58483-94-6Relevant articles and documents
Method for preparing aldehyde and acid by electrochemical dehydrochlorination of polychloromethylpyridine derivatives
-
Paragraph 0035-0037; 0057-0060, (2020/08/27)
The invention discloses a method for preparing aldehyde and an acid by electrochemical dechlorination of a polychloromethylpyridine derivative, the method comprises the following steps: dissolving thepolychloromethylpyridine derivative in an acetic acid and acetate- containing buffer solution to obtain an electrolytic reaction solution; taking the electrolytic reaction solution as a cathode liquid, performing electrolytic reduction dechlorination reaction at a cathode, and hydrolyzing in the solution to obtain a polychlorinated pyridylaldehyde or acid derivative. The polychloromethylpyridinederivative is shown in formula (I), and the product polychlorinated pyridylaldehyde or acid derivative is shown in formula (II): in the formula (I), m is 0, 1, 2, 3 or 4, n is 0 or 1, and R' is an easy-to-oxidize or easy-to-hydrolyze substituent. The m and the R' in the formula (II) are same as that in the formula (I), R is H or OH, no waste acid is generated in the preparation process, the easy-to-oxidize or easy-to-hydrolyze substituent contained in the polychloromethylpyridine derivative and carbon-chlorine bonds on pyridine rings are not affected, and the recovery conversion rate is high.
BICYCLIC ETHER O-GLYCOPROTEIN-2-ACETAMIDO-2-DEOXY-3-D-GLUCOPYRANOSIDASE INHIBITORS
-
Paragraph 00246, (2020/08/22)
Described herein are compounds represented by formula (I) or a pharmaceutically acceptable salt thereof, pharmaceutical compositions comprising the same and methods of preparing and using the same. The variables Ar, X, R1, R3, R 4, Y1, Y2, n and p are as defined herein.
Design, Synthesis and Characterization of Covalent KDM5 Inhibitors
Vazquez-Rodriguez, Saleta,Wright, Miranda,Rogers, Catherine M.,Cribbs, Adam P.,Velupillai, Srikannathasan,Philpott, Martin,Lee, Henry,Dunford, James E.,Huber, Kilian V. M.,Robers, Matthew B.,Vasta, James D.,Thezenas, Marie-Laetitia,Bonham, Sarah,Kessler, Benedikt,Bennett, James,Fedorov, Oleg,Raynaud, Florence,Donovan, Adam,Blagg, Julian,Bavetsias, Vassilios,Oppermann, Udo,Bountra, Chas,Kawamura, Akane,Brennan, Paul E.
supporting information, p. 515 - 519 (2018/12/14)
Histone lysine demethylases (KDMs) are involved in the dynamic regulation of gene expression and they play a critical role in several biological processes. Achieving selectivity over the different KDMs has been a major challenge for KDM inhibitor development. Here we report potent and selective KDM5 covalent inhibitors designed to target cysteine residues only present in the KDM5 sub-family. The covalent binding to the targeted proteins was confirmed by MS and time-dependent inhibition. Additional competition assays show that compounds were non 2-OG competitive. Target engagement and ChIP-seq analysis showed that the compounds inhibited the KDM5 members in cells at nano- to micromolar levels and induce a global increase of the H3K4me3 mark at transcriptional start sites.