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  • 1
    Publication Date: 2019-07-17
    Description: As part of the second Aerosol Characterization Experiment (ACE-2) during June and July of 1997, aerosol size distributions were measured on board the CIRPAS Pelican aircraft through the use of a DMA and two OPCS. During the campaign, the boundary layer aerosol typically possessed characteristics representative of a background marine aerosol or a continentally influenced aerosol, while the free tropospheric aerosol was characterized by the presence or absence of a Saharan dust layer. A range of radiative closure comparisons were made using the data obtained during vertical profiles flown on four missions. Of particular interest here are the comparisons made between the optical properties as determined through the use of measured aerosol size distributions and those measured directly by an airborne 14-wavelength sunphotometer and three nephelometers. Variations in the relative humidity associated with each of the direct measurements required consideration of the hygroscopic properties of the aerosol for size distribution based calculations. Simultaneous comparison with such a wide range of directly measured optical parameters not only offers evidence of the validity of the physicochemical description of the aerosol when closure is achieved, but also provides insight into potential sources of error when some or all of the comparisons result in disagreement. Agreement between the derived and directly measured optical properties varied for different measurements and for different cases. Averaged over the four case studies, the derived extinction coefficient at 525 nm exceeded that measured by the sunphotomoter by 2.5% in the clean boundary later, but underestimated measurements by 13% during pollution events. For measurements within the free troposphere, the mean derived extinction coefficient was 3.3% and 17% less than that measured by the sunphotometer during dusty and nondusty conditions, respectively. Likewise, averaged discrepancies between the derived and measured scattering coefficient were -9.6%, +4.7%, +17%, and -41% for measurements within the clean boundary layer, polluted boundary layer, free troposphere with a dust layer, and free troposphere without a dust layer, respectively. Each of these quantities, as well as the majority of the 〉 100 individual comparisons from which they were averaged, were within estimated uncertainties.
    Keywords: Environment Pollution
    Type: Analysis of Atmospheric Aerosol Data Sets and Application of Radiative Transfer Models to Compute Aerosol Effects
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  • 2
    Publication Date: 1998-11-13
    Description: The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-alpha converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-alpha (TNFalpha) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, the L-selectin adhesion molecule, and transforming growth factor-alpha (TGFalpha). The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peschon, J J -- Slack, J L -- Reddy, P -- Stocking, K L -- Sunnarborg, S W -- Lee, D C -- Russell, W E -- Castner, B J -- Johnson, R S -- Fitzner, J N -- Boyce, R W -- Nelson, N -- Kozlosky, C J -- Wolfson, M F -- Rauch, C T -- Cerretti, D P -- Paxton, R J -- March, C J -- Black, R A -- CA43793/CA/NCI NIH HHS/ -- DK53804/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101, USA. peschon@immunex.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812885" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cell Membrane/*metabolism ; Cells, Cultured ; Crosses, Genetic ; *Embryonic and Fetal Development ; L-Selectin/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/chemistry/genetics/*metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Protein Processing, Post-Translational ; Receptors, Tumor Necrosis Factor/metabolism ; Transforming Growth Factor alpha/metabolism ; Tumor Necrosis Factor-alpha/*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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  • 3
    Publication Date: 2000-04-25
    Description: Computerized tomography scans of a ferruginous concretion within the chest region of an ornithischian dinosaur reveal structures that are suggestive of a four-chambered heart and a single systemic aorta. The apparently derived condition of the cardiovascular system in turn suggests the existence of intermediate-to-high metabolic rates among dinosaurs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fisher, P E -- Russell, D A -- Stoskopf, M K -- Barrick, R E -- Hammer, M -- Kuzmitz, A A -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):503-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomedical Imaging Facility, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, USA. PaulvFisher@ncsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775107" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/anatomy & histology ; Basal Metabolism ; Birds/anatomy & histology/metabolism ; Body Weight ; *Fossils ; Heart/*anatomy & histology/radiography ; Image Processing, Computer-Assisted ; Iron Compounds/analysis ; Minerals ; Paleontology ; Reptiles/*anatomy & histology/*metabolism ; Tomography Scanners, X-Ray Computed ; Tomography, X-Ray Computed ; X-Ray Diffraction
    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
