234452-60-9Relevant academic research and scientific papers
Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
Chen, Huixiong,Roques, Bernard P.,Fournie-Zaluski, Marie-Claude
, p. 1511 - 1516 (2007/10/03)
A series of phosphinic compounds mimicking the transition state of substrates hydrolysed by aminopeptidase N (EC 3.4.11.2) were synthesized. These new compounds have potent inhibitory activities with Ki values in the nanomolar range. These derivatives behave as the most potent APN inhibitors designed to date.
