Showing 661 - 680 results of 149,868 for search '(( a we decrease ) OR ( 5 ((ng decrease) OR (((nn decrease) OR (a decrease)))) ))', query time: 1.71s Refine Results
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    A Dissolved Oxygen Threshold for Shifts in Bacterial Community Structure in a Seasonally Hypoxic Estuary by Rachel L. Spietz (782905)

    Published 2015
    “…To assess the effects of decreasing dissolved oxygen on bacteria, we examined shifts in bacterial community structure over space and time in Hood Canal, Washington, USA−a glacial fjord-like water body that experiences seasonal low dissolved oxygen levels known to be detrimental to fish and other marine organisms. …”
  3. 663

    <i>SLC2A2</i> is essential for liver differentiation in developing vertebrates by Yejin Kim (740789)

    Published 2025
    “…Total RNA was isolated from uninjected control and <i>SLC2A2</i> MO‐injected embryos (2.5, 5, and 10 ng). …”
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    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). …”
  8. 668

    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). …”
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    Deletion of murine <i>Rhoh</i> leads to de-repression of <i>Bcl-6</i> via decreased KAISO levels and accelerates a malignancy phenotype in a murine model of lymphoma by Hiroto Horiguchi (3215001)

    Published 2022
    “…The loss of Rhoh in Bcl-6<sup>Tg</sup> mice led to a more rapid disease progression. Mechanistically, we demonstrated that deletion of Rhoh in these murine lymphoma cells was associated with decreased levels of the RhoH binding partner KAISO, a dual-specific Zinc finger transcription factor, de-repression of KAISO target Bcl-6, and downregulation of the BCL-6 target Blimp-1. …”
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    MCP-1-deficiency decreased CD11c-expressing cells via impairing the production of ROS and decreased activation of PLCγ2, Akt, and ERK upon M-CSF stimulation in BMM. by Woon-Ki Kim (447798)

    Published 2013
    “…<p>BMMs from WT (open bar) and MCP-1-KO mice (oblique-lined bar) were incubated in the presence of M-CSF (30 ng/ml) with U73122 (10 µM), Akt inhibitor IV (0.3 µM), PD098059 (5 µM), DPI (50 nM), NAC (3 mM), or H<sub>2</sub>O<sub>2</sub> (300 µM) for 4 d (A). *, <i>P</i><0.05; ***, <i>P</i><0.001 compared with vehicle-treated WT cells. …”
  14. 674

    Significant decrease of SMAD4 protein in DBA iPSCs. by Jingping Ge (636557)

    Published 2015
    “…A) Slight decrease of mRNA level of <i>SMAD4</i> in the DBA iPSCs with <i>RPS19</i> or <i>RPL5</i> mutations. …”
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