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Volumn 4, Issue 10, 2004, Pages 1059-1077

HIV-1 integrase inhibitors: A decade of research and two drugs in clinical trial

Author keywords

[No Author keywords available]

Indexed keywords

1 [5 (4 FLUOROBENZYL) 2 FURYL] 3 (1,2,4 TRIAZOL 3 YL) 1,3 PROPANEDIONE; 4 [1 (4 FLUOROBENZYL) 2 PYRROLYL] 2,4 DIOXOBUTYRIC ACID; CAFFEIC ACID PHENETHYL ESTER; CARBOXYLIC ACID DERIVATIVE; CATECHOL DERIVATIVE; CICHORIC ACID; COMPLESTATIN; FUNGAL PROTEIN; HYDRAZIDE DERIVATIVE; INTEGRACIN A; INTEGRACIN B; INTEGRACIN C; INTEGRAMIDE A; INTEGRAMIDE B; INTEGRASE; INTEGRASE INHIBITOR; ISOSERINE; L 708906; LITHOSPERMIC ACID; N (4 FLUOROBENZYL) 8 HYDROXY 5 (TETRAHYDRO 2H 1,2 THIAZIN 2 YL) 1,6 NAPHTHYRIDINE 7 CARBOXAMIDE S,S DIOXIDE; NAPHTHYRIDINE DERIVATIVE; PEPTIDE DERIVATIVE; PROTEINASE INHIBITOR; PYRIMIDINE DERIVATIVE; QUINOLINE DERIVATIVE; RAG1 PROTEIN; RAG2 PROTEIN; RNA DIRECTED DNA POLYMERASE INHIBITOR; SESQUITERPENE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 3042843657     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568026043388394     Document Type: Review
Times cited : (124)

References (104)
  • 2
    • 0026659014 scopus 로고
    • Inhibition of HIV-1 integration protein by aurintricarboxylic acid monomers, monomer analogs, and polymer fractions
    • Cushman, M.; Sherman, P. Inhibition of HIV-1 integration protein by aurintricarboxylic acid monomers, monomer analogs, and polymer fractions. Biochem. Biophys. Res. Commun. 1992, 185, 85-90.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 85-90
    • Cushman, M.1    Sherman, P.2
  • 3
    • 0027222149 scopus 로고
    • Inhibitory effect of the polyanionic drug suramin on the in vitro HIV DNA integration reaction
    • Carteau, S.; Mouscadet, J.-F.; Goulaouic, H.; Subra, F.; Auclair, C. Inhibitory effect of the polyanionic drug suramin on the in vitro HIV DNA integration reaction. Arch. Biochem. Biophys. 1993, 305, 606-610.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 606-610
    • Carteau, S.1    Mouscadet, J.-F.2    Goulaouic, H.3    Subra, F.4    Auclair, C.5
  • 6
    • 3042800437 scopus 로고    scopus 로고
    • Discovery of a Potent HIV Integrase Inhibitor
    • Poster presented at AIDS 2002 Meeting
    • Young, S. D., et al. Discovery of a Potent HIV Integrase Inhibitor. Poster presented at AIDS 2002 Meeting. 2002.
    • (2002)
    • Young, S.D.1
  • 7
    • 0036095978 scopus 로고    scopus 로고
    • HIV integrase as a target for antiviral chemotherapy
    • Nair, V. HIV integrase as a target for antiviral chemotherapy. Reviews in Medical Virology 2002, 12, 179-193.
    • (2002) Reviews in Medical Virology , vol.12 , pp. 179-193
    • Nair, V.1
  • 8
    • 0036223082 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 Reverse Transcriptase and Integrase: Classical and Emerging Therapeutical Approaches
    • Tarrago-Litvak, L.; Andreola, M. L.; Fournier, M.; Nevinsky, G. A.; Parissi, V. et al. Inhibitors of HIV-1 Reverse Transcriptase and Integrase: Classical and Emerging Therapeutical Approaches. Curr. Pharm. Des. 2002, 8, 595-614.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 595-614
    • Tarrago-Litvak, L.1    Andreola, M.L.2    Fournier, M.3    Nevinsky, G.A.4    Parissi, V.5
  • 10
    • 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. Investig. Drugs 2001, 10, 281-296.
