Showing 641 - 660 results of 100,766 for search '(( 5 ((((nm decrease) OR (a decrease))) OR (nn decrease)) ) OR ( 2 step decrease ))', query time: 1.77s Refine Results
  1. 641

    Tonic nM DA stabilizes the timing of LP activity over the short term. by Wulf-Dieter C. Krenz (693267)

    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. …”
  2. 642

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  3. 643

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  4. 644

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  5. 645

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  6. 646

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  7. 647

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  8. 648

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  9. 649

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  10. 650

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  11. 651

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  12. 652

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  13. 653

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    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. …”
  14. 654

    Decreased 11ß-HSD1 protein level by IGF-I overexpression <i>in vivo</i> and a direct treatment with IGF-I. by Subrata Chowdhury (787208)

    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. …”
  15. 655
  16. 656
  17. 657

    Activation of mitoK<sub>ATP</sub> channels decreased the latency time of the transjunctional currents in slice. by Jiangping Wang (281901)

    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>. …”
  18. 658
  19. 659

    Decreased reactive gliosis following ES delivered 5d post-demyelination. by Nikki A. McLean (643606)

    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). …”
  20. 660