Results 71 to 80 of about 996,868 (382)

Targeting EZH2 reverses thyroid cell dedifferentiation and enhances iodide uptake in anaplastic thyroid cancer

open access: yesFEBS Letters, EarlyView.
Anaplastic thyroid cancer (ATC) lacks iodide uptake ability due to MAPK activation increasing the expression of the histone methyltransferase EZH2, which represses thyroid differentiation genes (TDGs) such as the sodium iodide symporter (NIS). Dual inhibition of MAPK (U0126) and EZH2 (EPZ6438/Tazemetostat) reverses this mechanism, thus restoring TDG ...
Diego Claro de Mello   +6 more
wiley   +1 more source

Co-Amorphous Andrographolide–Lysine with Unexpectedly Enhanced Solubility

open access: yesCrystals
Andrographolide (ADG) is a typical poorly water-soluble drug, and a co-amorphous strategy was used here to improve its aqueous solubility. Co-amorphous systems of ADG and amino acids with a 1:1 molar ratio were screened via the neat ball milling method ...
Haifeng Luo   +6 more
doaj   +1 more source

Variation in Protein Content and Amino Acids in the Leaves of Grain, Vegetable and Weedy Types of Amaranths

open access: yesAgronomy, 2013
Malnutrition has affected almost 31% of pre-school children. This paper provides the information of nutritional values (leaf protein, 15 amino acids, biomass and leaf dry matter) of grain, vegetable and weedy types of amaranths (n = 76 accessions ...
Ryo Ohsawa, Shigeki Yoshida, Rita Andini
doaj   +1 more source

Diets for Dairy Cows with Different Proportions of Crude Protein Originating from Red Clover Silage versus Soybean Meal: Ruminal Degradation and Intestinal Digestibility of Amino Acids

open access: yesAnimals, 2021
The purpose was to assess the effect of exchanging crude protein (CP) of soybean meal (SBM) with red clover silage (RCS) in total mixed rations (TMR) on ruminal degradation and intestinal digestibility (ID) of essential amino acids (EAA).
Edwin Westreicher-Kristen   +6 more
doaj   +1 more source

Regulation of Cellular Metabolism by Protein Lysine Acetylation

open access: yesScience, 2010
Metabolic Regulation Through Acetylation Covalent modification of lysine residues in various proteins in the nucleus is a recognized mechanism for control of transcription.
Shimin Zhao   +21 more
semanticscholar   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

Jugular-infused methionine, lysine and branched-chain amino acids does not improve milk production in Holstein cows experiencing heat stress

open access: yesAnimal, 2017
Poor utilization of amino acids contributes to losses of milk protein yield in dairy cows exposed to heat stress (HS). Our objective was to test the effect of essential amino acids on milk production in lactating dairy cows exposed to short-term HS ...
K.R. Kassube   +4 more
doaj   +1 more source

Arginine and Lysine Promote Skeletal Muscle Hypertrophy by Regulating the mTOR Signaling Pathway in Bovine Myocytes

open access: yesMeat and Muscle Biology, 2023
The objective of this study was to assess the effects of additional arginine (ARG) and lysine (LYS) on the regulatory factors associated with myogenic differentiation of bovine satellite cells and hypertrophy of myotubes.
Jongkyoo Kim, Won Seob Kim
doaj   +2 more sources

Lysine/RNA-interactions drive and regulate biomolecular condensation

open access: yesNature Communications, 2019
Cells form and use biomolecular condensates to execute biochemical reactions. The molecular properties of non-membrane-bound condensates are directly connected to the amino acid content of disordered protein regions.
T. Ukmar-Godec   +9 more
semanticscholar   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

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