Showing 161 - 180 results of 145,706 for search '(( a a decrease ) OR ((( 50 ((n decrease) OR (nn decrease)) ) OR ( 5 ng decrease ))))', query time: 0.83s Refine Results
  1. 161

    NatB inactivation decreased the level of MAPK and proposed model of EGFR/MAPK signaling regulation by NatB and the N-end rule pathways. by Zhentao Sheng (107495)

    Published 2020
    “…<p>(A-B) <i>psid-D1</i> (A) or <i>psid-D4</i> (B) clones in 3rd instar fat body, which were marked by GFP expression (pointed by arrowheads), showed decreased MAPK levels (anti-MAPK staining, red). …”
  2. 162

    Quantitative decrease of apolipoprotein-A1 by cohort. by Thierry Poynard (38084)

    Published 2020
    “…<p>Apolipoprotein-A1 decreased (P<0.001) in the three cohorts, starting early in January 2020 (red line with 95% confidence interval) in the US cohort (lower panel).…”
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    The decrease or inhibition of Hsp90 induced REST degradation. by Raúl Orozco-Díaz (7067624)

    Published 2019
    “…(D) The level of REST dramatically reduced in differentiated SH-SY5Y cells treated with GA (1 μM) or PU-H71 (50 nM) at 24 h. (E) The REST level decreased by GA more than 50% and (F) PU-H71 more than 80%, respectively. …”
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    Elevated IDO activity in HD mouse brains is decreased by <i>ex-vivo</i> iron chelation. by David W. Donley (3111198)

    Published 2021
    “…<p>Mouse pups were supplemented with carbonyl iron from postnatal days 10–17 and then were sacrificed at 14 weeks of age. <b>A.</b> Striatal IDO activity is increased in N171-82Q HD mice and significantly decreased by <i>ex vivo</i> iron (III) chelation (50 μM deferoxamine). …”
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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.…”