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This broad category refers to a diverse group of enzymes that are fundamental to the growth, maintenance, and stress resistance of malignant cells. Cellular kinases, including receptor tyrosine kinases (e.g., EGFR, HER2) and intracellular signaling kinases (e.g., PI3K, AKT, BRAF), function as molecular switches that relay growth signals and prevent programmed cell death (PubMed: 29149605). DNA polymerases and associated enzymes like PARP are critical for the rapid genomic replication and DNA damage repair required to sustain the high proliferative rate of tumors (UniProt: P15018). In oncology, these proteins are primary therapeutic targets; small-molecule inhibitors and monoclonal antibodies are used to block their activity, thereby inducing cell cycle arrest or apoptosis. However, the clinical utility of targeting these enzymes is often complicated by the emergence of bypass signaling pathways and secondary mutations that confer drug resistance (NIH: National Cancer Institute). Because many of these enzymes also perform essential functions in healthy tissues, therapeutic strategies must carefully balance efficacy against systemic toxicities such as immunosuppression and organ damage.
Inhibition of phosphate group transfer to protein substrates (kinases) or blocking the assembly of nucleotide polymers (polymerases) to disrupt oncogenic signaling and genomic integrity.
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