메뉴 건너뛰기




Volumn 15, Issue 3, 2011, Pages 733-750

Comparative docking and CoMFA analysis of curcumine derivatives as HIV-1 integrase inhibitors

Author keywords

CoMFA; Curcumine derivatives; Docking; HIV 1 integrase; Pharmacophore mapping

Indexed keywords

CURCUMIN; INTEGRASE INHIBITOR;

EID: 80051591469     PISSN: 13811991     EISSN: 1573501X     Source Type: Journal    
DOI: 10.1007/s11030-011-9304-7     Document Type: Article
Times cited : (33)

References (52)
  • 1
    • 0035045365 scopus 로고    scopus 로고
    • HIV-1 integrase: The next target for AIDS therapy?
    • DOI 10.1016/S0369-8114(01)00135-3
    • J d'Angelo JF Mouscadet D Desmaële F Zouhiri H Leh 2001 HIV-1 integrase: the next target for AIDS therapy? Pathol Biol 49 237 246 10.1016/S0369-8114(01)00135-3 11367559 10.1016/S0369-8114(01)00135-3 (Pubitemid 32299163)
    • (2001) Pathologie Biologie , vol.49 , Issue.3 , pp. 237-246
    • D'Angelo, J.1    Mouscadet, J.F.2    Desmaele, D.3    Zouhiri, F.4    Leh, H.5
  • 2
    • 0029075207 scopus 로고
    • Structure of HIV-1 RT/TIBOR 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors
    • 10.1038/nsb0595-407 7545077 10.1038/nsb0595-407 1:CAS:528: DyaK2MXlsFKltrY%3D
    • J Ding K Das H Moereels L Koymans K Andries PAJ Janssen SH Hughes E Arnold 1995 Structure of HIV-1 RT/TIBOR 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors Nat Struct Biol 2 407 415 10.1038/nsb0595-407 7545077 10.1038/nsb0595-407 1:CAS:528:DyaK2MXlsFKltrY%3D
    • (1995) Nat Struct Biol , vol.2 , pp. 407-415
    • Ding, J.1    Das, K.2    Moereels, H.3    Koymans, L.4    Andries, K.5    Janssen, P.A.J.6    Hughes, S.H.7    Arnold, E.8
  • 3
    • 3042843657 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors: A decade of research and two drugs in clinical trial
    • DOI 10.2174/1568026043388394
    • AA Johnson C Marchand Y Pommier 2004 HIV-1 integrase inhibitors: a decade of research and two drugs in clinical trial Curr Top Med Chem 4 1059 1077 15193139 10.2174/1568026043388394 1:CAS:528:DC%2BD2cXkslChtbg%3D (Pubitemid 38854857)
    • (2004) Current Topics in Medicinal Chemistry , vol.4 , Issue.10 , pp. 1059-1077
    • Johnson, A.A.1    Marchand, C.2    Pommier, Y.3
  • 4
    • 77951006096 scopus 로고    scopus 로고
    • Long-term probability of detecting drug-resistant hiv in treatment-naive patients initiating combination antiretroviral therapy
    • The UK collaborative group on HIV drug resistance and UK CHIC study group. 10.1086/651684 10.1086/651684
    • The UK collaborative group on HIV drug resistance and UK CHIC study group 2010 Long-term probability of detecting drug-resistant hiv in treatment-naive patients initiating combination antiretroviral therapy Clin Infect Dis 50 1275 1285 10.1086/651684 10.1086/651684
    • (2010) Clin Infect Dis , vol.50 , pp. 1275-1285
  • 5
    • 77951009588 scopus 로고    scopus 로고
    • Editorial commentary: HIV drug resistance over the long haul
    • 10.1086/651685 20353363 10.1086/651685
    • PR Harrigan 2010 Editorial commentary: HIV drug resistance over the long haul Clin Infect Dis 50 1286 1287 10.1086/651685 20353363 10.1086/651685
    • (2010) Clin Infect Dis , vol.50 , pp. 1286-1287
    • Harrigan, P.R.1
