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  • Articles  (49)
  • Kinetics
  • American Association for the Advancement of Science (AAAS)  (48)
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  • Articles  (49)
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  • American Association for the Advancement of Science (AAAS)  (48)
  • Springer  (1)
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  • American Meteorological Society
  • American Physical Society (APS)
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  • 1
    Electronic Resource
    Electronic Resource
    Effect of fractionation on the enzymatic state and behaviour of enzyme activities in different structural soil units (1987)
    Springer
    Biology and fertility of soils 4 (1987), S. 151-154 
    Details
    ISSN: 1432-0789
    Keywords: Kinetics ; pH activity curves ; Soil enzymes ; Structural soil units ; Thermal stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary The behaviour and state of soil catalase, dehydrogenases, urease and proteases associated with different soil structural fractions were studied. Assays of the enzymatic sensitivity to pH variation, thermal stability and the calculation of kinetics constants of Michaelis were performed. The results indicated that catalase and urease activity in these soils seem to be of the same type, because the activities presented a similar behaviour in the soil fractions studied. However, their state appeared different in each group of soil units. Dehydrogenases showed a similar state and behaviour while proteases were in a different state and behaviour in each soil fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256989
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  • 2
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    Molecular hydrogen as an energy source for Helicobacter pylori (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: The gastric pathogen Helicobacter pylori is known to be able to use molecular hydrogen as a respiratory substrate when grown in the laboratory. We found that hydrogen is available in the gastric mucosa of mice and that its use greatly increased the stomach colonization by H. pylori. Hydrogenase activity in H. pylori is constitutive but increased fivefold upon incubation with hydrogen. Hydrogen concentrations measured in the stomachs of live mice were found to be 10 to 50 times as high as the H. pylori affinity for hydrogen. A hydrogenase mutant strain is much less efficient in its colonization of mice. Therefore, hydrogen present in animals as a consequence of normal colonic flora is an energy-yielding substrate that can facilitate the maintenance of a pathogenic bacterium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, Jonathan W -- Maier, Robert J -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1788-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Georgia, Athens, GA 30602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459589" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catechol 2,3-Dioxygenase ; Colon/metabolism/microbiology ; *Dioxygenases ; Energy Metabolism ; Fermentation ; Gastric Mucosa/*metabolism/*microbiology ; Gene Expression Regulation, Bacterial ; Genes, Reporter ; Helicobacter pylori/growth & development/*metabolism ; Hydrogen/*metabolism ; Hydrogenase/genetics/*metabolism ; Kinetics ; Mice ; Mutation ; Oxidation-Reduction ; Oxygenases/genetics/metabolism ; Transcription, Genetic
    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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    Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: The second messenger cyclic adenosine monophosphate (cAMP) is the most important modulator of sympathetic control over cardiac contractility. In cardiac myocytes and many other cell types, however, cAMP transduces the signal generated upon stimulation of various receptors and activates different cellular functions, raising the issue of how specificity can be achieved. In the general field of signal transduction, the view is emerging that specificity is guaranteed by tight localization of signaling events. Here, we show that in neonatal rat cardiac myocytes, beta-adrenergic stimulation generates multiple microdomains with increased concentration of cAMP in correspondence with the region of the transverse tubule/junctional sarcoplasmic reticulum membrane. The restricted pools of cAMP show a range of action as small as approximately 1 micrometer, and free diffusion of the second messenger is limited by the activity of phosphodiesterases. Furthermore, we demonstrate that such gradients of cAMP specifically activate a subset of protein kinase A molecules anchored in proximity to the T tubule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaccolo, Manuela -- Pozzan, Tullio -- TCP00089/Telethon/Italy -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1711-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Sciences and Venetian Institute for Molecular Medicine, University of Padua, Via Orus 2, 35129 Padua, Italy. manuela.zaccolo@unipd.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872839" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; A Kinase Anchor Proteins ; Adaptor Proteins, Signal Transducing ; Animals ; Animals, Newborn ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Fluorescence ; Green Fluorescent Proteins ; Intracellular Membranes/metabolism ; Kinetics ; Luminescent Proteins ; Myocardium/*cytology/*metabolism/ultrastructure ; Norepinephrine/pharmacology ; Phosphodiesterase Inhibitors/pharmacology ; Proto-Oncogene Proteins/pharmacology ; Rats ; Receptors, Adrenergic, beta/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sarcoplasmic Reticulum/*metabolism ; Second Messenger Systems ; Transfection
