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  • Animals  (3)
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Institute of Physics (AIP)
  • Cell Press
  • Elsevier
  • Macmillian Magazines Ltd.
  • 2000-2004  (3)
  • 1960-1964
  • 1
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    The role of GTP-binding protein activity in fast central synaptic transmission (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-21
    Description: Guanosine 5'-triphosphate (GTP)-binding proteins (G proteins) are involved in exocytosis, endocytosis, and recycling of vesicles in yeast and mammalian secretory cells. However, little is known about their contribution to fast synaptic transmission. We loaded guanine nucleotide analogs directly into a giant nerve terminal in rat brainstem slices. Inhibition of G-protein activity had no effect on basal synaptic transmission, but augmented synaptic depression and significantly slowed recovery from depression. A nonhydrolyzable GTP analog blocked recovery of transmission from activity-dependent depression. Neither effect was accompanied by a change in presynaptic calcium currents. Thus, G proteins contribute to fast synaptic transmission by refilling synaptic vesicles depleted after massive exocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, T -- Hori, T -- Kajikawa, Y -- Tsujimoto, T -- New York, N.Y. -- Science. 2000 Jul 21;289(5478):460-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, University of Tokyo Faculty of Medicine, Tokyo 113-0033, Japan. ttakahas-tky@umin.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10903208" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Stem/metabolism ; Calcium/metabolism ; Excitatory Postsynaptic Potentials ; Exocytosis ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/*analogs & derivatives/pharmacology ; Guanosine Triphosphate/metabolism ; In Vitro Techniques ; Patch-Clamp Techniques ; Presynaptic Terminals/metabolism ; Rats ; Rats, Wistar ; *Synaptic Transmission ; Synaptic Vesicles/*metabolism ; Thionucleotides/pharmacology
    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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    Crystal structure of rhodopsin: A G protein-coupled receptor (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural features, including a bundle of seven transmembrane alpha helices connected by six loops of varying lengths. We determined the structure of rhodopsin from diffraction data extending to 2.8 angstroms resolution. The highly organized structure in the extracellular region, including a conserved disulfide bridge, forms a basis for the arrangement of the seven-helix transmembrane motif. The ground-state chromophore, 11-cis-retinal, holds the transmembrane region of the protein in the inactive conformation. Interactions of the chromophore with a cluster of key residues determine the wavelength of the maximum absorption. Changes in these interactions among rhodopsins facilitate color discrimination. Identification of a set of residues that mediate interactions between the transmembrane helices and the cytoplasmic surface, where G-protein activation occurs, also suggests a possible structural change upon photoactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palczewski, K -- Kumasaka, T -- Hori, T -- Behnke, C A -- Motoshima, H -- Fox, B A -- Le Trong, I -- Teller, D C -- Okada, T -- Stenkamp, R E -- Yamamoto, M -- Miyano, M -- EY09339/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):739-45.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ophthalmology, University of Washington, Seattle, WA 98195, USA. palczews@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10926528" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cattle ; Cell Membrane/chemistry ; Crystallography, X-Ray ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Hydrogen Bonding ; Light ; Molecular Sequence Data ; Receptors, Cell Surface/*chemistry/metabolism ; Retinaldehyde/chemistry/metabolism ; Rhodopsin/*chemistry/metabolism ; Schiff Bases ; Stereoisomerism ; Vision, Ocular
    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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  • 3
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    Control of regulatory T cell development by the transcription factor Foxp3 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-11
    Description: Regulatory T cells engage in the maintenance of immunological self-tolerance by actively suppressing self-reactive lymphocytes. Little is known, however, about the molecular mechanism of their development. Here we show that Foxp3, which encodes a transcription factor that is genetically defective in an autoimmune and inflammatory syndrome in humans and mice, is specifically expressed in naturally arising CD4+ regulatory T cells. Furthermore, retroviral gene transfer of Foxp3 converts naive T cells toward a regulatory T cell phenotype similar to that of naturally occurring CD4+ regulatory T cells. Thus, Foxp3 is a key regulatory gene for the development of regulatory T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hori, Shohei -- Nomura, Takashi -- Sakaguchi, Shimon -- New York, N.Y. -- Science. 2003 Feb 14;299(5609):1057-61. Epub 2003 Jan 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunopathology, Research Center for Allergy and Immunology, Institute for Physical and Chemical Research, Yokohama 230-0045, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12522256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/analysis ; Autoimmune Diseases/immunology/prevention & control ; CD4-Positive T-Lymphocytes/immunology ; Cytokines/biosynthesis ; DNA-Binding Proteins/genetics/*metabolism ; Forkhead Transcription Factors ; Gastritis/immunology/prevention & control ; *Immune Tolerance ; Inflammatory Bowel Diseases/immunology/prevention & control ; Lymphocyte Activation ; Mice ; Mice, Inbred BALB C ; Mice, SCID ; Mice, Transgenic ; Mutation ; Receptors, Antigen, T-Cell/immunology ; Receptors, Interleukin-2/analysis ; Recombinant Fusion Proteins/metabolism ; Self Tolerance ; T-Lymphocyte Subsets/cytology/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Regulatory/*immunology/*metabolism ; Thymus Gland/cytology/metabolism ; Transduction, Genetic
    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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