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  • Animals  (12)
  • ASTRONOMY
  • LUNAR AND PLANETARY EXPLORATION
  • Solar Physics
  • American Association for the Advancement of Science (AAAS)  (12)
  • 1995-1999  (12)
  • 1980-1984
  • 1996  (12)
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (12)
Years
  • 1995-1999  (12)
  • 1980-1984
Year
  • 1
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    Biosphere 2 and biodiversity: the lessons so far (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J E -- Tilman, D -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1150-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York 10021-6399, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arizona ; Atmosphere ; *Ecological Systems, Closed ; *Ecosystem ; Humans ; Plant Development
    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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    Role of GTP hydrolysis in fission of caveolae directly from plasma membranes (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: Caveolae are specialized invaginated cell surface microdomains of undefined function. A cell-free system that reconstituted fission of caveolae from lung endothelial plasma membranes was developed. Addition of cytosol and the hydrolysis of guanosine triphosphate (GTP) induced caveolar fission. The budded caveolae were isolated as vesicles rich in caveolin and the sialoglycolipid GM1 but not glycosyl-phosphatidylinositol (GPI)-anchored proteins. These vesicles contained the molecular machinery for endocytosis and transcytosis. In permeabilized endothelial cells, GTP stimulated, whereas GTPgammaS prevented, caveolar budding and endocytosis of the cholera toxin B chain to endosomes. Thus, caveolae may bud to form discrete carrier vesicles that participate in membrane trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schnitzer, J E -- Oh, P -- McIntosh, D P -- HL43278/HL/NHLBI NIH HHS/ -- HL52766/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215, USA. jschnitz@bih.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824187" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Cattle ; Caveolin 1 ; *Caveolins ; Cell Membrane/chemistry/*metabolism/ultrastructure ; Cell-Free System ; Centrifugation, Density Gradient ; Cholera Toxin/metabolism ; Endocytosis ; Endothelium, Vascular/cytology/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/*metabolism/pharmacology ; Hydrolysis ; Membrane Proteins/analysis/metabolism ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: The bacterial pathogen Salmonella typhimurium triggers host cell signaling pathways that lead to cytoskeletal and nuclear responses required for pathogenesis. Here, the role of the small guanosine triphosphate (GTP)-binding protein CDC42Hs in these responses was examined. Expression of a dominant interfering mutant of CDC42 (CDC42HsN17) prevented S. typhimurium-induced cytoskeletal reorganization and subsequent macropinocytosis and bacterial internalization into host cells. Cells expressing constitutively active CDC42 (CDC42HsV12) internalized an S. typhimurium mutant unable to trigger host cell responses. Furthermore, expression of CDC42HsN17 prevented S. typhimurium-induced JNK kinase activation. These results indicate that CDC42 is required for bacterial invasion and induction of nuclear responses in host cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, L M -- Hobbie, S -- Galan, J E -- GM52543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, NY, 11794-5222, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953049" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Cycle Proteins/genetics/*physiology ; Cell Nucleus/*metabolism ; Cytoskeleton/*ultrastructure ; Enzyme Activation ; GTP-Binding Proteins/genetics/*physiology ; JNK Mitogen-Activated Protein Kinases ; *Mitogen-Activated Protein Kinases ; Pinocytosis ; Salmonella typhimurium/*physiology ; Signal Transduction ; Transfection ; cdc42 GTP-Binding Protein ; rac GTP-Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Protein sorting by transport vesicles (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-12
