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Volumn 47, Issue 10, 2004, Pages 2561-2573

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

Author keywords

[No Author keywords available]

Indexed keywords

1 [5 (4 FLUOROBENZYL) 2 FURYL] 3 (1,2,4 TRIAZOL 3 YL) 1,3 PROPANEDIONE; BETA DIKETOACID DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; DIMER; INTEGRASE; INTEGRASE INHIBITOR; MAGNESIUM ION; METAL CHELATE; METAL ION; OLIGONUCLEOTIDE; OXOACID; TRIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; ZIDOVUDINE;

EID: 2342561153     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030559k     Document Type: Article
Times cited : (197)

References (49)
  • 1
    • 0004294950 scopus 로고    scopus 로고
    • Cold Spring Harbor Press: Cold Spring Harbor
    • Brown, P. O. Integration; Cold Spring Harbor Press: Cold Spring Harbor, 1999.
    • (1999) Integration
    • Brown, P.O.1
  • 2
    • 0032601403 scopus 로고    scopus 로고
    • HIV-1 integrase: Structural organization, conformational changes, and catalysis
    • Asante-Appiah, E.; Skalka, A. M. HIV-1 integrase: structural organization, conformational changes, and catalysis. Adv. Virus Res. 1999, 52, 351-369.
    • (1999) Adv. Virus Res , vol.52 , pp. 351-369
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 3
    • 0036050539 scopus 로고    scopus 로고
    • Strategies in the design of antiviral drugs
    • De Clercq, E. Strategies in the design of antiviral drugs. Nat. Rev. Drug Discovery 2002, 1, 13-25.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 13-25
    • De Clercq, E.1
  • 4
    • 0035912249 scopus 로고    scopus 로고
    • HIV chemotherapy
    • Richman, D. D. HIV chemotherapy. Nature 2001, 410, 995-1001.
    • (2001) Nature , vol.410 , pp. 995-1001
    • Richman, D.D.1
  • 5
    • 0036107683 scopus 로고    scopus 로고
    • Patented small molecule inhibitors of HIV-1 integrase: A ten-year saga
    • Neamati, N. Patented small molecule inhibitors of HIV-1 integrase: a ten-year saga. Expert Opin. Ther. Pat. 2002, 12, 709-724.
    • (2002) Expert Opin. Ther. Pat. , vol.12 , pp. 709-724
    • Neamati, N.1
  • 6
    • 0035147120 scopus 로고    scopus 로고
    • Structure-based HIV-1 integrase inhibitor design: A future perspective
    • Neamati, N. Structure-based HIV-1 integrase inhibitor design: a future perspective. Expert Opin. Invest. Drugs 2001, 10, 281-296.
    • (2001) Expert Opin. Invest. Drugs , vol.10 , pp. 281-296
    • Neamati, N.1
  • 7
    • 0041488800 scopus 로고    scopus 로고
    • Small-Molecule HIV-1 Integrase Inhibitors: The 2001-2002 Update
    • Dayam, R.; Neamati, N. Small-Molecule HIV-1 Integrase Inhibitors: the 2001-2002 Update. Curr. Pharm. Des. 2003, 9, 1789-1802.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1789-1802
    • Dayam, R.1    Neamati, N.2
  • 10
    • 0037303182 scopus 로고    scopus 로고
    • S-1360 Shionogi-GlaxoSmithKline
    • Billich, A. S-1360 Shionogi-GlaxoSmithKline. Curr. Opin. Investig. Drugs 2003, 4, 206-209.
    • (2003) Curr. Opin. Investig. Drugs , vol.4 , pp. 206-209
    • Billich, A.1
  • 18
    • 0036879016 scopus 로고    scopus 로고
    • Novel aryl diketo-containing inhibitors of HIV-1 integrase
    • Pais, G. C. G.; Burke, T. R. Novel aryl diketo-containing inhibitors of HIV-1 integrase. Drugs Future 2002, 27, 1101-1111.
    • (2002) Drugs Future , vol.27 , pp. 1101-1111
    • Pais, G.C.G.1    Burke, T.R.2
  • 20
    • 0032601402 scopus 로고    scopus 로고
    • HIV integrase structure and function
    • Esposito, D.; Craigie, R. HIV integrase structure and function. Adv. Virus Res. 1999, 52, 319-333.
    • (1999) Adv. Virus Res. , vol.52 , pp. 319-333
    • Esposito, D.1    Craigie, R.2
  • 22
    • 0025366844 scopus 로고
    • Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity
    • Sherman, P. A.; Fyfe, J. A. Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity. Proc. Natl. Acad. Sci. U S A 1990, 87, 5119-5123.
    • (1990) Proc. Natl. Acad. Sci. U S A , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 23
    • 0026665238 scopus 로고
    • Retroviral integrase functions as a multimer and can turn over catalytically
