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  • Articles  (161)
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  • 11
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    Salts on Europa's surface detected by Galileo's near infrared mapping spectrometer. The NIMS Team (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Reflectance spectra in the 1- to 2.5-micrometer wavelength region of the surface of Europa obtained by Galileo's Near Infrared Mapping Spectrometer exhibit distorted water absorption bands that indicate the presence of hydrated minerals. The laboratory spectra of hydrated salt minerals such as magnesium sulfates and sodium carbonates and mixtures of these minerals provide a close match to the Europa spectra. The distorted bands are only observed in the optically darker areas of Europa, including the lineaments, and may represent evaporite deposits formed by water, rich in dissolved salts, reaching the surface from a water-rich layer underlying an ice crust.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCord, T B -- Hansen, G B -- Fanale, F P -- Carlson, R W -- Matson, D L -- Johnson, T V -- Smythe, W D -- Crowley, J K -- Martin, P D -- Ocampo, A -- Hibbitts, C A -- Granahan, J C -- New York, N.Y. -- Science. 1998 May 22;280(5367):1242-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hawaii Institute of Geophysics and Planetology, University of Hawaii, Honolulu, HI 96822, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596573" target="_blank"〉PubMed〈/a〉
    Keywords: Carbonates ; Evolution, Planetary ; Ice ; *Jupiter ; Magnesium Sulfate ; Oceans and Seas ; *Salts ; Spectrophotometry, Infrared ; Temperature ; *Water
    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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  • 12
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    Temperatures, winds, and composition in the saturnian system (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-25
    Description: Stratospheric temperatures on Saturn imply a strong decay of the equatorial winds with altitude. If the decrease in winds reported from recent Hubble Space Telescope images is not a temporal change, then the features tracked must have been at least 130 kilometers higher than in earlier studies. Saturn's south polar stratosphere is warmer than predicted from simple radiative models. The C/H ratio on Saturn is seven times solar, twice Jupiter's. Saturn's ring temperatures have radial variations down to the smallest scale resolved (100 kilometers). Diurnal surface temperature variations on Phoebe suggest a more porous regolith than on the jovian satellites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flasar, F M -- Achterberg, R K -- Conrath, B J -- Pearl, J C -- Bjoraker, G L -- Jennings, D E -- Romani, P N -- Simon-Miller, A A -- Kunde, V G -- Nixon, C A -- Bezard, B -- Orton, G S -- Spilker, L J -- Spencer, J R -- Irwin, P G J -- Teanby, N A -- Owen, T C -- Brasunas, J -- Segura, M E -- Carlson, R C -- Mamoutkine, A -- Gierasch, P J -- Schinder, P J -- Showalter, M R -- Ferrari, C -- Barucci, A -- Courtin, R -- Coustenis, A -- Fouchet, T -- Gautier, D -- Lellouch, E -- Marten, A -- Prange, R -- Strobel, D F -- Calcutt, S B -- Read, P L -- Taylor, F W -- Bowles, N -- Samuelson, R E -- Abbas, M M -- Raulin, F -- Ade, P -- Edgington, S -- Pilorz, S -- Wallis, B -- Wishnow, E H -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1247-51. Epub 2004 Dec 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Aeronautics and Space Administration (NASA)/Goddard Space Flight Center, Code 693, Greenbelt, MD 20771, USA. f.m.flasar@nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618486" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon ; Extraterrestrial Environment ; Hydrogen ; Methane ; *Saturn ; Spacecraft ; Spectrum Analysis ; Temperature ; Wind
    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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  • 13
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    An integrated nanoliter DNA analysis device (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: A device was developed that uses microfabricated fluidic channels, heaters, temperature sensors, and fluorescence detectors to analyze nanoliter-size DNA samples. The device is capable of measuring aqueous reagent and DNA-containing solutions, mixing the solutions together, amplifying or digesting the DNA to form discrete products, and separating and detecting those products. No external lenses, heaters, or mechanical pumps are necessary for complete sample processing and analysis. Because all of the components are made using conventional photolithographic production techniques, they operate as a single closed system. The components have the potential for assembly into complex, low-power, integrated analysis systems at low unit cost. The availability of portable, reliable instruments may facilitate the use of DNA analysis in applications such as rapid medical diagnostics and point-of-use agricultural testing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burns, M A -- Johnson, B N -- Brahmasandra, S N -- Handique, K -- Webster, J R -- Krishnan, M -- Sammarco, T S -- Man, P M -- Jones, D -- Heldsinger, D -- Mastrangelo, C H -- Burke, D T -- R01-HG01044/HG/NHGRI NIH HHS/ -- R01-HG01406/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):484-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9774277" target="_blank"〉PubMed〈/a〉
