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Multiple kinases and proteins is a collective designation rather than a single therapeutic target, representing a group of proteins—primarily kinases—that are simultaneously inhibited by polypharmacological agents. This term is frequently used in drug discovery to describe the profile of multi-kinase inhibitors (MKIs) which target various members of the kinome, such as VEGFR, PDGFR, FGFR, and SRC family kinases (Source: Nature Reviews Drug Discovery). These targets are central to biological processes including signal transduction, cell cycle regulation, and angiogenesis, making them critical in the pathology of various malignancies and inflammatory conditions. While targeting multiple proteins can overcome pathway redundancy and resistance in cancer, it also presents significant challenges in terms of off-target toxicity and narrow therapeutic windows. In clinical databases, this entry serves as a placeholder for compounds whose efficacy is derived from a broad spectrum of molecular interactions rather than a single, well-defined protein-ligand event (Source: PubMed, PMC5439223). Examples of drugs targeting multiple kinases include sorafenib and sunitinib, which are used to treat renal cell carcinoma and other solid tumors by inhibiting both tumor cell proliferation and blood vessel formation. The complexity of these interactions often requires advanced proteomics and kinome-wide screening to fully characterize the drug's impact on the cellular signaling landscape (Source: Journal of Medicinal Chemistry).
Inhibition of multiple protein kinases and other cellular proteins, often through ATP-competitive binding across conserved domains.
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