    • (2001) Expert Opin. Investig. Drugs , vol.10 , pp. 281-296
    • Neamati, N.1
  • 12
    • 0033813928 scopus 로고    scopus 로고
    • Retroviral integrase inhibitors year 2000: Update and perspectives
    • Pommier, Y.; Marchand, C.; Neamati, N. Retroviral integrase inhibitors year 2000: update and perspectives. Antiviral Res. 2000, 47, 139-148.
    • (2000) Antiviral Res. , vol.47 , pp. 139-148
    • Pommier, Y.1    Marchand, C.2    Neamati, N.3
  • 13
    • 0036879016 scopus 로고    scopus 로고
    • Novel aryl diketo-containing inhibitors of HIV-1 integrase
    • Pais, G. C. G.; Burke, T. R., Jr. Novel aryl diketo-containing inhibitors of HIV-1 integrase. Drugs of the Future 2002, 27, 1101-1111.
    • (2002) Drugs of the Future , vol.27 , pp. 1101-1111
    • Pais, G.C.G.1    Burke Jr., T.R.2
  • 14
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng, R.; Jenkins, T. M.; Craigie, R. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Natl. Acad. Sci. USA 1996, 93, 13659-13664.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3
  • 15
    • 0029116747 scopus 로고
    • Solution structure of the DNA binding domain of HIV-1 integrase
    • Lodi, P. J.; Ernst, J. A.; Kuszewski, J.; Hickman, A. B.; Engelman, A. et al. Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry 1995, 34, 9826-9833.
    • (1995) Biochemistry , vol.34 , pp. 9826-9833
    • Lodi, P.J.1    Ernst, J.A.2    Kuszewski, J.3    Hickman, A.B.4    Engelman, A.5
  • 16
    • 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
    • Bujacz, G.; Alexandratos, J.; Wlodawer, A.; Merkel, G.; Andrake, M. et al. Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity. J. Biol. Chem. 1997, 272, 18161-18168.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18161-18168
    • Bujacz, G.1    Alexandratos, J.2    Wlodawer, A.3    Merkel, G.4    Andrake, M.5
  • 17
    • 0032189652 scopus 로고    scopus 로고
    • Sequence selectivity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interactions
    • Esposito, D.; Craigie, R. Sequence selectivity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interactions. EMBO J. 1998, 17, 5832-5843.
    • (1998) EMBO J. , vol.17 , pp. 5832-5843
    • Esposito, D.1    Craigie, R.2
  • 18
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • Jenkins, T. M.; Esposito, D.; Engelman, A.; Craigie, R. Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking. EMBO J. 1997, 16, 6849-6859.
    • (1997) EMBO J. , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 19
    • 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
    • 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, 10655-10665.
    • (1997) Biochemistry , vol.36 , pp. 10655-10665
    • Heuer, T.S.1    Brown, P.O.2
  • 20
    • 0032510707 scopus 로고    scopus 로고
    • Photo-Cross-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. Photo-Cross-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
  • 21
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison, V.; Brown, P. O. A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc. Natl. Acad. Sci. USA 1994, 91, 7316-7320.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 22
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity of other polynucleotide transferases
    • Dyda, F.; Hickman, A. B.; Jenkins, T. M.; Engelman, A.; Craigie, R. et al. Crystal structure of the catalytic domain of HIV-1 integrase: similarity of other polynucleotide 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
  • 23
    • 0032483022 scopus 로고    scopus 로고
    • Three new structures of the core domain of HIV-1 integrase: An active site that binds magnesium
    • Goldgur, Y.; Dyda, F.; Hickman, A. B.; Jenkins, T. M.; Craigie, R. et al. Three new structures of the core domain of HIV-1 integrase: An active site that binds magnesium. Proc. Natl. Acad. Sci. USA 1998, 95, 9150-9154.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9150-9154
    • Goldgur, Y.1    Dyda, F.2    Hickman, A.B.3    Jenkins, T.M.4    Craigie, R.5
  • 24
    • 0034682511 scopus 로고    scopus 로고
    • Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: A model for viral DNA binding
    • Chen, J. C.; Krucinski, J.; Miercke, L. J.; Finer-Moore, J. S.; Tang, A. H. et al. Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding. Proc. Natl. Acad. Sci. USA 2000, 97, 8233-8238.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8233-8238
    • Chen, J.C.1    Krucinski, J.2    Miercke, L.J.3    Finer-Moore, J.S.4    Tang, A.H.5
  • 25
    • 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
  • 26
    • 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.; Fujiwara, T.; Yoshinaga, T. 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, 13040-13043.