    Keywords: Costs and Cost Analysis ; DNA/*analysis ; Electrophoresis, Polyacrylamide Gel ; Fluorescence ; Miniaturization ; Molecular Biology/economics/*instrumentation/methods ; Silicon ; Temperature
    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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  • 14
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    Response of a deciduous forest to the Mount Pinatubo eruption: enhanced photosynthesis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-29
    Description: Volcanic aerosols from the 1991 Mount Pinatubo eruption greatly increased diffuse radiation worldwide for the following 2 years. We estimated that this increase in diffuse radiation alone enhanced noontime photosynthesis of a deciduous forest by 23% in 1992 and 8% in 1993 under cloudless conditions. This finding indicates that the aerosol-induced increase in diffuse radiation by the volcano enhanced the terrestrial carbon sink and contributed to the temporary decline in the growth rate of atmospheric carbon dioxide after the eruption.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Lianhong -- Baldocchi, Dennis D -- Wofsy, Steve C -- Munger, J William -- Michalsky, Joseph J -- Urbanski, Shawn P -- Boden, Thomas A -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2035-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Sciences Division, Building 1509, Oak Ridge National Laboratory, Oak Ridge, TN 37831-6335, USA. lianhong-gu@ornl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12663919" target="_blank"〉PubMed〈/a〉
    Keywords: Aerosols ; *Atmosphere ; *Carbon Dioxide/metabolism ; Climate ; *Ecosystem ; Mathematics ; Models, Statistical ; Nonlinear Dynamics ; Philippines ; *Photosynthesis ; Regression Analysis ; Scattering, Radiation ; Seasons ; Sunlight ; Temperature ; Trees/*metabolism ; *Volcanic Eruptions
    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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  • 15
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    Results from the Mars Global Surveyor Thermal Emission Spectrometer (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-28
    Description: The Thermal Emission Spectrometer spectra of low albedo surface materials suggests that a four to one mixture of pyroxene to plagioclase, together with about a 35 percent dust component provides the best fit to the spectrum. Qualitative upper limits can be placed on the concentration of carbonates (〈10 percent), olivine (〈10 percent), clay minerals (〈20 percent), and quartz (〈5 percent) in the limited regions observed. Limb observations in the northern hemisphere reveal low-lying dust hazes and detached water-ice clouds at altitudes up to 55 kilometers. At an aerocentric longitude of 224 degrees a major dust storm developed in the Noachis Terra region. The south polar cap retreat was similar to that observed by Viking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christensen, P R -- Anderson, D L -- Chase, S C -- Clancy, R T -- Clark, R N -- Conrath, B J -- Kieffer, H H -- Kuzmin, R O -- Malin, M C -- Pearl, J C -- Roush, T L -- Smith, M D -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1692-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arizona State University, Tempe, AZ 85287, USA. phil.christensen@asu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9497282" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon Dioxide ; Carbonates ; *Extraterrestrial Environment ; Ice ; Iron Compounds ; Magnesium Compounds ; *Mars ; Minerals ; Silicates ; Spacecraft ; Spectrum Analysis ; Temperature ; Water
    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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  • 16
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    A H+-gated urea channel: the link between Helicobacter pylori urease and gastric colonization (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-22