    • Jones, K. S.; Coleman, J.; Merkel, G. W.; Laue, T. M.; Skalka, A. M. Retroviral integrase functions as a multimer and can turn over catalytically. J. Biol. Chem. 1992, 267, 16037-16040.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16037-16040
    • Jones, K.S.1    Coleman, J.2    Merkel, G.W.3    Laue, T.M.4    Skalka, A.M.5
  • 24
    • 0027472085 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations
    • Vincent, K. A.; Ellison, V.; Chow, S. A.; Brown, P. O. Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations. J. Virol. 1996, 67, 425-437.
    • (1996) J. Virol. , vol.67 , pp. 425-437
    • Vincent, K.A.1    Ellison, V.2    Chow, S.A.3    Brown, P.O.4
  • 25
    • 0029980485 scopus 로고    scopus 로고
    • A soluble active mutant of HIV-1 integrase: Involvement of both the core and carboxyl-terminal domains in multimerization
    • Jenkins, T. M.; Engelman, A.; Ghirlando, R.; Craigie, R. A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxyl-terminal domains in multimerization. J. Biol. Chem. 1996, 271, 7712-7718.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 26
    • 0032510707 scopus 로고    scopus 로고
    • Photocross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex
    • Heuer, T. S.; Brown, P. O. Photocross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex. Biochemistry 1998, 37, 6667-6678.
    • (1998) Biochemistry , vol.37 , pp. 6667-6678
    • Heuer, T.S.1    Brown, P.O.2
  • 27
    • 0037126629 scopus 로고    scopus 로고
    • Structure of a two-domain fragment of HIV-1 integrase: Implications for domain organization in the intact protein
    • Wang, J. Y.; Ling, H.; Yang, W.; Craigie, R. Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. EMBO J. 2001, 20, 7333-7343.
    • (2001) EMBO J. , vol.20 , pp. 7333-7343
    • Wang, J.Y.1    Ling, H.2    Yang, W.3    Craigie, R.4
  • 29
    • 0037234457 scopus 로고    scopus 로고
    • Modeling HIV-1 integrase complexes based on their hydrodynamic properties
    • Podtelezhnikov, A. A.; Gao, K.; Bushman, F. D.; McCammon, J. A. Modeling HIV-1 integrase complexes based on their hydrodynamic properties. Biopolymers 2003, 68, 110-120.
    • (2003) Biopolymers , vol.68 , pp. 110-120
    • Podtelezhnikov, A.A.1    Gao, K.2    Bushman, F.D.3    McCammon, J.A.4
  • 32
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T. A. DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem. 1999, 274, 17395-17398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 33
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz, T. A. A mechanism for all polymerases. Nature 1998, 391, 231-232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 34
    • 0034104449 scopus 로고    scopus 로고
    • Investigations on human immunodeficiency virus type 1 integrase/DNA binding interactions via molecular dynamics and electrostatics calculations
    • Lins, R. D.; Adesokan, A.; Soares, T. A.; Briggs, J. M. Investigations on human immunodeficiency virus type 1 integrase/DNA binding interactions via molecular dynamics and electrostatics calculations. Pharmacol. Ther. 2000, 85, 123-131.
    • (2000) Pharmacol. Ther. , vol.85 , pp. 123-131
    • Lins, R.D.1    Adesokan, A.2    Soares, T.A.3    Briggs, J.M.4
  • 35
    • 0030566832 scopus 로고    scopus 로고
    • The catalytic domain of human immunodeficiency virus integrase: Ordered active site in the F185H mutant
    • Bujacz, G.; Alexandratos, J.; Qing, Z. L.; Clement-Mella, C.; Wlodawer, A. The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant. FEBS Lett. 1996, 398, 175-178.
    • (1996) FEBS Lett. , vol.398 , pp. 175-178
    • Bujacz, G.1    Alexandratos, J.2    Qing, Z.L.3    Clement-Mella, C.4    Wlodawer, A.5
  • 36
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F.; Hickman, A. B.; Jenkins, T. M.; Engelman, A.; Craigie, R.; Davies, D. R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 1994, 266, 1981-1986.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 39
    • 0033551443 scopus 로고    scopus 로고
    • The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity
