MYL10 Inhibitors are a set of chemical compounds that aim to specifically decrease the functional activity of MYL10 through targeting various signaling pathways and cellular processes. Y-27632 and H-1152, as ROCK inhibitors, directly reduce the phosphorylation of myosin light chains like MYL10, resulting in diminished myosin-mediated contractility. ML-7 and ML-9, both inhibitors of myosin light chain kinase, prevent the phosphorylation of MYL10, thereby limiting its capacity to facilitate muscle contraction. Similarly, Blebbistatin by inhibiting myosin II ATPase activity, and W-7 and KN-93 by antagonizing calmodulin and inhibiting CaMKII respectively, all contribute to the reduction in MYL10 activity by affecting the phosphorylation process that MYL10 undergoes to function effectively. These inhibitors work cohesively to suppress the activation and action of MYL10, ensuring that its role in muscle contraction and cell motility is attenuated.
Furthermore, Gö 6976, by inhibiting Protein kinase C, and BAPTA-AM, by chelating intracellular calcium, prevent the phosphorylation and subsequent activation of MYL10. Calyculin A's inhibition of phosphatases keeps MYL10 in a phosphorylated and less active state, while Marimastat impacts extracellular matrix remodeling, thus indirectly influencing the structural context within which MYL10 operates. NSC 23766, as a Rac1 inhibitor, disrupts the dynamics of the actin cytoskeleton, affecting MYL10's role in cell shape and motility. Collectively, these MYL10 inhibitors disrupt the signaling pathways and enzymatic reactions essential for the proper functioning of MYL10, thereby providing a multifaceted approach to diminish MYL10's activity in cellular processes.
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