Results 21 to 30 of about 4,202 (274)
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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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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Disease mutations in striated muscle myosins [PDF]
, 2020 Over 1000 disease-causing missense mutations have been found in human β-cardiac, α-cardiac, embryonic and adult fast myosin 2a myosin heavy chains. Most of these are found in human β-cardiac myosin heavy chain.
Peckham, M, Parker, F
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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
doaj +1 more source
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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eLife, 2017 Cardiac β-myosin variants cause hypertrophic (HCM) or dilated (DCM) cardiomyopathy by disrupting sarcomere contraction and relaxation. The locations of variants on isolated myosin head structures predict contractility effects but not the prominent ...
Lorenzo Alamo +6 more
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Cardiac Myosin Adenosinetriphosphatase of Rat and Mouse [PDF]
Circulation Research, 1974 Cardiac myosin obtained from rats and mice (smaller animals) had a higher adenosinetriphosphatase (ATPase) activity in the presence of calcium ions (Ca 2+ ) than did cardiac myosin from rabbits and dogs (larger animals).
Y, Yazaki, M S, Raben
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Functional Characterization of Cardiac Myosin Isoforms.
The Japanese Journal of Physiology, 1998 In this brief review, we have discussed the functional significance of cardiac myosin isoform redistribution. The development of in vitro motility assay techniques has greatly aided the research in this field. The next important step would be the integration of data at molecular or cellular level to account for the pathophysiology of animal or human ...
SUGIURA, Seiryo, YAMASHITA, Hiroshi
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Danicamtiv increases myosin recruitment and alters cross-bridge cycling in cardiac muscle [PDF]
, 2023 Background: Modulating myosin function is a novel therapeutic approach in patients with cardiomyopathy. Danicamtiv is a novel myosin activator with promising preclinical data that is currently in clinical trials.
Saffie Mohran +41 more
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Serum Response Factor in muscle tissues: from development to ageing
European Journal of Translational Myology, 2016 Skeletal, cardiac and smooth muscle cells share various common characteristic features. During development the embryonic mesodermal layer contribute at different proportions to the formation of these tissues.
Dario Coletti +4 more
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