139425-23-3Relevant articles and documents
Copper-catalyzed coupling of polymer bound iodide with organostannanes
Kang, Suk-Ku,Kim, Jae-Sun,Yoon, Seok-Keun,Lim, Kwon-Ho,Yoon, Seung Soo
, p. 3011 - 3012 (1998)
The copper iodide-catalyzed cross-coupling of polymer bound aryl iodide with organostannanes in N-methyl-2-pyrrolidone (NMP) was accomplished smoothly in the presence of NaCl.
Efficient Mizoroki–Heck coupling reactions using phosphine-modified Pd(II)–picolinate complex
Sharma, Sonam,Sarkar, Bibhas R.
supporting information, p. 906 - 914 (2018/03/21)
Efficient Mizoroki–Heck couplings were obtained using a very easily synthesizable palladium(II) complex of hemilabile N–O ligand (picolinate), with high turnover frequencies up to >10,000 h?1, in just 15 min, with high selectivity of >99% to the desired products. Wide applicability of the simple-looking palladium complex catalyst was established with differently functionalized substrates. Catalyst screening studies revealed intricate details of dependence of catalyst performance on different reaction parameters and conditions and arriving at the optimized facile methodology.
De-novo designed library of benzoylureas as inhibitors of BCL-X L: Synthesis, structural and biochemical characterization
Brady, Ryan M.,Vom, Amelia,Roy, Michael J.,Toovey, Nathan,Smith, Brian J.,Moss, Rebecca M.,Hatzis, Effie,Huang, David C. S.,Parisot, John P.,Yang, Hong,Street, Ian P.,Colman, Peter M.,Czabotar, Peter E.,Baell, Jonathan B.,Lessene, Guillaume
, p. 1323 - 1343 (2014/03/21)
The prosurvival BCL-2 proteins are attractive yet challenging targets for medicinal chemists. Their involvement in the initiation and progression of many, if not all, tumors makes them prime targets for developing new anticancer therapies. We present our approach based on de novo structure-based drug design. Using known structural information from complexes engaging opposing members of the BCL-2 family of proteins, we designed peptidomimetic compounds using a benzoylurea scaffold to reproduce key interactions between these proteins. A library stemming from the initial de novo designed scaffold led to the discovery of ligands with low micromolar potency (KD = 4 μM) and selectivity for BCL-XL. These compounds bind in the canonical BH3 binding groove in a binding mode distinct from previously known BCL-2 inhibitors. The results of our study provide insight into the design of a new class of antagonists targeting a challenging class of protein-protein interactions.
