Showing 301 - 320 results of 100,619 for search '(( 5 ((((nn decrease) OR (teer decrease))) OR (a decrease)) ) OR ( 2 step decrease ))', query time: 0.89s Refine Results
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    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.…”
  5. 305

    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. 306

    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. 307

    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. 308

    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. 309

    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. 310

    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. 311

    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. 312

    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. 313

    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. 314

    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. 315

    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. …”
  16. 316

    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. …”
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    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>. …”
  20. 320

    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). …”