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  • Animals  (75)
  • American Association for the Advancement of Science (AAAS)  (75)
  • 1
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    Solution to a conservation problem? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Hippel, F A -- von Hippel, W -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776681" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Asia ; *Conservation of Natural Resources ; Humans ; Male ; *Materia Medica ; Piperazines/*supply & distribution ; Purines ; Sildenafil Citrate ; Sulfones
    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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    Control of synaptic strength by glial TNFalpha (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: Activity-dependent modulation of synaptic efficacy in the brain contributes to neural circuit development and experience-dependent plasticity. Although glia are affected by activity and ensheathe synapses, their influence on synaptic strength has largely been ignored. Here, we show that a protein produced by glia, tumor necrosis factor alpha (TNFalpha), enhances synaptic efficacy by increasing surface expression of AMPA receptors. Preventing the actions of endogenous TNFalpha has the opposite effects. Thus, the continual presence of TNFalpha is required for preservation of synaptic strength at excitatory synapses. Through its effects on AMPA receptor trafficking, TNFalpha may play roles in synaptic plasticity and modulating responses to neural injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beattie, Eric C -- Stellwagen, David -- Morishita, Wade -- Bresnahan, Jacqueline C -- Ha, Byeong Keun -- Von Zastrow, Mark -- Beattie, Michael S -- Malenka, Robert C -- DA00439/DA/NIDA NIH HHS/ -- MH063394/MH/NIMH NIH HHS/ -- NS 31193/NS/NINDS NIH HHS/ -- NS38079/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, Palo Alto, CA 94304, USA. beattie.2@osu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/pharmacology ; Astrocytes/*metabolism ; Cells, Cultured ; Culture Media, Conditioned/pharmacology ; Gene Expression Regulation/drug effects ; Hippocampus/cytology/metabolism ; Neuronal Plasticity/drug effects ; Neurons/drug effects/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/metabolism ; Receptors, Tumor Necrosis Factor ; Receptors, Tumor Necrosis Factor, Type I ; Synapses/drug effects/*metabolism ; Synaptic Transmission/drug effects ; Tumor Necrosis Factor-alpha/antagonists & inhibitors/*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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  • 3
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    CD95/CD95 ligand interactions on epithelial cells in host defense to Pseudomonas aeruginosa (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-20
    Description: Pseudomonas aeruginosa causes severe infections, particularly of the lung, that are life threatening. Here, we show that P. aeruginosa infection induces apoptosis of lung epithelial cells by activation of the endogenous CD95/CD95 ligand system. Deficiency of CD95 or CD95 ligand on epithelial cells prevented apoptosis of lung epithelial cells in vivo as well as in vitro. The importance of CD95/CD95 ligand-mediated lung epithelial cell apoptosis was demonstrated by the rapid development of sepsis in CD95- or CD95 ligand-deficient mice, but not in normal mice, after P. aeruginosa infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grassme, H -- Kirschnek, S -- Riethmueller, J -- Riehle, A -- von Kurthy, G -- Lang, F -- Weller, M -- Gulbins, E -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):527-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Tuebingen, Gmelinstrasse 5, 72076 Tuebingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11039936" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/genetics/*metabolism ; *Apoptosis ; Bone Marrow Transplantation ; Cell Line ; Epithelial Cells/*immunology/microbiology/pathology ; Fas Ligand Protein ; Humans ; In Situ Nick-End Labeling ; Lung/*immunology/microbiology/pathology ; Lung Diseases/*immunology/microbiology/pathology ; Membrane Glycoproteins/genetics/*metabolism ; Mice ; Mice, Inbred C3H ; Pseudomonas Infections/*immunology/microbiology/pathology ; Pseudomonas aeruginosa/immunology/*pathogenicity ; Sepsis/microbiology ; Spleen/microbiology
    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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    Signal transduction. A new thread in an intricate web (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: Understanding how biochemical pathways are connected in the cell is one of the big challenges facing cell biologists. In a Perspective, von Zastrow and Mostov describe new work that identifies a protein called RGS-PX1 as the linchpin that connects signal transduction activated by G protein-coupled receptors with membrane trafficking events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Zastrow, M -- Mostov, K -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1845-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Psychiatry, University of California, San Francisco, CA 94143, USA. zastrow@itsa.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729293" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/metabolism ; Carrier Proteins/chemistry/*metabolism ; Databases, Genetic ; GTPase-Activating Proteins/chemistry/*metabolism ; Heterotrimeric GTP-Binding Proteins/chemistry/*metabolism ; Humans ; Protein Binding ; Protein Structure, Tertiary ; Protein Transport ; RGS Proteins/chemistry/*metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Signal Transduction ; Sorting Nexins