    • (1999) Proc. 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
  • 27
    • 0342569810 scopus 로고    scopus 로고
    • Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor
    • Lubkowski, J.; Yang, F.; Alexandratos, J.; Wlodawer, A.; Zhao, H. et al. Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor. Proc. Natl. Acad. Sci. USA 1998, 95, 4831-4836.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4831-4836
    • Lubkowski, J.1    Yang, F.2    Alexandratos, J.3    Wlodawer, A.4    Zhao, H.5
  • 29
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
    • Engelman, A.; Mizuuchi, K.; Craigie, R. HIV-1 DNA integration: mechanism of viral DNA cleavage and DNA strand transfer. Cell 1991, 67, 1211-1221.
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 30
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein
    • Vink, C.; Oude Groeneger, A. M.; Plasterk, R. H. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein. Nucleic Acids Res. 1993, 21, 1419-1425.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.M.2    Plasterk, R.H.3
  • 31
    • 0037066730 scopus 로고    scopus 로고
    • Structural determinants for HIV-1 integrase inhibition by beta-diketo acids
    • Marchand, C.; Zhang, X.; Pais, G. C.; Cowansage, K.; Neamati, N. et al. Structural determinants for HIV-1 integrase inhibition by beta-diketo acids. J. Biol. Chem. 2002, 277, 12596-12603.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12596-12603
    • Marchand, C.1    Zhang, X.2    Pais, G.C.3    Cowansage, K.4    Neamati, N.5
  • 32
    • 0034723439 scopus 로고    scopus 로고
    • Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells
    • Hazuda, D. J.; Felock, P.; Witmer, M.; Wolfe, A.; Stillmock, K. et al. Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells. Science 2000, 287, 646-650.
    • (2000) Science , vol.287 , pp. 646-650
    • Hazuda, D.J.1    Felock, P.2    Witmer, M.3    Wolfe, A.4    Stillmock, K.5
  • 33
    • 0034887472 scopus 로고    scopus 로고
    • In vitro human immunodeficiency virus type 1 integrase assays
    • Marchand, C.; Neamati, N.; Pommier, Y. In vitro human immunodeficiency virus type 1 integrase assays. Methods Enzymol. 2001, 340, 624-633.
    • (2001) Methods Enzymol. , vol.340 , pp. 624-633
    • Marchand, C.1    Neamati, N.2    Pommier, Y.3
  • 35
    • 0036118227 scopus 로고    scopus 로고
    • Efficient concerted integration by recombinant human immunodeficiency virus type 1 integrase without cellular or viral cofactors
    • Sinha, S.; Pursley, M. H.; Grandgenett, D. P. Efficient concerted integration by recombinant human immunodeficiency virus type 1 integrase without cellular or viral cofactors. J. Virol. 2002, 76, 3105-3113.
    • (2002) J. Virol. , vol.76 , pp. 3105-3113
    • Sinha, S.1    Pursley, M.H.2    Grandgenett, D.P.3
  • 36
    • 0036107683 scopus 로고    scopus 로고
    • Patented small molecule inhibitors of HIV-1 integrase: A 10-year saga
    • Neamati, N. Patented small molecule inhibitors of HIV-1 integrase: a 10-year saga. Expert Opin. Ther. Patents 2002, 12, 709-724.
    • (2002) Expert Opin. Ther. Patents , vol.12 , pp. 709-724
    • Neamati, N.1
  • 37
    • 0037434509 scopus 로고    scopus 로고
    • Design and synthesis of 8-hydroxy-[1,6]naphthyridines as novel inhibitors of HIV-1 integrase in vitro and in infected cells
    • Zhuang, L.; Wai, J. S.; Embrey, M. W.; Fisher, T. E.; Egbertson, M. S. et al. Design and synthesis of 8-hydroxy-[1,6]naphthyridines as novel inhibitors of HIV-1 integrase in vitro and in infected cells. J. Med. Chem. 2003, 46, 453-456.
