Corrigendum to "3D structure modeling of cytochrome P450 2C19 and its implication for personalized drug design" [Biochem. Biophys. Res. Commun. 355 (2007) 513-519] (DOI:10.1016/j.bbrc.2007.01.185);3D structure modeling of cytochrome P450 2C19 and its implication for personalized drug design

Biochemical and Biophysical Research Communications

Volumn 355, Issue 2, 2007, Pages 513-519

  Wang, Jing Fang ^a,b   Wei, Dong Qing ^a   Li, Lin ^a,c   Zheng, Si Yuan ^b   Li, Yi Xue ^a,b   Chou, Kuo Chen ^d  

^a SHANGHAI JIAO TONG UNIVERSITY   (China)

^b Shanghai Jiao Tong University Affiliated Sixth People s Hospital   (China)

^c PEKING UNIVERSITY   (China)

^d GORDON LIFE SCIENCE INSTITUTE   (United States)

Author keywords

CEC; CYP2C19; Cytochrome P 450; Fluvoxamine; Lescol; Personalized drug design; Structure activity relationship; Ticlopidine

Indexed keywords

3 CYANO 7 ETHOXYCOUMARIN; 7 ETHOXYCOUMARIN; CYTOCHROME P450 2C19; FLUINDOSTATIN; FLUVOXAMINE; TICLOPIDINE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; DRUG ACTIVITY; DRUG DESIGN; DRUG PROTEIN BINDING; DRUG STRUCTURE; ENZYME ANALYSIS; ENZYME STRUCTURE; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 33847129220     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.03.111     Document Type: Erratum

References (44)

