1023142-92-8Relevant academic research and scientific papers
Structure-activity relationship study of BACE1 inhibitors possessing a chelidonic or 2,6-pyridinedicarboxylic scaffold at the P2 position
Hamada, Yoshio,Suzuki, Kenji,Nakanishi, Tomoya,Sarma, Diganta,Ohta, Hiroko,Yamaguchi, Ryoji,Yamasaki, Moe,Hidaka, Koushi,Ishiura, Shoichi,Kiso, Yoshiaki
, p. 618 - 623 (2014/01/23)
We have previously reported potent substrate-based pentapeptidic BACE1 inhibitors possessing a hydroxymethylcarbonyl isostere as a substrate transition-state mimic. While these inhibitors exhibited potent activities in enzymatic and cellular assays (KMI-4
Novel BACE1 inhibitors possessing a 5-nitroisophthalic scaffold at the P2 position
Hamada, Yoshio,Nakanishi, Tomoya,Suzuki, Kenji,Yamaguchi, Ryoji,Hamada, Takashi,Hidaka, Koushi,Ishiura, Shoichi,Kiso, Yoshiaki
, p. 4640 - 4644 (2012/08/13)
Recently, we reported substrate-based pentapeptidic BACE1 inhibitors possessing a hydroxymethylcarbonyl isostere as a substrate transition-state mimic. These inhibitors showed potent inhibitory activities in enzymatic and cell assays. We also designed and
