681810-03-7Relevant articles and documents
Analysis of structure-activity relationships for the 'B-region' of N-(4-t-butylbenzyl)-N′-[4-(methylsulfonylamino)benzyl]-thiourea analogues as TRPV1 antagonists
Lee, Jeewoo,Jin, Mi-Kyoung,Kang, Sang-Uk,Su, Yeon Kim,Lee, Jiyoun,Shin, Myoungyoup,Hwang, Jaemin,Cho, Sookhyun,Choi, Yeon-Sil,Choi, Hyun-Kyung,Kim, Sung-Eun,Suh, Young-Ger,Lee, Yong-Sil,Kim, Young-Ho,Ha, Hee-Jin,Toth, Attila,Pearce, Larry V.,Tran, Richard,Szabo, Tamas,Welter, Jacqueline D.,Lundberg, Daniel J.,Wang, Yun,Lazar, Jozsef,Pavlyukovets, Vladimir A.,Morgan, Matthew A.,Blumberg, Peter M.
, p. 4143 - 4150 (2007/10/03)
The structure-activity relationships for the 'B-region' of N-(4-t-butylbenzyl)-N′-[4-(methylsulfonylamino)benzyl]thiourea analogues have been investigated as TRPV1 receptor antagonists. A docking model of potent antagonist 2 with the sensor region of TRPV1 is proposed.
Synthesis and tyrosinase inhibitory activity of novel N-hydroxybenzyl-N-nitrosohydroxylamines
Shiino, Mitsuhiro,Watanabe, Yumi,Umezawa, Kazuo
, p. 129 - 135 (2007/10/03)
Several novel N-substituted N-nitrosohydroxylamines were synthesized. They all inhibited mushroom tyrosinase, but the type of inhibition was different depending on the substituent. Some N-(mono- or dihydroxybenzyl)-N-nitrosohydroxylamines exhibited uncompetitive inhibition with respect to L-dopa. Among them, compound 6 was also a competitive inhibitor with respect to oxygen. This observation suggests that another interaction by the meta- or para-hydroxyl group might stabilize the binding of the inhibitor to the enzyme through the oxygen binding site.
