Results 11 to 20 of about 4,049 (222)
Myosin modulators: emerging approaches for the treatment of cardiomyopathies and heart failure
The Journal of Clinical Investigation, 2022 Myosin modulators are a novel class of pharmaceutical agents that are being developed to treat patients with a range of cardiomyopathies. The therapeutic goal of these drugs is to target cardiac myosins directly to modulate contractility and cardiac ...
Sharlene M. Day +2 more
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Frontiers in Cardiovascular Medicine, 2022 In this study, we investigated the rescue potential of two phosphomimetic mutants of the myosin regulatory light chain (RLC, MYL2 gene), S15D, and T160D RLCs.
Katarzyna Kazmierczak +3 more
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Biology Open, 2021 The fundamental basis of muscle contraction ‘the sliding filament model’ (Huxley and Niedergerke, 1954; Huxley and Hanson, 1954) and the ‘swinging, tilting crossbridge-sliding filament mechanism’ (Huxley, 1969; Huxley and Brown, 1967) nucleated a field ...
Manuel Schmid, Christopher N. Toepfer
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Binding pocket dynamics along the recovery stroke of human β-cardiac myosin.
PLoS Computational Biology, 2023 The druggability of small-molecule binding sites can be significantly affected by protein motions and conformational changes. Ligand binding, protein dynamics and protein function have been shown to be closely interconnected in myosins.
Fariha Akter +2 more
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Molecular Characteristics of Canine Cardiac Myosin [PDF]
Circulation Research, 1965 Cardiac myosin was obtained from the hearts of normal dogs by conventional extraction and precipitation techniques, followed by ammonium sulfate fractionation in the presence of 2.0 M lithium chloride. The molecular characteristics of this protein preparation are presented. Cardiac myosin prepared by this technique shows less tendency than
R J, LUCHI, E M, KRITCHER, H L, CONN
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Nanosurfer assay dissects β-cardiac myosin and cardiac myosin-binding protein C interactions
Biophysical Journal, 2022 Cardiac myosin-binding protein C (cMyBP-C) modulates cardiac contractility through putative interactions with the myosin S2 tail and/or the thin filament. The relative contribution of these binding-partner interactions to cMyBP-C modulatory function remains unclear. Hence, we developed a "nanosurfer" assay as a model system to interrogate these cMyBP-C
Anja M. Touma +8 more
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Ensemble Force Changes that Result from Human Cardiac Myosin Mutations and a Small-Molecule Effector
Cell Reports, 2015 Cardiomyopathies due to mutations in human β-cardiac myosin are a significant cause of heart failure, sudden death, and arrhythmia. To understand the underlying molecular basis of changes in the contractile system’s force production due to such mutations
Tural Aksel +4 more
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Bioinformatics and Biology Insights, 2012 Myosins are one of the largest protein superfamilies with 24 classes. They have conserved structural features and catalytic domains yet show huge variation at different domains resulting in a variety of functions.
Divya P. Syamaladevi +6 more
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Direct regulation of striated muscle myosins by nitric oxide and endogenous nitrosothiols.
PLoS ONE, 2010 BackgroundNitric oxide (NO) has long been recognized to affect muscle contraction, both through activation of guanylyl cyclase and through modification of cysteines in proteins to yield S-nitrosothiols. While NO affects the contractile apparatus directly,
Alicia M Evangelista +7 more
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Cardiac Myosin Binding Protein C [PDF]
Circulation Research, 1999 Abstract —Myosin binding protein C (MyBP-C) is one of a group of myosin binding proteins that are present in the myofibrils of all striated muscle. The protein is found at 43-nm repeats along 7 to 9 transverse lines in a portion of the A band where crossbridges are found (C zone).
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