3080-99-7Relevant articles and documents
REACTION BETWEEN N-ACYL-2,3-DIHYDROBENZO-1,4-THIAZINE AND N-ACYLPHENOTIAZINE WITH ORGANOMETALLIC REAGENTS
Ciminale, Francesco,Dunno, Leonardo Di,Florio, Saverio
, p. 3001 - 3002 (1980)
The title N-acyl-derivatives react with n-BuLi and Grignard reagents leading to products, which, formally, can be considered as derived from a Claisen-type condensation reaction.
Sodium Triethylborohydride-Catalyzed Controlled Reduction of Unactivated Amides to Secondary or Tertiary Amines
Yao, Wubing,He, Lili,Han, Deman,Zhong, Aiguo
, (2019/11/14)
The first transition-metal-free catalytic protocol for controlled reduction of amide functions using cheap and bench-stable hydrosilanes as reducing agents has been established. By altering the hydrosilane and solvent, the new method enables the selective cleavage of unactivated C-O bonds in amides and allows the C-N bonds to selectively break via the deacylated cleavage. Overall, this novel process may offer a versatile alternative to current methodologies employing stoichiometric metal systems for the controlled reduction of carboxamides.
Design, Synthesis, Safener Activity, and Molecular Docking of Novel N-Substituted Thiazide/Thiazole Derivatives
Fu, Ying,Yi, Ke-Han,Li, Ming-Qiang,Wang, Jing-Yi,Chen, Yu-Feng,Ye, Fei
, p. 180 - 187 (2018/11/25)
A series of novel substituted thiazide/thiazole compounds were designed by splicing active groups and bioisosterism. The title compounds were synthesized via the cyclization, acylation, and carbamylation. All the compounds were characterized by IR, 1H-NMR, 13C-NMR, and HRMS. The single crystal of compound 3f was determined by X-ray crystallography. The biological activity tests indicated that all the compounds showed potential safener activity to the herbicide chlorsulfuron, in which compound 3e showed almost the same level as the commercialized safener AD-67. The molecular docking results were in good agreement with the bioassay results, which demonstrated that compound 3e might compete with chlorsulfuron in the acetolactate synthase active site, causing the herbicide ineffective in maize.