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Volumn 38, Issue 4, 2011, Pages 338-346

Study on the binding mode and mobility of HIV-1 integrase with L708, 906 inhibitor

Author keywords

906; Drug design; Integrase; L708; Motion correlativity; Motion mode

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 79955811835     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2010.00438     Document Type: Article
Times cited : (3)

References (34)
  • 1
    • 36749088862 scopus 로고    scopus 로고
    • HIV drug development: The next 25 years
    • DOI 10.1038/nrd2336, PII NRD2336
    • Flexner C. HIV drug development: the next 25 years. Nat Rev Drug Discov, 2007, 6(12):959-966 (Pubitemid 350201786)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.12 , pp. 959-966
    • Flexner, C.1
  • 2
    • 77955092239 scopus 로고    scopus 로고
    • Evaluation of HIV-1 integrase inhibitors on human primary macrophages using a luciferase-based single-cycle phenotypic assay
    • Michelini Z, Galluzzo C M, Negri D R M, et al. Evaluation of HIV-1 integrase inhibitors on human primary macrophages using a luciferase-based single-cycle phenotypic assay. J Virol Methods, 2010, 168 (1-2): 272-276
    • (2010) J. Virol. Methods , vol.168 , Issue.1-2 , pp. 272-276
    • Michelini, Z.1    Galluzzo, C.M.2    Negri, D.R.M.3
  • 3
    • 79955836111 scopus 로고    scopus 로고
    • Docking study of HIV-1 integrase tetramer with different length segments of viral end DNA
    • Ke G T, Li P, Hu J P, et al. Docking study of HIV-1 integrase tetramer with different length segments of viral end DNA. Acta Biophys Sin, 2010, 26(10):902-906
    • (2010) Acta Biophys. Sin. , vol.26 , Issue.10 , pp. 902-906
    • Ke, G.T.1    Li, P.2    Hu, J.P.3
  • 4
    • 38749109227 scopus 로고    scopus 로고
    • Treatment of heavily antiretroviral-experienced HIV-infected patients
    • Van Lunzen J. Treatment of heavily antiretroviral-experienced HIV-infected patients. AIDS Rev, 2007, 9(4):246-253
    • (2007) AIDS Rev. , vol.9 , Issue.4 , pp. 246-253
    • Van Lunzen, J.1
  • 5
    • 62949189676 scopus 로고    scopus 로고
    • Amide-containing diketoacids as HIV-1 integrase inhibitors: Synthesis, structure-activity relationship analysis and biological activity
    • Li H C, Wang C, Sanchez T, et al. Amide-containing diketoacids as HIV-1 integrase inhibitors: synthesis, structure-activity relationship analysis and biological activity. Bioorg Med Chem, 2009, 17(7):2913-2919
    • (2009) Bioorg Med. Chem. , vol.17 , Issue.7 , pp. 2913-2919
    • Li, H.C.1    Wang, C.2    Sanchez, T.3
  • 6
    • 79955874802 scopus 로고    scopus 로고
    • Study on the interactions between HIV-1 integrase and Aryl Diketoacid inhibitors with molecular simulation methods
    • Hu J P, Zhang X Y, Tang D Y, et al. Study on the interactions between HIV-1 integrase and Aryl Diketoacid inhibitors with molecular simulation methods. Acta Chim Sin, 2009, 67(19):2177-2183
    • (2009) Acta Chim. Sin. , vol.67 , Issue.19 , pp. 2177-2183
    • Hu, J.P.1    Zhang, X.Y.2    Tang, D.Y.3
  • 8
    • 0027470432 scopus 로고
    • Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro
    • Leavitt A D, Shiue L, Varmus H E. Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro. J Biol Chem, 1993, 268(3):2113-2119 (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
  • 9
    • 0028225959 scopus 로고
    • Human immunodeficiency virus type 1 integrase: Effect on viral replication of mutations at highly conserved residues
    • Cannon P M, Wilson W, Byles E, et al. Human immunodeficiency virus type 1 integrase: effect on viral replication of mutations at highly conserved residues. J Virol, 1994, 68(8):4768-4775
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 4768-4775
    • Cannon, P.M.1    Wilson, W.2    Byles, E.3
  • 10
    • 12944270496 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase
    • Espeseth A S, Felock P, Wolfe A, et al. HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase. Proc Natl Acad Sci USA, 2000, 97(21):11244-11249
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.21 , pp. 11244-11249
    • Espeseth, A.S.1    Felock, P.2    Wolfe, A.3
  • 11
    • 13044295993 scopus 로고    scopus 로고
    • Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: A platform for antiviral drug design
