Results 211 to 220 of about 663,430 (263)
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Muscle contraction and muscle proteins
Proceedings of the Royal Society of London. Series B - Biological Sciences, 1950Abstract There are three ways in which we can gain knowledge of the change of protein structure connected with muscular contraction. The first way is the observation of the contracting muscle itself. The changes of structural qualities and their time sequence have to be investigated.
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Muscle proteins — their actions and interactions
Current Opinion in Structural Biology, 1996Muscle contracts by the myosin cross-bridges "rowing' the actin filaments past the myosin filaments. In the past year many structural details of this mechanism have become clear. Structural studies indicate distinct states for myosin S1 in the rigor, ATP or "down' conformation and in the products complex (ADP.Pi) or "up' to state.
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Heat Coagulation of Muscle Proteins
Nature, 1945A CHANGE in pH when proteins are denatured has been reported by other workers1,2. When making observations of the change in pH of meat resulting from heat coagulation, we were struck both by the magnitude and by the variability of the change. Muscle is a highly buffered system3, and a change such as that observed, for example, from 5·6 to 5·9 ...
E C, BATE-SMITH, J R, BENDALL
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Insulin and protein synthesis in muscle
Archives of Biochemistry and Biophysics, 1970Abstract Insulin stimulates in vitro the incorporation of labeled amino acid into muscle protein. A study of this phenomenon has been carried out in which various incubation conditions have been varied. The insulin stimulatory effect is lost when sodium ion is removed from the medium, when the amino acid concentration of the medium is increased to ...
S, Goldstein, W J, Reddy
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The action of a muscle proteinase on the myofibrillar proteins of bovine muscle
Journal of the Science of Food and Agriculture, 1974AbstractMyofibrillar proteins from bovine muscle have been treated with a Ca2+ activated muscle proteinase and the consequent changes in these proteins have been examined by various techniques. Tropomyosin, α‐actinin and troponin were substrates for the enzyme, the last losing its property of inhibiting actomyosin ATPase in the absence of Ca2+ ions ...
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Electrophoresis of avian muscle proteins
British Poultry Science, 19781. The electrophoretic patterns of water-soluble proteins of avian muscle showed differences due both to species and to muscle type. 2. Each muscle pattern within a species showed a unique protein band which distinguished that species from other species.
C C, Wilkinson, J M, Jones
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Muscle proteins and muscular dystrophy
Current Opinion in Cell Biology, 1989In recent years, muscle biology has been transformed by the use of recombinant DNA technology. A result of this approach of great practical importance is the localization on the human X-chromosome of the site of mutation(s) causing Duchenne muscular dystrophy (DMD). DMD is a devastating disease causing degeneration of skeletal muscle fibres and leading
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Muscle Intermediate Filament Proteins
2004Publisher Summary Intermediate filaments (IFs) appear to function as mechanical integrators of cellular space and provide the overall cytoskeletal integrity and strength, as well as the organization, necessary for supporting contraction. The five muscle cell IF proteins include desmin, vimentin, synemin, paranemin (avian)/nestin (mammalian ortholog),
Richard M, Robson +2 more
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Myofibrillar Proteins of Skeletal Muscle
1971Publisher Summary Muscle is a highly integrated chemical machine. One of the most impressive aspects of this integration is the ability to increase the rate of energy utilization by approximately 2500-fold within milliseconds. This efficient transduction of chemical into mechanical energy occurs through the subtleties of the interactions of myosin ...
E J, Briskey, T, Fukazawa
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Transcriptional control of muscle proteins
Trends in Cardiovascular Medicine, 1991The development of a muscle cell from a precursor cell involves a massive adjustment of gene expression such that over 50 previously silent genes are expressed to produce the muscle proteins required for contractile functions. In differentiated muscle, hormonal and physiologic stimuli modify the expression of these proteins primarily at the level of ...
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