يعرض 121 - 140 نتائج من 145,817 نتيجة بحث عن '(( a a decrease ) OR ((( 50 ng decrease ) OR ( 50 ((mean decrease) OR (we decrease)) ))))', وقت الاستعلام: 0.90s تنقيح النتائج
  1. 121
  2. 122

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

    منشور في 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).…"
  3. 123
  4. 124

    IL-17A inhibits apoptosis of OCPs. حسب Hao Tang (44155)

    منشور في 2023
    الموضوعات:
  5. 125
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  7. 127
  8. 128

    The decrease or inhibition of Hsp90 induced REST degradation. حسب Raúl Orozco-Díaz (7067624)

    منشور في 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. …"
  9. 129
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  11. 131

    NEMA IEC body phantom. حسب Masakazu Tsujimoto (22339504)

    منشور في 2025
    الموضوعات:
  12. 132
  13. 133

    JS-10 phantom. حسب Masakazu Tsujimoto (22339504)

    منشور في 2025
    الموضوعات:
  14. 134
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  18. 138

    Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket حسب Lilia Leisle (11356934)

    منشور في 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.…"
  19. 139

    Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket حسب Lilia Leisle (11356934)

    منشور في 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.…"
  20. 140