    • Greenwald, J.; Le, V.; Butler, S. L.; Bushman, F. D.; Choe, S. The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity. Biochemistry 1999, 38, 8892-8898.
    • (1999) Biochemistry , vol.38 , pp. 8892-8898
    • Greenwald, J.1    Le, V.2    Butler, S.L.3    Bushman, F.D.4    Choe, S.5
  • 40
    • 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
    • Maignan, S.; Guilloteau, J. P.; Zhou-Liu, Q.; Clement-Mella, C.; Mikol, V. 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. 1998, 282, 359-368.
    • (1998) J. Mol. Biol. , vol.282 , pp. 359-368
    • Maignan, S.1    Guilloteau, J.P.2    Zhou-Liu, Q.3    Clement-Mella, C.4    Mikol, V.5
  • 41
    • 0028356582 scopus 로고
    • One step reduction of diaryl ketones to hydrocarbons by etherated boron trifluoride-triethylsilane system
    • Smonou, I. One step reduction of diaryl ketones to hydrocarbons by etherated boron trifluoride-triethylsilane system. Synth. Commun. 1994, 24, 1999-2002.
    • (1994) Synth. Commun. , vol.24 , pp. 1999-2002
    • Smonou, I.1
  • 42
    • 27844466269 scopus 로고
    • N-Methoxy-N-methylamides as effective acylating agents
    • Nahm, S.; Weinreb, S. M. N-Methoxy-N-methylamides as effective acylating agents. Tetrahedron Lett. 1981, 22, 3815-3818.
    • (1981) Tetrahedron Lett. , vol.22 , pp. 3815-3818
    • Nahm, S.1    Weinreb, S.M.2
  • 43
    • 0001368361 scopus 로고
    • The total synthesis of the sex hormone Equilenin and its stereoisomers
    • Bachmann, W. E.; Cole, W.; Wilds, A. L. The total synthesis of the sex hormone Equilenin and its stereoisomers. J. Am. Chem. Soc. 1940, 62, 824-839.
    • (1940) J. Am. Chem. Soc. , vol.62 , pp. 824-839
    • Bachmann, W.E.1    Cole, W.2    Wilds, A.L.3
  • 44
    • 0141789700 scopus 로고    scopus 로고
    • Highly Efficient Preparation of Aryl beta-Diketo Acids with tert-Butyl Methyl Oxalate
    • Jiang, X. H.; Song, L. D.; Long, Y. Q. Highly Efficient Preparation of Aryl beta-Diketo Acids with tert-Butyl Methyl Oxalate. J. Org. Chem. 2003, 68, 7555-7558.
    • (2003) J. Org. Chem. , vol.68 , pp. 7555-7558
    • Jiang, X.H.1    Song, L.D.2    Long, Y.Q.3
  • 45
    • 0034725381 scopus 로고    scopus 로고
    • HIV-1 Integrase inhibitor interactions at the active site: Prediction of binding modes unaffected by crystal packing
    • Sotriffer, C. A.; Ni, H.; McCammon, A. J. HIV-1 Integrase inhibitor interactions at the active site: prediction of binding modes unaffected by crystal packing. J. Am. Chem. Soc 2000, 122, 6136-6137.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6136-6137
    • Sotriffer, C.A.1    Ni, H.2    McCammon, A.J.3
  • 46
    • 0037339235 scopus 로고    scopus 로고
    • Molecular Dynamics Studies of the Wild-Type and Double Mutant HIV-1 Integrase Complexed with the 5CITEP Inhibitor: Mechanism for Inhibition and Drug Resistance
    • Barreca, M. L.; Lee, K. W.; Chimirri, A.; Briggs, J. M. Molecular Dynamics Studies of the Wild-Type and Double Mutant HIV-1 Integrase Complexed with the 5CITEP Inhibitor: Mechanism for Inhibition and Drug Resistance. Biophys. J. 2003, 84, 1450-1463.
    • (2003) Biophys. J. , vol.84 , pp. 1450-1463
    • Barreca, M.L.1    Lee, K.W.2    Chimirri, A.3    Briggs, J.M.4
  • 47
    • 0024578841 scopus 로고
    • New soluble-formazan assay for HIV-1 cytopathic effects: Application to high-flux screening of synthetic and natural products for AIDS antiviral activity
    • Weislow, O. W.; Kiser, R.; Fine, D.; Bader, J.; Shoemaker, R. H.; Boyd, M. R. New soluble-formazan assay for HIV-1 cytopathic effects: application to high-flux screening of synthetic and natural products for AIDS antiviral activity. J. Natl. Cancer Inst. 1989, 81, 577-586.
    • (1989) J. Natl. Cancer Inst. , vol.81 , pp. 577-586
    • Weislow, O.W.1    Kiser, R.2    Fine, D.3    Bader, J.4    Shoemaker, R.H.5    Boyd, M.R.6
  • 48
    • 84986522856 scopus 로고
    • Poling - Promoting Conformational Variation
    • Smellie, A.; Teig, S. L.; Towbin, P. Poling - Promoting Conformational Variation. J. Comput. Chem. 1995, 16, 171-187.
    • (1995) J. Comput. Chem. , vol.16 , pp. 171-187
    • Smellie, A.1    Teig, S.L.2    Towbin, P.3


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