123403-76-9Relevant academic research and scientific papers
Histone deacetylase activators: N-acetylthioureas serve as highly potent and isozyme selective activators for human histone deacetylase-8 on a fluorescent substrate
Singh, Raushan K.,Mandal, Tanmay,Balsubramanian, Narayanaganesh,Viaene, Tajae,Leedahl, Travis,Sule, Nitesh,Cook, Gregory,Srivastava
, p. 5920 - 5923 (2011/10/18)
We report, for the first time, that certain N-acetylthiourea derivatives serve as highly potent and isozyme selective activators for the recombinant form of human histone deacetylase-8 in the assay system containing Fluor-de-Lys as a fluorescent substrate. The experimental data reveals that such activating feature is manifested via decrease in the Km value of the enzyme's substrate and increase in the catalytic turnover rate of the enzyme.
Synthesis and activity of quinolinyl-methylene-thiazolinones as potent and selective cyclin-dependent kinase 1 inhibitors
Chen, Shaoqing,Chen, Li,Le, Nam T.,Zhao, Chunlin,Sidduri, Achyutharao,Lou, Jian Ping,Michoud, Christophe,Portland, Louis,Jackson, Nicole,Liu, Jin-Jun,Konzelmann, Fred,Chi, Feng,Tovar, Christian,Xiang, Qing,Chen, Yingsi,Wen, Yang,Vassilev, Lyubomir T.
, p. 2134 - 2138 (2008/02/03)
A novel series of quinolinyl-methylene-thiazolinones has been identified as potent and selective cyclin-dependent kinase 1 (CDK1) inhibitors. Their synthesis and structure activity relationships (SAR) are described. Representative compounds from this class reversibly inhibit CDK1 activity in vitro, and block cell cycle progression in human tumor cell lines, suggesting a potential use as antitumor agents.
