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Showing 341 - 360 results of 224,730 for search '(( 2 step decrease ) OR ( 10 ((teer decrease) OR (((a decrease) OR (nn decrease)))) ))', query time: 1.52s Refine Results
  1. 341
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  2. 342
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  3. 343
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  4. 344
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  5. 345
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  6. 346
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  7. 347
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  8. 348
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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. …”
    Save to List
    Saved in:
  9. 349
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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. …”
    Save to List
    Saved in:
  10. 350
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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. …”
    Save to List
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  11. 351
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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. …”
    Save to List
    Saved in:
  12. 352
    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics

    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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  13. 353
    Mean values and 95% confidence intervals for recovery time, Average NN Interval (AVNN); Standard Deviation of NN Intervals (SDNN), Low Frequency/ High Frequency Ratio (LF/HF); and heart rate (HR) across the three conditions.

    Mean values and 95% confidence intervals for recovery time, Average NN Interval (AVNN); Standard Deviation of NN Intervals (SDNN), Low Frequency/ High Frequency Ratio (LF/HF); and... by Robert Trybulski (10998702)

    Published 2025
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  14. 354
    Activation of mitoK<sub>ATP</sub> channels decreased the latency time of the transjunctional currents in slice.

    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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  15. 355
    Identification of metabolites with cell type-specific-dynamics reveals the amino acid class as highly conserved in hiPSC and hNSC and that most of the cell type-specific amino acids decreased their steady-state upon glutamine step increase.

    Identification of metabolites with cell type-specific-dynamics reveals the amino acid class as highly conserved in hiPSC and hNSC and that most of the cell type-specific amino acid... by João Vasconcelos e Sá (8721594)

    Published 2020
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  16. 356
    Decrease of junctional zone area in low protein placentas at E10.5, E17.5 and E18.5.

    Decrease of junctional zone area in low protein placentas at E10.5, E17.5 and E18.5. by Paula N. Gonzalez (372538)

    Published 2016
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  17. 357
    Results of XCOM and step velocity.

    Results of XCOM and step velocity. by Saori Miyagishima (14593506)

    Published 2023
    Subjects:
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  18. 358
    Down-regulation of <i>ATXN-10</i> in SCA10 fibroblasts decreases PKCδ localization in mitochondria.

    Down-regulation of <i>ATXN-10</i> in SCA10 fibroblasts decreases PKCδ localization in mitochondria. by Misti C. White (247602)

    Published 2010
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  19. 359
    WNF decreases Aβ peptides generation in HEK293 and SH-SY5Y human cells.

    WNF decreases Aβ peptides generation in HEK293 and SH-SY5Y human cells. by Htut Htut Htoo (3686641)

    Published 2017
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  20. 360
    Timeline representation of the different steps of the study procedure.

    Timeline representation of the different steps of the study procedure. by Sofia Sacchetti (9647845)

    Published 2021
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