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Tyrosine kinases are a group of enzymes that play a critical role in cell signaling. They are a subclass of protein kinases, which transfer phosphate groups from adenosine triphosphate (ATP) to proteins. Specifically, tyrosine kinases catalyze the transfer of a phosphate group to a tyrosine residue on a target protein. This phosphorylation event can alter the protein's activity, leading to a cascade of downstream effects within the cell.

These enzymes are involved in a wide range of cellular processes, including cell growth, proliferation, differentiation, and survival. They act as key regulators of many signal transduction pathways. For instance, they are crucial for the proper functioning of the immune system and for the development of embryos.

Dysregulation of tyrosine kinase activity is often implicated in various diseases, most notably cancer. Aberrant activation of certain tyrosine kinases can drive uncontrolled cell division and tumor formation. Consequently, tyrosine kinases have become important targets for drug development in oncology. Many targeted cancer therapies are designed to inhibit the activity of specific overactive tyrosine kinases, thereby halting or slowing tumor growth. Examples of such drugs include imatinib and gefitinib. Research continues to uncover the complex roles of tyrosine kinases and to develop more precise therapeutic strategies.