Search alternatives:
greatest decrease » treatment decreased (Expand Search), greater increase (Expand Search)
greater decrease » greater increase (Expand Search), greater increases (Expand Search), rate decreased (Expand Search)
linear decrease » linear increase (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a greatest » a greater (Expand Search)
greatest decrease » treatment decreased (Expand Search), greater increase (Expand Search)
greater decrease » greater increase (Expand Search), greater increases (Expand Search), rate decreased (Expand Search)
linear decrease » linear increase (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a greatest » a greater (Expand Search)
-
141
-
142
-
143
-
144
-
145
-
146
HFD induces LDs and decreases ER and mitochondria in nephrocytes.
Published 2021“…(<b>E</b>) Low and high magnification views of pericardial nephrocytes (dotted outlines) from STD and HFD larvae, showing that HFD decreases mitochondria (marked with anti-ATP5A) and ER (marked with anti-KDEL) but increases LDs (marked with LipidTOX). …”
-
147
In superadditive networks, more enhancers decrease noise and fidelity.
Published 2023“…<p>(A) Superadditivity is implemented in our model by linearly increasing <i>k</i><sub>on</sub> rates and linearly decreasing <i>k</i><sub>off</sub> rates. …”
-
148
-
149
-
150
-
151
-
152
-
153
-
154
-
155
-
156
-
157
-
158
-
159
-
160
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.…”