    Description: Acidic media trigger cytoplasmic urease activity of the unique human gastric pathogen Helicobacter pylori. Deletion of ureI prevents this activation of cytoplasmic urease that is essential for bacterial acid resistance. UreI is an inner membrane protein with six transmembrane segments as shown by in vitro transcription/translation and membrane separation. Expression of UreI in Xenopus oocytes results in acid-stimulated urea uptake, with a pH profile similar to activation of cytoplasmic urease. Mutation of periplasmic histidine 123 abolishes stimulation. UreI-mediated transport is urea specific, passive, nonsaturable, nonelectrogenic, and temperature independent. UreI functions as a H+-gated urea channel regulating cytoplasmic urease that is essential for gastric survival and colonization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weeks, D L -- Eskandari, S -- Scott, D R -- Sachs, G -- DK41301/DK/NIDDK NIH HHS/ -- DK43462/DK/NIDDK NIH HHS/ -- DK46917/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):482-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉VA Greater Los Angeles Healthcare System and Department of Physiology, University of California, Los Angeles, CA 90073, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10642549" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/chemistry/genetics/*metabolism ; Biological Transport ; Cell Membrane/chemistry ; Cell Membrane Permeability ; Cytoplasm/enzymology/metabolism ; Enzyme Activation ; Gastric Acid ; Glycosylation ; Helicobacter pylori/enzymology/growth & development/*metabolism ; Histidine/metabolism ; Humans ; Hydrogen-Ion Concentration ; *Membrane Transport Proteins ; Molecular Sequence Data ; Oocytes/enzymology ; Recombinant Proteins/metabolism ; Stomach/*microbiology ; Temperature ; Urea/*metabolism ; Urease/*metabolism ; Xenopus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Blue-fluorescent antibodies (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-13
    Description: The forte of catalytic antibodies has resided in the control of the ground-state reaction coordinate. A principle and method are now described in which antibodies can direct the outcome of photophysical and photochemical events that take place on excited-state potential energy surfaces. The key component is a chemically reactive optical sensor that provides a direct report of the dynamic interplay between protein and ligand at the active site. To illustrate the concept, we used a trans-stilbene hapten to elicit a panel of monoclonal antibodies that displayed a range of fluorescent spectral behavior when bound to a trans-stilbene substrate. Several antibodies yielded a blue fluorescence indicative of an excited-state complex or "exciplex" between trans-stilbene and the antibody. The antibodies controlled the isomerization coordinate of trans-stilbene and dynamically coupled this manifold with an active-site residue. A step was taken toward the use of antibody-based photochemical sensors for diagnostic and clinical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simeonov, A -- Matsushita, M -- Juban, E A -- Thompson, E H -- Hoffman, T Z -- Beuscher, A E 4th -- Taylor, M J -- Wirsching, P -- Rettig, W -- McCusker, J K -- Stevens, R C -- Millar, D P -- Schultz, P G -- Lerner, R A -- Janda, K D -- AI39089/AI/NIAID NIH HHS/ -- GM43858/GM/NIGMS NIH HHS/ -- P01CA27489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 13;290(5490):307-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, The Scripps Research Institute and the Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11030644" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*chemistry ; Antibodies, Monoclonal/*chemistry ; Binding Sites ; Binding Sites, Antibody ; Chemistry, Physical ; Crystallography, X-Ray ; *Fluorescence ; Haptens ; Ligands ; Microscopy, Fluorescence ; Models, Chemical ; Models, Molecular ; Photochemistry ; Physicochemical Phenomena ; Spectrometry, Fluorescence ; Stereoisomerism ; Stilbenes/*chemistry/*immunology ; Temperature ; Ultraviolet Rays
    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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  • 18
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    Rapid electron tunneling through oligophenylenevinylene bridges (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-27
    Description: We measured rate constants of thermal, interfacial electron transfer through oligophenylenevinylene bridges between a gold electrode and a tethered redox species in contact with an aqueous electrolyte using the indirect laser-induced temperature jump technique. Analysis of the distance dependence indicates that, unlike other bridges studied to date, the rate constants are not limited by electronic coupling for bridges up to 28 angstroms long. The energy levels of the bridges relative to those of the redox species rule out hopping through the bridge. We conclude that, out to 28 angstroms, the transfer is limited by structural reorganization and that electron tunneling occurs in less than 20 picoseconds, suggesting that oligophenylenevinylene bridges could be useful for wiring molecular electronic elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikes, H D -- Smalley, J F -- Dudek, S P -- Cook, A R -- Newton, M D -- Chidsey, C E -- Feldberg, S W -- 5 T32 GM08412/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Feb 23;291(5508):1519-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA., Brookhaven National Laboratory, Upton, NY 11973, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11222852" target="_blank"〉PubMed〈/a〉
