proline and phosphotyrosine

proline has been researched along with phosphotyrosine in 14 studies

Research

Studies (14)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's5 (35.71)18.2507
2000's6 (42.86)29.6817
2010's3 (21.43)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chardin, P; Cussac, D; Frech, M1
Anafi, M; Gish, GD; Kay, LE; Pawson, T; Rosen, MK1
Avraham, H; Avraham, S; Fu, Y; Hiregowdara, D; London, R1
Charest, A; Côté, JF; Tremblay, ML; Wagner, J1
Baumann, M; Gires, O; Hammerschmidt, W; Kaiser, C; Kieser, A; Kilger, E; Kohlhuber, F; Scheffer, B; Ueffing, M; Zeidler, R1
Aster, JC; Fletcher, JA; McCarthy, JG; Xiao, S1
Gutkind, JS; Sanchez-Arevalo, VJ; Sanchez-Prieto, R; Servitja, JM1
Alarcón, B; Gil, D; Montoya, M; Sánchez-Madrid, F; Schamel, WW1
Campellone, KG; Leong, JM; Robbins, D1
Lawrence, DS; Lee, SY; Liang, F; Liang, J; Zhang, ZY1
Abmayr, SM; Kocherlakota, KS; McDermott, J; Wu, JM1
Frilling, A; Habib, NA; Hajitou, A; Mintz, PJ; Nicholls, JP; Reebye, V1
Artemenko, KA; Bergquist, J; Bergström Lind, S; Elfineh, L; Pettersson, U; Zhao, Y1
Adler, J; Bryansker Kraitshtein, Z; Keshet, R; Reuven, N; Shanzer, M; Shaul, Y1

Reviews

1 review(s) available for proline and phosphotyrosine

ArticleYear
A perspective on non-catalytic Src homology (SH) adaptor signalling proteins.
    Cellular signalling, 2012, Volume: 24, Issue:2

    Topics: Adaptor Proteins, Signal Transducing; Animals; Cytokines; Humans; Intercellular Signaling Peptides and Proteins; Mice; Phosphotyrosine; Proline; Protein Binding; Signal Transduction; src Homology Domains

2012

Other Studies

13 other study(ies) available for proline and phosphotyrosine

ArticleYear
Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs.
    The EMBO journal, 1994, Sep-01, Volume: 13, Issue:17

    Topics: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Base Sequence; ErbB Receptors; GRB2 Adaptor Protein; Humans; Membrane Proteins; Molecular Sequence Data; Mutation; Peptides; Phosphotyrosine; Proline; Protein Binding; Proteins; Recombinant Proteins; Sequence Homology, Amino Acid; Son of Sevenless Proteins; Spectrometry, Fluorescence; Tyrosine

1994
A potential SH3 domain-binding site in the Crk SH2 domain.
    The Journal of biological chemistry, 1996, Aug-30, Volume: 271, Issue:35

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cell Line; Cloning, Molecular; Humans; Magnetic Resonance Spectroscopy; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphorylation; Phosphotyrosine; Proline; Protein Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-crk; Sequence Homology, Amino Acid; Signal Transduction; src Homology Domains

1996
Tyrosine phosphorylation of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation and its association with paxillin.
    The Journal of biological chemistry, 1997, Apr-18, Volume: 272, Issue:16

    Topics: Binding Sites; Calcimycin; Cell Adhesion Molecules; Cell Line; Cytochalasin D; Cytoskeletal Proteins; Egtazic Acid; Humans; Megakaryocytes; Naphthalenes; Paxillin; Phosphoproteins; Phosphorylation; Phosphotyrosine; Proline; Protein-Tyrosine Kinases; Proteins; Recombinant Fusion Proteins; Signal Transduction; Stem Cell Factor; Tetradecanoylphorbol Acetate; TYK2 Kinase

1997
Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model.
    Biochemistry, 1998, Sep-22, Volume: 37, Issue:38

