Forskolin, which raises intracellular cAMP levels, thereby activating protein kinase A (PKA). The activation of PKA can lead to the phosphorylation of proteins that are part of WDR81's functional network. Similarly, Ionomycin increases intracellular calcium concentrations, which may affect calcium-dependent proteins that interact with or regulate WDR81. PMA is another activator that triggers protein kinase C (PKC), which can alter the phosphorylation state of proteins within WDR81-associated pathways. Epidermal growth factor (EGF), through its receptor EGFR, initiates a cascade that can result in the modulation of protein interactions with WDR81. Dibutyryl cAMP, a cAMP analog, activates cAMP-dependent pathways, influencing WDR81's activity by similar means as Forskolin.
Chemicals like 5-Azacytidine, which inhibits DNA methyltransferases, lead to changes in gene expression patterns, potentially causing an increase in WDR81 expression or the expression of its regulatory partners. SB203580 and U0126, inhibitors of p38 MAPK and MEK respectively, modify the stress response and MAPK/ERK pathways that can regulate WDR81. LY294002, an inhibitor of PI3K, can affect AKT signaling, while PD98059, a MEK1/2 inhibitor, influences the MAPK/ERK pathway, both of which are important for the regulation of WDR81. Rapamycin specifically inhibits mTOR, a central regulator of cell growth and protein synthesis, which could have implications for WDR81's role in these processes. Staurosporine, a potent kinase inhibitor, broadly affects kinase activity and thus might impact multiple pathways that converge on WDR81.
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