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  • 1
    Publication Date: 2019
    Description: 〈p〉To examine the contributions of impaired gut microbial community development to childhood undernutrition, we combined metabolomic and proteomic analyses of plasma samples with metagenomic analyses of fecal samples to characterize the biological state of Bangladeshi children with severe acute malnutrition (SAM) as they transitioned, after standard treatment, to moderate acute malnutrition (MAM) with persistent microbiota immaturity. Host and microbial effects of microbiota-directed complementary food (MDCF) prototypes targeting weaning-phase bacterial taxa underrepresented in SAM and MAM microbiota were characterized in gnotobiotic mice and gnotobiotic piglets colonized with age- and growth-discriminatory bacteria. A randomized, double-blind controlled feeding study identified a lead MDCF that changes the abundances of targeted bacteria and increases plasma biomarkers and mediators of growth, bone formation, neurodevelopment, and immune function in children with MAM.〈/p〉
    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: 1991-09-20
    Description: Bean leaf stomata provide a topographical signal that induces germlings of the phytopathogen Uromyces appendiculatus to develop specialized infection structures. Protoplasts from germ tubes of this fungus, when examined with patch-clamp electrodes, displayed the activities of a 600-picosiemen mechanosensitive ion channel. This channel passes a variety of cations, including Ca2+, and is blocked by Gd3+ at 50 micromolar. This channel could transduce the membrane stress induced by the leaf topography into an influx of ions, including Ca2+, that may trigger differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, X L -- Stumpf, M A -- Hoch, H C -- Kung, C -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1415-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716786" target="_blank"〉PubMed〈/a〉
    Keywords: Barium/pharmacology ; Basidiomycota/*physiology/ultrastructure ; Cell Membrane/physiology/ultrastructure ; Gadolinium/pharmacology ; Ion Channels/drug effects/*physiology/ultrastructure ; Mechanoreceptors/physiology ; Membrane Potentials ; Pressure ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology
    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: 2012-03-10
    Description: We showed that alumina (Al(2)O(3)) overcoating of supported metal nanoparticles (NPs) effectively reduced deactivation by coking and sintering in high-temperature applications of heterogeneous catalysts. We overcoated palladium NPs with 45 layers of alumina through an atomic layer deposition (ALD) process that alternated exposures of the catalysts to trimethylaluminum and water at 200 degrees C. When these catalysts were used for 1 hour in oxidative dehydrogenation of ethane to ethylene at 650 degrees C, they were found by thermogravimetric analysis to contain less than 6% of the coke formed on the uncoated catalysts. Scanning transmission electron microscopy showed no visible morphology changes after reaction at 675 degrees C for 28 hours. The yield of ethylene was improved on all ALD Al(2)O(3) overcoated Pd catalysts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Junling -- Fu, Baosong -- Kung, Mayfair C -- Xiao, Guomin -- Elam, Jeffrey W -- Kung, Harold H -- Stair, Peter C -- New York, N.Y. -- Science. 2012 Mar 9;335(6073):1205-8. doi: 10.1126/science.1212906.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Energy Systems Division, Argonne National Laboratory, Argonne, IL 60439, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22403386" target="_blank"〉PubMed〈/a〉
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    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoch, H C -- Kung, C -- Zhou, X L -- Stumpf, M A -- New York, N.Y. -- Science. 1992 May 29;256(5061):1336.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17736765" target="_blank"〉PubMed〈/a〉
    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
    Publication Date: 1984-07-27
    Description: Two different divalent cation-selective channels from Paramecium cilia were incorporated into planar lipid bilayers. Both channels were much more permeable to divalent than univalent cations, and one of them discriminated significantly among the divalent cations. The selectivity and voltage dependence of the latter channel are comparable to those of voltage-dependent calcium channels found in a variety of cells. A combined biochemical, biophysical, and genetic study of calcium channels is now possible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrlich, B E -- Finkelstein, A -- Forte, M -- Kung, C -- GM 22714/GM/NIGMS NIH HHS/ -- GM 29210/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jul 27;225(4660):427-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6330895" target="_blank"〉PubMed〈/a〉
    Keywords: Barium/metabolism ; Calcium/*metabolism ; Chlorides/metabolism ; Cilia/*metabolism ; Electrophysiology ; Ion Channels/*metabolism/physiology ; Lipid Bilayers/*metabolism ; Magnesium/metabolism ; Paramecium/*metabolism ; Potassium/metabolism