  • 6
    • 14944374558 scopus 로고    scopus 로고
    • Integrase inhibitors to treat HIV/AIDS
    • DOI 10.1038/nrd1660
    • Y Pommier AA Johnson C Marchand 2005 Integrase inhibitors to treat HIV/AIDS Nat Rev Drug Discov 4 236 248 10.1038/nrd1660 15729361 10.1038/nrd1660 1:CAS:528:DC%2BD2MXhslSns70%3D (Pubitemid 40372557)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.3 , pp. 236-248
    • Pommier, Y.1    Johnson, A.A.2    Marchand, C.3
  • 7
    • 0035912249 scopus 로고    scopus 로고
    • HIV chemotherapy
    • DOI 10.1038/35073673
    • DD Richman 2001 HIV chemotherapy Nature 410 995 1001 10.1038/35073673 11309630 10.1038/35073673 1:CAS:528:DC%2BD3MXjt1Kqs7Y%3D (Pubitemid 32335851)
    • (2001) Nature , vol.410 , Issue.6831 , pp. 995-1001
    • Richman, D.D.1
  • 8
    • 13044295993 scopus 로고    scopus 로고
    • Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: A platform for antiviral drug design
    • 10.1073/pnas.96.23.13040 1:CAS:528:DyaK1MXns1GmsrY%3D
    • Y Goldgur R Craigie GH Cohen T Fujiwara T Yoshinaga T Fujishita H Sugimoto T Endo H Murai DR Davies 1999 Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design P Natl Acad Sci USA 96 13040 13043 10.1073/pnas.96.23.13040 1:CAS:528:DyaK1MXns1GmsrY%3D
    • (1999) P Natl Acad Sci USA , vol.96 , pp. 13040-13043
    • Goldgur, Y.1    Craigie, R.2    Cohen, G.H.3    Fujiwara, T.4    Yoshinaga, T.5    Fujishita, T.6    Sugimoto, H.7    Endo, T.8    Murai, H.9    Davies, D.R.10
  • 9
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • DOI 10.1073/pnas.93.24.13659
    • R Zheng TM Jenkins R Craigie 1996 Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity P Natl Acad Sci USA 93 13659 13664 10.1073/pnas.93.24.13659 1:CAS:528: DyaK28Xnt1Gnsrg%3D (Pubitemid 26424175)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.24 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3
  • 10
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro
    • 1404595 1:CAS:528:DyaK3sXivFWq
    • A Engelman R Craigie 1992 Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro J Virol 66 6361 6369 1404595 1:CAS:528:DyaK3sXivFWq
    • (1992) J Virol , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 11
    • 0027470432 scopus 로고
    • Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro
    • AD Leavitt L Shiue HE Varmus 1993 Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro J Biol Chem 268 2113 2119 8420982 1:CAS:528:DyaK3sXhvVGjsr0%3D (Pubitemid 23033621)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.3 , pp. 2113-2119
    • Leavitt, A.D.1    Shiue, L.2    Varmus, H.E.3
  • 12
    • 2942553781 scopus 로고    scopus 로고
    • Structure and function of HIV-1 integrase
    • DOI 10.2174/1568026043388547
    • TK Chiu DR Davies 2004 Structure and function of HIV-1 integrase Curr Top Med Chem 4 965 977 15134551 10.2174/1568026043388547 1:CAS:528: DC%2BD2cXjslGhtLY%3D (Pubitemid 38854849)
    • (2004) Current Topics in Medicinal Chemistry , vol.4 , Issue.9 , pp. 965-979
    • Chiu, T.K.1    Davies, D.R.2
  • 13
    • 0030922072 scopus 로고    scopus 로고
    • A metal-induced conformational change and activation of HIV-1 integrase
    • DOI 10.1074/jbc.272.26.16196
