بدائل البحث:
nn decrease » _ decrease (توسيع البحث), gy decreased (توسيع البحث), b1 decreased (توسيع البحث)
ms decrease » _ decrease (توسيع البحث), use decreased (توسيع البحث), gy decreased (توسيع البحث)
a decrease » _ decrease (توسيع البحث), _ decreased (توسيع البحث), _ decreases (توسيع البحث)
50 ms » 50 mg (توسيع البحث), 50 mm (توسيع البحث)
nn decrease » _ decrease (توسيع البحث), gy decreased (توسيع البحث), b1 decreased (توسيع البحث)
ms decrease » _ decrease (توسيع البحث), use decreased (توسيع البحث), gy decreased (توسيع البحث)
a decrease » _ decrease (توسيع البحث), _ decreased (توسيع البحث), _ decreases (توسيع البحث)
50 ms » 50 mg (توسيع البحث), 50 mm (توسيع البحث)
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81
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82
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83
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84
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85
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86
Quantitative decrease of apolipoprotein-A1 by cohort.
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).…"
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87
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88
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89
The decrease or inhibition of Hsp90 induced REST degradation.
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. …"
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90
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91
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92
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93
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94
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95
Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
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.…"
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96
Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
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.…"
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97
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98
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99
Decreased activity of FASII favors the cold growth of the <i>ΔcshA</i> strain.
منشور في 2020"…<p><b>(A)</b><i>fapR</i> mRNA levels decrease in ACC and biotin related suppressor strains. …"
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100
Expression of IR21a, IR93a, and IR25a proteins decreases in DOCCs at the late third instar.
منشور في 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). …"