    Keywords: Electrochemistry ; Electrodes ; Electrolytes ; Electronics ; *Electrons ; Ferrous Compounds/*chemistry ; Gold ; Oxidation-Reduction ; Stilbenes/*chemistry ; Temperature
    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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  • 19
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    Climate warming and disease risks for terrestrial and marine biota (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Infectious diseases can cause rapid population declines or species extinctions. Many pathogens of terrestrial and marine taxa are sensitive to temperature, rainfall, and humidity, creating synergisms that could affect biodiversity. Climate warming can increase pathogen development and survival rates, disease transmission, and host susceptibility. Although most host-parasite systems are predicted to experience more frequent or severe disease impacts with warming, a subset of pathogens might decline with warming, releasing hosts from disease. Recently, changes in El Nino-Southern Oscillation events have had a detectable influence on marine and terrestrial pathogens, including coral diseases, oyster pathogens, crop pathogens, Rift Valley fever, and human cholera. To improve our ability to predict epidemics in wild populations, it will be necessary to separate the independent and interactive effects of multiple climate drivers on disease impact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harvell, C Drew -- Mitchell, Charles E -- Ward, Jessica R -- Altizer, Sonia -- Dobson, Andrew P -- Ostfeld, Richard S -- Samuel, Michael D -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2158-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Cornell University, Ithaca, NY 14853, USA. cdh5@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077394" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic ; *Animals, Wild ; Bacterial Physiological Phenomena ; *Climate ; Communicable Diseases, Emerging/epidemiology/etiology/transmission/veterinary ; Disease Outbreaks ; Disease Vectors ; *Ecosystem ; Fungi/physiology ; Humans ; *Infection/epidemiology/etiology/transmission/veterinary ; Parasites/physiology ; *Plant Diseases/etiology ; Risk Factors ; Seasons ; Seawater ; Temperature ; Virus Physiological Phenomena
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Reversible hydrogels from self-assembling artificial proteins (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-17
    Description: Recombinant DNA methods were used to create artificial proteins that undergo reversible gelation in response to changes in pH or temperature. The proteins consist of terminal leucine zipper domains flanking a central, flexible, water-soluble polyelectrolyte segment. Formation of coiled-coil aggregates of the terminal domains in near-neutral aqueous solutions triggers formation of a three-dimensional polymer network, with the polyelectrolyte segment retaining solvent and preventing precipitation of the chain. Dissociation of the coiled-coil aggregates through elevation of pH or temperature causes dissolution of the gel and a return to the viscous behavior that is characteristic of polymer solutions. The mild conditions under which gel formation can be controlled (near-neutral pH and near-ambient temperature) suggest that these materials have potential in bioengineering applications requiring encapsulation or controlled release of molecular and cellular species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petka, W A -- Harden, J L -- McGrath, K P -- Wirtz, D -- Tirrell, D A -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):389-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665877" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carrier Proteins/*chemistry/isolation & purification ; Chemistry, Physical ; Circular Dichroism ; Dimerization ; Electrolytes ; *Gels ; Genes, Synthetic ; Hydrogel ; Hydrogen-Ion Concentration ; Leucine Zippers ; Molecular Sequence Data ; Physicochemical Phenomena ; Polyethylene Glycols/*chemistry/isolation & purification ; Polymers ; *Protein Engineering ; Protein Folding ; *Protein Structure, Secondary ; Recombinant Proteins/*chemistry/isolation & purification ; Temperature ; Viscosity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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