    • E Asante-Appiah AM Skalka 1997 A metal-induced conformational change and activation of HIV-1 integrase J Biol Chem 272 16196 16205 10.1074/jbc.272.26. 16196 9195919 10.1074/jbc.272.26.16196 1:CAS:528:DyaK2sXkt1ajsL0%3D (Pubitemid 27276437)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16196-16205
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 14
    • 0026740842 scopus 로고
    • Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 in protein in vitro
    • 10.1016/0042-6822(92)90499-F 1585629 10.1016/0042-6822(92)90499-F 1:CAS:528:DyaK38Xlt1Oht7o%3D
    • M Drelich R Wilhelm J Mous 1992 Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro Virology 188 459 468 10.1016/0042-6822(92)90499-F 1585629 10.1016/0042-6822(92)90499-F 1:CAS:528:DyaK38Xlt1Oht7o%3D
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 15
    • 0030746054 scopus 로고    scopus 로고
    • Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity
    • DOI 10.1074/jbc.272.29.18161
    • G Bujacz J Alexandratos A Wlodawer G Merkel M Andrake RA Katz AM Skalka 1997 Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity J Biol Chem 272 18161 18168 10.1074/jbc.272.29.18161 9218451 10.1074/jbc.272.29.18161 1:CAS:528:DyaK2sXkslKmtrk%3D (Pubitemid 27306402)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18161-18168
    • Bujacz, G.1    Alexandratos, J.2    Wlodawer, A.3    Merkel, G.4    Andrake, M.5    Katz, R.A.6    Skalka, A.M.7
  • 18
    • 0032544311 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: High level of similarity of the active site with other viral integrases
    • DOI 10.1006/jmbi.1998.2002
    • S Maignan JP Guilloteau Q Zhou-Liu C Clément-Mella V Mikol 1998 Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases J Mol Biol 282 359 368 10.1006/jmbi.1998.2002 9735293 10.1006/jmbi.1998.2002 1:CAS:528:DyaK1cXmtlClsb8%3D (Pubitemid 28418789)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.2 , pp. 359-368
    • Maignan, S.1    Guilloteau, J.-P.2    Zhou-Liu, Q.3    Clement-Mella, C.4    Mikol, V.5
  • 20
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • DOI 10.1038/34542
    • TA Steitz 1998 A mechanism for all polymerases Nature 391 231 232 10.1038/34542 9440683 10.1038/34542 1:CAS:528:DyaK1cXnsVansw%3D%3D (Pubitemid 28098994)
    • (1998) Nature , vol.391 , Issue.6664 , pp. 231-232
    • Steltz, T.A.1
  • 21
    • 44949212848 scopus 로고    scopus 로고
    • Modeling, Analysis, and Validation of a Novel HIV Integrase Structure Provide Insights into the Binding Modes of Potent Integrase Inhibitors
    • DOI 10.1016/j.jmb.2008.04.054, PII S0022283608005123
    • X Chen M Tsiang F Yu M Hung GS Jones A Zeynalzadegan X Qi H Jin CU Kim S Swaminathan 2008 Modeling, analysis, and validation of a novel HIV integrase structure provide insights into the binding modes of potent integrase inhibitors J Mol Biol 380 504 519 10.1016/j.jmb.2008.04.054 18565342 10.1016/j.jmb.2008. 04.054 1:CAS:528:DC%2BD1cXns1eitLs%3D (Pubitemid 351815132)
    • (2008) Journal of Molecular Biology , vol.380 , Issue.3 , pp. 504-519
    • Chen, X.1    Tsiang, M.2    Yu, F.3    Hung, M.4    Jones, G.S.5    Zeynalzadegan, A.6    Qi, X.7    Jin, H.8    Kim, C.U.9    Swaminathan, S.10    Chen, J.M.11
