4-(4-(3-adamantan-1-ylureido)cyclohexyloxy)benzoic-acid and Inflammation

4-(4-(3-adamantan-1-ylureido)cyclohexyloxy)benzoic-acid has been researched along with Inflammation* in 3 studies

Other Studies

3 other study(ies) available for 4-(4-(3-adamantan-1-ylureido)cyclohexyloxy)benzoic-acid and Inflammation

ArticleYear
Ligand-based optimization to identify novel 2-aminobenzo[d]thiazole derivatives as potent sEH inhibitors with anti-inflammatory effects.
    European journal of medicinal chemistry, 2021, Feb-15, Volume: 212

    Inhibition of the soluble epoxide hydrolase (sEH) is a promising new therapeutic approach in the treatment of inflammation. Driven by the in-house database product lead 1, a hybridization strategy was utilized for the design of a series of novel benzo [d]thiazol derivatives. To our delight, D016, a byproduct of compound 9, was obtained with an extraordinarily low IC

    Topics: Animals; Anti-Inflammatory Agents, Non-Steroidal; Benzothiazoles; Carrageenan; Cell Survival; Dose-Response Relationship, Drug; Edema; Enzyme Inhibitors; Epoxide Hydrolases; Hep G2 Cells; Humans; Inflammation; Ligands; Male; Mice; Mice, Inbred BALB C; Microsomes, Liver; Molecular Docking Simulation; Molecular Structure; Rats; Rats, Sprague-Dawley; Structure-Activity Relationship

2021
Further exploration of the structure-activity relationship of dual soluble epoxide hydrolase/fatty acid amide hydrolase inhibitors.
    Bioorganic & medicinal chemistry, 2021, 12-01, Volume: 51

    Topics: Acute Pain; Amidohydrolases; Animals; Anti-Inflammatory Agents, Non-Steroidal; Dose-Response Relationship, Drug; Enzyme Inhibitors; Epoxide Hydrolases; Formaldehyde; Inflammation; Male; Molecular Docking Simulation; Molecular Structure; Rats; Rats, Sprague-Dawley; Structure-Activity Relationship; Thiazoles

2021
Microsphere-based flow cytometry protease assays for use in protease activity detection and high-throughput screening.
    Current protocols in cytometry, 2010, Volume: Chapter 13

    This protocol describes microsphere-based protease assays for use in flow cytometry and high-throughput screening. This platform measures a loss of fluorescence from the surface of a microsphere due to the cleavage of an attached fluorescent protease substrate by a suitable protease enzyme. The assay format can be adapted to any site or protein-specific protease of interest and results can be measured in both real time and as endpoint fluorescence assays on a flow cytometer. Endpoint assays are easily adapted to microplate format for flow cytometry high-throughput analysis and inhibitor screening.

    Topics: Animals; Biotinylation; Flow Cytometry; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; High-Throughput Screening Assays; Humans; Inflammation; Kinetics; Microspheres; Peptide Hydrolases; Peptides; Reproducibility of Results; Temperature

2010