206190-28-5Relevant articles and documents
Visible-Light Photosynthesis of CHF2/CClF2/CBrF2-Substituted Ring-fused Quinazolinones in Dimethyl Carbonate
Gui, Qing-Wen,He, Wei-Min,Huang, Wen-Jie,Lu, Zi-Qin,Ouyang, Wen-Tao,Teng, Fan,Xun, Changping,Yang, Hao,Zhu, Meng-Xue
, (2021/12/01)
With eco-friendly and sustainable CO2-derived dimethyl carbonate as the sole solvent, the visible-light-induced cascade radical reactions have been established as a green and efficient tool for constructing various CHF2/CClF2/CBrF2-substituted ring-fused quinazolinones.
Visible-light induced copper(i)-catalyzed oxidative cyclization of: O -aminobenzamides with methanol and ethanol via HAT
Bhargava Reddy, Mandapati,Prasanth, Kesavan,Anandhan, Ramasamy
, p. 9601 - 9605 (2020/12/28)
The use of the in situ generated ligand-copper superoxo complex absorbing light energy to activate the alpha C(sp3)-H of MeOH and EtOH via the hydrogen atom transfer (HAT) process for the synthesis of quinazolinones by oxidative cyclization of alcohols with o-aminobenzamide has been investigated. The synthetic utility of this protocol offers an efficient synthesis of a quinazolinone intermediate for erlotinb (anti-cancer agent) and 30 examples were reported.
Structure-metabolism relationships in human-AOX: Chemical insights from a large database of aza-aromatic and amide compounds
Lepri, Susan,Ceccarelli, Martina,Milani, Nicolò,Tortorella, Sara,Cucco, Andrea,Valeri, Aurora,Goracci, Laura,Brink, Andreas,Cruciani, Gabriele
, p. E3178 - E3187 (2017/04/24)
Aldehyde oxidase (AOX) is a metabolic enzyme catalyzing the oxidation of aldehyde and aza-aromatic compounds and the hydrolysis of amides, moieties frequently shared by the majority of drugs. Despite its key role in human metabolism, to date only fragmentary information about the chemical features responsible for AOX susceptibility are reported and only "very local" structure-metabolism relationships based on a small number of similar compounds have been developed. This study reports a more comprehensive coverage of the chemical space of structures with a high risk of AOX phase I metabolism in humans. More than 270 compounds were studied to identify the site of metabolism and themetabolite(s). Both electronic [supported by density functional theory (DFT) calculations] and exposure effects were considered when rationalizing the structure-metabolism relationship.
Selective inhibitors of bacterial t-RNA-(N1G37) methyltransferase (TrmD) that demonstrate novel ordering of the lid domain
Hill, Pamela J.,Abibi, Ayome,Albert, Robert,Andrews, Beth,Gagnon, Moriah M.,Gao, Ning,Grebe, Tyler,Hajec, Laurel I.,Huang, Jian,Livchak, Stephania,Lahiri, Sushmita D.,McKinney, David C.,Thresher, Jason,Wang, Hongming,Olivier, Nelson,Buurman, Ed T.
supporting information, p. 7278 - 7288 (2013/10/21)
The tRNA-(N1G37) methyltransferase (TrmD) is essential for growth and highly conserved in both Gram-positive and Gram-negative bacterial pathogens. Additionally, TrmD is very distinct from its human orthologue TRM5 and thus is a suitable target for the design of novel antibacterials. Screening of a collection of compound fragments using Haemophilus influenzae TrmD identified inhibitory, fused thieno-pyrimidones that were competitive with S-adenosylmethionine (SAM), the physiological methyl donor substrate. Guided by X-ray cocrystal structures, fragment 1 was elaborated into a nanomolar inhibitor of a broad range of Gram-negative TrmD isozymes. These compounds demonstrated no activity against representative human SAM utilizing enzymes, PRMT1 and SET7/9. This is the first report of selective, nanomolar inhibitors of TrmD with demonstrated ability to order the TrmD lid in the absence of tRNA.
4-aminoquinazolone derivatives
-
, (2008/06/13)
This invention relates to certain 4-aminoquinazoline derivatives of the formula and their pharmaceutically acceptable salts wherein R1, Q1, m, n, and Z are defined as in the specification. The compounds of formula I and pharmaceutically acceptable salts are useful for the treatment of hyperproliferative disorders and conditions in mammals.