  • 22
    • 2342561153 scopus 로고    scopus 로고
    • Rational Design and Synthesis of Novel Dimeric Diketoacid-Containing Inhibitors of HIV-1 Integrase: Implication for Binding to Two Metal Ions on the Active Site of Integrase
    • DOI 10.1021/jm030559k
    • YQ Long XH Jiang R Dayam T Sanchez R Shoemaker S Sei N Neamati 2004 Rational design and synthesis of novel dimeric diketoacid-containing inhibitors of HIV-1 integrase: implication for binding to two metal ions on the active site of integrase J Med Chem 47 2561 2573 10.1021/jm030559k 15115398 10.1021/jm030559k 1:CAS:528:DC%2BD2cXjtVSqsrs%3D (Pubitemid 38580093)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.10 , pp. 2561-2573
    • Long, Y.-Q.1    Jiang, X.-H.2    Dayam, R.3    Sanchez, T.4    Shoemaker, R.5    Sei, S.6    Neamati, N.7
  • 24
    • 33750532296 scopus 로고    scopus 로고
    • A platform for designing HIV integrase inhibitors. Part 2: A two-metal binding model as a potential mechanism of HIV integrase inhibitors
    • DOI 10.1016/j.bmc.2006.08.043, PII S0968089606007176
    • T Kawasuji M Fuji T Yoshinaga A Sato T Fujiwara R Kiyama 2006 A platform for designing HIV integrase inhibitors. Part 2: a two-metal binding model as a potential mechanism of HIV integrase inhibitors Bioorgan Med Chem 14 8420 8429 10.1016/j.bmc.2006.08.043 10.1016/j.bmc.2006.08.043 1:CAS:528:DC%2BD28XhtFOjt7rP (Pubitemid 44667542)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.24 , pp. 8420-8429
    • Kawasuji, T.1    Fuji, M.2    Yoshinaga, T.3    Sato, A.4    Fujiwara, T.5    Kiyama, R.6
  • 25
    • 34147128555 scopus 로고    scopus 로고
    • In-Silico docking of HIV-1 integrase inhibitors reveals a novel drug type acting on an enzyme/DNA reaction intermediate
    • DOI 10.1186/1742-4690-4-21
    • A Savarino 2007 In-silico docking of HIV-1 integrase inhibitors reveals a novel drug type acting on an enzyme/DNA reaction intermediate Retrovirology 4 21 10.1186/1742-4690-4-21 17374162 10.1186/1742-4690-4-21 (Pubitemid 46563216)
    • (2007) Retrovirology , vol.4 , pp. 21
    • Savarino, A.1
  • 26
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • 10.1038/nature08784 20118915 10.1038/nature08784 1:CAS:528: DC%2BC3cXht1yntLg%3D
    • S Hare SS Gupta E Valkov A Engelman P Cherepanov 2010 Retroviral intasome assembly and inhibition of DNA strand transfer Nature 464 232 236 10.1038/nature08784 20118915 10.1038/nature08784 1:CAS:528:DC%2BC3cXht1yntLg%3D
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 27
    • 58549092798 scopus 로고    scopus 로고
    • Functional and structural characterization of the integrase from the prototype foamy virus
    • 10.1093/nar/gkn938 19036793 10.1093/nar/gkn938 1:CAS:528: DC%2BD1MXktlelsQ%3D%3D
    • E Valkov SS Gupta S Hare A Helander P Roversi M McClure P Cherepanov 2009 Functional and structural characterization of the integrase from the prototype foamy virus Nucleic Acids Res 37 243 255 10.1093/nar/gkn938 19036793 10.1093/nar/gkn938 1:CAS:528:DC%2BD1MXktlelsQ%3D%3D
    • (2009) Nucleic Acids Res , vol.37 , pp. 243-255
    • Valkov, E.1    Gupta, S.S.2    Hare, S.3    Helander, A.4    Roversi, P.5    McClure, M.6    Cherepanov, P.7
  • 28
