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greater decrease » greater increase (Expand Search), greater increases (Expand Search), rate decreased (Expand Search)
linear decrease » linear increase (Expand Search)
large decrease » marked decrease (Expand Search), large increases (Expand Search), large degree (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
i large » _ large (Expand Search), a large (Expand Search), i larvae (Expand Search)
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681
Overview of study procedures.
Published 2025“…VIDEO and CONTROL were associated with a similar rise in intent to decrease OTC NSAID use (1.92 (SD: 4.41) vs. 1.36 (SD: 3.46), p = 0.150) and a similar decrease in NSAIDs exposure (−32.8% in VIDEO and −36.5% in CONTROL, p = 0.520) 4 weeks post-intervention. …”
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682
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683
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684
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685
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686
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687
Volitional control frequency and intensity in VH (Kapsner-Smith et al., 2025)
Published 2025“…Specifically, unusually large responses to perturbations of vocal auditory feedback cannot be explained by a broader impairment of the ability to make small changes in the vocal parameters <i>F</i>0 or intensity. …”
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688
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689
H‑NOX Influences Biofilm Formation, Central Metabolism, and Quorum Sensing in <i>Paracoccus denitrificans</i>
Published 2024“…In many species, the heme nitric oxide/oxygen binding proteins (H-NOX) play an important role in this process, although the signaling mechanisms and pathways in which they participate are quite diverse and largely unknown. In <i>Paracoccus denitrificans</i>, deletion of the <i>hnox</i> gene results in a severe biofilm-deficient phenotype. …”
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690
H‑NOX Influences Biofilm Formation, Central Metabolism, and Quorum Sensing in <i>Paracoccus denitrificans</i>
Published 2024“…In many species, the heme nitric oxide/oxygen binding proteins (H-NOX) play an important role in this process, although the signaling mechanisms and pathways in which they participate are quite diverse and largely unknown. In <i>Paracoccus denitrificans</i>, deletion of the <i>hnox</i> gene results in a severe biofilm-deficient phenotype. …”
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691
H‑NOX Influences Biofilm Formation, Central Metabolism, and Quorum Sensing in <i>Paracoccus denitrificans</i>
Published 2024“…In many species, the heme nitric oxide/oxygen binding proteins (H-NOX) play an important role in this process, although the signaling mechanisms and pathways in which they participate are quite diverse and largely unknown. In <i>Paracoccus denitrificans</i>, deletion of the <i>hnox</i> gene results in a severe biofilm-deficient phenotype. …”
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692
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693
Decreased frequency of sEPSCs in <i>Dyt1</i> heterozygous KO mice.
Published 2015“…<p>(A) Representative traces for sEPSCs. <i>Dyt1</i> heterozygous KO mice had a significantly decreased frequency of sEPSCs (B), but no change in either the amplitude (C), or rise (D) and decay (E) times of these events. …”
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694
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695
Comparison of Final Palaeolithic Core Areas (based on data A) from GI-1d-a to GS-1.
Published 2025Subjects: -
696
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697
Expression of IR21a, IR93a, and IR25a proteins decreases in DOCCs at the late third instar.
Published 2021“…Right: <i>Ir21a>GFP-</i>labeled DOCCs express IR21a (Fig 4A), IR93a (Fig 4C) and IR25a (Fig 4E) proteins at 72 hr AEL (top), which are significantly decreased at 120 hr AEL (bottom). …”
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698
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.…”
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699
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.…”
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700
GluN2A(D731N) decreases current amplitudes and shortens synaptic-like response time course.
Published 2017Subjects: