بدائل البحث:
ng decrease » nn decrease (توسيع البحث), _ decrease (توسيع البحث), gy decreased (توسيع البحث)
we decrease » _ decrease (توسيع البحث), nn decrease (توسيع البحث), teer decrease (توسيع البحث)
a decrease » _ decrease (توسيع البحث), _ decreased (توسيع البحث), _ decreases (توسيع البحث)
50 ng » 50 mg (توسيع البحث), 10 ng (توسيع البحث), 5 ng (توسيع البحث)
ng decrease » nn decrease (توسيع البحث), _ decrease (توسيع البحث), gy decreased (توسيع البحث)
we decrease » _ decrease (توسيع البحث), nn decrease (توسيع البحث), teer decrease (توسيع البحث)
a decrease » _ decrease (توسيع البحث), _ decreased (توسيع البحث), _ decreases (توسيع البحث)
50 ng » 50 mg (توسيع البحث), 10 ng (توسيع البحث), 5 ng (توسيع البحث)
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121
IL-17A promotes OCP autophagy through the ERK/mTOR/Beclin1 pathway induced by RANKL.
منشور في 2023الموضوعات: -
122
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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123
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124
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125
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126
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127
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128
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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129
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130
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131
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132
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133
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134
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135
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136
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137
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138
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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139
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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140