    • Goldgur Y, Craigie R, Cohen G H, et al. Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design. Proc Natl Acad Sci USA, 1999, 96(23):13040-13043
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.23 , pp. 13040-13043
    • Goldgur, Y.1    Craigie, R.2    Cohen, G.H.3
  • 13
    • 0034979318 scopus 로고    scopus 로고
    • Biomolecular simulations: Recent developments in force fields, simulations of enzyme catalysis, protein-ligand, protein-protein, and protein-nucleic acid noncovalent interactions
    • DOI 10.1146/annurev.biophys.30.1.211
    • Wang W, Donini O, Reyes C, et al. Biomolecular simulations: recent developments in force fields, simulations of enzyme catalysis, protein-ligand, protein-protein, and protein-nucleic acid noncovalent interactions. Annu Rev Biophys Biomol Struct, 2001, 30:211-243 (Pubitemid 32566163)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 211-243
    • Wang, W.1    Donini, O.2    Reyes, C.M.3    Kollman, P.A.4
  • 14
    • 0035312551 scopus 로고    scopus 로고
    • Macromolecular electrostatics: Continuum models and their growing pains
    • DOI 10.1016/S0959-440X(00)00197-4
    • Simonson T. Macromolecular electrostatics: continuum models and their growing pains. Curr Opin Struct Biol, 2001, 11(2):243-252 (Pubitemid 32289429)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.2 , pp. 243-252
    • Simonson, T.1
  • 15
    • 0033654297 scopus 로고    scopus 로고
    • Generalized born models of macromolecular solvation effects
    • Bashford D, Case D A. Generalized born models of macromolecular solvation effects. Ann Rev Phys Chem, 2000, 51:129-152
    • (2000) Ann. Rev. Phys. Chem. , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.A.2
  • 16
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still W C, Tempczyk A, Hawley R C, et al. Semianalytical treatment of solvation for molecular mechanics and dynamics. J Am Chem Soc, 1990, 112(16):6127-6129
    • (1990) J. Am. Chem. Soc. , vol.112 , Issue.16 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3
  • 17
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser J, Shenkin P S, Still W C. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO). J Comput Chem, 1999, 20(2):217-230 (Pubitemid 129653030)
    • (1999) Journal of Computational Chemistry , vol.20 , Issue.2 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 19
    • 0029985860 scopus 로고    scopus 로고
    • An efficient method for sampling the essential subspace of proteins
    • Amadei A, Linssen A B M, de Groot B L, et al. An efficient method for sampling the essential subspace of proteins. J Biomol Struct Dynam, 1996, 13(4):615-626
    • (1996) J. Biomol. Struct Dynam , vol.13 , Issue.4 , pp. 615-626
    • Amadei, A.1    Linssen, A.B.M.2    De Groot, B.L.3
  • 20
    • 0033995345 scopus 로고    scopus 로고
    • Efficient sampling in collective coordinate space
    • DOI 10.1002/(SICI)1097-0134(20000401) 39:1<82::AID-PROT9>3.0.CO;2-S
    • Abseher R, Nilges M. Efficient sampling in collective coordinate space. Proteins, 2000, 39(1):82-88 (Pubitemid 30124134)
    • (2000) Proteins: Structure, Function and Genetics , vol.39 , Issue.1 , pp. 82-88
    • Abseher, R.1    Nilges, M.2
  • 21
    • 36348968387 scopus 로고    scopus 로고
    • Essential dynamics of helices provide a functional classification of EF-hand proteins
    • DOI 10.1021/pr070314m
    • Capozzi F, Luchinat C, Micheletti C, et al. Essential dynamics of helices provide a functional classification of EF-hand proteins. J Proteome Res, 2007, 6(11):4245-4255 (Pubitemid 350158502)
    • (2007) Journal of Proteome Research , vol.6 , Issue.11 , pp. 4245-4255
    • Capozzi, F.1    Luchinat, C.2    Micheletti, C.3    Pontiggia, F.4
  • 22
    • 61749092017 scopus 로고    scopus 로고
    • Structural domains and main-chain flexibility in prion proteins
    • Blinov N, Berjanskii M, Wishart D S, et al. Structural domains and main-chain flexibility in prion proteins. Biochemistry, 2009, 48(7):1488-1497
    • (2009) Biochemistry , vol.48 , Issue.7 , pp. 1488-1497
    • Blinov, N.1    Berjanskii, M.2    Wishart, D.S.3
  • 23
    • 33746104463 scopus 로고    scopus 로고
    • Do collective atomic fluctuations account for cooperative effects? Molecular dynamics studies of the U1A-RNA complex
    • DOI 10.1021/ja0606071