    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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    Skinny hedgehog, an acyltransferase required for palmitoylation and activity of the hedgehog signal (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-04
    Description: One of the most dominant influences in the patterning of multicellular embryos is exerted by the Hedgehog (Hh) family of secreted signaling proteins. Here, we identify a segment polarity gene in Drosophila melanogaster, skinny hedgehog (ski), and show that its product is required in Hh-expressing cells for production of appropriate signaling activity in embryos and in the imaginal precursors of adult tissues. The ski gene encodes an apparent acyltransferase, and we provide genetic and biochemical evidence that Hh proteins from ski mutant cells retain carboxyl-terminal cholesterol modification but lack amino-terminal palmitate modification. Our results suggest that ski encodes an enzyme that acts within the secretory pathway to catalyze amino-terminal palmitoylation of Hh, and further demonstrate that this lipid modification is required for the embryonic and larval patterning activities of the Hh signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chamoun, Z -- Mann, R K -- Nellen, D -- von Kessler, D P -- Bellotto, M -- Beachy, P A -- Basler, K -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2080-4. Epub 2001 Aug 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie and Zoologisches Institut, Universitat Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11486055" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Acyltransferases/chemistry/*genetics/*metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Body Patterning ; Cholesterol/metabolism ; *Drosophila Proteins ; Drosophila melanogaster/embryology/*genetics/growth & development/metabolism ; Gene Expression ; Genes, Insect ; Hedgehog Proteins ; Insect Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Palmitic Acid/*metabolism ; Protein Structure, Tertiary ; *Signal Transduction ; Transgenes
    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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    Natural iron isotope variations in human blood (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-16
    Description: Isotopic analysis of human blood and liver and muscle tissue indicates that each individual bears a long-term iron (Fe) isotope signature in the blood. Blood and tissue differ slightly in isotopic composition and are depleted by up to 2.6 per mil in 56Fe relative to 54Fe when compared to dietary Fe. The 56Fe/54Fe isotope ratio in the blood of males is, on average, lower by 0.3 per mil than that of females. These results suggest that Fe isotope effects in the blood reflect differences in intestinal Fe absorption between individuals and genotypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walczyk, Thomas -- von Blanckenburg, Friedhelm -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2065-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Nutrition, Institute of Food Sciences, Swiss Federal Institute of Technology (ETH) Zurich, Seestrasse 72, CH-8803 Ruschlikon, Switzerland. thomas.walczyk@ilw.agrl.ethz.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896276" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Child ; Female ; Food Analysis ; Humans ; Infant ; Intestinal Absorption ; Iron/*blood/metabolism ; Iron Isotopes/*blood/metabolism ; Iron, Dietary/administration & dosage/*metabolism ; Liver/metabolism ; Male ; Meat ; Muscles/metabolism ; Reference Values ; Sex Characteristics
    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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  • 7
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    Impaired immunoproteasome assembly and immune responses in PA28-/- mice (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-11
    Description: In vitro PA28 binds and activates proteasomes. It is shown here that mice with a disrupted PA28b gene lack PA28a and PA28b polypeptides, demonstrating that PA28 functions as a hetero-oligomer in vivo. Processing of antigenic epitopes derived from exogenous or endogenous antigens is altered in PA28-/- mice. Cytotoxic T lymphocyte responses are impaired, and assembly of immunoproteasomes is greatly inhibited in mice lacking PA28. These results show that PA28 is necessary for immunoproteasome assembly and is required for efficient antigen processing, thus demonstrating the importance of PA28-mediated proteasome function in immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preckel, T -- Fung-Leung, W P -- Cai, Z -- Vitiello, A -- Salter-Cid, L -- Winqvist, O -- Wolfe, T G -- Von Herrath, M -- Angulo, A -- Ghazal, P -- Lee, J D -- Fourie, A M -- Wu, Y -- Pang, J -- Ngo, K -- Peterson, P A -- Fruh, K -- Yang, Y -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2162-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The R. W. Johnson Pharmaceutical Research Institute, 3210 Merryfield Row, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10591649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Autoantigens ; Cysteine Endopeptidases/chemistry/*metabolism ; Enzyme Activators/*metabolism ; Epitopes, T-Lymphocyte/immunology ; Female ; H-Y Antigen/immunology ; Herpesviridae Infections/immunology ; Histocompatibility Antigens Class I/immunology/metabolism ; Interferons/pharmacology ; Lymphocytic Choriomeningitis/immunology ; Lymphocytic choriomeningitis virus/immunology ; Male ; Mice ; Multienzyme Complexes/chemistry/*metabolism ; Muromegalovirus/immunology ; Ovalbumin/immunology ; Peptide Fragments/immunology ; Proteasome Endopeptidase Complex ; Proteins/genetics/*metabolism ; T-Lymphocytes, Cytotoxic/*immunology
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  • 8
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    Regulation of mammalian circadian behavior by non-rod, non-cone, ocular photoreceptors (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-16
    Description: Circadian rhythms of mammals are entrained by light to follow the daily solar cycle (photoentrainment). To determine whether retinal rods and cones are required for this response, the effects of light on the regulation of circadian wheel-running behavior were examined in mice lacking these photoreceptors. Mice without cones (cl) or without both rods and cones (rdta/cl) showed unattenuated phase-shifting responses to light. Removal of the eyes abolishes this behavior. Thus, neither rods nor cones are required for photoentrainment, and the murine eye contains additional photoreceptors that regulate the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freedman, M S -- Lucas, R J -- Soni, B -- von Schantz, M -- Munoz, M -- David-Gray, Z -- Foster, R -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):502-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Alexander Fleming Building, Imperial College of Science, Technology and Medicine, London, SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205061" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/*physiology ; Circadian Rhythm/*physiology ; *Light ; Mice ; Mice, Transgenic ; Motor Activity ; *Ocular Physiological Phenomena ; Photoreceptor Cells, Vertebrate/*physiology ; Pigments, Biological/physiology ; Retinal Cone Photoreceptor Cells/physiology ; Retinal Pigments/physiology ; Retinal Rod Photoreceptor Cells/physiology
    Print ISSN: 0036-8075
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  • 9
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    GAD, a single autoantigen for diabetes (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Boehmer, H -- Sarukhan, A -- New York, N.Y. -- Science. 1999 May 14;284(5417):1135, 1137.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U373, Faculte Necker, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10366347" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantigens/genetics/*immunology/physiology ; DNA, Antisense ; Diabetes Mellitus, Type 1/enzymology/*immunology/therapy ; Glutamate Decarboxylase/genetics/*immunology/physiology ; Humans ; Islets of Langerhans/*enzymology/immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred NOD ; Mice, Transgenic ; Self Tolerance ; T-Lymphocytes/immunology ; Transgenes
    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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  • 10
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    How snapping shrimp snap: through cavitating bubbles (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-23
    Description: The snapping shrimp (Alpheus heterochaelis) produces a loud snapping sound by an extremely rapid closure of its snapper claw. One of the effects of the snapping is to stun or kill prey animals. During the rapid snapper claw closure, a high-velocity water jet is emitted from the claw with a speed exceeding cavitation conditions. Hydrophone measurements in conjunction with time-controlled high-speed imaging of the claw closure demonstrate that the sound is emitted at the cavitation bubble collapse and not on claw closure. A model for the bubble dynamics based on a Rayleigh-Plesset-type equation quantitatively accounts for the time dependence of the bubble radius and for the emitted sound.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Versluis, M -- Schmitz, B -- von der Heydt, A -- Lohse, D -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Physics and J. M. Burgers Research Center for Fluid Dynamics, University of Twente, Post Office Box 217, 7500 AE Enschede, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11000111" target="_blank"〉PubMed〈/a〉
    Keywords: Air ; Animals ; Biophysical Phenomena ; Biophysics ; Decapoda (Crustacea)/*anatomy & histology/*physiology ; Mathematics ; Models, Biological ; Pressure ; Seawater ; *Sound
    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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