Page last updated: 2024-08-23

phosphotyrosine and Hypogammaglobulinemia

phosphotyrosine has been researched along with Hypogammaglobulinemia in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (50.00)18.2507
2000's2 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Aoki, Y; Isselbacher, KJ; Pillai, S1
Nilsson, L; Smith, CI; Vihinen, M1
Bäckesjö, CM; Brockmann, E; Lappalainen, I; Laurén, S; Mattsson, PT; Smith, CI; Vihinen, M1
Chen, SH; Cheng, JW; Lei, B; Lung, FD; Pai, MT; Roller, PP; Soong, WJ; Tu, SC; Tzeng, SR; Wei, CJ; Wu, CW1

Other Studies

4 other study(ies) available for phosphotyrosine and Hypogammaglobulinemia

ArticleYear
Bruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells.
    Proceedings of the National Academy of Sciences of the United States of America, 1994, Oct-25, Volume: 91, Issue:22

    Topics: Agammaglobulinaemia Tyrosine Kinase; Agammaglobulinemia; Animals; B-Lymphocytes; Cell Line; Enzyme Activation; Hematopoietic Stem Cells; Humans; Immunoglobulin M; Kinetics; Mice; Mice, Mutant Strains; Models, Biological; Mutation; Phosphorylation; Phosphotyrosine; Protein-Tyrosine Kinases; Receptors, Antigen, T-Cell; Signal Transduction; Tyrosine; X Chromosome

1994
Structural basis of SH2 domain mutations in X-linked agammaglobulinemia.
    Biochemical and biophysical research communications, 1994, Dec-15, Volume: 205, Issue:2

    Topics: Agammaglobulinaemia Tyrosine Kinase; Agammaglobulinemia; Amino Acid Sequence; Binding Sites; Conserved Sequence; Crystallography, X-Ray; DNA Transposable Elements; Humans; Models, Molecular; Molecular Sequence Data; Oncogene Protein pp60(v-src); Phosphotyrosine; Point Mutation; Protein Structure, Secondary; Protein-Tyrosine Kinases; Sequence Deletion; Tyrosine; X Chromosome

1994
Six X-linked agammaglobulinemia-causing missense mutations in the Src homology 2 domain of Bruton's tyrosine kinase: phosphotyrosine-binding and circular dichroism analysis.
    Journal of immunology (Baltimore, Md. : 1950), 2000, Apr-15, Volume: 164, Issue:8

    Topics: Agammaglobulinaemia Tyrosine Kinase; Agammaglobulinemia; Amino Acid Substitution; Arginine; Circular Dichroism; Genetic Linkage; Glycine; Histidine; Humans; Mutation, Missense; Peptide Fragments; Phosphotyrosine; Protein Binding; Protein Conformation; Protein-Tyrosine Kinases; Solubility; src Homology Domains; Structure-Activity Relationship; X Chromosome

2000
Stability and peptide binding specificity of Btk SH2 domain: molecular basis for X-linked agammaglobulinemia.
    Protein science : a publication of the Protein Society, 2000, Volume: 9, Issue:12

    Topics: Agammaglobulinaemia Tyrosine Kinase; Agammaglobulinemia; Amino Acid Sequence; Binding Sites; Drug Stability; Genetic Linkage; Humans; Kinetics; Molecular Sequence Data; Phosphopeptides; Phosphotyrosine; Point Mutation; Protein Binding; Protein-Tyrosine Kinases; Sequence Alignment; src Homology Domains; X Chromosome

2000