Forskolin, by raising cAMP levels, and ionomycin, through increasing intracellular calcium, both serve as examples of activators that can elicit changes in protein activity by altering secondary messenger levels. Substances like PMA activate PKC, which phosphorylates a broad range of target proteins, thus potentially regulating their function. Sodium orthovanadate's inhibition of protein tyrosine phosphatases can enhance tyrosine phosphorylation signaling, affecting proteins that are regulated by this post-translational modification.
LY294002 and wortmannin, both PI3K inhibitors, along with rapamycin, an mTOR inhibitor, demonstrate how interruption of a signaling pathway can indirectly impact protein activity by preventing downstream signaling events. Similarly, SB203580 and U0126, along with PD98059, are inhibitors of the MAPK pathway components, which can lead to alterations in the activity of proteins that are regulated by this pathway. AICAR's activation of AMPK highlights the role of metabolic state in the regulation of protein functions, indicating how energy balance within the cell can be a significant factor in modulating protein activity. Zinc ions, as a cofactor, underscore the importance of metal ions in protein function, as they are essential for the catalytic activity of many enzymes and can influence the conformation and activity of various proteins.
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