The molecular basis for coxib inhibition of p38α MAP kinase
✍ Scribed by Gilberto M. Sperandio da Silva; Lidia M. Lima; Carlos A.M. Fraga; Carlos M.R. Sant’Anna; Eliezer J. Barreiro
- Book ID
- 108073695
- Publisher
- Elsevier Science
- Year
- 2005
- Tongue
- English
- Weight
- 360 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0960-894X
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The crystal structure of unphosphorylated p38 MAP kinase complexed with a representative pyrrolotriazine-based inhibitor led to the elucidation of the high-affinity binding mode of this class of compounds at the ATP-binding site. The ligand binds in an extended conformation, with one end interacting
p38 MAP kinases are central signalling molecules that mediate cellular responses to numerous environmental conditions and signalling molecules. Their proper function is required for many processes, including stress response, apoptosis, differentiation, growth and even learning and memory. Abnormal a