Showing 261 - 280 results of 224,586 for search '(( a ((((laser decrease) OR (a decrease))) OR (linear decrease)) ) OR ( via large decrease ))', query time: 1.50s Refine Results
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    Reversely Exploring Higher-Order Effects in a Fiber Laser through Physics-Informed Recursive Neural Network by Jingxuan Sun (11998724)

    Published 2024
    “…In ultrafast fiber lasers, the influence of higher-order effects on mode-locked pulses becomes increasingly notable as the pulse width decreases from the subpicosecond to the femtosecond level. …”
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    Wnt5a expressing tumors demonstrate a decrease in markers of the basal tumor subtype. by Stephanie L. Easter (662168)

    Published 2014
    “…Values are means +/− standard error (n = 6 MMTV-Wnt1, 3 fields per tumor; n = 5 MMTV-Wnt1;MMTV-Wnt5a, 3 fields per tumor). MMTV-Wnt1;MMTV-Wnt5a tumors demonstrated a significant decrease in K6-expressing cells as measured by T-test (* = p<0.05).…”
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    Decreased frequency of sEPSCs in <i>Dyt1</i> heterozygous KO mice. by Fumiaki Yokoi (170876)

    Published 2015
    “…<p>(A) Representative traces for sEPSCs. <i>Dyt1</i> heterozygous KO mice had a significantly decreased frequency of sEPSCs (B), but no change in either the amplitude (C), or rise (D) and decay (E) times of these events. …”
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    Expression of IR21a, IR93a, and IR25a proteins decreases in DOCCs at the late third instar. by Jordan J. Tyrrell (10535989)

    Published 2021
    “…Right: <i>Ir21a>GFP-</i>labeled DOCCs express IR21a (Fig 4A), IR93a (Fig 4C) and IR25a (Fig 4E) proteins at 72 hr AEL (top), which are significantly decreased at 120 hr AEL (bottom). …”
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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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