    • 70349766723 scopus 로고    scopus 로고
    • Docking-based 3D-QSAR study of HIV-1 integrase inhibitors
    • 10.1016/j.ejmech.2009.07.010 19647906 10.1016/j.ejmech.2009.07.010 1:CAS:528:DC%2BD1MXht1Ggtb%2FL
    • P Gupta N Roy P Garg 2009 Docking-based 3D-QSAR study of HIV-1 integrase inhibitors Eur J Med Chem 44 4276 4287 10.1016/j.ejmech.2009.07.010 19647906 10.1016/j.ejmech.2009.07.010 1:CAS:528:DC%2BD1MXht1Ggtb%2FL
    • (2009) Eur J Med Chem , vol.44 , pp. 4276-4287
    • Gupta, P.1    Roy, N.2    Garg, P.3
  • 29
    • 0347593982 scopus 로고    scopus 로고
    • Application of CoMFA and CoMSIA 3D-QSAR and Docking Studies in Optimization of Mercaptobenzenesulfonamides as HIV-1 Integrase Inhibitors
    • DOI 10.1021/jm030378i
    • CL Kuo H Assefa S Kamath Z Brzozowski J Slawinski F Saczewski JK Buolamwini N Neamati 2004 Application of CoMFA and CoMSIA 3D-QSAR and docking studies in optimization of mercaptobenzenesulfonamides as HIV-1 integrase inhibitors J Med Chem 47 385 399 10.1021/jm030378i 14711310 10.1021/jm030378i 1:CAS:528:DC%2BD3sXps1GmtLk%3D (Pubitemid 38057882)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.2 , pp. 385-399
    • Kuo, C.-L.1    Assefa, H.2    Kamath, S.3    Brzozowski, Z.4    Slawinski, J.5    Saczewski, F.6    Buolamwini, J.K.7    Neamati, N.8
  • 30
    • 0037075132 scopus 로고    scopus 로고
    • CoMFA and CoMSIA 3D QSAR and docking studies on conformationally- restrained cinnamoyl HIV-1 integrase inhibitors: Exploration of a binding mode at the active site
    • DOI 10.1021/jm010399h
    • JK Buolamwini H Assefa 2002 CoMFA and CoMSIA 3D QSAR and docking studies on conformationally-restrained cinnamoyl HIV-1 integrase inhibitors: exploration of a binding mode at the active site J Med Chem 45 841 852 10.1021/jm010399h 11831895 10.1021/jm010399h 1:CAS:528:DC%2BD38XntlKisA%3D%3D (Pubitemid 34173934)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.4 , pp. 841-852
    • Buolamwini, J.K.1    Assefa, H.2
  • 31
    • 20644442241 scopus 로고    scopus 로고
    • Active site binding modes of curcumin in HIV-1 protease and integrase
    • DOI 10.1016/j.bmcl.2005.05.032, PII S0960894X05006165
    • O Vajragupta P Boonchoong GM Morris AJ Olson 2005 Active site binding modes of curcumin in HIV-1 protease and integrase Bioorgan Med Chem 15 3364 3368 10.1016/j.bmcl.2005.05.032 10.1016/j.bmcl.2005.05.032 1:CAS:528: DC%2BD2MXlsVCmu7w%3D (Pubitemid 40835737)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.14 , pp. 3364-3368
    • Vajragupta, O.1    Boonchoong, P.2    Morris, G.M.3    Olson, A.J.4
  • 32
    • 8844247763 scopus 로고    scopus 로고
    • Active site binding modes of the β-diketoacids: A multi-active site approach in HIV-1 integrase inhibitor design
    • DOI 10.1016/j.bmc.2004.09.035, PII S096808960400731X
    • R Dayam N Neamati 2004 Active site binding modes of the -diketoacids: a multi-active site approach in HIV-1 integrase inhibitor design Bioorg Med Chem 12 6371 6381 10.1016/j.bmc.2004.09.035 15556755 10.1016/j.bmc.2004.09.035 1:CAS:528:DC%2BD2cXhtVSnsr3K (Pubitemid 39535161)
    • (2004) Bioorganic and Medicinal Chemistry , vol.12 , Issue.24 , pp. 6371-6381
    • Dayam, R.1    Neamati, N.2
  • 34