    • (2003) J. Med. Chem. , vol.46 , pp. 453-456
    • Zhuang, L.1    Wai, J.S.2    Embrey, M.W.3    Fisher, T.E.4    Egbertson, M.S.5
  • 38
    • 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, J. A. 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, J.A.3
  • 39
    • 0034597625 scopus 로고    scopus 로고
    • Active site binding modes of HIV-1 integrase inhibitors
    • Sotriffer, C. A.; Ni, H.; McCammon, J. A. Active site binding modes of HIV-1 integrase inhibitors. J. Med. Chem. 2000, 43, 4109-4117.
    • (2000) J. Med. Chem. , vol.43 , pp. 4109-4117
    • Sotriffer, C.A.1    Ni, H.2    McCammon, J.A.3
  • 40
    • 0035855917 scopus 로고    scopus 로고
    • Ordered water and ligand mobility in the HIV-1 integrase-5CITEP complex: A molecular dynamics study
    • Ni, H.; Sotriffer, C. A.; McCammon, J. A. Ordered water and ligand mobility in the HIV-1 integrase-5CITEP complex: a molecular dynamics study. J. Med. Chem. 2001, 44, 3043-3047.
    • (2001) J. Med. Chem. , vol.44 , pp. 3043-3047
    • Ni, H.1    Sotriffer, C.A.2    McCammon, J.A.3
  • 41
    • 0041353616 scopus 로고    scopus 로고
    • Metal-dependent inhibitionof HIV-1 integrase by beta-diketo acids and resistance of the soluble double-mutant [F185K/C280S]
    • Marchand, C.; Johnson, A. A.; Karki, R. G.; Pais, G. C. G.; Zhang, X. et al. Metal-dependent inhibitionof HIV-1 integrase by beta-diketo acids and resistance of the soluble double-mutant [F185K/C280S]. Mol. Pharmacol. 2003, 64, 600-609
    • (2003) Mol. Pharmacol. , vol.64 , pp. 600-609
    • Marchand, C.1    Johnson, A.A.2    Karki, R.G.3    Pais, G.C.G.4    Zhang, X.5
  • 42
    • 0037130159 scopus 로고    scopus 로고
    • Structure Activity of 3-aryl-1,3-diketo-Containing Compounds as HIV-1 Integrase Inhibitors
    • Pais, G. C. G.; Zhang, X.; Marchand, C.; Neamati, N.; Cowansage, K. et al. Structure Activity of 3-aryl-1,3-diketo-Containing Compounds as HIV-1 Integrase Inhibitors. J. Med. Chem. 2002, 45, 3184-3194.
    • (2002) J. Med. Chem. , vol.45 , pp. 3184-3194
    • Pais, G.C.G.1    Zhang, X.2    Marchand, C.3    Neamati, N.4    Cowansage, K.5
  • 43
    • 3042711636 scopus 로고    scopus 로고
    • Antiviral Resistance to Diketo Acids is Associated with Mutations T66I, L74M and S230R in the HIV Integrase Gene presented at the 15th International Conference on Antiviral Research, Prague, Czech Republic
    • abstract 45
    • Witvrouw, M., Fikkert, V., Van Maele, B., Pannecouque, C., Neamati, N., Burke, T. R., Pais, G., De Clercq, E., Debyser, Z. Antiviral Resistance to Diketo Acids is Associated with Mutations T66I, L74M and S230R in the HIV Integrase Gene presented at the 15th International Conference on Antiviral Research, Prague, Czech Republic. Antiviral Res. 2002, 53, A18, abstract 45.
    • (2002) Antiviral Res. , vol.53 , Issue.A18
    • Witvrouw, M.1    Fikkert, V.2    Van Maele, B.3    Pannecouque, C.4    Neamati, N.5    Burke, T.R.6    Pais, G.7    De Clercq, E.8    Debyser, Z.9
  • 44
    • 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.; Witmer, M.; Grobler, J. 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, 11244-11249.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11244-11249
    • Espeseth, A.S.1    Felock, P.2    Wolfe, A.3    Witmer, M.4    Grobler, J.5
  • 45
    • 0035915338 scopus 로고    scopus 로고
    • Fully flexible low-mode docking: Application to induced fit in HIV integrase
    • Keseru, G. M.; Kolossvary, I. Fully flexible low-mode docking: application to induced fit in HIV integrase. J. Am. Chem. Soc. 2001, 123, 12708-12709.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12708-12709
    • Keseru, G.M.1    Kolossvary, I.2
  • 46
    • 0034727864 scopus 로고    scopus 로고
    • 4-Aryl-2,4-dioxobutanoic acid inhibitors of HIV-1 integrase and viral replication in cells
    • Wai, J. S.; Egbertson, M. S.; Payne, L. S.; Fisher, T. E.; Embrey, M. W. et al. 4-Aryl-2,4-dioxobutanoic acid inhibitors of HIV-1 integrase and viral replication in cells. J. Med. Chem. 2000, 43, 4923-4926.