    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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    A photoactivatable GFP for selective photolabeling of proteins and cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: We report a photoactivatable variant of the Aequorea victoria green fluorescent protein (GFP) that, after intense irradiation with 413-nanometer light, increases fluorescence 100 times when excited by 488-nanometer light and remains stable for days under aerobic conditions. These characteristics offer a new tool for exploring intracellular protein dynamics by tracking photoactivated molecules that are the only visible GFPs in the cell. Here, we use the photoactivatable GFP both as a free protein to measure protein diffusion across the nuclear envelope and as a chimera with a lysosomal membrane protein to demonstrate rapid interlysosomal membrane exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patterson, George H -- Lippincott-Schwartz, Jennifer -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1873-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, 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/12228718" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Substitution ; Antigens, CD/metabolism ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; *Fluorescence ; Green Fluorescent Proteins ; Intracellular Membranes/metabolism ; Kinetics ; *Light ; Luminescent Proteins/*chemistry/genetics/isolation & purification/*metabolism ; Lysosome-Associated Membrane Glycoproteins ; Lysosomes/*metabolism ; Membrane Glycoproteins/metabolism ; Nuclear Envelope/metabolism ; Protein Engineering ; Protein Transport ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Spectrometry, Fluorescence
    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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    Parallel single-cell monitoring of receptor-triggered membrane translocation of a calcium-sensing protein module (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Time courses of translocation of fluorescently conjugated proteins to the plasma membrane were simultaneously measured in thousands of individual rat basophilic leukemia cells. We found that the C2 domain---a calcium-sensing, lipid-binding protein module that is an essential regulator of protein kinase C and numerous other proteins---targeted proteins to the plasma membrane transiently if calcium was released from internal stores, and persistently in response to entry of extracellular calcium across the plasma membrane. The C2 domain translocation time courses of stimulated cells clustered into only two primary modes. Hence, the reversible recruitment of families of signaling proteins from one cellular compartment to another is a rapid bifurcation mechanism for inducing discrete states of cellular signaling networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teruel, Mary N -- Meyer, Tobias -- CA83229/CA/NCI NIH HHS/ -- GM062144/GM/NIGMS NIH HHS/ -- HG00057/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1910-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Stanford University Medical School, 269 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Calcium/*metabolism ; *Calcium Signaling ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Fluorescence ; Fluorescent Dyes ; Isoenzymes/chemistry/*metabolism ; Kinetics ; Luminescent Proteins ; Platelet Activating Factor/pharmacology ; Protein Binding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; Rats ; Receptors, Cell Surface/*metabolism ; Recombinant Fusion Proteins/metabolism ; Software ; Thapsigargin/pharmacology ; Transfection ; Tumor Cells, Cultured
    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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    Essential role for the SMN complex in the specificity of snRNP assembly (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: The Survival of Motor Neurons (SMN) protein, the product of the spinal muscular atrophy-determining gene, is part of a large macromolecular complex (SMN complex) that functions in the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). Using cell extracts and purified components, we demonstrated that the SMN complex is necessary and sufficient to mediate the ATP-dependent assembly of the core of seven Sm proteins on uridine-rich, small nuclear ribonucleic acids (U snRNAs). In vitro experiments revealed strict requirements for ordered binding of the Sm proteins and the U snRNAs to the SMN complex. Importantly, the SMN