    • 63549089353 scopus 로고    scopus 로고
    • Raltegravir, elvitegravir, and metoogravir: The birth of "me-too" HIV-1 integrase inhibitors
    • 10.1186/1742-4690-6-25 19265512 10.1186/1742-4690-6-25
    • E Serrao S Odde K Ramkumar N Neamati 2009 Raltegravir, elvitegravir, and metoogravir: the birth of "me-too" HIV-1 integrase inhibitors Retrovirology 6 25 10.1186/1742-4690-6-25 19265512 10.1186/1742-4690-6-25
    • (2009) Retrovirology , vol.6 , pp. 25
    • Serrao, E.1    Odde, S.2    Ramkumar, K.3    Neamati, N.4
  • 35
    • 0034597625 scopus 로고    scopus 로고
    • Active site binding modes of HIV-1 integrase inhibitors
    • 10.1021/jm000194t 11063607 10.1021/jm000194t 1:CAS:528: DC%2BD3cXnt1Slu7c%3D
    • CA Sotriffer H Ni JA McCammon 2000 Active site binding modes of HIV-1 integrase inhibitors J Med Chem 43 4109 4117 10.1021/jm000194t 11063607 10.1021/jm000194t 1:CAS:528:DC%2BD3cXnt1Slu7c%3D
    • (2000) J Med Chem , vol.43 , pp. 4109-4117
    • Sotriffer, C.A.1    Ni, H.2    McCammon, J.A.3
  • 36
    • 77955423893 scopus 로고    scopus 로고
    • Active site binding modes of dimeric phloroglucinols for HIV-1 reverse transcriptase, protease and integrase
    • 10.1016/j.bmcl.2010.06.057 20594846 10.1016/j.bmcl.2010.06.057 1:CAS:528:DC%2BC3cXptVSktr8%3D
    • P Gupta R Kumar P Garg IP Singh 2010 Active site binding modes of dimeric phloroglucinols for HIV-1 reverse transcriptase, protease and integrase Bioorg Med Chem Lett 20 4427 4431 10.1016/j.bmcl.2010.06.057 20594846 10.1016/j.bmcl.2010.06.057 1:CAS:528:DC%2BC3cXptVSktr8%3D
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 4427-4431
    • Gupta, P.1    Kumar, R.2    Garg, P.3    Singh, I.P.4
  • 37
    • 0347301799 scopus 로고    scopus 로고
    • 2,6-Bis(3,4,5-trihydroxybenzylydene) derivatives of cyclohexanone: Novel potent HIV-1 integrase inhibitors that prevent HIV-1 multiplication in cell-based assays
    • DOI 10.1016/j.bmc.2003.10.005
    • R Costi RD Santo M Artico S Massa R Ragno R Loddo M La Colla E Tramontano P La Colla A Pani 2004 2, 6-Bis (3, 4, 5-trihydroxybenzylydene) derivatives of cyclohexanone novel potent HIV-1 integrase inhibitors that prevent HIV-1 multiplication in cell-based assays Bioorg Med Chem 12 199 215 10.1016/j.bmc.2003.10.005 14697785 10.1016/j.bmc.2003.10.005 1:CAS:528:DC%2BD3sXhtVSjtLfK (Pubitemid 38096232)
    • (2004) Bioorganic and Medicinal Chemistry , vol.12 , Issue.1 , pp. 199-215
    • Costi, R.1    Di Santo, R.2    Artico, M.3    Massa, S.4    Ragno, R.5    Loddo, R.6    La Colla, M.7    Tramontano, E.8    La Colla, P.9    Pani, A.10
  • 38
    • 34047130148 scopus 로고    scopus 로고
    • A novel range based QSAR study of human neuropeptide Y (NPY) Y5 receptor inhibitors
    • DOI 10.1016/j.ejmech.2006.09.011, PII S0223523406003291
    • S Deswal N Roy 2007 A novel range based QSAR study of human neuropeptide Y (NPY) Y5 receptor inhibitors Eur J Med Chem 42 463 470 10.1016/j.ejmech.2006. 09.011 17083999 10.1016/j.ejmech.2006.09.011 1:CAS:528:DC%2BD2sXktVensL8%3D (Pubitemid 46517780)
    • (2007) European Journal of Medicinal Chemistry , vol.42 , Issue.4 , pp. 463-470
    • Deswal, S.1    Roy, N.2
  • 39
    • 0036006911 scopus 로고    scopus 로고
    • 2!
