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increases » increased (Expand Search), increase (Expand Search)
larger decrease » marked decrease (Expand Search)
site decrease » sizes decrease (Expand Search), step decrease (Expand Search), rate decreased (Expand Search)
i larger » _ larger (Expand Search), i large (Expand Search), _ large (Expand Search)
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Decreased expression of circ_0020397 in intracranial aneurysms may be contributing to decreased vascular smooth muscle cell proliferation via increased expression of miR-138 and subsequent decreased KDR expression
Published 2019“…In conclusion, our findings demonstrated that decreased expression of circRNA_0020397 in IA may contribute to the decreased VSMC proliferation via increasing miR-138 expression and subsequently decreasing KDR expression.…”
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Knockdown of <i>Pepck</i> delayed pupation and decreased hemolymph glucose levels.
Published 2022“…</b> ChIP assay showing 20E promoted <i>Pepck</i> expression via KLF15 binding to KLF bs. <b>C.</b> Phenotypes after injection of <i>dsPepck</i> and <i>dsGFP</i> from 6th-6 h to 72 h; the ruler represents 1 cm. …”
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The introduction of mutualisms into assembled communities increases their connectance and complexity while decreasing their richness.
Published 2025“…(B) Even though higher proportions of mutualism promote higher richness, introducing this type of interaction into already assembled large communities promotes a sudden drop in richness, while stopping mutualism promotes a slight boost in richness increase. …”
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Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
Published 2021“…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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Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
Published 2021“…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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