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Design and synthesis of the first generation of novel potent, selective, and in vivo active (benzothiazol-2-yl)acetonitrile inhibitors of the c-Jun N-terminal kinase.
Gaillard P, Jeanclaude-Etter I, Ardissone V, Arkinstall S, Cambet Y, Camps M, Chabert C, Church D, Cirillo R, Gretener D, Halazy S, Nichols A, Szyndralewiez C, Vitte PA, Gotteland JP. Gaillard P, et al. Among authors: arkinstall s. J Med Chem. 2005 Jul 14;48(14):4596-607. doi: 10.1021/jm0310986. J Med Chem. 2005. PMID: 15999997
Design, synthesis, and biological activity of novel, potent, and selective (benzoylaminomethyl)thiophene sulfonamide inhibitors of c-Jun-N-terminal kinase.
Rückle T, Biamonte M, Grippi-Vallotton T, Arkinstall S, Cambet Y, Camps M, Chabert C, Church DJ, Halazy S, Jiang X, Martinou I, Nichols A, Sauer W, Gotteland JP. Rückle T, et al. Among authors: arkinstall s. J Med Chem. 2004 Dec 30;47(27):6921-34. doi: 10.1021/jm031112e. J Med Chem. 2004. PMID: 15615541
Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress-activated protein kinases in the presence of the constitutively active GTP-binding protein Rac1.
Maundrell K, Antonsson B, Magnenat E, Camps M, Muda M, Chabert C, Gillieron C, Boschert U, Vial-Knecht E, Martinou JC, Arkinstall S. Maundrell K, et al. Among authors: arkinstall s. J Biol Chem. 1997 Oct 3;272(40):25238-42. doi: 10.1074/jbc.272.40.25238. J Biol Chem. 1997. PMID: 9312139 Free article.
The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity.
Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S. Muda M, et al. Among authors: arkinstall s. J Biol Chem. 1998 Apr 10;273(15):9323-9. doi: 10.1074/jbc.273.15.9323. J Biol Chem. 1998. PMID: 9535927 Free article.
., Camps, M., Gillieron, C., Davies, K., Ashworth, A., and Arkinstall, S. (1996) J. Biol. Chem. 271, 27205-27208). We now show that MKP-3 enzymatic specificity is paralleled by tight binding to both ERK1 and ERK2 while, in contrast, little or no interaction with eit …
., Camps, M., Gillieron, C., Davies, K., Ashworth, A., and Arkinstall, S. (1996) J. Biol. Chem. 271, 27205-27208). We now show …
45 results