1532540-17-2Relevant academic research and scientific papers
Modulating the interaction between CDK2 and cyclin A with a quinoline-based inhibitor
Deng, Yongqi,Shipps Jr., Gerald W.,Zhao, Lianyun,Siddiqui, M. Arshad,Popovici-Muller, Janeta,Curran, Patrick J.,Duca, Jose S.,Hruza, Alan W.,Fischmann, Thierry O.,Madison, Vincent S.,Zhang, Rumin,McNemar, Charles W.,Mayhood, Todd W.,Syto, Rosalinda,Annis, Allen,Kirschmeier, Paul,Lees, Emma M.,Parry, David A.,Windsor, William T.
, p. 199 - 203 (2014)
A new class of quinoline-based kinase inhibitors has been discovered that both disrupt cyclin dependent 2 (CDK2) interaction with its cyclin A subunit and act as ATP competitive inhibitors. The key strategy for discovering this class of protein-protein disrupter compounds was to screen the monomer CDK2 in an affinity-selection/mass spectrometry-based technique and to perform secondary assays that identified compounds that bound only to the inactive CDK2 monomer and not the active CDK2/cyclin A heterodimer. Through a series of chemical modifications the affinity (Kd) of the original hit improved from 1 to 0.005 μM.