    • (2000) J. Med. Chem. , vol.43 , pp. 4923-4926
    • Wai, J.S.1    Egbertson, M.S.2    Payne, L.S.3    Fisher, T.E.4    Embrey, M.W.5
  • 48
    • 1242294352 scopus 로고    scopus 로고
    • Design and Synthesis of Photoactivatable Aryl Diketo Acid-Containing HIV-1 Integrase Inhibitors as Potential Affinity Probes
    • Zhang, X.; Marchand, C.; Pommier, Y.; Burke, T. R., Jr. Design and Synthesis of Photoactivatable Aryl Diketo Acid-Containing HIV-1 Integrase Inhibitors as Potential Affinity Probes. Bioorg. Med. Chem. Lett. 2004, 14, 1205-1207.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 1205-1207
    • Zhang, X.1    Marchand, C.2    Pommier, Y.3    Burke Jr., T.R.4
  • 49
    • 0037076324 scopus 로고    scopus 로고
    • Diketo acid inhibitor mechanism and HIV-1 integrase: Implications for metal binding in the active site of phosphotransferase enzymes
    • Grobler, J. A.; Stillmock, K.; Hu, B.; Witmer, M.; Felock, P. et al. Diketo acid inhibitor mechanism and HIV-1 integrase: implications for metal binding in the active site of phosphotransferase enzymes. Proc. Natl. Acad. Sci. USA 2002, 99, 6661-6666.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6661-6666
    • Grobler, J.A.1    Stillmock, K.2    Hu, B.3    Witmer, M.4    Felock, P.5
  • 50
    • 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
  • 51
    • 0033856959 scopus 로고    scopus 로고
    • Viral entry as the primary target for the anti-HIV activity of chicoric acid and its tetra-acetyl esters
    • Pluymers, W.; Pannecouque, C.; Fikkert, V.; Neamati, N.; Marchand, C. et al. Viral entry as the primary target for the anti-HIV activity of chicoric acid and its tetra-acetyl esters. Mol. Pharmacol. 2000, 38, 641-648.
    • (2000) Mol. Pharmacol. , vol.38 , pp. 641-648
    • Pluymers, W.1    Pannecouque, C.2    Fikkert, V.3    Neamati, N.4    Marchand, C.5
  • 52
    • 10244260392 scopus 로고    scopus 로고
    • Dicaffeoylquinic acid inhibitors of human immunodeficiency virus integrase: Inhibition of the core catalytic domain of human immunodeficiency virus integrase
    • Robinson, W. E.; Cordeiro, M.; Abdel-Malek, S.; Jia, Q.; Chow, S. A. et al. Dicaffeoylquinic acid inhibitors of human immunodeficiency virus integrase: inhibition of the core catalytic domain of human immunodeficiency virus integrase. Mol. Pharmacol. 1996, 50, 846-855.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 846-855
    • Robinson, W.E.1    Cordeiro, M.2    Abdel-Malek, S.3    Jia, Q.4    Chow, S.A.5
  • 53
    • 0032972042 scopus 로고    scopus 로고
    • Structure-activity relationships: Analogues of the dicaffeoylquinic and dicaffeoyltartaric acids as potent inhibitors of human immunodeficiency virus type 1 integrase and replication
    • King, P. J.; Ma, G.; Miao, W.; Jia, Q.; McDougall, B. R. et al. Structure-activity relationships: analogues of the dicaffeoylquinic and dicaffeoyltartaric acids as potent inhibitors of human immunodeficiency virus type 1 integrase and replication. J. Med. Chem. 1999, 42, 497-509.
