Results 171 to 180 of about 4,049 (222)

Super-relaxed myosins contribute to respiratory muscle hibernation in mechanically ventilated patients. [PDF]

Sci Transl Med
van den Berg M, Shi Z, Claassen WJ, Hooijman P, Lewis CTA, Andersen JL, van der Pijl RJ, Bogaards SJP, Conijn S, Peters EL, Begthel LPL, Uijterwijk B, Lindqvist J, Langlais PR, Girbes ARJ, Stapel S, Granzier H, Campbell KS, Ma W, Irving T, Hwee DT, Hartman JJ, Malik FI, Paul M, Beishuizen A, Ochala J, Heunks L, Ottenheijm CAC.   +27 more
europepmc   +1 more source

A novel deep intronic mutation expands the genotype spectrum of MYH7-related myopathies. [PDF]

Acta Myol
Barp A, Neri LM, Maggi L, Iascone M, Gualandi F.   +4 more
europepmc   +1 more source

Mavacamten and atrial fibrillation: assessing the risk through FAERS and meta-analysis. [PDF]

BMC Cardiovasc Disord
Ding L, Liao X, Yang Y, Chen C, Xiao J.
europepmc   +1 more source

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Myosin from cardiac muscle

Biochimica et Biophysica Acta, 1951
Abstract Myosin from cardiac muscle was prepared which seems to be free from contamination by F-actin. The electrophoretic mobility and sedimentation constant are the same as for crystallized myosin from skeletal muscle, but the sedimentation constant has another concentration dependence.
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Biochemical characteristics of human cardiac myosin

Journal of Molecular and Cellular Cardiology, 1977
Abstract Myosin was purified from the left ventricles of eight patients. Samples of the ventricle were obtained immediately after the death of three patients whereas the rest were obtained from 2 1 2 to 20 h after the death. Human cardiac myosin, like the cardiac myosin from other mammalian species has only two light chains. The corresponding
A, Malhotra, A, Bhan, J, Scheuer
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β-Adrenergic regulation of cardiac myosin

Canadian Journal of Physiology and Pharmacology, 1987
Calcium-independent regulation of the contractile proteins of cardiac muscle has been studied using hyperpermeable cells from rat ventricles and sections of quickly frozen rat hearts. These preparations have been used to study maximum calcium-activated force, myosin ATPase activity, and the maximum velocity of unloaded shortening.
S, Winegrad, G, McClellan, A, Weisberg, L E, Lin, S, Weindling, R, Horowits   +5 more
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Cardiac myosin Phylogenic and pathological changes

1977
Several proteins of the sarcomere differ from one muscle to the other, but it is also becoming evident that cardiac myosin, tropomyosin and troponin are species specific. Moreover, several properties of cardiac myosin could be modified under the influence of thyroxine, exercise, or overloading.
B, Swynghedauw, K, Schwartz, J J, Léger
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Studies on cardiac myosin light chains: Comparison of the sequences of cardiac and skeletal myosin LC-2

Biochemical and Biophysical Research Communications, 1977
Abstract Partial sequence analysis of bovine cardiac myosin LC-2 indicates that it is closely related to LC-2, the “DTNB light chain” of skeletal muscle myosin. The results suggest that myosins from a variety of sources have related light chains of two distinct types, although the sizes and properties of the light chains can vary substantially.
J J, Léger, M, Elzinga
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Methylation of canine cardiac myosin in culture

Experientia, 1980
N epsilon, N epsilon, N epsilon, trimethyllysine and an unidentified methylated amino acid which co-electrophoresed and co-chromatographed with the hydrolysis product of S-adenosyl-L-methionine, occur in fetal canine cardiac myosin and are isotopically labeled in vitro with S-adenosyl-L-(methyl 3H) methionine between the 10th and 12th day of culture.
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The Calmodulin-Dependent Phosphorylation of Cardiac Myosin

1985
Cardiac myosin light chains are phosphorylated in vivo and in vitro. The enzyme myosin light-chain kinase, has been purified and found to be very specific for cardiac myosin light chains. Experiments with skinned cardiac fibers suggest that phosphorylation of myosin light chain-2-decreases ATP consumption, presumably by lowering the cross-bridge cycle.
F, Hofmann, M, Zimmer
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