Showing 841 - 860 results of 230,677 for search '(( 5 ((non decrease) OR (point decrease)) ) OR ( 10 ((we decrease) OR (a decrease)) ))', query time: 1.82s Refine Results
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  5. 845

    The dependence of (a) the <em>H<sub>P</sub></em> + <em>H<sub>s</sub></em> and (b) the total Hamiltonian <em>H</em> on δ and <em>y</em><sub>0</sub>, with parameters <em>N</em> = 5 <... by Shu-Wei Song (557396)

    Published 2013
    “…</strong> The dependence of (a) the <em>H<sub>P</sub></em> + <em>H<sub>s</sub></em> and (b) the total Hamiltonian <em>H</em> on δ and <em>y</em><sub>0</sub>, with parameters <em>N</em> = 5 <b>×</b> 10<sup>4</sup>, κ = 2.0, η = 0.0096 and R = 64 in the <sup>23</sup>Na condensate. …”
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  14. 854

    Supplementary Material for: Prenatal Infection Decreases Calbindin, Decreases Purkinje Cell Volume and Density and Produces Long-Term Motor Deficits in Sprague-Dawley Rats by Wallace K. (4120819)

    Published 2010
    “…Pups in the <i>E. coli</i> group also had a decrease in the number of Purkinje cells, as well as a decrease in Purkinje cell density and volume. …”
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    ApoER2 expression increases Aβ production while decreasing Amyloid Precursor Protein (APP) endocytosis: Possible role in the partitioning of APP into lipid rafts and in the regulat... by Rodrigo A Fuentealba (77901)

    Published 2011
    “…<p><b>Copyright information:</b></p><p>Taken from "ApoER2 expression increases Aβ production while decreasing Amyloid Precursor Protein (APP) endocytosis: Possible role in the partitioning of APP into lipid rafts and in the regulation of γ-secretase activity"</p><p>http://www.molecularneurodegeneration.com/content/2/1/14</p><p>Molecular Neurodegeneration 2007;2():14-14.…”
  19. 859

    Influence of Thiolate Ligands on Reductive N−O Bond Activation. Probing the O<sub>2</sub><sup>−</sup> Binding Site of a Biomimetic Superoxide Reductase Analogue and Examining the P... by Gloria Villar-Acevedo (2232583)

    Published 2011
    “…Like NO-bound <i>trans</i>-cysteinate-ligated SOR (SOR-NO), the rhombic <i>S</i> = 3/2 EPR signal of NO-bound <i>cis</i>-thiolate-ligated [Fe(S<sup>Me<sub>2</sub></sup>N<sub>4</sub>(tren)(NO)]<sup>+</sup> (<b>2</b>; <i>g</i> = 4.44, 3.54, 1.97), the isotopically sensitive ν<sub>NO</sub>(ν<sub><sup>15</sup>NO</sub>) stretching frequency (1685(1640) cm<sup>−1</sup>), and the 0.05 Å decrease in Fe−S bond length are shown to be consistent with <i>the oxidative addition of NO to Fe(II)</i> to afford an Fe(III)−NO<sup>−</sup> {FeNO}<sup>7</sup> species containing high-spin (<i>S</i> = 5/2) Fe(III) antiferromagnetically coupled to NO<sup>−</sup> (<i>S</i> = 1). …”
  20. 860

    Influence of Thiolate Ligands on Reductive N−O Bond Activation. Probing the O<sub>2</sub><sup>−</sup> Binding Site of a Biomimetic Superoxide Reductase Analogue and Examining the P... by Gloria Villar-Acevedo (2232583)

    Published 2011
    “…Like NO-bound <i>trans</i>-cysteinate-ligated SOR (SOR-NO), the rhombic <i>S</i> = 3/2 EPR signal of NO-bound <i>cis</i>-thiolate-ligated [Fe(S<sup>Me<sub>2</sub></sup>N<sub>4</sub>(tren)(NO)]<sup>+</sup> (<b>2</b>; <i>g</i> = 4.44, 3.54, 1.97), the isotopically sensitive ν<sub>NO</sub>(ν<sub><sup>15</sup>NO</sub>) stretching frequency (1685(1640) cm<sup>−1</sup>), and the 0.05 Å decrease in Fe−S bond length are shown to be consistent with <i>the oxidative addition of NO to Fe(II)</i> to afford an Fe(III)−NO<sup>−</sup> {FeNO}<sup>7</sup> species containing high-spin (<i>S</i> = 5/2) Fe(III) antiferromagnetically coupled to NO<sup>−</sup> (<i>S</i> = 1). …”