    • DOI 10.1016/S1093-3263(01)00123-1, PII S1093326301001231
    • A Golbraikh A Tropsha 2002 Beware of q2! J Mol Graph Model 20 269 276 11858635 10.1016/S1093-3263(01)00123-1 1:CAS:528:DC%2BD3MXpt1art7o%3D (Pubitemid 34017544)
    • (2002) Journal of Molecular Graphics and Modelling , vol.20 , Issue.4 , pp. 269-276
    • Golbraikh, A.1    Tropsha, A.2
  • 40
    • 0032738842 scopus 로고    scopus 로고
    • Evaluation of the FlexX incremental construction algorithm for protein- ligand docking
    • DOI 10.1002/(SICI)1097-0134(19991101)37:2<228::AID-PROT8>3.0.CO;2-8
    • B Kramer M Rarey T Lengauer 1999 Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking Proteins 37 228 241 10.1002/(SICI)1097-0134(19991101)37:2<228:AID-PROT8>3.0.CO;2-8 10584068 10.1002/(SICI)1097-0134(19991101)37:2<228::AID-PROT8>3.0.CO;2-8 1:CAS:528:DyaK1MXmvFWrsrs%3D (Pubitemid 29503004)
    • (1999) Proteins: Structure, Function and Genetics , vol.37 , Issue.2 , pp. 228-241
    • Kramer, B.1    Rarey, M.2    Lengauer, T.3
  • 41
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges
    • 10.1016/0040-4020(80)80168-2 10.1016/0040-4020(80)80168-2 1:CAS:528:DyaL3MXhslCjtbs%3D
    • J Gasteiger M Marsili 1980 Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges Tetrahedron 36 3219 3228 10.1016/0040-4020(80)80168-2 10.1016/0040-4020(80)80168-2 1:CAS:528: DyaL3MXhslCjtbs%3D
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 42
    • 33846446220 scopus 로고
    • Restart procedures for the conjugate gradient method
    • 10.1007/BF01593790 10.1007/BF01593790
    • MJD Powell 1977 Restart procedures for the conjugate gradient method Math Program 12 241 254 10.1007/BF01593790 10.1007/BF01593790
    • (1977) Math Program , vol.12 , pp. 241-254
    • Powell, M.J.D.1
  • 43
    • 77954381613 scopus 로고    scopus 로고
    • A cooperative and specific DNA-binding mode of HIV-1 integrase depends on the nature of the metallic cofactor and involves the zinc-containing N-terminal domain
    • 10.1093/nar/gkq087 20164093 10.1093/nar/gkq087 1:CAS:528: DC%2BC3cXnvVOitL8%3D
    • K Carayon H Leh E Henry F Simon JF Mouscadet E Deprez 2010 A cooperative and specific DNA-binding mode of HIV-1 integrase depends on the nature of the metallic cofactor and involves the zinc-containing N-terminal domain Nucleic Acids Res 38 3692 3708 10.1093/nar/gkq087 20164093 10.1093/nar/gkq087 1:CAS:528:DC%2BC3cXnvVOitL8%3D
    • (2010) Nucleic Acids Res , vol.38 , pp. 3692-3708
    • Carayon, K.1    Leh, H.2    Henry, E.3    Simon, F.4    Mouscadet, J.F.5    Deprez, E.6
  • 44
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • GM Morris DS Goodsell RS Halliday R Huey WE Hart RK Belew AJ Olson 1998 Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J Comput Chem 19 1639 1662 10.1002/(SICI)1096- 987X(19981115)19:14<1639:AID-JCC10>3.0.CO;2-B 10.1002/(SICI)1096- 987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B 1:CAS:528: DyaK1cXntFemur4%3D (Pubitemid 128590223)