    Publication Date: 2001-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nadeau, J H -- Balling, R -- Barsh, G -- Beier, D -- Brown, S D -- Bucan, M -- Camper, S -- Carlson, G -- Copeland, N -- Eppig, J -- Fletcher, C -- Frankel, W N -- Ganten, D -- Goldowitz, D -- Goodnow, C -- Guenet, J L -- Hicks, G -- Hrabe de Angelis, M -- Jackson, I -- Jacob, H J -- Jenkins, N -- Johnson, D -- Justice, M -- Kay, S -- Kingsley, D -- Lehrach, H -- Magnuson, T -- Meisler, M -- Poustka, A -- Rinchik, E M -- Rossant, J -- Russell, L B -- Schimenti, J -- Shiroishi, T -- Skarnes, W C -- Soriano, P -- Stanford, W -- Takahashi, J S -- Wurst, W -- Zimmer, A -- International Mouse Mutagenesis Consortium -- New York, N.Y. -- Science. 2001 Feb 16;291(5507):1251-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, BRB 624, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106, USA. jhn4@po.cwru.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11233449" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *Computational Biology ; Costs and Cost Analysis ; Genes/physiology ; Genetic Techniques ; *Genome ; *Genomics ; International Cooperation ; Mice/*genetics ; Mutagenesis ; Mutation ; Phenotype ; Private Sector ; Public Sector ; Research Support as Topic ; *Sequence Analysis, DNA
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-05-16
    Description: Ruminant animals and ruminal microorganisms have a symbiotic relationship that facilitates fiber digestion, but domestic ruminants in developed countries are often fed an abundance of grain and little fiber. When ruminants are fed fiber-deficient rations, physiological mechanisms of homeostasis are disrupted, ruminal pH declines, microbial ecology is altered, and the animal becomes more susceptible to metabolic disorders and, in some cases, infectious disease. Some disorders can be counteracted by feed additives (for example, antibiotics and buffers), but these additives can alter the composition of the ruminal ecosystem even further.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, J B -- Rychlik, J L -- New York, N.Y. -- Science. 2001 May 11;292(5519):1119-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Agricultural Research Service, U.S. Department of Agriculture, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11352069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic/anatomy & histology/microbiology/parasitology/physiology ; Bacteria/metabolism/pathogenicity ; Digestive System/anatomy & histology/*microbiology/parasitology/physiopathology ; *Digestive System Physiological Phenomena ; Drug Resistance, Microbial ; *Ecology ; Eukaryota/metabolism ; Fermentation ; Homeostasis ; Host-Parasite Interactions ; Humans ; Hydrogen-Ion Concentration ; Ruminants/anatomy & histology/*microbiology/parasitology/*physiology ; Symbiosis/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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  • 6
    Publication Date: 2001-02-13
    Description: "Limited control" models of reproductive skew in cooperative societies suggest that the frequency of breeding by subordinates is determined by the outcome of power struggles with dominants. In contrast, "optimal skew" models suggest that dominants have full control of subordinate reproduction and allow subordinates to breed only when this serves to retain subordinates' assistance with rearing dominants' own litters. The results of our 7-year field study of cooperative meerkats, Suricata suricatta, support the predictions of limited control models and provide no indication that dominant females grant reproductive concessions to subordinates to retain their assistance with future breeding attempts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clutton-Brock, T H -- Brotherton, P N -- Russell, A F -- O'Riain, M J -- Gaynor, D -- Kansky, R -- Griffin, A -- Manser, M -- Sharpe, L -- McIlrath, G M -- Small, T -- Moss, A -- Monfort, S -- New York, N.Y. -- Science. 2001 Jan 19;291(5503):478-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK. thcb@hermes.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11161200" target="_blank"〉PubMed〈/a〉
    Keywords: Africa, Southern ; Aging ; Animals ; Behavior, Animal ; Body Weight ; Carnivora/*physiology ; *Cooperative Behavior ; *Dominance-Subordination ; Female ; Male ; Models, Biological ; Rain ; *Reproduction ; Seasons ; *Sexual Behavior, Animal
    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
    Publication Date: 2001-09-29
    Description: Although breeding success is known to increase with group size in several cooperative mammals, the mechanisms underlying these relationships are uncertain. We show that in wild groups of cooperative meerkats, Suricata suricatta, reductions in the ratio of helpers to pups depress the daily weight gain and growth of pups and the daily weight gain of helpers. Increases in the daily weight gain of pups are associated with heavier weights at independence and at 1 year of age, as well as with improved foraging success as juveniles and higher survival rates through the first year of life. These results suggest that the effects of helpers on the fitness of pups extend beyond weaning and that helpers may gain direct as well as indirect benefits by feeding pups.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clutton-Brock, T H -- Russell, A F -- Sharpe, L L -- Brotherton, P N -- McIlrath, G M -- White, S -- Cameron, E Z -- New York, N.Y. -- Science. 2001 Sep 28;293(5539):2446-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK. thcb@hermes.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11577235" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breeding ; Carnivora/growth & development/*physiology ; *Cooperative Behavior ; Feeding Behavior ; Female ; Male ; Survival Rate ; *Weight Gain
    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
    Publication Date: 2000-06-17
