Protein tyrosine kinase plays a role in this task, too.

Additional instances of factor-influenced protein tyrosine kinase activity, similar to this one, exist.

The balance between protein tyrosine kinase and phosphatase activity is an integral part of this regulatory mechanism.

Emodin, a protein tyrosine kinase inhibitor from Polygonum cuspidatum.

Much research has already noted the significant effect that inhibitors of the radically functioning protein tyrosine kinase enzymes have on related ailments.

In the absence of cytokine, JAKs lack protein tyrosine kinase activity.

The Lymphocyte specific protein tyrosine kinase Lck (also called p56-LCK)

Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene.

Lck (or lymphocyte-specific protein tyrosine kinase) is a protein that is found inside specialized cells of the immune system called lymphocytes.

This gene encodes a cytosolic protein tyrosine kinase that is found concentrated in the focal adhesions that form among cells attaching to extracellular matrix constituents.

Both the protein kinase C pathway and the protein tyrosine kinase pathways are activated, resulting in upregulating production of proinflammatory cytokines.

Mammalian Bruton's tyrosine kinase (Btk), a protein tyrosine kinase involved in modulation of diverse cellular processes.

Phosphorylates of tyrosine and protein tyrosine kinase, related to the src oncoprotein seem to be important as links between the integrin and intracellular signalling pathways.

A protein tyrosine kinase called pp125 is likely at hand in the influence of cellular focal adhesions, as indicated by an immunofluorescent localization of the said kinase.

FAK is a highly conserved, non-receptor tyrosine kinase originally identified as a substrate for the oncogene protein tyrosine kinase v-src.

This fused gene encodes for a protein that displays high protein tyrosine kinase activity (this activity is due to the "ABL1" half of the protein).

The PDGFs bind to the protein tyrosine kinase receptors PDGF receptor-α and -β.

Erbin's C-terminal PDZ domain is able to bind to ErbB2, a protein tyrosine kinase which is often associated with poor prognosis in epidermal oncogenesis.

GAB2 along with many other adaptor, scaffold, and docking proteins, was discovered in the mid 1990s during the isolation and cloning of protein tyrosine kinase substrates and association partners.

The ABL1 proto-oncogene encodes a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response.

The protein tyrosine kinase pp125 is one of the major phosphotyrosine-containing proteins in unaffected (untransformed) avian and rodent fibroblast cells (fibroblast cells are explained above in some detail).

The lipid malhamensilipin A, isolated by the groups of Slate and Gerwick in 1994, displayed both antimicrobial activity as well as an inhibition of the pp60 protein tyrosine kinase.

This GPCR-mediated regulation of ion channels also depends on the coordination and parallel regulation of protein tyrosine kinase and protein tyrosine phosphatase activities [ 24 ] .

Included among the protein ligands of this domain are ankyrin, protein 4.2, protein 4.1, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), phosphofructokinase, aldolase, hemoglobin, hemichromes, and the protein tyrosine kinase (p72syk).

In similar manner, protein tyrosine kinase inhibitor STI571 was found to significantly reduce the physical size of tumors; they decreased roughly 65% in size in 4 months of trialing, and continued to diminish.