Modeling the activity of furin inhibitors using artificial neural network

European Journal of Medicinal Chemistry

Volumn 44, Issue 4, 2009, Pages 1664-1673

  Worachartcheewan, Apilak ^a   Nantasenamat, Chanin ^a   Naenna, Thanakorn ^a   Isarankura Na Ayudhya, Chartchalerm ^a   Prachayasittikul, Virapong ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Anthrax; Furin; Neural network; QSAR

Indexed keywords

2 DEOXYSTREPTAMINE; ANTIGEN; FURIN; FURIN INHIBITOR; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ACCURACY; ALGORITHM; ANTHRAX; ARTICLE; ARTIFICIAL NEURAL NETWORK; CHEMICAL MODIFICATION; COMPUTER PROGRAM; DRUG ACTIVITY; ELECTRICITY; MOLECULAR MODEL; MOLECULE; PREDICTION; PROTON TRANSPORT; QUANTITATIVE STRUCTURE ACTIVITY RELATION;

DRUG DESIGN; ENZYME INHIBITORS; FURIN; HEXOSAMINES; LEAST-SQUARES ANALYSIS; MODELS, MOLECULAR; NEURAL NETWORKS (COMPUTER); PROTONS; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; SOFTWARE;

EID: 61349110709     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2008.09.028     Document Type: Article

References (41)

1. Mock M., and Fouet A. Annu. Rev. Microbiol. 55 (2001) 647-671
2. Dixon T.C., Meselson M., Guillemin J., and Hanna P.C. N. Engl. J. Med. 341 (1999) 815-826
3. Banks D.J., Ward S.C., and Bradley K.A. Expert Rev. Mol. Med. 8 (2006) 1-18
4. Young J.A., and Collier R.J. Annu. Rev. Biochem. 76 (2007) 243-265
5. Brossier F., and Mock M. Toxicon 39 (2001) 1747-1755
6. Ascenzi P., Visca P., Ippolito G., Spallarossa A., Bolognesi M., and Montecucco C. FEBS Lett. 531 (2002) 384-388
7. Jean F., Stella K., Thomas L., Liu G., Xiang Y., Reason A.J., and Thomas G. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 7293-7298
8. Sarac M.S., Peinado J.R., Leppla S.H., and Lindberg I. Infect. Immun. 72 (2004) 602-605
9. Liu Z.X., Fei H., and Chi C.W. FEBS Lett. 556 (2004) 116-120
10. Komiyama T., and Fuller R.S. Biochemistry 39 (2000) 15156-15165
11. Bolt G., and Pedersen I.R. Virology 252 (1998) 387-398
12. Jiao G.S., Cregar L., Wang J., Millis S.Z., Tang C., O'Malley S., Johnson A.T., Sareth S., Larson J., and Thomas G. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 19707-19712
13. ChemAxon Ltd., Marvin, Version 3.5.4, Budapest, Hungary.
14. Milano Chemometrics and QSAR Research Group, E-Dragon, Version 1.0, Italy.
15. Rensselaer Polytechnic Institute, RECON, Version 5.5, New York, USA.
16. Tetko I.V., Gasteiger J., Todeschini R., Mauri A., Livingstone D., Ertl P., Palyulin V.A., Radchenko E.V., Zefirov N.S., Makarenko A.S., Tanchuk V.Y., and Prokopenko V.V. J. Comput. Aided Mol. Des. 19 (2005) 453-463
17. Todeschini R., Consonni V., Mannhold R., Kubinyi H., and Timmerman H. Handbook of Molecular Descriptors (2000), Wiley-VCH, Weinheim
18. Brenemen C.M., and Rhem M. J. Comput. Chem. 18 (1997) 182-197
19. Bader R.F.W., Anderson S.G., and Duke A.J. J. Am. Chem. Soc. 101 (1979) 1389-1395
20. Breneman C.M., Sundling C.M., Sukumar N., Shen L., Katt W.P., and Embrechts M.J. J. Comput. Aided Mol. Des. 17 (2003) 231-240
21. Mazza C.B., Rege K., Breneman C.M., Sukumar N., Dordick J.S., and Cramer S.M. Biotechnol. Bioeng. 80 (2002) 60-72
22. Witten I.H., and Frank E. Data Mining: Practical Machine Learning Tools and Techniques. second ed. (2005), Morgan Kaufmann, San Francisco
23. Whitley D.C., Ford M.G., and Livingstone D.J. J. Chem. Inf. Comput. Sci. 40 (2000) 1160-1168
24. Nantasenamat C., Naenna T., Isarankura Na Ayudhya C., and Prachayasittikul V. J. Comput. Aided Mol. Des. 19 (2005) 509-524
25. Camo Software AS, The Unscrambler, Version 9.6, Norway.
26. Haaland D.M., and Thomas E.V. Anal. Chem. 60 (1988) 1193-1202
27. Nantasenamat C., Isarankura-Na-Ayudhya C., Naenna T., and Prachayasittikul V. Biosens. Bioelectron. 22 (2007) 3309-3317
28. Nantasenamat C., Isarankura-Na-Ayudhya C., Tansila N., Naenna T., and Prachayasittikul V. J. Comput. Chem. 28 (2007) 1275-1289
29. Zupan J., and Gasteiger J. Neural Networks in Chemistry and Drug Design. second ed (1999), Wiley-VCH, Weinheim
30. Fernandez M., Caballero J., Helguera A.M., Castro E.A., and Gonzalez M.P. Bioorg. Med. Chem. 13 (2005) 3269-3277
31. Duchowicz P.R., Fernandez M., Caballero J., Castro E.A., and Fernandez F.M. Bioorg. Med. Chem. 14 (2006) 5876-5889
32. Caballero J., Zampini F.M., Collina S., and Fernandez M. Chem. Biol. Drug Des. 69 (2007) 48-55
33. Tantishaiyakul V., and Wongpuwarak W. J. Mol. Struct. (Theochem) 718 (2005) 183-189
34. Nantasenamat C., Tantimongcolwat T., Naenna T., Isarankura Na Ayudhya C., and Prachayasittikul V. Excli J. 5 (2006) 150-163
35. Murray J.S., Politzer P., and Famini G.R. J. Mol. Struct. (Theochem) 454 (1998) 299-306
36. Lavine B.K., Davidson C.E., Breneman C., and Katt W. J. Chem. Inf. Comput. Sci. 43 (2003) 1890-1905
37. Eriksson L., Johansson E., Müller M., and Wold S. J. Chemometr. 14 (2000) 599-616
38. Guha R., and Jurs P.C. J. Chem. Inf. Model. 45 (2005) 65-73
39. He L., and Jurs P.C. J. Mol. Graphics Model. 23 (2005) 503-523
40. Henrich S., Cameron A., Bourenkov G.P., Kiefersauer R., Huber R., Lindberg I., Bode W., and Than M.E. Nat. Struct. Biol. 10 (2003) 520-526
41. Breneman C.M., Thomson T.R., Rhem M., and Dung M. Comput. Chem. 19 (1995) 161-179