Tracking error comparison of obstacle avoidance trajectories in scenarios with obstacles moving at a constant linear speed. by Long Di (9977453)

HFD induces LDs and decreases ER and mitochondria in nephrocytes. by Aleksandra Lubojemska (10746241)

“…(<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). …”

Pulsed-pedestal task video demonstrates a trial in the pulsed-pedestal paradigm. by Xiaohua Zhuang (11890694)

Steady-pedestal task video demonstrates a trial in the steady-pedestal paradigm. by Xiaohua Zhuang (11890694)

In superadditive networks, more enhancers decrease noise and fidelity. by Alvaro Fletcher (15675430)

“…<p>(A) Superadditivity is implemented in our model by linearly increasing <i>k</i>_on rates and linearly decreasing <i>k</i>_off rates. …”

A taxonomy of marine ecosystem models taking part in the Fish-MIP project (modified from (Heneghan et al., 2021; Lotze et al., 2019; Tittensor et al., 2021)). by Vianney Guibourd de Luzinais (16871842)

Effect of noradrenaline (NA) alone (A) and NA with α1A- (B), α1B- (C), α1D- (D) and α1A,B,D (E)–adrenoreceptors (ARs) antagonists (a dose of 10⁻⁴ M) on the tension of co... by Barbara Jana (9110179)

Effect of noradrenaline (NA) alone (A) and NA with α1A- (B), α1B- (C), α1D- (D) and α1A,B,D (E)–adrenoreceptors (ARs) antagonists (a dose of 10⁻⁴ M) on the tension of co... by Barbara Jana (9110179)

Effect of noradrenaline (NA) alone (A) and NA with α1A- (B), α1B- (C), α1D- (D) and α1A,B,D (E)–adrenoreceptors (ARs) antagonists (a dose of 10⁻⁴ M) on the amplitude of... by Barbara Jana (9110179)

Effect of noradrenaline (NA) alone (A) and NA with α1A- (B), α1B- (C), α1D- (D) and α1A,B,D (E)–adrenoreceptors (ARs) antagonists (a dose of 10⁻⁴ M) on the amplitude of... by Barbara Jana (9110179)

Effect of noradrenaline (NA) alone (A) and NA with α1A- (B), α1B- (C), α1D- (D) and α1A,B,D (E)–adrenoreceptors (ARs) antagonists (a dose of 10⁻⁴ M) on the frequency of... by Barbara Jana (9110179)

Pendulum trajectories of Exp. 2 with decreased target radius (↓ <i>r</i>_<i>t</i>). by Annika Schmidt (2502097)

MPA induced cell proliferation in CAFs of obese women by decreasing the expression of stromal differentiation genes. by Intan Sofia Omar (10451088)

Ethnic identity as a moderator among APIDA students. by Ronna Bañada (19233063)

Prediction of linear and discontinuous epitopes in SmTPI and TsTPIs. by Pedro Jimenez-Sandoval (831603)

Stimulus (black) and participant response (red) for two participants (p101, an average participant, and p126, a high performer) for the condition DENSE–FAST. by Björn Jörges (9258411)

Pharmacological inhibition of EGFR decreases reduces a subset of the inflammatory response at day 2 post-infection. by Marc Swidergall (185453)

Ultrasound imaging shows decreased density in treatment tumors. by Anthony B. Eason (6294305)

Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket by Lilia Leisle (11356934)

“…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.…”

Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket by Lilia Leisle (11356934)

“…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.…”