Showing 41 - 60 results of 150,558 for search '(( via large increases ) OR ((( i larvae increases ) OR ( a ((a decrease) OR (nn decrease)) ))))', query time: 1.75s Refine Results
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    Metabolites and pathways that increased in BSF larvae fed with <i>Candida tropicalis</i> compared to larvae without any supplemented fungi in the substrate. by Lilach Ben-Mordechai (21655940)

    Published 2025
    “…<p>Metabolites and pathways that increased in BSF larvae fed with <i>Candida tropicalis</i> compared to larvae without any supplemented fungi in the substrate.…”
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    Pharmacological inhibition of Nampt alleviates stress and skin inflammation in Spint1a-deficient larvae. by Francisco J. Martínez-Morcillo (11663364)

    Published 2021
    “…<b>(C)</b> Neutrophil distribution of wild-type and Spint1a-deficient zebrafish larvae treated with increasing doses of FK-866. …”
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    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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    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.…”