Mare Inhibitors

Chemical inhibitors of Mare target various kinases and receptors that participate in signaling pathways which Mare is known to be involved with. Imatinib, for example, is a potent inhibitor of the Abl kinase, an enzyme which Mare relies upon for necessary phosphorylation events. By inhibiting Abl kinase, Imatinib effectively hampers the downstream effects that Mare exerts within the cell. Similarly, Dasatinib and Bosutinib both target Src-family kinases, which are another group of enzymes that can phosphorylate Mare or its associated proteins. By inhibiting these kinases, Mare's activity is decreased due to a lack of necessary phosphorylation which is critical for its function. Nilotinib also joins this group by specifically inhibiting the Bcr-Abl tyrosine kinase, likely reducing the phosphorylation state of proteins upstream of Mare, and thus, Mare's activity is decreased.

In addition to tyrosine kinase inhibitors, Mare's function is indirectly diminished by chemicals that inhibit the receptors Mare functions downstream of. Erlotinib and Gefitinib, for instance, both inhibit EGFR tyrosine kinase, disrupting the signaling pathways Mare is part of. Without active EGFR signaling, Mare's role in propagating cellular responses is impaired. Lapatinib extends this approach by inhibiting both ErbB2 and EGFR, further ensuring that Mare signaling is diminished through lack of upstream activator signals. Sorafenib and Sunitinib, while broadly targeting multiple tyrosine kinases, would similarly lead to a reduction in Mare's activity by curtailing the activity of kinases that Mare may be downstream of. Pazopanib and Axitinib, by targeting VEGFR, PDGFR, and c-Kit, also reduce the upstream signals that lead to Mare activation, thereby reducing Mare's overall functional activity within the cell. Vandetanib's inhibition of VEGFR and EGFR signaling pathways offers a similar reduction in Mare's activity, ensuring that Mare is less able to contribute to its normal cellular functions.