    Description: Eukaryotic life depends on the spatial and temporal organization of cellular membrane systems. Recent advances in understanding the machinery of vesicle transport have established general principles that underlie a broad variety of physiological processes, including cell surface growth, the biogenesis of distinct intracellular organelles, endocytosis, and the controlled release of hormones and neurotransmitters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothman, J E -- Wieland, F T -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):227-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602507" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; Cell Compartmentation ; Cell Membrane/*metabolism ; Coated Vesicles/metabolism ; Endocytosis ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Hormones/metabolism ; Intracellular Membranes/*metabolism ; Membrane Fusion ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Neurotransmitter Agents/metabolism ; Organelles/*metabolism ; Proteins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Bimodal interaction of coatomer with the p24 family of putative cargo receptors (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Cytoplasmic domains of members of the p24 family of putative cargo receptors were shown to bind to coatomer, the coat protein of COPI-coated transport vesicles. Domains that contained dilysine endoplasmic reticulum retrieval signals bound the alpha-, beta'-, and epsilon-COP subunits of coatomer, whereas other p24 domains bound the beta-, gamma-, and zeta-COP subunits and required a phenylalanine-containing motif. Transit of a CD8-p24 chimera from the endoplasmic reticulum through the Golgi complex was slowed when the phenylalanine motif was mutated, suggesting that this motif may function as an anterograde transport signal. The either-or bimodal binding of coatomer to p24 tails suggests models for how coatomer can potentially package retrograde-directed and anterograde-directed cargo into distinct COPI-coated vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fiedler, K -- Veit, M -- Stamnes, M A -- Rothman, J E -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1396-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; Carrier Proteins/chemistry/*metabolism ; Cell Membrane/metabolism ; Coated Vesicles/*metabolism ; Coatomer Protein ; Cricetinae ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Lysine/analysis ; Membrane Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Nuclear Envelope/metabolism ; Phenylalanine/analysis ; Recombinant Fusion Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Activation of ventrolateral preoptic neurons during sleep (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: The rostral hypothalamus and adjacent basal forebrain participate in the generation of sleep, but the neuronal circuitry involved in this process remains poorly characterized. Immunocytochemistry was used to identify the FOS protein, an immediate-early gene product, in a group of ventrolateral preoptic neurons that is specifically activated during sleep. The retrograde tracer cholera toxin B, in combination with FOS immunocytochemistry, was used to show that sleep-activated ventrolateral preoptic neurons innervate the tuberomammillary nucleus, a posterior hypothalamic cell group thought to participate in the modulation of arousal. This monosynaptic pathway in the hypothalamus may play a key role in determining sleep-wake states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherin, J E -- Shiromani, P J -- McCarley, R W -- Saper, C B -- MH10709/MH/NIMH NIH HHS/ -- NS22835/NS/NINDS NIH HHS/ -- NS30140/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):216-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539624" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Chemistry ; Cholera Toxin ; Circadian Rhythm ; Immunohistochemistry ; Mammillary Bodies/*physiology ; Neural Pathways ; Neurons/chemistry/*physiology ; Preoptic Area/cytology/*physiology ; Proto-Oncogene Proteins c-fos/analysis ; Rats ; Sleep/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
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    Evidence for physical and functional association between EMB-5 and LIN-12 in Caenorhabditis elegans (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-05
    Description: The Caenorhabditis elegans LIN-12 and GLP-1 proteins are members of the LIN-12/Notch family of receptors for intercellular signals that specify cell fate. Evidence presented here suggests that the intracellular domains of LIN-12 and GLP-1 interact with the C. elegans EMB-5 protein and that the emb-5 gene functions in the same pathway as the lin-12 and glp-1 genes. EMB-5 is similar in sequence to a yeast protein that controls chromatin structure. Hence, a direct consequence of LIN-12 or GLP-1 activation may be an alteration of chromatin structure that produces changes in transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hubbard, E J -- Dong, Q -- Greenwald, I -- GM37602/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*cytology/embryology/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cell Lineage ; Chromatin/metabolism ; Gene Expression Regulation, Developmental ; Genes, Helminth ; Helminth Proteins/genetics/*metabolism ; Meiosis ; Membrane Proteins/genetics/*metabolism ; Mitosis ; Mutation ; Receptors, Notch ; *Signal Transduction ; Temperature ; Transcription Factors/genetics/*metabolism
