432501-92-3Relevant academic research and scientific papers
The design and synthesis of novel phenothiazine derivatives as potential cytotoxic agents
Gao, Jianjun,Liu, Jinyi,Luan, Yepeng,Wang, Jinhua
, p. 57 - 67 (2020)
Background: Cancer incidence and mortality have been increasing and cancer is still the leading cause of death all over the world. Despite the enormous progress in cancer treatment, many patients died of ineffective chemotherapy and drug resistance. There
Novel CRAC channel conditioning agent, and preparation method and applications thereof
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Paragraph 0346; 0347; 0348; 0349; 0352, (2016/10/08)
The invention provides a novel CRAC (calcium release-activated calcium) channel conditioning agent, and a preparation method and applications thereof, and more specifically, the invention provides a compound represented by formula I, and the groups are defined in the patent specification. The invention also provides the preparation method of the compound represented by formula I, and applications of the compound as a CRAC channel conditioning agent.
Differential binding of phenothiazine urea derivatives to wild-type human cholinesterases and butyrylcholinesterase mutants
Darvesh, Sultan,Pottie, Ian R.,Darvesh, Katherine V.,McDonald, Robert S.,Walsh, Ryan,Conrad, Sarah,Penwell, Andrea,Mataija, Diane,Martin, Earl
experimental part, p. 2232 - 2244 (2010/05/18)
A series of N-10 urea derivatives of phenothiazine was synthesized and each compound was evaluated for its ability to inhibit human cholinesterases. Most were specific inhibitors of BuChE. However, the potent inhibitory effects on both cholinesterases of one sub-class, the cationic aminoureas, provide an additional binding mechanism to cholinesterases for these compounds. The comparative effects of aminoureas on wild-type BuChE and several BuChE mutants indicate a binding process involving salt linkage with the aspartate of the cholinesterase peripheral anionic site. The effect of such compounds on cholinesterase activity at high substrate concentration supports ionic interaction of aminoureas at the peripheral anionic site.
