… phosphorylated tyrosine as a stable yet reversible mod ification of proteins implies the
existence of one or more protein kinases capable of phosphorylating tyrosine and also of protein …

… are the protein tyrosine kinases (PTKs), which catalyzethe transfer of the γ phosphate of
ATP to tyrosine residues on proteinsubstrates. Phosphorylation of tyrosine residues modulates …

… tyrosine kinases in human cancers has been identified. In this article, the mechanisms by …
protein tyrosine kinases may participate in malignant transformation and the tyrosine kinases …

… To create a catalog of protein tyrosine kinase coding regions in the human genome, we
performed iterative BLAST searches against the six-frame translations of the human genomic …

… proteintyrosine kinase (PTK) activity and belongs to the receptor proteir~-tyrosine kinase (…
are secreted, soluble proteins, but membrane-bound proteins as well as extracellular matrix …

… differences between kinases allow the design of compounds which inhibit only an acceptable
few. This review gives a general overview of protein tyrosine kinase structural biology, …

… tyrosine kinases (RTKs) and non-receptor tyrosine kinases (NRTKs) ( … a tyrosine kinase
domain, NRTKs often contain within the same polypeptide chain several protein-protein or protein…

Protein tyrosine kinases (PTKs) play a key role in normal cell and tissue development.
Enhanced PTK activity is intimately correlated with proliferative diseases, such as cancers, …

… phosphatases (PTPs) identified as negative regulators of receptor tyrosine kinase (RTK) …
tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shp1. …

… The ErbB/HER protein-tyrosine kinases, which include the epidermal growth factor
receptor, … He discovered that the EGF receptor was a protein-tyrosine kinase, which was a …