These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
7. Sequence, structure, and active site analyses of p38 MAP kinase: exploiting DFG-out conformation as a strategy to design new type II leads. Badrinarayan P, Sastry GN. J Chem Inf Model; 2011 Jan 24; 51(1):115-29. PubMed ID: 21141877 [Abstract] [Full Text] [Related]
15. Switch control pocket inhibitors of p38-MAP kinase. Durable type II inhibitors that do not require binding into the canonical ATP hinge region. Ahn YM, Clare M, Ensinger CL, Hood MM, Lord JW, Lu WP, Miller DF, Patt WC, Smith BD, Vogeti L, Kaufman MD, Petillo PA, Wise SC, Abendroth J, Chun L, Clark R, Feese M, Kim H, Stewart L, Flynn DL. Bioorg Med Chem Lett; 2010 Oct 01; 20(19):5793-8. PubMed ID: 20800479 [Abstract] [Full Text] [Related]
19. Biochemical and biophysical characterization of unique switch pocket inhibitors of p38α. Swann SL, Merta PJ, Kifle L, Groebe D, Sarris K, Hajduk PJ, Sun C. Bioorg Med Chem Lett; 2010 Oct 01; 20(19):5787-92. PubMed ID: 20471255 [Abstract] [Full Text] [Related]
20. Analysis of c-Met kinase domain complexes: a new specific catalytic site receptor model for defining binding modes of ATP-competitive ligands. Asses Y, Leroux V, Tairi-Kellou S, Dono R, Maina F, Maigret B. Chem Biol Drug Des; 2009 Dec 01; 74(6):560-70. PubMed ID: 19909299 [Abstract] [Full Text] [Related] Page: [Next] [New Search]