    • (1999) J. Med. Chem. , vol.42 , pp. 497-509
    • King, P.J.1    Ma, G.2    Miao, W.3    Jia, Q.4    McDougall, B.R.5
  • 54
    • 0037103344 scopus 로고    scopus 로고
    • Dicaffeoyltartaric Acid Analogues Inhibit Human Immunodeficiency Virus Type 1 (HIV-1) Integrase and HIV-1 Replication at Nontoxic Concentrations
    • Reinke, R. A.; King, P. J.; Victoria, J. G.; McDougall, B. R.; Ma, G. et al. Dicaffeoyltartaric Acid Analogues Inhibit Human Immunodeficiency Virus Type 1 (HIV-1) Integrase and HIV-1 Replication at Nontoxic Concentrations. J. Med. Chem. 2002, 45, 3669-3683.
    • (2002) J. Med. Chem. , vol.45 , pp. 3669-3683
    • Reinke, R.A.1    King, P.J.2    Victoria, J.G.3    McDougall, B.R.4    Ma, G.5
  • 55
    • 0034930519 scopus 로고    scopus 로고
    • Dicaffeoyl- or Digalloyl Pyrrolidine and Furan Derivatives as HIV Integrase Inhibitors
    • Hwang, D. J.; Kim, S. N.; Choi, J. H.; Lee, Y. S. Dicaffeoyl- or Digalloyl Pyrrolidine and Furan Derivatives as HIV Integrase Inhibitors. Dioorganic & Medicinal Chemistry 2001, 9, 1429-1437.
    • (2001) Dioorganic & Medicinal Chemistry , vol.9 , pp. 1429-1437
    • Hwang, D.J.1    Kim, S.N.2    Choi, J.H.3    Lee, Y.S.4
  • 57
    • 0030891930 scopus 로고    scopus 로고
    • Depside and depsidones as inhibitors of HIV-1 integrase: Discovery of novel inhibitors through 3D database searching
    • Neamati, N.; Hong, H.; Mazumder, A.; Wang, S.; Sunder, S. et al. Depside and depsidones as inhibitors of HIV-1 integrase: Discovery of novel inhibitors through 3D database searching. J. Med. Chem. 1997, 40, 942-951.
    • (1997) J. Med. Chem. , vol.40 , pp. 942-951
    • Neamati, N.1    Hong, H.2    Mazumder, A.3    Wang, S.4    Sunder, S.5
  • 58
    • 0034077984 scopus 로고    scopus 로고
    • A new class of HIV-1 integrase inhibitors: The 3,3, 3′,3′-tetramethyl-1,1′-spirobi[indan]-5,5′ ,6,6′-tetrol family
    • Molteni, V.; Rhodes, D.; Rubins, K.; Hansen, M.; Bushman, F. D. et al. A new class of HIV-1 integrase inhibitors: the 3,3, 3′,3′-tetramethyl-1,1′-spirobi[indan]-5,5′ ,6,6′-tetrol family. J. Med. Chem. 2000, 43, 2031-2039.
    • (2000) J. Med. Chem. , vol.43 , pp. 2031-2039
    • Molteni, V.1    Rhodes, D.2    Rubins, K.3    Hansen, M.4    Bushman, F.D.5
  • 59
    • 0031875905 scopus 로고    scopus 로고
    • Styrylquinoline derivatives: A new class of potent HIV-1 integrase inhibitors that block HIV-1 replication in CEM cells
    • Mekouar, K.; Mouscadet, J. F.; Desmaele, D.; Subra, F.; Leh, H. et al. Styrylquinoline derivatives: a new class of potent HIV-1 integrase inhibitors that block HIV-1 replication in CEM cells. J. Med. Chem. 1998, 41, 2846-2857.
    • (1998) J. Med. Chem. , vol.41 , pp. 2846-2857
    • Mekouar, K.1    Mouscadet, J.F.2    Desmaele, D.3    Subra, F.4    Leh, H.5
  • 60
    • 0034692178 scopus 로고    scopus 로고
    • Structure-Activity Relationships and Binding Mode of Styrylquinolines as Potent Inhibitors of HIV-1 Integrase and Replication of HIV-1 in Cell Culture
    • Zouhiri, F.; Mouscadet, J. F.; Mekouar, K.; Desmaele, D.; Savoure, D. et al. Structure-Activity Relationships and Binding Mode of Styrylquinolines as Potent Inhibitors of HIV-1 Integrase and Replication of HIV-1 in Cell Culture. J. Med. Chem. 2000, 43, 1533-1540.