complex is necessary to ensure that Sm cores assemble only on correct RNA targets and prevent their otherwise promiscuous association with other RNAs. Thus, the SMN complex functions as a specificity factor essential for the efficient assembly of Sm proteins on U snRNAs and likely protects cells from illicit, and potentially deleterious, nonspecific binding of Sm proteins to RNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellizzoni, Livio -- Yong, Jeongsik -- Dreyfuss, Gideon -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1775-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459587" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Carrier Proteins/metabolism ; Cell Extracts ; Cyclic AMP Response Element-Binding Protein ; DEAD Box Protein 20 ; DEAD-box RNA Helicases ; HeLa Cells ; Humans ; Kinetics ; Models, Biological ; Nerve Tissue Proteins/isolation & purification/*metabolism ; Nuclear Proteins/metabolism ; Oligoribonucleotides/metabolism ; Protein Binding ; RNA Helicases/metabolism ; RNA, Small Nuclear/*metabolism ; RNA-Binding Proteins ; Ribonucleoproteins, Small Nuclear/isolation & purification/*metabolism ; SMN Complex 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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  • 7
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    Correlating structural dynamics and function in single ribozyme molecules (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: We have studied the correlation between structural dynamics and function of the hairpin ribozyme. The enzyme-substrate complex exists in either docked (active) or undocked (inactive) conformations. Using single-molecule fluorescence methods, we found complex structural dynamics with four docked states of distinct stabilities and a strong memory effect where each molecule rarely switches between different docked states. We also found substrate cleavage to be rate-limited by a combination of conformational transitions and reversible chemistry equilibrium. The complex structural dynamics quantitatively explain the heterogeneous cleavage kinetics common to many catalytic RNAs. The intimate coupling of structural dynamics and function is likely a general phenomenon for RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhuang, Xiaowei -- Kim, Harold -- Pereira, Miguel J B -- Babcock, Hazen P -- Walter, Nils G -- Chu, Steven -- GM62357/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 24;296(5572):1473-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029135" target="_blank"〉PubMed〈/a〉
    Keywords: Carbocyanines/metabolism ; Catalysis ; Enzymes, Immobilized ; Fluorescence ; Hydrogen Bonding ; Kinetics ; Nepovirus/genetics ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/*metabolism ; RNA, Satellite ; RNA, Viral/*chemistry/*metabolism ; Spectrometry, Fluorescence ; Thermodynamics
    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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  • 8
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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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
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  • 10
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    Fusion pore dynamics and insulin granule exocytosis in the pancreatic islet (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-24
    Description: Insulin secretion from intact mouse pancreatic islets was investigated with two-photon excitation imaging. Insulin granule exocytosis occurred mainly toward the interstitial space, away from blood vessels. The fusion pore was unusually stable with a lifetime of 1.8 seconds. Opening of the 1.4-nanometer-diameter pore was preceded by unrestricted lateral diffusion of lipids along the inner wall of the pore, supporting the idea that this structure is composed of membrane lipids. When the pore dilated to 12 nanometers, the granules rapidly flattened and discharged their contents. Thus, our methodology reveals fusion pore dynamics in intact tissues at nanometer resolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, Noriko -- Kishimoto, Takuya -- Nemoto, Tomomi -- Kadowaki, Takashi -- Kasai, Haruo -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, National Institute for Physiological Sciences, and the Graduate University of Advanced Studies, Myodaiji, Okazaki 444-8585, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193788" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/physiology/*ultrastructure ; Cell Polarity ; Colforsin/pharmacology ; Diffusion ; *Exocytosis ; Extracellular Space ; Fluorescence ; Glucose/pharmacology ; Guinea Pigs ; Image Processing, Computer-Assisted ; Insulin/*secretion ; Intracellular Membranes/physiology/ultrastructure ; Islets of Langerhans/blood supply/*physiology/secretion/*ultrastructure ; Kinetics ; Membrane Fusion ; Membrane Lipids/physiology ; Mice ; Mice, Inbred ICR ; Permeability ; Pyridinium Compounds ; Quaternary Ammonium Compounds ; Rhodamines ; Secretory Vesicles/physiology/*ultrastructure
    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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