99-56-9Relevant articles and documents
ACTIVATORS OF THE RETINOIC ACID INDUCIBLE GENE "RIG-I' PATHWAY AND METHODS OF USE THEREOF
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Page/Page column 55, (2020/03/05)
The present invention is directed to compounds of Formula (I), which are activators of the RIG-I pathway.
Excellent photocatalytic reduction of nitroarenes to aminoarenes by BiVO4 nanoparticles grafted on reduced graphene oxide (rGO/BiVO4)
Azad, Roya,Bezaatpour, Abolfazl,Amiri, Mandana,Eskandari, Habibollah,Nouhi, Sima,Taffa, Dereje H.,Wark, Michael,Boukherroub, Rabah,Szunerits, Sabine
, (2019/07/03)
A novel heterogeneous composite material based on reduced graphene oxide (rGO) and bismuth vanadate (BiVO4) was prepared and characterized by various techniques such as powder XRD, HRTEM, EADX, UV–Vis-DRS, FT-IR, Raman, BET and XPS analyses. The characterization results reveal that the rGO well decorated by BiVO4. The electrochemical impedance spectroscopy (EIS) shows the increasing of charge transfer of rGO/BiVO4 in presence of light irradiation. In this research, the pure BiVO4 and rGO/BiVO4 composite have been explored for photocatalytic reduction of nitroarenes. Among the prepared nanocomposites, rGO loaded with 10% BiVO4 catalyst (noted as rGO/BiVO4–10%) shows the best performance for the photo-reduction of various nitroaromatic molecules to their corresponding amine compounds under visible-light irradiation at room temperature. The catalyst exhibited in particular excellent photocatalytic activity for the conversion of 1,4-dinitrobenzene to 4-nitroanilline (100% conversion) in 20?min, 4-chloronitrobenzene to 4-chloroaniline and 2-nitrophenol to 2-aminophenol (100% conversion) in only 30?min. In addition, the conversion of 4-bromonitrobenzene, 4-iodonitrobenzene to their corresponding amine compounds (100% conversion) was achieved in 60?min. The catalyst was recovered for several times and reused without decreasing of its efficiency.
Novel cathepsin K inhibitors block osteoclasts in vitro and increase spinal bone density in zebrafish
Xue, Si-Tu,Wang, Ya-Li,Han, Xiao-Wan,Yi, Hong,Jiang, Wei,Si, Shu-Yi,Guo, Hui-Fang,Li, Zhuo-Rong
, p. 8600 - 8607 (2019/03/21)
Cathepsin K (Cat K) is a predominant cysteine protease and highly potent collagenase expressed in osteoclasts. Cat K inhibitors are anti-resorptive agents to treat osteoporosis. A novel scaffold of cathepsin K inhibitors, exemplified by lead compound 1x, was used as the template for designing and synthesizing a total of 61 derivatives that have not been reported before. An exploratory structure-activity relationship analysis identified the potent Cat K inhibitor A22, which displayed an IC50 value of 0.44 μM against Cat K. A22 was very specific for Cat K and caused a significantly higher in vitro inhibition of the enzyme as compared to that of lead compound 1x. A surface plasmon resonance analysis confirmed in vitro binding of A22 to Cat K. Molecular docking studies indicated several favourable interaction sites for A22 within the active pocket of Cat K. Furthermore, A22 also blocked active osteoclasts in vitro and increased spinal bone density in zebrafish, in which it showed an activity that was higher than that of the marketed therapeutic bone metabolizer etidronate disodium. A22 represents a very promising lead compound for the development of novel antiresorptive agents functioning as orthosteric inhibitors of Cat K.