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phosphotyrosine and benzyloxycarbonylleucyl-leucyl-leucine aldehyde

phosphotyrosine has been researched along with benzyloxycarbonylleucyl-leucyl-leucine aldehyde in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's6 (85.71)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Darnell, JE; Haspel, RL; Salditt-Georgieff, M1
Carpino, N; Feng, J; Ihle, JN; Marine, JC; Moriggl, R; Stravopodis, D; Teglund, S; Wang, D1
Ram, PA; Waxman, DJ1
Gao, B; Holtzman, MJ; Shen, X; Tian, Z1
Goh, EL; Leong, WY; Lobie, PE; Zhu, T1
Kramer, D; Rondinone, CM1
Brazil, DP; Byun, HS; Chun, T; Hemmings, BA; Hong, J; Hur, GM; Kweon, GR; Li, Y; Park, J; Park, KA; Piao, L; Seok, JH; Shin, E; Shin, S; Won, M; Yang, KJ1

Other Studies

7 other study(ies) available for phosphotyrosine and benzyloxycarbonylleucyl-leucyl-leucine aldehyde

ArticleYear
The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.
    The EMBO journal, 1996, Nov-15, Volume: 15, Issue:22

    Topics: Acetylcysteine; Blotting, Western; Cell Nucleus; Cysteine Endopeptidases; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Fibroblasts; Humans; Interferon-gamma; Leupeptins; Multienzyme Complexes; Nuclear Proteins; Phosphorylation; Phosphotyrosine; Proteasome Endopeptidase Complex; Protein Tyrosine Phosphatases; Receptors, Interferon; Signal Transduction; STAT1 Transcription Factor; Staurosporine; Trans-Activators; Vanadates

1996
A small amphipathic alpha-helical region is required for transcriptional activities and proteasome-dependent turnover of the tyrosine-phosphorylated Stat5.
    The EMBO journal, 2000, Feb-01, Volume: 19, Issue:3

    Topics: Acetylcysteine; Animals; Cell Line; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; DNA-Binding Proteins; Leupeptins; Milk Proteins; Multienzyme Complexes; Phosphorylation; Phosphotyrosine; Proteasome Endopeptidase Complex; Protein Structure, Secondary; STAT5 Transcription Factor; Trans-Activators; Transcriptional Activation; Tyrosine

2000
Role of the cytokine-inducible SH2 protein CIS in desensitization of STAT5b signaling by continuous growth hormone.
    The Journal of biological chemistry, 2000, Dec-15, Volume: 275, Issue:50

    Topics: Animals; Binding Sites; Binding, Competitive; Blotting, Western; Carrier Proteins; Cell Nucleus; COS Cells; Cysteine Endopeptidases; Cytokines; Cytoplasm; DNA-Binding Proteins; Dose-Response Relationship, Drug; Down-Regulation; Enzyme Activation; Female; Genes, Dominant; Glucose-1-Phosphate Adenylyltransferase; Growth Hormone; Immediate-Early Proteins; Janus Kinase 2; Leupeptins; Liver; Microscopy, Confocal; Microscopy, Fluorescence; Milk Proteins; Models, Biological; Multienzyme Complexes; Nucleotidyltransferases; Phosphotyrosine; Plant Proteins; Plasmids; Proteasome Endopeptidase Complex; Protein Structure, Tertiary; Protein Transport; Protein-Tyrosine Kinases; Proteins; Proto-Oncogene Proteins; Rats; Repressor Proteins; Signal Transduction; STAT5 Transcription Factor; Suppressor of Cytokine Signaling 1 Protein; Suppressor of Cytokine Signaling 3 Protein; Suppressor of Cytokine Signaling Proteins; Time Factors; Trans-Activators; Transcription Factors; Transfection

2000
Cross-talk between interleukin 1beta (IL-1beta) and IL-6 signalling pathways: IL-1beta selectively inhibits IL-6-activated signal transducer and activator of transcription factor 1 (STAT1) by a proteasome-dependent mechanism.
    The Biochemical journal, 2000, Dec-15, Volume: 352 Pt 3

    Topics: Acute-Phase Proteins; Cysteine Endopeptidases; DNA; DNA-Binding Proteins; Down-Regulation; Enzyme Activation; Hepatocytes; Humans; Interleukin-1; Interleukin-6; Janus Kinase 1; Janus Kinase 2; Leupeptins; Models, Biological; Multienzyme Complexes; Mutation; NF-kappa B; NF-kappaB-Inducing Kinase; Phosphorylation; Phosphotyrosine; Proteasome Endopeptidase Complex; Protein Serine-Threonine Kinases; Protein Tyrosine Phosphatases; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Receptor Cross-Talk; Signal Transduction; STAT1 Transcription Factor; STAT3 Transcription Factor; Trans-Activators; Tumor Cells, Cultured

2000
c-Cbl is a negative regulator of GH-stimulated STAT5-mediated transcription.
    Endocrinology, 2002, Volume: 143, Issue:9

    Topics: 3T3 Cells; Animals; Cell Nucleus; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; DNA; DNA-Binding Proteins; Enzyme Activation; Gene Expression Regulation; Human Growth Hormone; Janus Kinase 2; Leupeptins; Mice; Milk Proteins; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinase 3; Mitogen-Activated Protein Kinases; Multienzyme Complexes; Phosphorylation; Phosphotyrosine; Proteasome Endopeptidase Complex; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-cbl; Receptors, Somatotropin; Signal Transduction; STAT5 Transcription Factor; Trans-Activators; Transcription, Genetic; Transfection; Ubiquitin; Ubiquitin-Protein Ligases

2002
Proteasome inhibitors regulate tyrosine phosphorylation of IRS-1 and insulin signaling in adipocytes.
    Biochemical and biophysical research communications, 2002, Sep-06, Volume: 296, Issue:5

    Topics: 3T3 Cells; Acetylcysteine; Adipocytes; Animals; Biological Transport; Cell Line; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; Enzyme Inhibitors; Glucose; Insulin; Insulin Receptor Substrate Proteins; Kinetics; Leupeptins; Mice; Multienzyme Complexes; Phosphatidylinositol 3-Kinases; Phosphoproteins; Phosphorylation; Phosphotyrosine; Proteasome Endopeptidase Complex; Protein Serine-Threonine Kinases; Protein Tyrosine Phosphatases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-akt; Signal Transduction

2002
Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding.
    The Journal of biological chemistry, 2008, Jan-18, Volume: 283, Issue:3

    Topics: 3-Phosphoinositide-Dependent Protein Kinases; Cell Line; Disease; Enzyme Activation; Enzyme Stability; HSP90 Heat-Shock Proteins; Humans; Leupeptins; Models, Biological; Mutant Proteins; Phosphorylation; Phosphotyrosine; Proteasome Inhibitors; Protein Binding; Protein Serine-Threonine Kinases; Protein Transport; Proto-Oncogene Proteins c-crk; Proto-Oncogene Proteins pp60(c-src); Recombinant Fusion Proteins; src Homology Domains; Subcellular Fractions

2008