATPase by oxyradical generating systems." In Cellular Interactions in Cardiac Pathophysiology. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2005-4_18.

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Rupp, Heinz, R. Wahl, and R. Jacob. "Chronic cardiac reactions. IV. Effect of drugs and altered functional loads on cardiac energetics as inferred from myofibrillar ATPase and the myosin isoenzyme population." In Cardiac Energetics. Steinkopff, 1987. http://dx.doi.org/10.1007/978-3-662-11289-2_17.

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Wes, Paul D., and Craig Montell. "Myosin III (NINAC)." In Guidebook to the Cytoskeletal and Motor Proteins. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.00132.

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Abstract Skeletal, cardiac, and smooth muscle myosins are very similar in structure to the cytoplasmic myosin 11s. Unconventional myosins like the myosin I family are quite different in structure, but retain the elements of the ATPase and force-producing domains.
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Journal articles
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