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Evolutionary Conservation
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Publication Abstract from PubMed
The design, synthesis, and structure-activity relationships (SAR) of a series of 2-aminothiazol-5-yl-pyrimidines as novel p38alpha MAP kinase inhibitors are described. These efforts led to the identification of 41 as a potent p38alpha inhibitor that utilizes a unique nitrogen-sulfur intramolecular nonbonding interaction to stabilize the conformation required for binding to the p38alpha active site. X-ray crystallographic studies that confirm the proposed binding mode of this class of inhibitors in p38alpha and provide evidence for the proposed intramolecular nitrogen-sulfur interaction are discussed.
Utilization of a nitrogen-sulfur nonbonding interaction in the design of new 2-aminothiazol-5-yl-pyrimidines as p38alpha MAP kinase inhibitors.,Lin S, Wrobleski ST, Hynes J Jr, Pitt S, Zhang R, Fan Y, Doweyko AM, Kish KF, Sack JS, Malley MF, Kiefer SE, Newitt JA, McKinnon M, Trzaskos J, Barrish JC, Dodd JH, Schieven GL, Leftheris K Bioorg Med Chem Lett. 2010 Jul 30. PMID:20732813[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Lin S, Wrobleski ST, Hynes J Jr, Pitt S, Zhang R, Fan Y, Doweyko AM, Kish KF, Sack JS, Malley MF, Kiefer SE, Newitt JA, McKinnon M, Trzaskos J, Barrish JC, Dodd JH, Schieven GL, Leftheris K. Utilization of a nitrogen-sulfur nonbonding interaction in the design of new 2-aminothiazol-5-yl-pyrimidines as p38alpha MAP kinase inhibitors. Bioorg Med Chem Lett. 2010 Jul 30. PMID:20732813 doi:10.1016/j.bmcl.2010.07.102
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