    Topics: Adaptor Proteins, Signal Transducing; Animals; Binding Sites; Cell Line; Crk-Associated Substrate Protein; Embryo, Mammalian; Fibroblasts; Gene Targeting; Glutathione Transferase; Mice; Models, Biological; Peptide Fragments; Phosphoproteins; Phosphorylation; Phosphotyrosine; Proline; Protein Tyrosine Phosphatase, Non-Receptor Type 12; Protein Tyrosine Phosphatases; Proteins; Recombinant Fusion Proteins; Retinoblastoma-Like Protein p130; src Homology Domains; Substrate Specificity; Transfection

1998
Latent membrane protein 1 of Epstein-Barr virus interacts with JAK3 and activates STAT proteins.
    The EMBO journal, 1999, Jun-01, Volume: 18, Issue:11

    Topics: Amino Acid Sequence; Animals; B-Lymphocytes; Cell Line; Consensus Sequence; DNA; DNA-Binding Proteins; Enzyme Activation; Herpesvirus 4, Human; Humans; Janus Kinase 3; Mice; Molecular Sequence Data; Phosphorylation; Phosphotyrosine; Proline; Protein Binding; Protein-Tyrosine Kinases; Receptors, Nerve Growth Factor; Recombinant Fusion Proteins; Repetitive Sequences, Amino Acid; Sequence Deletion; Signal Transduction; STAT1 Transcription Factor; Trans-Activators; Viral Matrix Proteins

1999
ZNF198-FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain.
    Blood, 2000, Jul-15, Volume: 96, Issue:2

    Topics: Animals; Binding Sites; Carrier Proteins; Cell Transformation, Neoplastic; DNA-Binding Proteins; Enzyme Activation; Hematopoietic Stem Cells; Lymphoma, T-Cell; Macromolecular Substances; Mice; Phosphorylation; Phosphotyrosine; Proline; Receptor Protein-Tyrosine Kinases; Receptor, Fibroblast Growth Factor, Type 1; Receptors, Fibroblast Growth Factor; Recombinant Fusion Proteins; Structure-Activity Relationship; Transcription Factors; Tumor Cells, Cultured

2000
Regulation of p73 by c-Abl through the p38 MAP kinase pathway.
    Oncogene, 2002, Jan-31, Volume: 21, Issue:6

    Topics: Bone Neoplasms; Calcium-Calmodulin-Dependent Protein Kinases; Cell Line; DNA-Binding Proteins; Enzyme Activation; Enzyme Inhibitors; Epithelial Cells; Genes, abl; Genes, Tumor Suppressor; Humans; Imidazoles; JNK Mitogen-Activated Protein Kinases; Kidney; MAP Kinase Kinase 1; MAP Kinase Kinase 6; MAP Kinase Kinase 7; MAP Kinase Signaling System; Mitogen-Activated Protein Kinase Kinases; Mitogen-Activated Protein Kinases; Multigene Family; Nuclear Proteins; Osteosarcoma; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Phosphoserine; Phosphotyrosine; Proline; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Protein-Tyrosine Kinases; Proto-Oncogene Proteins c-abl; Pyridines; Recombinant Fusion Proteins; src Homology Domains; Transcription, Genetic; Transfection; Tumor Cells, Cultured; Tumor Protein p73; Tumor Suppressor Proteins

2002
Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation.
    Cell, 2002, Jun-28, Volume: 109, Issue:7

    Topics: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; Antigen-Presenting Cells; Binding Sites; CD3 Complex; Humans; Jurkat Cells; Ligands; Lymphocyte Activation; Mice; Molecular Sequence Data; Oncogene Proteins; Phosphorylation; Phosphotyrosine; Proline; Protein Binding; Receptors, Antigen, T-Cell; Signal Transduction; src Homology Domains; T-Lymphocytes

