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point decrease » point increase (Expand Search)
fold decrease » fold increase (Expand Search), fold increased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
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DataSheet_1_Decrease in Serum Urate Level Is Associated With Loss of Visceral Fat in Male Gout Patients.docx
Published 2021“…</p>Results<p>ULT resulted in a mean (standard deviation) decrease in SU level (464.22 ± 110.21 μmol/L at baseline, 360.93 ± 91.66 μmol/L at the final visit, p <0.001) accompanied by a decrease in median (interquartile range) VFA [97.30 (81.15–118.55) at baseline, 90.90 (75.85–110.05) at the final visit, p < 0.001]. …”
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The primers related to FAM50A.
Published 2025“…Knockdown of FAM50A decreased cell proliferation ability, the proportion of EdU positive cells, and the number of CRC cell colonies, whereas overexpressing FAM50A promoted proliferative phenotypes. …”
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Decreased methylglyoxal-mediated protein glycation in the healthy aging mouse model of ectopic expression of UCP1 in skeletal muscle
Published 2023“…We found both young and aged HSA-mUCP1 mice had decreased advanced glycation endproducts (AGEs) formed from MG, lysine-derived Nε(1-carboxyethyl)lysine (CEL) and arginine-derived hydroimidazolone, MG-H1, whereas protein glycation by glucose forming Nε-fructosyl-lysine (FL) was increased ca. 2-fold, compared to wildtype controls. …”
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Changes in the number of muscle fibers per unit area in pectoral muscle tissue of <i>Wenchang chicken</i> embryos from embryonic day 7 to embryonic day 15.
Published 2024“…<p>There is a trend of increasing fiber quantity followed by a decrease, with the inflection point occurring at E12.…”
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Decreased methylglyoxal-mediated protein glycation in the healthy aging mouse model of ectopic expression of UCP1 in skeletal muscle
Published 2023“…We found both young and aged HSA-mUCP1 mice had decreased advanced glycation endproducts (AGEs) formed from MG, lysine-derived Nε(1-carboxyethyl)lysine (CEL) and arginine-derived hydroimidazolone, MG-H1, whereas protein glycation by glucose forming Nε-fructosyl-lysine (FL) was increased ca. 2-fold, compared to wildtype controls. …”
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