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Evidence indicates that diseased hearts show basal sarcomeric activation capable of impairing diastolic performance. By activating human cardiomyopathy muscle in ADP-containing solutions without Ca\n            <jats:sup>2+<\/jats:sup>\n            , we showed that actin\u2013myosin blockade is disrupted. This may be caused by the presence of mutations and\/or the reduced phosphorylation of myofilament proteins. Our mechanistic study supports the novel idea that protein kinase A-target phosphorylation and myosin-binding protein C regulate the OFF\u2013ON transition of the thin filaments. ADP increased myofilament force and stiffness in the presence of Ca\n            <jats:sup>2+<\/jats:sup>\n            in cardiomyopathy samples, suggesting this condition limits muscle relaxation through increased actin\u2013myosin interactions. 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