Abstract
Mammalian cells make decisions to divide, differentiate, adhere, chemotax, secrete, quiesce or apoptose on the basis of their developmental history, extracellular matrix composition, and the presence or absence of growth factors/differentiatiation agents and other cellular activators. From extensive research over the past ten years it has become clear that these decisions are mediated in most cases by the activation of specific protein kinases in the cytosol of the cell. A typical mammalian cell expresses hundreds of different protein-Ser/Thr kinases and protein-Tyr kinases. Thus, in order for a cellular activator to elicit a specific cellular response it is necessary that a specific subset of these kinases be activated and that these kinases find specific targets to phosphorylate. This manuscript focuses on a new approach to determining the structural basis for how protein kinases find their specific targets in the cell interior. The primary focus is on protein-Tyr kinases.
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Cantley, L.C., Songyang, Z. (1996). The Structural Basis for Specificity in Protein-Tyrosine Kinase Signaling. In: Tsiftsoglou, A.S., Sartorelli, A.C., Housman, D.E., Dexter, T.M. (eds) Tumor Biology. NATO ASI Series, vol 99. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61180-3_2
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DOI: https://doi.org/10.1007/978-3-642-61180-3_2
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