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    Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: Protein tyrosine phosphatases (PTPs) represent a diverse family of enzymes that exist as integral membrane and nonreceptor forms. The PTPs, with specific activities in vitro 10 to 1000 times greater than those of the protein tyrosine kinases would be expected to effectively control the amount of phosphotyrosine in the cell. They dephosphorylate tyrosyl residues in vivo and take part in signal transduction and cell cycle regulation. Most of the transmembrane forms, such as the leukocyte common antigen (CD45), contain two conserved intracellular catalytic domains; but their external segments are highly variable. The structural features of the transmembrane forms suggest that these receptor-linked PTPs are capable of transducing external signals; however, the ligands remain unidentified. A hypothesis is proposed explaining how phosphatases might act synergistically with the kinases to elicit a full physiological response, without regard to the state of phosphorylation of the target proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischer, E H -- Charbonneau, H -- Tonks, N K -- DK07902/DK/NIDDK NIH HHS/ -- GM15731/GM/NIGMS NIH HHS/ -- GM42508/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):401-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1650499" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Cycle ; Genetic Variation ; Humans ; Isoenzymes/*genetics/metabolism ; Membrane Proteins/genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Phosphoprotein Phosphatases/*genetics/metabolism ; Protein Kinases/metabolism ; Protein Tyrosine Phosphatases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Tyrosine phosphorylation of CD22 during B cell activation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-06
    Description: Ligation of the antigen receptor on B cells induces the rapid phosphorylation of tyrosine on a number of cellular proteins. A monoclonal antibody that recognized a tyrosine-phosphorylated cell surface protein that was present in activated B cells was generated. Amino acid sequence analysis showed that this 140-kilodalton protein was CD22, a B cell-specific cell surface glycoprotein and putative extracellular ligand of the protein tyrosine phosphatase CD45. Tyrosine phosphorylation of CD22 may be important in B cell signal transduction, possibly through regulation of the adhesiveness of activated B cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulte, R J -- Campbell, M A -- Fischer, W H -- Sefton, B M -- CA 14195/CA/NCI NIH HHS/ -- CA17289/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):1001-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279802" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/*metabolism ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; B-Lymphocytes/*immunology ; Burkitt Lymphoma ; *Cell Adhesion Molecules ; Chymotrypsin/metabolism ; Humans ; Immunoblotting ; Immunosorbent Techniques ; *Lectins ; *Lymphocyte Activation ; Peptide Mapping ; Phosphorylation ; Phosphotyrosine ; Sialic Acid Binding Ig-like Lectin 2 ; Signal Transduction/physiology ; Tumor Cells, Cultured ; Tyrosine/*analogs & derivatives/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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