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CA2 — DMD

Text-mined interactions from Literome

Notarianni et al., J Muscle Res Cell Motil 2000 : Thin filament activation of myosin MgATPase is Ca2+ regulated but thin filaments assembled from smooth muscle actin, tropomyosin and caldesmon plus brain or aorta calmodulin are not Ca2+ regulated at 25 degrees C/50 mM KCl
Sadeghi et al., Am J Physiol Cell Physiol 2002 (Disease Models, Animal...) : In the present study, we employed immunohistochemical and electrophysiological techniques to investigate the potential regulation of cardiac L-type Ca2+ channel activity by dystrophin and alpha-actinin in cardiac myocytes and in heterologous cells
Marston et al., Biochem J 1980 : Thin-filament activation of myosin ATPase activity increased markedly in the range 10 ( -6 ) -10 ( -5 ) M-Ca2+ and was half maximal at 2.7 x 10 ( -6 ) M ( pCa2+ 5.6 )
Denetclaw et al., Mol Biol Cell 1993 (Muscular Dystrophy, Animal) : These results support the view that dystrophin expression in heterokaryons allows for efficient control of [Ca2+ ] i
Maltin et al., Biosci Rep 1993 : The rate of dystrophin degradation and nature of the proteolytic fragments formed at pH 5.5 and pH 7.5 ( corresponding to the two major protease groups of relevance to intracellular protein catabolism ) were broadly similar ; incorporation of protease inhibitors in the above system suggested that Ca2+ activated proteinase and cathepsin D are principally responsible for the degradation of dystrophin at pH 7.5 and pH 5.5 respectively