    • Kormos B L, Baranger A M, Beveridge D L. Do collective atomic fluctuations account for cooperative effects? molecular dynamics studies of the U1A-RNA complex. J Am Chem Soc, 2006, 128(28):8992-8993 (Pubitemid 44078957)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.28 , pp. 8992-8993
    • Kormos, B.L.1    Baranger, A.M.2    Beveridge, D.L.3
  • 24
    • 33847178767 scopus 로고    scopus 로고
    • A study of collective atomic fluctuations and cooperativity in the U1A-RNA complex based on molecular dynamics simulations
    • Kormos B L, Baranger A M, Beveridge D L. A study of collective atomic fluctuations and cooperativity in the U1A-RNA complex based on molecular dynamics simulations. J Struct Biol, 2007, 157(3):500-513
    • (2007) J. Struct Biol. , vol.157 , Issue.3 , pp. 500-513
    • Kormos, B.L.1    Baranger, A.M.2    Beveridge, D.L.3
  • 25
    • 77952515445 scopus 로고    scopus 로고
    • Molecular dynamics simulation of HIV-1 integrase dimer complexed with viral DNA
    • Hu J P, Wang C X. Molecular dynamics simulation of HIV-1 integrase dimer complexed with viral DNA. Chin J Chem, 2010, 28:33-40
    • (2010) Chin. J. Chem. , vol.28 , pp. 33-40
    • Hu, J.P.1    Wang, C.X.2
  • 27
    • 34748816224 scopus 로고    scopus 로고
    • Study on the drug resistance and the binding mode of HIV-1 integrase with LCA inhibitor
    • DOI 10.1007/s11426-007-0043-7
    • Hu J P, Chang S, Chen W Z, et al. Study on the drug resistance and the binding mode of HIV-1 integrase with LCA inhibitor. Sci China SerB Chem, 2007, 50(5):665-674 (Pubitemid 47477027)
    • (2007) Science in China, Series B: Chemistry , vol.50 , Issue.5 , pp. 665-674
    • Hu, J.1    Chang, S.2    Chen, W.3    Wang, C.4
  • 28
    • 22144463200 scopus 로고    scopus 로고
    • Model of full-length HIV-1 integrase complexed with viral DNA as template for anti-HIV drug design
    • DOI 10.1007/s10822-005-0365-5
    • Karki R G, Tang Y, Burke TRJ, et al. Model of full-length HIV-1 integrase complexed with viral DNA as template for anti-HIV drug design. J Comput Aided Mol Des, 2004, 18(12):739-760 (Pubitemid 40973864)
    • (2004) Journal of Computer-Aided Molecular Design , vol.18 , Issue.12 , pp. 739-760
    • Karki, R.G.1    Tang, Y.2    Burke Jr., T.R.3    Nicklaus, M.C.4
  • 29
    • 37049001192 scopus 로고    scopus 로고
    • Study on the molecular mechanism of inhibiting HIV-1 integrase by EBR28 peptide via molecular modeling approach
    • DOI 10.1016/j.bpc.2007.09.008, PII S030146220700227X
    • Hu J P, Gong X Q, Su J G, et al. Study on the molecular mechanism of inhibiting HIV-1 integrase by EBR28 peptide via molecular modeling approach. Biophys Chem, 2008, 132 (2-3): 69-80 (Pubitemid 350251878)
    • (2008) Biophysical Chemistry , vol.132 , Issue.2-3 , pp. 69-80
    • Hu, J.P.1    Gong, X.Q.2    Su, J.G.3    Chen, W.Z.4    Wang, C.X.5
  • 30
    • 50049106274 scopus 로고    scopus 로고
    • Studies on the binding modes of HIV-1 integrase with viral DNA via molecular docking method
    • Hu J P, Ke G T, Chang S, et al. Studies on the binding modes of HIV-1 integrase with viral DNA via molecular docking method. Chem J Chinese U, 2008, 29(7):1432-1437
    • (2008) Chem. J. Chinese U , vol.29 , Issue.7 , pp. 1432-1437
    • Hu, J.P.1    Ke, G.T.2    Chang, S.3
  • 32
    • 26644456674 scopus 로고    scopus 로고
    • A three-dimensional model of the human immunodeficiency virus type 1 integration complex
    • DOI 10.1007/s10822-005-5256-2
    • Wielens J, Crosby I T, Chalmers D K. A three-dimensional model of the human immunodeficiency virus type 1 integration complex. J Comput Aided Mol Des, 2005, 19(5):301-317 (Pubitemid 41439998)
    • (2005) Journal of Computer-Aided Molecular Design , vol.19 , Issue.5 , pp. 301-317
    • Wielens, J.1    Crosby, I.T.2    Chalmers, D.K.3
  • 33
    • 0030875813 scopus 로고    scopus 로고
    • Mapping features of HIV-1 integrase near selected sites on viral and target DNA molecules in an active enzyme - DNA complex by photo-cross- linking
    • DOI 10.1021/bi970782h
    • Heuer T S, Brown P O. Mapping features of HIV-1 integrase near selected sites on viral and target DNA molecules in an active enzyme-DNA complex by photo-cross-linking. Biochemistry, 1997, 36(35):10655-10665 (Pubitemid 27382555)
    • (1997) Biochemistry , vol.36 , Issue.35 , pp. 10655-10665
    • Heuer, T.S.1    Brown, P.O.2


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