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nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
n decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
step decrease » sizes decrease (Expand Search), teer decrease (Expand Search), we decrease (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
n decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
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841
Brain uptake of [<sup>3</sup>H]mannitol in 2-, 8-, 12-, and 24-month-old mice.
Published 2023Subjects: -
842
MFSD2A expression levels in brain microvessels from 2-, 8-, 12-, and 24-month-old mice.
Published 2023Subjects: -
843
Brain uptake of [<sup>14</sup>C]docosahexaenoic acid (DHA) in 2-, 8-, 12-, and 24-month-old mice.
Published 2023Subjects: -
844
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845
Brain uptake rate of [<sup>14</sup>C]sucrose in the whole brain and individual brain regions.
Published 2023Subjects: -
846
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847
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848
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849
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...
Published 2011“…Herein we use NO to probe the superoxide binding site of our thiolate-ligated biomimetic SOR model [Fe<sup>II</sup>(S<sup>Me<sub>2</sub></sup>N<sub>4</sub>(tren))]<sup>+</sup> (<b>1</b>). 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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850
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...
Published 2011“…Herein we use NO to probe the superoxide binding site of our thiolate-ligated biomimetic SOR model [Fe<sup>II</sup>(S<sup>Me<sub>2</sub></sup>N<sub>4</sub>(tren))]<sup>+</sup> (<b>1</b>). 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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