    • (1998) Journal of Computational Chemistry , vol.19 , Issue.14 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 45
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins
    • 10.1021/ja00226a005 10.1021/ja00226a005
    • DC Richard III EP David DB Jeffrey 1988 Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins J Am Chem Soc 110 5959 5967 10.1021/ja00226a005 10.1021/ja00226a005
    • (1988) J Am Chem Soc , vol.110 , pp. 5959-5967
    • Richard Iii, D.C.1    David, E.P.2    Jeffrey, D.B.3
  • 46
    • 70349972385 scopus 로고    scopus 로고
    • Pharmacophore modeling and virtual screening for the discovery of new transforming growth factor- type i receptor (ALK5) inhibitors
    • 10.1016/j.ejmech.2009.07.008 19640613 10.1016/j.ejmech.2009.07.008 1:CAS:528:DC%2BD1MXht1Ggtb%2FJ
    • JX Ren LL Li J Zou L Yang JL Yang SY Yang 2009 Pharmacophore modeling and virtual screening for the discovery of new transforming growth factor- type I receptor (ALK5) inhibitors Eur J Med Chem 44 4259 4265 10.1016/j.ejmech.2009.07. 008 19640613 10.1016/j.ejmech.2009.07.008 1:CAS:528:DC%2BD1MXht1Ggtb%2FJ
    • (2009) Eur J Med Chem , vol.44 , pp. 4259-4265
    • Ren, J.X.1    Li, L.L.2    Zou, J.3    Yang, L.4    Yang, J.L.5    Yang, S.Y.6
  • 47
    • 33745221417 scopus 로고    scopus 로고
    • The discovery of new 11β-hydroxysteroid dehydrogenase type 1 inhibitors by common feature pharmacophore modeling and virtual screening
    • DOI 10.1021/jm0600794
    • D Schuster EM Maurer C Laggner LG Nashev T Wilckens T Langer A Odermatt 2006 The discovery of new 11 [beta]-hydroxysteroid dehydrogenase type 1 inhibitors by common feature pharmacophore modeling and virtual screening J Med Chem 49 3454 3466 10.1021/jm0600794 16759088 10.1021/jm0600794 1:CAS:528:DC%2BD28XkslKhsbk%3D (Pubitemid 43904337)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.12 , pp. 3454-3466
    • Schuster, D.1    Maurer, E.M.2    Laggner, C.3    Nashev, L.G.4    Wilckens, T.5    Langer, T.6    Odermatt, A.7
  • 49
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • TM Jenkins D Esposito A Engelman R Craigie 1997 Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking EMBO J 16 6849 6859 10.1093/emboj/16.22.6849 9362498 10.1093/emboj/16.22.6849 1:CAS:528:DyaK1cXisVWluw%3D%3D (Pubitemid 27503496)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 52
    • 14944359976 scopus 로고    scopus 로고
    • Dynamic receptor-based pharmacophore model development and its application in designing novel HIV-1 integrase inhibitors
    • DOI 10.1021/jm049410e
    • J Deng KW Lee T Sanchez M Cui N Neamati JM Briggs 2005 Dynamic receptor-based pharmacophore model development and its application in designing novel HIV-1 integrase inhibitors J Med Chem 48 1496 1505 10.1021/jm049410e 15743192 10.1021/jm049410e 1:CAS:528:DC%2BD2MXht1ygt7s%3D (Pubitemid 40364557)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.5 , pp. 1496-1505
    • Deng, J.1    Lee, K.W.2    Sanchez, T.3    Cui, M.4    Neamati, N.5    Briggs, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.