Results 341 to 350 of about 514,942 (384)
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Non-receptor protein tyrosine kinases as immune targets of viruses
Immunology Today, 1997Abstract Non-receptor protein tyrosine kinases (NRPTKs) are critically involved in signaling pathways that modulate growth, differentiation and (mature) cell function. Here, Yves Collette and Daniel Olive reviaw the recently identified interactions of virus proteins from Herpesviridae, Retroviridae and Papavaviridae with NRPTKs, mid propose that these
Yves Collette, Daniel Olive
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Regulation of antigen receptor signal transduction by protein tyrosine kinases
Current Opinion in Immunology, 1996The past two years have seen further clarification of the early events occurring in antigen receptor signal transduction that are mediated by the immunoreceptor tyrosine-based activation motif (ITAM). The ITAM was shown to be a specific binding site for the ZAP-70/Syk protein tyrosine kinases and the structure of this complex was solved.
Andrey S. Shaw, Andrew C. Chan
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Src-related protein tyrosine kinases and T-cell receptor signalling
Trends in Genetics, 1992Upon antigen stimulation, the T-cell receptor for antigen transduces an intracellular protein tyrosine phosphorylation signal that is critical for subsequent T-lymphocyte activation. As the antigen receptor does not possess an intrinsic protein tyrosine kinase activity, the mechanism by which it regulates protein tyrosine phosphorylation is ...
André Veillette, Dominique Davidson
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Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
Trends in Cell Biology, 2001Signaling through receptor tyrosine kinases (RTKs) is a major mechanism for intercellular communication during development and in the adult organism, as well as in disease-associated processes. The phosphorylation status and signaling activity of RTKs is determined not only by the kinase activity of the RTK but also by the activities of protein ...
Frank-D. Böhmer, Arne Östman
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Salicylanilides as Inhibitors of the Protein Tyrosine Kinase Epidermal Growth Factor Receptor.
ChemInform, 2004AbstractFor Abstract see ChemInform Abstract in Full Text.
Pascal Furet +5 more
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Current Opinion in Cell Biology, 1991
T-cell receptor stimulation leads to a rapid increase in tyrosine phosphorylation which is regulated by both the CD45 transmembrane protein tyrosine phosphatase and by intracellular protein tyrosine kinases. The Src-family members, Fyn and Lck, have been implicated in T-cell receptor signalling and may be regulated by CD45.
Andrey S. Shaw, Matthew L. Thomas
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T-cell receptor stimulation leads to a rapid increase in tyrosine phosphorylation which is regulated by both the CD45 transmembrane protein tyrosine phosphatase and by intracellular protein tyrosine kinases. The Src-family members, Fyn and Lck, have been implicated in T-cell receptor signalling and may be regulated by CD45.
Andrey S. Shaw, Matthew L. Thomas
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Journal of Medicinal Chemistry, 1995
[(Alkylamino)methyl]acrylophenones and (alkylamino)propiophenones, bearing a spacer moiety such as the benzyloxy or (benzoylsulfonyl)oxy group in the 4-position, represent a novel class of inhibitors of the epidermal growth factor (EGF) receptor protein ...
P. Traxler +8 more
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[(Alkylamino)methyl]acrylophenones and (alkylamino)propiophenones, bearing a spacer moiety such as the benzyloxy or (benzoylsulfonyl)oxy group in the 4-position, represent a novel class of inhibitors of the epidermal growth factor (EGF) receptor protein ...
P. Traxler +8 more
semanticscholar +1 more source
Signalling pathways initiated by receptor protein tyrosine kinases in Drosophila
Current Opinion in Cell Biology, 1994The isolation and characterization of Drosophila mutations in receptor protein tyrosine kinases (RPTKs) have allowed a detailed analysis of the cellular processes regulated by these proteins. Recent investigations have identified a number of putative ligands involved in the activation of the receptors, and have demonstrated that these RPTKs trigger an ...
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
On immunoprecipitation using a specific antiphosphotyrosine antibody, phosphatidylinositol kinase (EC 2.7.1.67) activity was separated from the protein-tyrosine kinase (EC 2.7.1.112) activity of the wheat germ agglutinin (WGA) -purified insulin receptor from human placenta.
José M. Carrascosa +4 more
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On immunoprecipitation using a specific antiphosphotyrosine antibody, phosphatidylinositol kinase (EC 2.7.1.67) activity was separated from the protein-tyrosine kinase (EC 2.7.1.112) activity of the wheat germ agglutinin (WGA) -purified insulin receptor from human placenta.
José M. Carrascosa +4 more
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Annexin I as a Potential Inhibitor of Insulin Receptor Protein Tyrosine Kinase
Biochemical and Biophysical Research Communications, 1994Insulin receptor (IR) purified from human placenta by wheat germ agglutinin affinity chromatography was incubated in the presence of insulin, [gamma-32P]ATP and annexin I. In parallel to its own tyrosine phosphorylation, annexin I promoted a dose-dependent inhibition of IR autophosphorylation (IC50 0.5 microM).
Hugues Chap +5 more
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