2002
EspFU is a translocated EHEC effector that interacts with Tir and N-WASP and promotes Nck-independent actin assembly.
    Developmental cell, 2004, Volume: 7, Issue:2

    Topics: Actins; Adaptor Proteins, Signal Transducing; Blotting, Western; Carrier Proteins; Cell Nucleus; Escherichia coli; Escherichia coli O157; Escherichia coli Proteins; Gene Deletion; Genetic Complementation Test; Genomic Islands; HeLa Cells; Humans; Immunoblotting; Intracellular Signaling Peptides and Proteins; Microscopy, Fluorescence; Mutation; Nerve Tissue Proteins; Oncogene Proteins; Phosphotyrosine; Plasmids; Precipitin Tests; Proline; Protein Binding; Protein Structure, Tertiary; Protein Transport; Receptors, Cell Surface; Subcellular Fractions; Two-Hybrid System Techniques; Wiskott-Aldrich Syndrome Protein, Neuronal

2004
The role of protein-tyrosine phosphatase 1B in integrin signaling.
    The Journal of biological chemistry, 2005, Jul-01, Volume: 280, Issue:26

    Topics: Amino Acid Motifs; Binding Sites; Cell Line; Cell Movement; Crk-Associated Substrate Protein; Dose-Response Relationship, Drug; Down-Regulation; Enzyme Inhibitors; Fibronectins; Focal Adhesion Kinase 1; Focal Adhesion Protein-Tyrosine Kinases; Humans; Immunoblotting; Immunoprecipitation; Integrins; Kinetics; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinase 3; Models, Biological; Models, Chemical; Mutation; Phosphorylation; Phosphotyrosine; Proline; Protein Binding; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Protein Tyrosine Phosphatases; Protein-Tyrosine Kinases; Proteins; Retinoblastoma-Like Protein p130; Signal Transduction; src-Family Kinases; Transfection; Tyrosine

2005
Analysis of the cell adhesion molecule sticks-and-stones reveals multiple redundant functional domains, protein-interaction motifs and phosphorylated tyrosines that direct myoblast fusion in Drosophila melanogaster.
    Genetics, 2008, Volume: 178, Issue:3

    Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Cell Adhesion Molecules; Cell Fusion; Conserved Sequence; Drosophila melanogaster; Drosophila Proteins; Embryo, Nonmammalian; Immunoglobulins; Molecular Sequence Data; Myoblasts; Phenotype; Phosphoserine; Phosphotyrosine; Proline; Protein Structure, Tertiary; Structure-Activity Relationship; Transgenes

2008
The phosphoproteome of the adenovirus type 2 virion.
    Virology, 2012, Nov-10, Volume: 433, Issue:1

    Topics: Adenoviridae; Amino Acid Sequence; Chromatography, Liquid; HeLa Cells; Humans; Leucine; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Peptides; Phosphoproteins; Phosphorylation; Phosphotyrosine; Proline; Proteome; Proteomics; Viral Proteins; Virion

2012
c-Abl tyrosine kinase promotes adipocyte differentiation by targeting PPAR-gamma 2.
    Proceedings of the National Academy of Sciences of the United States of America, 2014, Nov-18, Volume: 111, Issue:46

    Topics: 3T3-L1 Cells; Adipocytes; Adipogenesis; Animals; Benzamides; HEK293 Cells; Humans; Imatinib Mesylate; Mice; Mutation, Missense; NIH 3T3 Cells; Phosphorylation; Phosphotyrosine; Piperazines; Point Mutation; Polymorphism, Single Nucleotide; PPAR gamma; Proline; Protein Binding; Protein Interaction Mapping; Protein Isoforms; Protein Kinase Inhibitors; Protein Processing, Post-Translational; Protein Stability; Protein Structure, Tertiary; Proto-Oncogene Proteins c-abl; Pyrimidines; Sequence Homology, Amino Acid; Species Specificity; Transcription, Genetic

2014