Results 221 to 230 of about 4,202 (274)

The Network of Exosomes miRNA and p-MLC2 Regulatory Pathway Induced Pathological Cardiac Hypertrophy in Vasn Deficient Mice. [PDF]

J Cell Mol Med
Huang B, Li Q, Yin S, Zhang J, Guo X, Yu N, Hu B, Li L, Huang Q, He M, Sun J.   +10 more
europepmc   +1 more source

Hypertrophic Cardiomyopathy Mutation R723G in MYH7 Enhances Its mRNA‐Stability

Acta Physiologica, Volume 242, Issue 6, June 2026.
Kathrin Kowalski, Luisa Schwarze, Theresia Kraft, Judith Montag   +3 more
wiley   +1 more source

A therapeutic leap: how myosin inhibitors moved from cardiac interventions to skeletal muscle myopathy solutions. [PDF]

J Clin Invest
Bogomolovas J, Chen J.
europepmc   +1 more source

Poster Sessions

HemaSphere, Volume 10, Issue S1, June 2026.
wiley   +1 more source

Internal flexibility of cardiac myosins

Journal of Thermal Analysis, 1996
Conventional and saturation transfer electron paramagnetic resonance spectroscopy (EPR and ST EPR) and differential scanning calorimetry (DSC) were used to study the motional dynamics and segmental flexibility of cardiac myosins. Cardiac myosins isolated from bovine and human heart muscle were spin-labelled with isothiocyanate- or maleimide-based probe
D Lőrinczy, J Belágyi, Belágyi J
exaly   +3 more sources

Two Monoclonal Antibodies Against Human Cardiac Myosins

Protides of the Biological Fluids; Proceedings of the Colloquium, 1983
J Leger, F Pons, Bernard Pau
exaly   +2 more sources

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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.
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources