بدائل البحث:
2022 decrease » 026 decrease (توسيع البحث)
mg decrease » nn decrease (توسيع البحث), we decrease (توسيع البحث), mean decrease (توسيع البحث)
a decrease » _ decreased (توسيع البحث), _ decreases (توسيع البحث)
_ decrease » _ decreased (توسيع البحث)
2020 2022 » 2020 2021 (توسيع البحث), 2021 2022 (توسيع البحث), 2010 2020 (توسيع البحث)
12 mg » 10 mg (توسيع البحث), 2 mg (توسيع البحث), 15 mg (توسيع البحث)
2022 decrease » 026 decrease (توسيع البحث)
mg decrease » nn decrease (توسيع البحث), we decrease (توسيع البحث), mean decrease (توسيع البحث)
a decrease » _ decreased (توسيع البحث), _ decreases (توسيع البحث)
_ decrease » _ decreased (توسيع البحث)
2020 2022 » 2020 2021 (توسيع البحث), 2021 2022 (توسيع البحث), 2010 2020 (توسيع البحث)
12 mg » 10 mg (توسيع البحث), 2 mg (توسيع البحث), 15 mg (توسيع البحث)
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Overview of predicted and observed number of hunters in the 2020/2021 and 2021/2022 hunting season.
منشور في 2024الموضوعات: -
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Decreased methylglyoxal-mediated protein glycation in the healthy aging mouse model of ectopic expression of UCP1 in skeletal muscle
منشور في 2023"…We investigated protein glycation and oxidative damage in skeletal muscle of mice with UCP1 expression under control of the human skeletal actin promoter (HSA-mUCP1) at age 12 weeks (young) and 70 weeks (aged). 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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Decreased methylglyoxal-mediated protein glycation in the healthy aging mouse model of ectopic expression of UCP1 in skeletal muscle
منشور في 2023"…We investigated protein glycation and oxidative damage in skeletal muscle of mice with UCP1 expression under control of the human skeletal actin promoter (HSA-mUCP1) at age 12 weeks (young) and 70 weeks (aged). 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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