5957-96-0Relevant articles and documents
Nickel-Catalyzed Amination of Aryl Chlorides with Amides
Li, Jinpeng,Huang, Changyu,Wen, Daheng,Zheng, Qingshu,Tu, Bo,Tu, Tao
supporting information, p. 687 - 691 (2021/01/09)
A nickel-catalyzed amination of aryl chlorides with diverse amides via C-N bond cleavage has been realized under mild conditions. A broad substrate scope with excellent functional group tolerance at a low catalyst loading makes the protocol powerful for synthesizing various aromatic amines. The aryl chlorides could selectively couple to the amino fragments rather than the carbonyl moieties of amides. Our protocol complements the conventional amination of aryl chlorides and expands the usage of inactive amides.
Monoamine Oxidase (MAO-N) Whole Cell Biocatalyzed Aromatization of 1,2,5,6-Tetrahydropyridines into Pyridines
Toscani, Anita,Risi, Caterina,Black, Gary W.,Brown, Nicola L.,Shaaban, Ali,Turner, Nicholas J.,Castagnolo, Daniele
, p. 8781 - 8787 (2018/09/06)
A sustainable MAO-N biocatalyzed process for the synthesis of pyridines from aliphatic tetrahydropyridines (THP) has been developed. Pyridine compounds were synthesized under mild reaction conditions and with high conversion, exploiting MAO-N whole cells as aromatizing biocatalysts. The kinetic profile of the whole cell biocatalytic transformation was finally investigated via in situ 19F NMR.
Discovery of an in Vivo Tool to Establish Proof-of-Concept for MAP4K4-Based Antidiabetic Treatment
Ammirati, Mark,Bagley, Scott W.,Bhattacharya, Samit K.,Buckbinder, Leonard,Carlo, Anthony A.,Conrad, Rebecca,Cortes, Christian,Dow, Robert L.,Dowling, Matthew S.,El-Kattan, Ayman,Ford, Kristen,Guimar?es, Cristiano R. W.,Hepworth, David,Jiao, Wenhua,Laperle, Jennifer,Liu, Shenping,Londregan, Allyn,Loria, Paula M.,Mathiowetz, Alan M.,Munchhof, Michael,Orr, Suvi T. M.,Petersen, Donna N.,Price, David A.,Skoura, Athanasia,Smith, Aaron C.,Wang, Jian
supporting information, p. 1128 - 1133 (2015/11/24)
Recent studies in adipose tissue, pancreas, muscle, and macrophages suggest that MAP4K4, a serine/threonine protein kinase may be a viable target for antidiabetic drugs. As part of the evaluation of MAP4K4 as a novel antidiabetic target, a tool compound,