Search alternatives:
step decrease » sizes decrease (Expand Search), teer decrease (Expand Search), we decrease (Expand Search)
nm decrease » _ decrease (Expand Search), we decrease (Expand Search), gy decreased (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
2 step » _ step (Expand Search), a step (Expand Search)
step decrease » sizes decrease (Expand Search), teer decrease (Expand Search), we decrease (Expand Search)
nm decrease » _ decrease (Expand Search), we decrease (Expand Search), gy decreased (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
2 step » _ step (Expand Search), a step (Expand Search)
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641
Tonic nM DA stabilizes the timing of LP activity over the short term.
Published 2015“…<p><b>(A) Pyloric output is altered by 1mM 4AP</b>. Representative experiments showing the motor output at three time points for a preparation continuously superfused with 1mM 4AP (blue) or 1mM 4AP + 5nM DA (green) beginning at t = 0. …”
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642
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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643
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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644
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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645
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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646
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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647
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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648
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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649
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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650
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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651
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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652
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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653
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a...
Published 2009“…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
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654
Decreased 11ß-HSD1 protein level by IGF-I overexpression <i>in vivo</i> and a direct treatment with IGF-I.
Published 2015“…<p><b>A</b>. IGF-I overexpression decreased the levels of 11ß-HSD1 in pancreatic islets, liver and visceral fat, shown in Western blots. …”
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655
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656
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657
Activation of mitoK<sub>ATP</sub> channels decreased the latency time of the transjunctional currents in slice.
Published 2013“…<p>(<b>A</b>) Currents in S<sub>cell</sub> induced by a pair of ±160 mV voltage steps and the transjunctional currents received by the R<sub>cell</sub>. …”
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658
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659
Decreased reactive gliosis following ES delivered 5d post-demyelination.
Published 2014“…Contralateral intact control nerves displayed only minimal GFAP IF (A). However 5d post-lysophosphatidyl choline (LPC)/FG injection there was a marked increase in GFAP IF (B). …”
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660