1. Tanmay S.P., Shaun F.N., Sanish D., Vishal M.S., Nilima A.K., and Nithya J.G. Evaluation of the activity of CYP2C19 in Gujrati and Marwadi subjects living in Mumbasi (Bombay). BMC Clin. Pharm. 6 (2006) 1-5
2. Gonzale F.J., Radek C., and Daniel W. Characterization of the common genetic defect in humans deficient in debrisoquine metabolism. J. Nature 331 (1988) 442-444
3. Regina E., Tammy L.D., Arne Z., and Romy M. Identification and functional characterization of eight CYP3A4 protein variants. Pharmacogenetics 11 (2001) 447-458
4. M. Ingelman-Sundberg, M. Oscarson, A. K. Daly, S. Garte, D. W. Nebert, Human cytochrome P450 (CYP) alleles a web page for the nomenclature of alleles [http://www.imm.ki.se/CYPalleles/] (accessed 22.11.2005).
5. Desta Z., Zhao X., Shin J.G., and Flockhart D.A. Clinical significance of the cytochrome P450 2C19 genetic polymorphism. Clin. Pharmacokinet 41 (2002) 913-958
6. Kumana C.R., Lauder I.J., Chan M., Ko W., and Lin H.J. Differences in diazepam pharmacokinetics in Chinese and white Caucasians-relation to body lipid stores. Eur. J. Clin. Pharmacol. 32 (1987) 211-215
7. Daly A.K. Pharmacogenetics of the cytochromes P450. Curr. Top Med. Chem. 4 (2004) 1733-1744
8. Chou K.C. Review: structural bioinformatics and its impact to biomedical science. Curr. Med. Chem. 11 (2004) 2105-2134
9. Wester M.R., Yano J.K., Schoch G.A., Yang C., Griffin K.J., Stout C.D., and Johnson E.F. The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0 Å resolution. J. Bio. Chem. 279 (2004) 35630-35637
10. Tanira M.O., Al-Mukhaini M.K., Al-Hinai A.T., Al-Balushi K.A., and Ahmed I.S. Frequency of CYP2C9 genotypes among omani patients receiving warfarin and its correlation with warfarin dose. Community Genet. 10 (2007) 32-37
11. Claessens M., Cutsem E.V., Lasters I., and Wodak S. Modeling the polypeptide backbone with 'spare parts' from known protein structures. Protein Eng. 4 (1989) 335-345
12. Jones T.A., and Thirup S. Using known substructures in protein model building and crystallography. EMBO J. 5 (1986) 819-822
13. Blundell T.L., Sibanda B.L., Sternberg M.J.E., and Thornton J.M. Knowledge-based prediction of protein structures and design of novel molecules. Nature (London) 326 (1987) 347-352
14. Chou K.C., Nemethy G., Pottle M., and Scheraga H.A. Energy of stabilization of the right-handed beta-alpha-beta crossover in proteins. J. Mol. Biol. 205 (1989) 241-249
15. Fechteler T., Dengler U., and Schomburg D. Predition of protein three-dimensional structures in insertion and deletion regions: a procedure for searching data bases of representative protein fragments using geometric scoring criteria. J. Mol. Biol. 253 (1995) 114-131
16. Chou K.C., Jones D., and Heinrikson R.L. Prediction of the tertiary structure and substrate binding site of caspase-8. FEBS Lett. 419 (1997) 49-54
17. Rotonda J., Nicholson D.W., Fazil K.M., Gallant M., Gareau Y., Labelle M., Peterson E.P., Rasper D.M., Ruel R., Vaillancourt J.P., Thornberry N.A., and Becker J.W. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat. Struct. Biol. 3 (1996) 619-625
18. Watt W., Koeplinger K.A., Mildner A.M., Heinrikson R.L., Tomasselli A.G., and Watenpaugh K.D. The atomic resolution structure of human caspase-8, a key activator of apoptosis. Structure 7 (1999) 1135-1143
19. Chou J.J., Matsou H., Duan J., and Wagner G. Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell 94 (1998) 171-180
20. Chou K.C., Watenpaugh K.D., and Heinrikson R.L. A model of the complex between cyclin-dependent kinase 5( Cdk5) and the activation domain of neuronal Cdk5 activator. Biochem. Biophys. Res. Commun. 259 (1999) 420-428
21. Chou K.C., Tomasselli A.G., and Heinrikson R.L. Prediction of the tertiary structure of a caspase-9/inhibitor complex. FEBS Lett. 470 (2000) 249-256
22. Tarricone C., Dhavan R., Peng J., Arecces L.B., Tsai L.H., and Musacchio A. Structure and regulation of the Cdk5-p25 (Nck5a) complex. Mol. Cell 8 (2001) 657-669
23. Zhang J., Luan C.H., Chou K.C., and Johnson G.V.W. Identification of the N-terminal functional domains of Cdk5 by molecular truncation and computer modeling. Proteins Struct. Funct. Genet. 48 (2002) 447-453
24. Chou K.C., and Howe W.J. Prediction of the tertiary structure of the beta-secretase zymogen. Biochem. Biophys. Res. Commun. 292 (2002) 702-708
25. Shi X.P., Chen E., Yin K.C., Na S., Garsky V.M., Lai M.T., Li Y.M., Platchek M., Register R.B., Sardana M.K., Tam M.J., Thiebeau J., Wood T., Shafer J.A., and Gardell S.J. The pro domain of beta-secretase does not confer strict zymogen-like properties but does assist proper folding of the protease domain. J. Biol. Chem. 276 (2001) 10336-10373
26. Benjannet S., Elagoz A., Wickham L., Mamarbachi M., Munzer J.S., Basak A., Lazure C., Cromlish J.A., Sisodia S., Checler F., Chretien M., and Seidah N.G. Post-translational processing of beta-secretase-amylodi-converting enzyme and its ectodomain shedding. J. Biol. Chem. 276 (2001) 10879-10887
27. Chou K.C. Modeling extracellular domains of GABA-A receptors: subtypes 1, 2, 3 and 5. Biochem. Biophys. Res. Commun. 316 (2004) 636-642
28. Chou K.C. Insights from modelling the tertiary structure of BACE2. J. Proteome Res. 3 (2004) 1069-1072
29. Wei D.Q., Du Q.S., Sun H., and Chou K.C. Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands. Biochem. Biophys. Res. Commun. 344 (2006) 1048-1055
30. Chou K.C. Molecular therapeutic target for type-2 diabetes. J. Proteome Res. 3 (2004) 1284-1288
31. Chou K.C. Modeling the tertiary structure of human cathepsin-E. Biochem. Biophys. Res. Commun. 331 (2005) 56-60
32. Chou K.C. Insights from modeling the 3D structure of the extracellular domain of alpha 7 nicotinic acetylcholine receptor. Biochem. Biophys. Res. Commun. 319 (2004) 433-438
33. Chou K.C. Insights from modeling three-dimensional structures of the human potassium and sodium channels. J. Proteome Res. 3 (2004) 856-861
34. Kuntz I.D., Meng E.C., and Shoichet B.K. Structure-based strategies for drug design and discovery. Acc. Chem. Res. 27 (1994) 117-123
35. Morris G.M., Goodesll D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., and Olson A.J. Automated docking using a Lamarckian Genetic Algorithm and empirical binding free energy function. J. Comput. Chem. 19 (1998) 1639-1662
36. Chou K.C. Low-frequency resonance and cooperativity of hemoglobin. Trends Biochem. Sci. 14 (1989) 212
37. Chou K.C. Review: Low-frequency collective motion in biomacromolecules and its biological functions. Biophys. Chem. 30 (1988) 3-48
38. Chou K.C., and Carlacci L. Simulated annealing approach to the study of protein structures. Protein Eng. 4 (1991) 661-667
39. Glover F. Tabu search: a tutorial. Interfaces 20 (1990) 74-94
40. MacKerell Jr. A.D., Bashford D., Bellott M., Dunbrack Jr. R.L., Evanseck J.D., Field M.J., Fischer S., Gao J., Guo H., Ha S., Joseph-McCarthy D., Kuchnir L., Kuczear K., Lau F.T.K., Mattos C., Michnick S., Ngo T., Nguyen D.T., Prodhom B., Reither III W.E., Roux B., Schlenkrich M., Smith J.C., Stoe R., Straub J., Watanabe M., Wiorkiewicz-Kuczera J., Yin D., and Karplus M. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102 (1998) 3586-3616
41. Morris G.M., Goodsell D.S., Huey R., and Olson A.J. Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4. J. Comput. Aided Mol. Des. 10 (1996) 293-304
42. Wei D.Q., Sirois S., Du Q.S., Arias H.R., and Chou K.C. Theoretical studies of Alzheimer's disease drug candidate [(2,4-dimethoxy) benzylidene]-anabaseine dihydrochloride (GTS-21) and its derivatives. Biochem. Biophys. Res. Commun. 338 (2005) 1059-1064
43. Wei D.Q., Zhang R., Du Q.S., Gao W.N., Li Y., Gao H., Wang S.Q., Zhang X., Li A.X., Sirois S., and Chou K.C. Anti-SARS drug screening by molecular docking. Amino Acids 31 (2006) 73-80
44. Chou K.C., Wei D.Q., Du Q.S., Sirois S., and Zhong W.Z. Review: Progress in computational approach to drug development against SARS. Curr. Med. Chem. 13 (2006) 3263-3270