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The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.
Skeletal muscles present a non-cross-bridge increase in sarcomere stiffness and tension on Ca(2+) activation, referred to as static stiffness and static tension, respectively. It has beenExpand
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Non-crossbridge forces in activated striated muscles: a titin dependent mechanism of regulation?
When skeletal muscles are stretched during activation in the absence of myosin-actin interactions, the force increases significantly. The force remains elevated throughout the activation period. TheExpand
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Reduced passive force in skeletal muscles lacking protein arginylation.
Arginylation is a posttranslational modification that plays a global role in mammals. Mice lacking the enzyme arginyltransferase in skeletal muscles exhibit reduced contractile forces that have beenExpand
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Residual force depression in single sarcomeres is abolished by MgADP-induced activation
The mechanisms behind the shortening-induced force depression commonly observed in skeletal muscles remain unclear, but have been associated with sarcomere length non-uniformity and/or crossbridgeExpand
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Arginylation of myosin heavy chain regulates skeletal muscle strength.
Protein arginylation is a posttranslational modification with an emerging global role in the regulation of actin cytoskeleton. To test the role of arginylation in the skeletal muscle, we generated aExpand
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Posttranslational Arginylation Regulates Striated Muscle Function
In this article, we propose the hypothesis that the posttranslational arginylation of proteins, a process catalyzed by the enzyme arginyl-tRNA-transferase, regulates active and passive forceExpand
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Shortening-Induced Force Depression in Single Sarcomeres is Abolished by MgADP-Activation
The mechanisms behind the shortening-induced force depression (FD) commonly observed in skeletal muscles remain unclear, but have been associated with sarcomere length non-uniformity and/orExpand
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The load dependence and the force-velocity relation in intact myosin filaments from skeletal and smooth muscles.
In the present study we evaluated the load dependence of force produced by isolated muscle myosin filaments interacting with fluorescently labeled actin filaments, using for the first time, wholeExpand
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