Compounds > phosphotyrosine
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phosphotyrosine and phosphorylcholine

phosphotyrosine has been researched along with phosphorylcholine in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's1 (33.33)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Rozengurt, E; Seufferlein, T1
Gu, H; Lowell, CA; Neel, BG; Yu, M1
Holyst, T; Lytle, BL; Newman, DK; Newman, PJ; Paddock, C; Peterson, FC; Volkman, BF1

Other Studies

3 other study(ies) available for phosphotyrosine and phosphorylcholine

ArticleYear
Sphingosylphosphorylcholine rapidly induces tyrosine phosphorylation of p125FAK and paxillin, rearrangement of the actin cytoskeleton and focal contact assembly. Requirement of p21rho in the signaling pathway.
    The Journal of biological chemistry, 1995, Oct-13, Volume: 270, Issue:41

    Topics: 3T3 Cells; Actins; ADP Ribose Transferases; Animals; Blotting, Western; Bombesin; Botulinum Toxins; Calcium; Calcium-Calmodulin-Dependent Protein Kinases; Cell Adhesion Molecules; Cytoskeletal Proteins; Cytoskeleton; Enzyme Activation; Enzyme Inhibitors; Focal Adhesion Kinase 1; Focal Adhesion Protein-Tyrosine Kinases; GTP-Binding Proteins; Indoles; Kinetics; Maleimides; Mice; Microinjections; Paxillin; Phorbol 12,13-Dibutyrate; Phosphoproteins; Phosphorylcholine; Phosphotyrosine; Protein-Tyrosine Kinases; rho GTP-Binding Proteins; Signal Transduction; Sphingosine

1995
Scaffolding adapter Grb2-associated binder 2 requires Syk to transmit signals from FcepsilonRI.
    Journal of immunology (Baltimore, Md. : 1950), 2006, Feb-15, Volume: 176, Issue:4

    Topics: Adaptor Proteins, Signal Transducing; Animals; Binding Sites; Cells, Cultured; Enzyme Activation; Intracellular Signaling Peptides and Proteins; Mice; Mice, Knockout; Phosphatidylinositol 3-Kinases; Phosphoproteins; Phosphorylcholine; Phosphotyrosine; Protein-Tyrosine Kinases; Receptors, IgE; Signal Transduction; src Homology Domains; src-Family Kinases; Syk Kinase

2006
Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation.
    Blood, 2011, Jun-02, Volume: 117, Issue:22

    Topics: Cell Membrane; Circular Dichroism; Cytoplasm; Humans; Micelles; Peptide Fragments; Phosphorylation; Phosphorylcholine; Phosphotyrosine; Platelet Activation; Platelet Aggregation; Platelet Endothelial Cell Adhesion Molecule-1; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2011