7543-22-8Relevant academic research and scientific papers
Identification of 1,5-naphthyridine derivatives as a novel series of potent and selective TGF-β type I receptor inhibitors
Gellibert, Fran?oise,Woolven, James,Fouchet, Marie-Hélène,Mathews, Neil,Goodland, Helen,Lovegrove, Victoria,Laroze, Alain,Nguyen, Van-Loc,Sautet, Stéphane,Wang, Ruolan,Janson, Cheryl,Smith, Ward,Krysa, Ga?l,Boullay, Valérie,De Gouville, Anne-Charlotte,Huet, Stéphane,Hartley, David
, p. 4494 - 4506 (2007/10/03)
Optimization of the screening hit 1 led to the identification of novel 1,5-naphthyridine aminothiazole and pyrazole derivatives, which are potent and selective inhibitors of the transforming growth factor-β type I receptor, ALK5. Compounds 15 and 19, whic
Synthesis and activity of new aryl- and heteroaryl-substituted 5,6-dihydro-4H-pyrrolo[1,2-b]pyrazole inhibitors of the transforming growth factor-β type I receptor kinase domain
Sawyer, J. Scott,Beight, Douglas W.,Britt, Karen S.,Anderson, Bryan D.,Campbell, Robert M.,Goodson Jr., Theodore,Herron, David K.,Li, Hong-Yu,McMillen, William T.,Mort, Nicholas,Parsons, Stephen,Smith, Edward C. R.,Wagner, Jill R.,Yan, Lei,Zhang, Faming,Yingling, Jonathan M.
, p. 3581 - 3584 (2007/10/03)
We have expanded our previously reported series of pyrazole-based inhibitors of the TGF-β type I receptor kinase domain (TβR-I) to now include new 5,6-dihydro-4H-pyrrolo[1,2-b]pyrazole analogues. Limited examination of the SAR of this new series in both e
Synthesis and activity of new aryl- and heteroaryl-substituted pyrazole inhibitors of the transforming growth factor-β type I receptor kinase domain
Sawyer, J. Scott,Anderson, Bryan D.,Beight, Douglas W.,Campbell, Robert M.,Jones, Michael L.,Herron, David K.,Lampe, John W.,McCowan, Jefferson R.,McMillen, William T.,Mort, Nicholas,Parsons, Stephen,Smith, Edward C. R.,Vieth, Michal,Weir, Leonard C.,Yan, Lei,Zhang, Faming,Yingling, Jonathan M.
, p. 3953 - 3956 (2007/10/03)
Pyrazole-based inhibitors of the transforming growth factor-β type I receptor kinase domain (TβR-I) are described. Examination of the SAR in both enzyme- and cell-based in vitro assays resulted in the emergence of two subseries featuring differing selectivity versus p38 MAP kinase. A common binding mode at the active site has been established by successful cocrystallization and X-ray analysis of potent inhibitors with the TβR-I receptor kinase domain.