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    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-10-08
    Description: The rates of activation and deactivation of the currents carried by calcium, strontium, or barium ions through the voltage-sensitive calcium channel of Paramecium are different. The differences cannot be attributed to complications due to internal ion concentration, calcium channel inactivation, potassium current activation, surface charge effects, or incomplete space clamping. The findings indicate participation of the divalent cations in the voltage-driven calcium channel gating process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saimi, Y -- Kung, C -- GM22714/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 8;218(4568):153-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Barium/metabolism ; Calcium/*metabolism ; Cell Membrane/physiopathology ; Ion Channels/*metabolism ; Kinetics ; Membrane Potentials ; Paramecium/*physiology ; Strontium/metabolism
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    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-11-04
    Description: Mechanosensitive ion channels use mechanical energy to gate the dissipation of electrochemical gradients across cell membranes. This function is fundamental to physiological processes such as hearing and touch. In electrophysiological studies of ion channels in the plasma membrane of the yeast Saccharomyces cerevisiae, channels were observed that were activated by, and adapted to, stretching of the membrane. Adaptation of channel activity to mechanical stimuli was voltage-dependent. Because these mechanosensitive channels pass both cations and anions, they may play a role in turgor regulation in this walled organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gustin, M C -- Zhou, X L -- Martinac, B -- Kung, C -- GM37925/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):762-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2460920" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Anions/physiology ; Cations/physiology ; Cell Membrane/*physiology ; Cell Membrane Permeability ; Hydrostatic Pressure ; Ion Channels/*physiology ; Membrane Potentials ; Saccharomyces cerevisiae/*physiology ; Surface Tension ; Water-Electrolyte Balance
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  • 8
    Publication Date: 1986-04-25
    Description: A combination of genetics, biochemistry, and biophysics was used to show that calmodulin is involved in the regulation of an ion channel. Calmodulin restored the Ca2+-dependent K+ current in pantophobiac, a mutant in Paramecium that lacks this current. The restoration of the current occurred within 2 hours after the injection of 1 picogram of wild-type calmodulin into the mutant. The current remained for approximately 30 hours before the mutant phenotype returned. The injection of calmodulin isolated from pantophobiac had no effect. These results imply that calmodulin is required for the function or regulation of the Ca2+-dependent K+ current in Paramecium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinrichsen, R D -- Burgess-Cassler, A -- Soltvedt, B C -- Hennessey, T -- Kung, C -- 1 F 32 NS 07502-01/NS/NINDS NIH HHS/ -- GM 22714/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):503-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2421410" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/physiology ; Calmodulin/*pharmacology ; Dictyostelium/metabolism ; Ion Channels/*drug effects/physiology ; Mutation ; Paramecium/drug effects/genetics/*metabolism ; Potassium/*metabolism
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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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-12
    Description: Voltage-dependent ion channels have been found in the plasma membrane of the yeast Saccharomyces cerevisiae. Ion channel activities were recorded from spheroplasts or patches of plasma membrane with the patch-clamp technique. The most prominent activities came from a set of potassium channels with the properties of activation by positive but not negative voltages, high selectivity for potassium over sodium ion, unit conductance of 20 picosiemens, inhibition by tetraethylammonium or barium ions, and bursting kinetics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gustin, M C -- Martinac, B -- Saimi, Y -- Culbertson, M R -- Kung, C -- GM-22714/GM/NIGMS NIH HHS/ -- GM-26217/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 12;233(4769):1195-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426783" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/physiology ; Electrophysiology ; Ion Channels/*physiology ; Membrane Potentials ; Potassium/metabolism ; Saccharomyces cerevisiae/*physiology ; Sodium/metabolism
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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