    Print ISSN: 0036-8075
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  • 8
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    Arrested DNA replication in Xenopus and release by Escherichia coli mutagenesis proteins (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Xenopus oocytes and oocyte nuclear extracts repair ultraviolet photoproducts on double-stranded (ds) DNA and replicate single-stranded (ss) to ds DNA. M13 ss DNA molecules containing cyclobutane pyrimidine dimers were maintained but not replicated in Xenopus oocytes yet were replicated in progesterone-matured oocytes. The replication arrest functioned only in cis. The replication arrest was alleviated by injection into oocytes of messenger RNAs encoding the prokaryotic mutagenesis proteins UmuD'C or MucA'B. These results may help explain how cells stabilize repair or replication events on DNA with unrepairable lesions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oda, N -- Levin, J D -- Spoonde, A Y -- Frank, E G -- Levine, A S -- Woodgate, R -- Ackerman, E J -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1644-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Office of Scientific Director, National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK), National Institutes of Health, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658137" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*physiology ; Bacteriophage M13/genetics ; Bacteriophage phi X 174/genetics ; DNA/biosynthesis ; DNA Damage ; DNA Repair ; *DNA Replication ; DNA, Single-Stranded/biosynthesis ; DNA-Directed DNA Polymerase ; Escherichia coli/*genetics ; *Escherichia coli Proteins ; Oocytes/*metabolism ; Ultraviolet Rays ; Xenopus
    Print ISSN: 0036-8075
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  • 9
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    Opposite modulation of cocaine-seeking behavior by D1- and D2-like dopamine receptor agonists (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Activation of the mesolimbic dopamine system is known to trigger relapse in animal models of cocaine-seeking behavior. We found that this "priming" effect was selectively induced by D2-like, and not by D1-like, dopamine receptor agonists in rats. Moreover, D1-like receptor agonists prevented cocaine-seeking behavior induced by cocaine itself, whereas D2-like receptor agonists enhanced this behavior. These results demonstrate an important dissociation between D1- and D2-like receptor processes in cocaine-seeking behavior and support further evaluation of D1-like receptor agonists as a possible pharmacotherapy for cocaine addiction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Self, D W -- Barnhart, W J -- Lehman, D A -- Nestler, E J -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1586-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Psychiatry, Department of Psychiatry, Yale University School of Medicine, Connecticut Mental Health Center, New Haven, 06508, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599115" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Addictive/*etiology ; Behavior, Animal/drug effects ; Benzazepines/pharmacology ; Caffeine/pharmacology ; *Cocaine/administration & dosage ; Dopamine Agonists/*pharmacology ; Ergolines/pharmacology ; Male ; Motor Activity/drug effects ; Quinpirole ; Rats ; Rats, Sprague-Dawley ; Receptors, Dopamine D1/agonists/*physiology ; Receptors, Dopamine D2/agonists/*physiology ; Recurrence ; Reinforcement (Psychology) ; Substance-Related Disorders/*etiology ; Tetrahydronaphthalenes/pharmacology
    Print ISSN: 0036-8075
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  • 10
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    Neonatal tolerance revisited: turning on newborn T cells with dendritic cells (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-22
    Description: For some time it has been thought that antigenic challenge in neonatal life is a tolerogenic rather than immunogenic event. Reexamination of the classic neonatal tolerance experiments of Billingham, Brent, and Medawar showed that tolerance is not an intrinsic property of the newborn immune system, but that the nature of the antigen-presenting cell determines whether the outcome is neonatal tolerance or immunization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ridge, J P -- Fuchs, E J -- Matzinger, P -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn/*immunology ; B-Lymphocytes/immunology ; Cytotoxicity Tests, Immunologic ; Cytotoxicity, Immunologic ; Dendritic Cells/*immunology ; Female ; H-Y Antigen/immunology ; *Immune Tolerance ; *Immunization ; Male ; Mice ; Mice, Inbred C57BL ; Self Tolerance ; T-Lymphocytes/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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