Showing 241 - 260 results of 145,317 for search '(( a ((a decrease) OR (linear decrease)) ) OR ( a ((largest decrease) OR (greater decrease)) ))', query time: 0.72s Refine Results
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    In superadditive networks, more enhancers decrease noise and fidelity. by Alvaro Fletcher (15675430)

    Published 2023
    “…<p>(A) Superadditivity is implemented in our model by linearly increasing <i>k</i><sub>on</sub> rates and linearly decreasing <i>k</i><sub>off</sub> rates. …”
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    Schematic drawing of IAPV (A) and ERCC (B). by Denis Witham (12517162)

    Published 2025
    “…PaCO2 reduced after 20 minutes with both techniques (IAPV: from 65 to 52 mmHg, p < 0.01, relative effect (CI) 0.15 (0.01–0.28); ERCC: from 61 to 51 mmHg, p= < 0.01, relative effect (CI) 0.22 (0.07–0.37)). A transient decrease in oxygenation was fully and rapidly reversible. …”
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    Validating the stability of the analysis against nonuniform coverage of a fish’s trajectory. by Lear Cohen (15353793)

    Published 2023
    “…The tuning curves either gradually decreased (<b>A</b>), were quasi-uniformly distributed in space (<b>B</b>), or gradually increased (<b>C</b>) with position along the vertical axis of the water tank. …”
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    Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket by Lilia Leisle (11356934)

    Published 2021
    “…We confirmed experimentally that the interaction is predominantly driven by electrostatic forces, and using noncanonical amino acids as photo-cross-linkers, we identified 16 residues in ASIC1a contributing to Big Dyn binding. Covalently tethering Big Dyn to its ASIC1a binding site dramatically decreased the proton sensitivity of channel activation, suggesting that Big Dyn stabilizes a resting conformation of ASIC1a and dissociates from its binding site during channel opening.…”
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    Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket by Lilia Leisle (11356934)

    Published 2021
    “…We confirmed experimentally that the interaction is predominantly driven by electrostatic forces, and using noncanonical amino acids as photo-cross-linkers, we identified 16 residues in ASIC1a contributing to Big Dyn binding. Covalently tethering Big Dyn to its ASIC1a binding site dramatically decreased the proton sensitivity of channel activation, suggesting that Big Dyn stabilizes a resting conformation of ASIC1a and dissociates from its binding site during channel opening.…”
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