Rapid Development of a Potent Photo-triggered Inhibitor of the Serine Hydrolase RBBP9

ChemBioChem

Volumn 13, Issue 14, 2012, Pages 2082-2093

  Liu, Xiaodan ^a   Dix, Melissa ^b   Speers, Anna E ^b   Bachovchin, Daniel A ^b   Zuhl, Andrea M ^b   Cravatt, Benjamin F ^b   Kodadek, Thomas J ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

ABPP; CALI; One bead one compound; Peptoid librarys; RBBP9; Serine hydrolases

Indexed keywords

HYDROLASE INHIBITOR; PEPTOID; PROTEOME; SERINE HYDROLASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONCENTRATION RESPONSE; CONTROLLED STUDY; COVALENT BOND; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG SCREENING; DRUG SELECTIVITY; DRUG STRUCTURE; DRUG SYNTHESIS; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MODIFICATION; FLUORESCENCE SPECTROSCOPY; MAGNETISM; MASS SPECTROMETRY; PEPTIDE LIBRARY; PHOTOACTIVATION; PRIORITY JOURNAL;

CATALYTIC DOMAIN; CELL CYCLE PROTEINS; ENZYME INHIBITORS; EOSINE YELLOWISH-(YS); FLUORESCEIN; HELA CELLS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LIGHT; MAGNETICS; NEOPLASM PROTEINS; PEPTOIDS; PROTEIN BINDING; PROTEOME; RUTHENIUM;

EID: 84866445356     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201200445     Document Type: Article

References (25)

1. E. S. Lander, L. M. Linton et al., Nature 2001, 409, 860-921;
2. J. C. Venter, M. D. Adams et al., Science 2001, 291, 1304-1351;
3. J. Z. Long, B. F. Cravatt, Chem. Rev. 2011, 111, 6022-6063.
4. K. S. Lam, S. E. Salmon, E. M. Hersh, V. J. Hruby, W. M. Kazmierski, R. J. Knapp, Nature 1991, 354, 82-84.
5. M. A. Clark, Curr. Opin. Chem. Biol. 2010, 14, 396-403.
6. D. J. Shields, S. Niessen, E. A. Murphy, A. Mielgo, J. S. Desgrosellier, S. K. Lau, L. A. Barnes, J. Lesperance, M. Bouvet, D. Tarin, B. F. Cravatt, D. A. Cheresh, Proc. Natl. Acad. Sci. USA 2010, 107, 2189-2194.
7. D. A. Bachovchin, S. J. Brown, H. Rosen, B. F. Cravatt, Nat. Biotechnol. 2009, 27, 387-394.
8. G. M. Figliozzi, R. Goldsmith, S. C. Ng, S. C. Banville, R. N. Zuckermann, Methods Enzymol. 1996, 267, 437-447.
9. J. M. Astle, L. S. Simpson, Y. Huang, M. M. Reddy, R. Wilson, S. Connell, J. Wilson, T. Kodadek, Chem. Biol. 2010, 17, 38-45.
10. J. Lee, P. Yu, X. Xiao, T. Kodadek, Mol. Biosyst. 2008, 4, 59-65.
11. V. Novakova, P. Zimcik, M. Miletin, K. Kopecky, J. Ivincová, Tetrahedron Lett. 2010, 51, 1016-1018.
12. K. Takemoto, T. Matsuda, M. McDougall, D. H. Klaubert, A. Hasegawa, G. V. Los, K. V. Wood, A. Miyawaki, T. Nagai, ACS Chem. Biol. 2011, 6, 401-406.
13. D. A. Fancy, T. Kodadek, Proc. Natl. Acad. Sci. USA 1999, 96, 6020-6024;
14. D. A. Fancy, C. Denison, K. Kim, Y. Xie, T. Holdeman, F. Amini, T. Kodadek, Chem. Biol. 2000, 7, 697-708.
15. Y. Liu, M. P. Patricelli, B. F. Cravatt, Proc. Natl. Acad. Sci. USA 1999, 96, 14694-14699.
16. D. G. Jay, Proc. Natl. Acad. Sci. USA 1988, 85, 5454-5458;
17. J. C. Liao, J. Roider, D. G. Jay, Proc. Natl. Acad. Sci. USA 1994, 91, 2659-2663;
18. B. K. Eustace, A. Buchstaller, D. G. Jay, Briefings Funct. Genomics Proteomics 2002, 1, 257-265.
19. J. Lee, D. G. Udugamasooriya, H. S. Lim, T. Kodadek, Nat. Chem. Biol. 2010, 6, 258-260.
20. B. K. Sarma, M. Yousufuddin, T. Kodadek, Chem. Commun. 2011, 47, 10590-10592;
21. C. Aquino, M. Sarkar, M. J. Chalmers, K. Mendes, T. Kodadek, G. C. Micalizio, Nat. Chem. 2012, 4, 99-104.
22. Y. Zhang, S. Zhou, A. S. Wavreille, J. DeWille, D. Pei, J. Comb. Chem. 2008, 10, 247-255;
23. T. Liu, Y. Liu, H. Y. Kao, D. H. Pei, J. Med. Chem. 2010, 53, 2494-2501.
24. R. Liu, J. Marik, K. S. Lam, J. Am. Chem. Soc. 2002, 124, 7678-7680.
25. H. J. Olivos, P. G. Alluri, M. M. Reddy, D. Salony, T. Kodadek, Org. Lett. 2002, 4, 4057-4059.