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  • Kinetics
  • American Association for the Advancement of Science (AAAS)  (5)
  • Cambridge University Press
  • Societe Geologique de France
  • 2000-2004  (5)
  • 1980-1984
  • 2002  (5)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (5)
  • Cambridge University Press
  • Societe Geologique de France
Years
  • 2000-2004  (5)
  • 1980-1984
Year
  • 1
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    Enzyme dynamics during catalysis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenmesser, Elan Zohar -- Bosco, Daryl A -- Akke, Mikael -- Kern, Dorothee -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1520-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859194" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Isomerism ; Kinetics ; Mathematics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation
    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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    Phototransduction by retinal ganglion cells that set the circadian clock (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: Light synchronizes mammalian circadian rhythms with environmental time by modulating retinal input to the circadian pacemaker-the suprachiasmatic nucleus (SCN) of the hypothalamus. Such photic entrainment requires neither rods nor cones, the only known retinal photoreceptors. Here, we show that retinal ganglion cells innervating the SCN are intrinsically photosensitive. Unlike other ganglion cells, they depolarized in response to light even when all synaptic input from rods and cones was blocked. The sensitivity, spectral tuning, and slow kinetics of this light response matched those of the photic entrainment mechanism, suggesting that these ganglion cells may be the primary photoreceptors for this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berson, David M -- Dunn, Felice A -- Takao, Motoharu -- EY12793/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1070-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI, 02912 USA. David_Berson@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834835" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/ultrastructure ; *Biological Clocks ; *Circadian Rhythm ; Dendrites/ultrastructure ; Isoquinolines ; Kinetics ; Light ; *Light Signal Transduction ; Patch-Clamp Techniques ; Rats ; Rats, Sprague-Dawley ; Retinal Ganglion Cells/chemistry/cytology/*physiology ; Rod Opsins/analysis/physiology ; Suprachiasmatic Nucleus/cytology/*physiology
    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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    Rapid total destruction of chlorophenols by activated hydrogen peroxide (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: A practical, inexpensive, green chemical process for degrading environmental pollutants is greatly needed, especially for persistent chlorinated pollutants. Here we describe the activation of hydrogen peroxide by tetraamidomacrocylic ligand (TAML) iron catalysts, to destroy the priority pollutants pentachlorophenol (PCP) and 2,4,6-trichlorophenol (TCP). In water, in minutes, under ambient conditions of temperature and pressure, PCP and TCP are completely destroyed at catalyst:substrate ratios of 1:715 and 1:2000, respectively. The fate of about 90% of the carbon and about 99% of the chlorine has been determined in each case. Neither dioxins nor any other toxic compounds are detectable products, and the catalysts themselves show low toxicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, Sayam Sen -- Stadler, Matthew -- Noser, Christopher A -- Ghosh, Anindya -- Steinhoff, Bradley -- Lenoir, Dieter -- Horwitz, Colin P -- Schramm, Karl-Werner -- Collins, Terrence J -- GM44867-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):326-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951040" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Chlorine Compounds/chemistry ; Chlorophenols/*chemistry ; Dioxins/chemistry ; Environmental Pollutants ; Ferric Compounds/*chemistry/toxicity ; Gas Chromatography-Mass Spectrometry ; Heterocyclic Compounds with 4 or More Rings/*chemistry/toxicity ; Hydrogen Peroxide/*chemistry ; Hydrogen-Ion Concentration ; Kinetics ; Magnetic Resonance Spectroscopy ; Oxidation-Reduction ; Pentachlorophenol/*chemistry ; Pressure ; Spectrometry, Mass, Electrospray Ionization ; Temperature
    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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  • 4
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    A kinetic framework for a mammalian RNA polymerase in vivo (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: We have analyzed the kinetics of assembly and elongation of the mammalian RNA polymerase I complex on endogenous ribosomal genes in the nuclei of living cells with the use of in vivo microscopy. We show that components of the RNA polymerase I machinery are brought to ribosomal genes as distinct subunits and that assembly occurs via metastable intermediates. With the use of computational modeling of imaging data, we have determined the in vivo elongation time of the polymerase, and measurements of recruitment and incorporation frequencies show that incorporation of components into the assembling polymerase is inefficient. Our data provide a kinetic and mechanistic framework for the function of a mammalian RNA polymerase in living cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dundr, Miroslav -- Hoffmann-Rohrer, Urs -- Hu, Qiyue -- Grummt, Ingrid -- Rothblum, Lawrence I -- Phair, Robert D -- Misteli, Tom -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1623-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute (NCI), 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/12446911" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalytic Domain ; Cell Line ; Cell Nucleolus/metabolism ; Cell Nucleus/*metabolism ; Computer Simulation ; DNA, Ribosomal/genetics ; Fluorescence ; Fluorescence Recovery After Photobleaching ; Fluorescent Dyes ; Green Fluorescent Proteins ; Haplorhini ; Humans ; In Situ Hybridization, Fluorescence ; Kinetics ; Least-Squares Analysis ; Luminescent Proteins ; Microscopy ; Pol1 Transcription Initiation Complex Proteins/metabolism ; Probability ; Promoter Regions, Genetic ; Protein Subunits ; RNA Polymerase I/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Transcription, Genetic ; Transfection
    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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  • 5
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    Special essay. The seven pillars of life (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshland, Daniel E Jr -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2215-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910092" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Biological Evolution ; DNA/physiology ; Energy Metabolism ; Feedback, Physiological ; Humans ; Kinetics ; *Life ; Origin of Life ; Reproduction ; Substrate Specificity ; *Terminology as Topic ; Thermodynamics
    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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