Ameliorative Effects of Fermented Red Ginseng Extract on Muscle Atrophy in Dexamethasone-Induced C2C12 Cell And Hind Limb-Immobilized C57BL/6J Mice.

Fermented red ginseng (FRG) enhances the bioactivity and bioavailability of ginsenosides, which possess various immunomodulatory, antiaging, anti-obesity, and antidiabetic properties. However, the effects of FRG extract on muscle atrophy and the underlying molecular mechanisms remain unclear. This study aimed to elucidate the effects of FRG extract on muscle atrophy using both and models.

Ginsenosides Rh1, Rg2, and Rg3 ameliorate dexamethasone-induced muscle atrophy in C2C12 myotubes.

High doses or prolonged use of the exogenous synthetic glucocorticoid dexamethasone (Dex) can lead to muscle atrophy. In this study, the anti-atrophic effects of ginsenosides Rh1, Rg2, and Rg3 on Dex-induced C2C12 myotube atrophy were assessed by XTT, myotube diameter, fusion index, and western blot analysis. The XTT assay results showed that treatment with Rh1, Rg2, and Rg3 enhanced cell viability in Dex-injured C2C12 myotubes.

Root Extract Alleviates Airway Inflammation in Mice with Ovalbumin-Induced Allergic Asthma.

Miq. ( family) is a traditional herb used for relieving cough and phlegm in East Asia. This study explored the effects of root extract (AsE) in ovalbumin (OVA)-induced allergic asthma and lipopolysaccharide (LPS)-stimulated macrophages.

Root Extract Protects Lung Injury from Exposure to Particulate Matter 2.5 in Mice.

Chronic exposure of particulate matter of less than 2.5 μm (PM) has been considered as one of the major etiologies for various respiratory diseases. Miq.

Immunomodulatory Effect of Polysaccharide from Fermented L. (Noni) on RAW 264.7 Macrophage and Balb/c Mice.

This study aims to determine the immunomodulatory effects of a polysaccharide fraction from fermented L. (FMP) in RAW 264.7 macrophages and Balb/c mice.

Ultra-sensitive detection of kanamycin for food safety using a reduced graphene oxide-based fluorescent aptasensor.

Overuse of antibiotics has caused serious problems, such as appearance of super bacteria, whose accumulation in the human body through the food chain is a concern. Kanamycin is a common antibiotic used to treat diverse infections; however, residual kanamycin can cause many side effects in humans. Thus, development of an ultra-sensitive, precise, and simple detection system for residual kanamycin in food products is urgently needed for food safety.

Mutational analysis of critical residues of FAD-independent catabolic acetolactate synthase from Enterococcus faecalis V583.

Catabolic acetolactate synthase (cALS) from Enterococcus faecalis is a FAD-independent enzyme, which catalyzes the condensation of two molecules of pyruvate to produce acetolactate. Mutational and kinetic analyses of variants suggested the importance of H111, Q112, and Q411 residues for catalysis in cALS. The wild-type and variants were expressed as equally soluble proteins and co-migrated to a size of 60 kDa on SDS-PAGE.

Characterization of recombinant FAD-independent catabolic acetolactate synthase from Enterococcus faecalis V583.

The catabolic acetolactate synthase (cALS) of Enterococcus faecalis V583 was cloned, expressed in Escherichia coli, and purified to homogeneity. The purified protein had a molecular weight of 60 kDa. The cALS of E.

Cloning, characterization and evaluation of potent inhibitors of Shigella sonnei acetohydroxyacid synthase catalytic subunit.

Acetohydroxyacid synthase (AHAS) is a thiamin diphosphate (ThDP)- and flavin adenine dinucleotide (FAD)-dependent plant and microbial enzyme that catalyzes the first common step in the biosynthesis of essential amino acids such as leucine, isoleucine and valine. To identify strong potent inhibitors against Shigella sonnei (S. sonnei) AHAS, we cloned and characterized the catalytic subunit of S.

Evaluation of substituted triazol-1-yl-pyrimidines as inhibitors of Bacillus anthracis acetohydroxyacid synthase.

Acetohydroxyacid synthase (AHAS), a potential target for antimicrobial agents, catalyzes the first common step in the biosynthesis of the branched-chain amino acids. The genes of both catalytic and regulatory subunits of AHAS from Bacillus anthracis (Bantx), a causative agent of anthrax, were cloned, overexpressed in Escherichia coli, and purified to homogeneity. To develop novel anti-anthracis drugs that inhibit AHAS, a chemical library was screened, and four chemicals, AVS2087, AVS2093, AVS2387, and AVS2236, were identified as potent inhibitors of catalytic subunit with IC(50) values of 1.