33026-77-6Relevant articles and documents
Vinylogous Aza-Michael Addition of Urea Derivatives with p-Quinone Methides Followed by Oxidative Dearomative Cyclization: Approach to Spiroimidazolidinone Derivatives
Kaur, Navpreet,Singh, Priyanka,Banerjee, Prabal
supporting information, p. 2813 - 2824 (2021/04/21)
Herein, we report an efficient protocol for the synthesis of spiro-imidazolidinone-cyclohexadienones from p-quinone methides (p-QMs) and dialkyloxy ureas under mild conditions. The strategy follows a two-step process involving an initial vinylogous conjugate addition of urea derivatives to p-QMs, followed by oxidative dearomative cyclization of open-chain product to the projected spiro-imidazolidinones. This protocol exhibits good functional group tolerance and provides a straightforward method to access spiro-imidazolidinone-cyclohexadienones. In follow-up chemistry, we have shown the debenzylation of spiroimidazolidinones to give N-hydroxycyclic ureas. (Figure presented.).
Synthesis and SAR of 1-hydroxy-1 H -benzo[ d ]imidazol-2(3 H)-ones as inhibitors of d -amino acid oxidase
Berry, James F.,Rais, Rana,Slusher, Barbara S.,Tsukamoto, Takashi,Ferraris, Dana V.,Duvall, Bridget,Hin, Niyada,Alt, Jesse,Thomas, Ajit G.,Rojas, Camilo,Hashimoto, Kenji
supporting information, p. 839 - 843,5 (2020/09/15)
A series of 1-hydroxy-1H-benzo[d]imidazol-2(3H)-ones were synthesized and evaluated for their ability to inhibit human and porcine forms of d-amino acid oxidase (DAAO). The inhibitory potency is largely dependent on the size and position of substituents o
N-substituted hydroxyureas as urease inhibitors
Uesato, Shinichi,Hashimoto, Yuichiro,Nishino, Masaru,Nagaoka, Yasuo,Kuwajima, Hiroshi
, p. 1280 - 1282 (2007/10/03)
In order to seek a urease inhibitor more potent than hydroxyurea (1), its alkyl- or phenyl-substituted derivatives were synthesized and evaluated for their effect on the jack bean urease. Of 16 compounds tested, m-methyl-(10) and m-methoxy-phenyl substituted hydroxyurea (13) showed the most potent inhibitory activities against the enzyme.