Showing 721 - 740 results of 225,047 for search '(( 10 ((((ng decrease) OR (a decrease))) OR (nn decrease)) ) OR ( 2 step decrease ))', query time: 1.33s Refine Results
  1. 721

    Decrease in invasion of HTR-8/SVneo trophoblastic cells by interferon gamma involves cross-communication of STAT1 and BATF2 that regulates the expression of JUN by Sonam Verma (4818036)

    Published 2018
    “…Interestingly, phosphorylated JUN is also regulated by BATF2 and STAT1. Collectively, these findings showed that decrease in the invasion of HTR-8/SVneo cells after IFNG treatment is controlled by STAT1 and BATF2, which further regulates the expression of JUN.…”
  2. 722

    A heatmap of the -log10(adj.pvalues) from AME enrichment testing within increasing and decreasing sites. by Spencer L. Nystrom (8730641)

    Published 2021
    “…<p>A heatmap of the -log10(adj.pvalues) from AME enrichment testing within increasing and decreasing sites.…”
  3. 723

    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. 724

    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. 725

    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. 726

    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. 727

    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. 728

    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. 729

    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. 730

    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. 731

    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. 732

    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. 733

    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. 734

    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. …”
  15. 735
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  17. 737

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

    Published 2013
    “…The time of the maximal current rise slope from both the S<sub>cell</sub> (b - a) and R<sub>cell</sub> (c - a) were calculated using the Clampfit 10.2 software. …”
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  19. 739
  20. 740