    Description: Using fluorescence microscopy, we studied the catalysis by and folding of individual Tetrahymena thermophila ribozyme molecules. The dye-labeled and surface-immobilized ribozymes used were shown to be functionally indistinguishable from the unmodified free ribozyme in solution. A reversible local folding step in which a duplex docks and undocks from the ribozyme core was observed directly in single-molecule time trajectories, allowing the determination of the rate constants and characterization of the transition state. A rarely populated docked state, not measurable by ensemble methods, was observed. In the overall folding process, intermediate folding states and multiple folding pathways were observed. In addition to observing previously established folding pathways, a pathway with an observed folding rate constant of 1 per second was discovered. These results establish single-molecule fluorescence as a powerful tool for examining RNA folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhuang, X -- Bartley, L E -- Babcock, H P -- Russell, R -- Ha, T -- Herschlag, D -- Chu, S -- GM49423/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 16;288(5473):2048-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Stanford University, Stanford, CA 94305-4060, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10856219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biotinylation ; Carbocyanines ; Catalysis ; Fluorescent Dyes ; Guanosine/metabolism ; Kinetics ; Microscopy, Fluorescence ; Models, Molecular ; *Nucleic Acid Conformation ; Oligoribonucleotides/metabolism ; RNA, Catalytic/*chemistry/*metabolism ; RNA, Protozoan/*chemistry/metabolism ; Tetrahymena thermophila
    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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  • 9
    Publication Date: 1998-09-11
    Description: The gastric stomach of humans is a barrier to food-borne pathogens, but Escherichia coli can survive at pH 2.0 if it is grown under mildly acidic conditions. Cattle are a natural reservoir for pathogenic E. coli, and cattle fed mostly grain had lower colonic pH and more acid-resistant E. coli than cattle fed only hay. On the basis of numbers and survival after acid shock, cattle that were fed grain had 10(6)-fold more acid-resistant E. coli than cattle fed hay, but a brief period of hay feeding decreased the acid-resistant count substantially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diez-Gonzalez, F -- Callaway, T R -- Kizoulis, M G -- Russell, J B -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1666-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, Section of Microbiology, Cornell University and Agricultural Research Service, U.S. Department of Agriculture, Ithaca, NY 14853-8101, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733511" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Feed ; Animal Husbandry ; Animals ; Bacteria, Anaerobic/growth & development ; Cattle/*microbiology ; Colon/chemistry/*microbiology ; Colony Count, Microbial ; Culture Media ; Diet ; *Edible Grain ; Escherichia coli/*growth & development ; Fatty Acids, Volatile/analysis ; Hydrogen-Ion Concentration ; Lactic Acid/analysis ; *Poaceae ; Random Allocation ; Rumen/chemistry/microbiology ; Succinates/analysis
    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
    Publication Date: 2009-11-27
    Description: Protein design provides a rigorous test of our knowledge about proteins and allows the creation of novel enzymes for biotechnological applications. Whereas progress has been made in designing proteins that mimic native proteins structurally, it is more difficult to design functional proteins. In comparison to recent successes in designing non-metalloproteins, it is even more challenging to rationally design metalloproteins that reproduce both the structure and function of native metalloenzymes. This is because protein metal-binding sites are much more varied than non-metal-containing sites, in terms of different metal ion oxidation states, preferred geometry and metal ion ligand donor sets. Because of their variability, it has been difficult to predict metal-binding site properties in silico, as many of the parameters, such as force fields, are ill-defined. Therefore, the successful design of a structural and functional metalloprotein would greatly advance the field of protein design and our understanding of enzymes. Here we report a successful, rational design of a structural and functional model of a metalloprotein, nitric oxide reductase (NOR), by introducing three histidines and one glutamate, predicted as ligands in the active site of NOR, into the distal pocket of myoglobin. A crystal structure of the designed protein confirms that the minimized computer model contains a haem/non-haem Fe(B) centre that is remarkably similar to that in the crystal structure. This designed protein also exhibits NO reduction activity, and so models both the structure and function of NOR, offering insight that the active site glutamate is required for both iron binding and activity. These results show that structural and functional metalloproteins can be rationally designed in silico.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4297211/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4297211/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeung, Natasha -- Lin, Ying-Wu -- Gao, Yi-Gui -- Zhao, Xuan -- Russell, Brandy S -- Lei, Lanyu -- Miner, Kyle D -- Robinson, Howard -- Lu, Yi -- GM062211/GM/NIGMS NIH HHS/ -- R01 GM062211/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Dec 24;462(7276):1079-82. doi: 10.1038/nature08620. Epub 2009 Nov 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19940850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; Iron/metabolism ; Models, Molecular ; Myoglobin/chemistry ; Nitric Oxide/metabolism ; Oxidoreductases/*chemical synthesis/*chemistry/metabolism ; Protein Binding ; Protein Structure, Tertiary
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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