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  • *Fresh Water  (1)
  • Aldehyde Oxidoreductases/*chemistry/*metabolism  (1)
  • Amygdala/physiology  (1)
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Chemical Society
  • American Physical Society
  • American Physical Society (APS)
  • Institute of Physics
  • Wiley-Blackwell
  • 2005-2009
  • 2000-2004  (3)
  • 1990-1994
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  • 2001  (3)
  • 1930
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  • American Association for the Advancement of Science (AAAS)  (3)
  • American Chemical Society
  • American Physical Society
  • American Physical Society (APS)
  • Institute of Physics
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  • 2005-2009
  • 2000-2004  (3)
  • 1990-1994
  • 1980-1984
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  • 2001  (3)
  • 1930
  • 1
    Publication Date: 2001-04-09
    Description: A comparative (15)N-tracer study of nitrogen dynamics in headwater streams from biomes throughout North America demonstrates that streams exert control over nutrient exports to rivers, lakes, and estuaries. The most rapid uptake and transformation of inorganic nitrogen occurred in the smallest streams. Ammonium entering these streams was removed from the water within a few tens to hundreds of meters. Nitrate was also removed from stream water but traveled a distance 5 to 10 times as long, on average, as ammonium. Despite low ammonium concentration in stream water, nitrification rates were high, indicating that small streams are potentially important sources of atmospheric nitrous oxide. During seasons of high biological activity, the reaches of headwater streams typically export downstream less than half of the input of dissolved inorganic nitrogen from their watersheds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peterson, B J -- Wollheim, W M -- Mulholland, P J -- Webster, J R -- Meyer, J L -- Tank, J L -- Marti, E -- Bowden, W B -- Valett, H M -- Hershey, A E -- McDowell, W H -- Dodds, W K -- Hamilton, S K -- Gregory, S -- Morrall, D D -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):86-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecosystems Center, Marine Biological Laboratory, Woods Hole, MA 02543, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292868" target="_blank"〉PubMed〈/a〉
    Keywords: Absorption ; Animals ; Bacteria/metabolism ; Biofilms ; *Ecosystem ; Eukaryota/metabolism ; *Fresh Water ; Fungi/metabolism ; Geologic Sediments ; Nitrates/metabolism ; Nitrogen/*metabolism ; Oxidation-Reduction ; Photosynthesis ; Quaternary Ammonium Compounds/metabolism ; Seasons ; United States
    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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  • 2
    Publication Date: 2001-07-14
    Description: The endogenous opioid system is involved in stress responses, in the regulation of the experience of pain, and in the action of analgesic opiate drugs. We examined the function of the opioid system and mu-opioid receptors in the brains of healthy human subjects undergoing sustained pain. Sustained pain induced the regional release of endogenous opioids interacting with mu-opioid receptors in a number of cortical and subcortical brain regions. The activation of the mu-opioid receptor system was associated with reductions in the sensory and affective ratings of the pain experience, with distinct neuroanatomical involvements. These data demonstrate the central role of the mu-opioid receptors and their endogenous ligands in the regulation of sensory and affective components of the pain experience.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zubieta, J K -- Smith, Y R -- Bueller, J A -- Xu, Y -- Kilbourn, M R -- Jewett, D M -- Meyer, C R -- Koeppe, R A -- Stohler, C S -- R01 DE 12059/DE/NIDCR NIH HHS/ -- R01 DE 12743/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 13;293(5528):311-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Mental Health Research Institute, Medical School, The University of Michigan, Ann Arbor, MI 48104-1687, USA. zubieta@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11452128" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amygdala/physiology ; Analgesics, Opioid/administration & dosage ; Brain/*physiology ; Brain Mapping ; Female ; Fentanyl/administration & dosage/*analogs & derivatives ; Humans ; Magnetic Resonance Imaging ; Male ; Masseter Muscle ; Opioid Peptides/physiology ; *Pain ; Pain Measurement ; Receptors, Opioid, mu/*physiology ; Thalamus/physiology ; Tomography, Emission-Computed
    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
    Publication Date: 2001-08-18
    Description: The homodimeric nickel-containing CO dehydrogenase from the anaerobic bacterium Carboxydothermus hydrogenoformans catalyzes the oxidation of CO to CO2. A crystal structure of the reduced enzyme has been solved at 1.6 angstrom resolution. This structure represents the prototype for Ni-containing CO dehydrogenases from anaerobic bacteria and archaea. It contains five metal clusters of which clusters B, B', and a subunit-bridging, surface-exposed cluster D are cubane-type [4Fe-4S] clusters. The active-site clusters C and C' are novel, asymmetric [Ni-4Fe-5S] clusters. Their integral Ni ion, which is the likely site of CO oxidation, is coordinated by four sulfur ligands with square planar geometry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dobbek, H -- Svetlitchnyi, V -- Gremer, L -- Huber, R -- Meyer, O -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1281-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. dobbek@biochem.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509720" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/*metabolism ; Bacteria, Anaerobic/*enzymology ; Binding Sites ; Carbon Dioxide/metabolism ; Carbon Monoxide/*metabolism ; Catalysis ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Electron Transport ; Hydrogen Bonding ; Iron/*chemistry/metabolism ; Ligands ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry/metabolism ; Oxidation-Reduction ; Peptococcaceae/*enzymology ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Sulfur/*chemistry/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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