Search alternatives:
greater decrease » greater increase (Expand Search), greater increases (Expand Search), rate decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
ai large » i large (Expand Search), via large (Expand Search), _ large (Expand Search)
a large » _ large (Expand Search)
greater decrease » greater increase (Expand Search), greater increases (Expand Search), rate decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
ai large » i large (Expand Search), via large (Expand Search), _ large (Expand Search)
a large » _ large (Expand Search)
-
121
-
122
-
123
-
124
-
125
-
126
-
127
-
128
Opening the Black Box(es)
Published 2025“…<p dir="ltr">A talk which explores challenges for contemporary work in digital humanities stemming from the increasing use of generative large language models.…”
-
129
-
130
-
131
-
132
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.…”
-
133
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.…”
-
134
-
135
-
136
Decreased activity of FASII favors the cold growth of the <i>ΔcshA</i> strain.
Published 2020“…<p><b>(A)</b><i>fapR</i> mRNA levels decrease in ACC and biotin related suppressor strains. …”
-
137
-
138
Light-Controlled Anticancer Activity and Cellular Uptake of a Photoswitchable Cisplatin Analogue
Published 2024“…The <i>trans</i> photoisomer was bound stronger by bovine serum albumin and induced a greater decrease in cellular glutathione levels than the <i>cis</i> photoisomer.…”
-
139
Light-Controlled Anticancer Activity and Cellular Uptake of a Photoswitchable Cisplatin Analogue
Published 2024“…The <i>trans</i> photoisomer was bound stronger by bovine serum albumin and induced a greater decrease in cellular glutathione levels than the <i>cis</i> photoisomer.…”
-
140
Light-Controlled Anticancer Activity and Cellular Uptake of a Photoswitchable Cisplatin Analogue
Published 2024“…The <i>trans</i> photoisomer was bound stronger by bovine serum albumin and induced a greater decrease in cellular glutathione levels than the <i>cis</i> photoisomer.…”