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  • *Penicillin-Binding Proteins  (1)
  • Crystallography, X-Ray
  • Mice
  • Superfluidity and superconductivity
  • 2000-2004  (2)
  • 1
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    Roles of PLC-beta2 and -beta3 and PI3Kgamma in chemoattractant-mediated signal transduction (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-11
    Description: The roles of phosphoinositide 3-kinase (PI3K) and phospholipase C (PLC) in chemoattractant-elicited responses were studied in mice lacking these key enzymes. PI3Kgamma was required for chemoattractant-induced production of phosphatidylinositol 3,4,5-trisphosphate [PtdIns (3,4,5)P3] and has an important role in chemoattractant-induced superoxide production and chemotaxis in mouse neutrophils and in production of T cell-independent antigen-specific antibodies composed of the immunoglobulin lambda light chain (TI-IglambdaL). The study of the mice lacking PLC-beta2 and -beta3 revealed that the PLC pathways have an important role in chemoattractant-mediated production of superoxide and regulation of protein kinases, but not chemotaxis. The PLC pathways also appear to inhibit the chemotactic activity induced by certain chemoattractants and to suppress TI-IglambdaL production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Z -- Jiang, H -- Xie, W -- Zhang, Z -- Smrcka, A V -- Wu, D -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1046-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Rochester, Rochester, NY 14642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Chemokine CCL4 ; Chemotactic Factors/*pharmacology ; Chemotaxis, Leukocyte/*physiology ; Immunoglobulin lambda-Chains/biosynthesis ; Isoenzymes/*metabolism ; Macrophage Inflammatory Proteins/pharmacology ; Mice ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophil Infiltration ; Neutrophils/metabolism/*physiology ; Peritonitis/immunology ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C beta ; Phosphorylation ; *Signal Transduction ; Skin Ulcer/pathology ; Superoxides/metabolism ; Type C Phospholipases/*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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  • 2
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    A proteolytic transmembrane signaling pathway and resistance to beta-lactams in staphylococci (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-10
    Description: beta-Lactamase and penicillin-binding protein 2a mediate staphylococcal resistance to beta-lactam antibiotics, which are otherwise highly clinically effective. Production of these inducible proteins is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which autoactivates, and the repressor, which is inactivated, unblocking gene transcription. Compounds that disrupt this regulatory pathway could restore the activity of beta-lactam antibiotics against drug-resistant strains of staphylococci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, H Z -- Hackbarth, C J -- Chansky, K M -- Chambers, H F -- AI4005804/AI/NIAID NIH HHS/ -- AI46610/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1962-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, San Francisco General Hospital, Department of Medicine, University of California at San Francisco, 1001 Potrero Avenue, San Francisco, CA 94110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11239156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Anti-Bacterial Agents/metabolism/pharmacology ; Bacterial Proteins/chemistry/metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Catalysis ; Cell Membrane/metabolism ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/metabolism ; Genes, Regulator ; Metalloendopeptidases/chemistry/metabolism ; Mutagenesis, Site-Directed ; *Penicillin-Binding Proteins ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/chemistry/genetics/*metabolism ; *Signal Transduction ; Staphylococcus aureus/*drug effects/genetics/*metabolism ; Transformation, Bacterial ; *beta-Lactam Resistance ; beta-Lactamases/*biosynthesis ; beta-Lactams
    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)
    Location Call Number Expected Availability
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    PAPER CURRENT
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