Search alternatives:
significant contribution » significant correlation (Expand Search), significant correlations (Expand Search), significant interaction (Expand Search)
contribution decreases » contribution rates (Expand Search), contribution descriptors (Expand Search)
teer decrease » mean decrease (Expand Search), greater decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
significant contribution » significant correlation (Expand Search), significant correlations (Expand Search), significant interaction (Expand Search)
contribution decreases » contribution rates (Expand Search), contribution descriptors (Expand Search)
teer decrease » mean decrease (Expand Search), greater decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
-
1
-
2
-
3
-
4
-
5
-
6
-
7
-
8
Y-27632 collaborated with BA to attenuate the increase in the integrity and decrease in the permeability of epithelial barrier injury induced by LPS in Caco2 monolayers.
Published 2024“…<p>(<b>A)</b> Y-27632 collaborated with BA to attenuate the effect of LPS on TEER in Caco2 cells on days 1–22. …”
-
9
-
10
-
11
-
12
-
13
-
14
-
15
Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
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.…”
-
16
Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
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.…”
-
17
-
18
-
19
-
20