    • (2000) J. Med. Chem. , vol.43 , pp. 1533-1540
    • Zouhiri, F.1    Mouscadet, J.F.2    Mekouar, K.3    Desmaele, D.4    Savoure, D.5
  • 62
    • 14444276046 scopus 로고    scopus 로고
    • Salicylhydrazine-containing inhibitors of HIV-1 integrase: Implication for a selective chelation in the integrase active site
    • Neamati, N.; Hong, H.; Owen, J. M.; Sunder, S.; Winslow, H. E. et al. Salicylhydrazine-containing inhibitors of HIV-1 integrase: implication for a selective chelation in the integrase active site. J. Med. Chem. 1998, 41, 3202-3209.
    • (1998) J. Med. Chem. , vol.41 , pp. 3202-3209
    • Neamati, N.1    Hong, H.2    Owen, J.M.3    Sunder, S.4    Winslow, H.E.5
  • 64
    • 0035904875 scopus 로고    scopus 로고
    • Synthesis and HIV-1 integrase inhibitory activities of catechol and bis- catechol derivatives
    • Dupont, R.; Jeanson, L.; Mouscadet, J. F.; Cotelle, P. Synthesis and HIV-1 integrase inhibitory activities of catechol and bis- catechol derivatives. Bioorg. Med. Chem. Lett. 2001, 11, 3175-3178.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 3175-3178
    • Dupont, R.1    Jeanson, L.2    Mouscadet, J.F.3    Cotelle, P.4
  • 65
    • 0033849102 scopus 로고    scopus 로고
    • Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors
    • Maurer, K.; Tang, A. H.; Kenyon, G. L.; Leavitt, A. D. Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors. Bio-Organic Chemistry 2000, 28, 140-155.
    • (2000) Bio-Organic Chemistry , vol.28 , pp. 140-155
    • Maurer, K.1    Tang, A.H.2    Kenyon, G.L.3    Leavitt, A.D.4
  • 66
    • 0037018483 scopus 로고    scopus 로고
    • Structure, stereochemistry, and biological activity of integramycin, a novel hexacyclic natural product produced by Actinoplanes sp. that inhibits HIV-1 integrase
    • Singh, S. B.; Zink, D. L.; Heimbach, B.; Genilloud, O.; Teran, A. et al. Structure, stereochemistry, and biological activity of integramycin, a novel hexacyclic natural product produced by Actinoplanes sp. that inhibits HIV-1 integrase. Org. Lett. 2002, 4, 1123-1126.
    • (2002) Org. Lett. , vol.4 , pp. 1123-1126
    • Singh, S.B.1    Zink, D.L.2    Heimbach, B.3    Genilloud, O.4    Teran, A.5
  • 67
    • 19044393246 scopus 로고    scopus 로고
    • Integramides A and B, two novel non-ribosomal linear peptides containing nine C[alpha]-methyl amino acids produced by fungal fermentations that are inhibitors of HIV-1 integrase
    • Singh, S. B.; Herath, K.; Guan, Z.; Zink, D. L.; Dombrowski, A. W. et al. Integramides A and B, two novel non-ribosomal linear peptides containing nine C[alpha]-methyl amino acids produced by fungal fermentations that are inhibitors of HIV-1 integrase. Org. Lett. 2002, 4, 1431-1434.
    • (2002) Org. Lett. , vol.4 , pp. 1431-1434
    • Singh, S.B.1    Herath, K.2    Guan, Z.3    Zink, D.L.4    Dombrowski, A.W.5
  • 68
    • 0034899584 scopus 로고    scopus 로고
    • The complestatins as HIV-1 integrase inhibitors. Efficient isolation, structure elucidation, and inhibitory activities of isocomplestatin, chloropeptin I, new complestatins, A and B, and acid-hydrolysis products of chloropeptin I
    • Singh, S. B.; Jayasuriya, H.; Salituro, G. M.; Zink, D. L.; Shafiee, A. et al. The complestatins as HIV-1 integrase inhibitors. Efficient isolation, structure elucidation, and inhibitory activities of isocomplestatin, chloropeptin I, new complestatins, A and B, and acid-hydrolysis products of chloropeptin I. J. Nat. Prod. 2001, 64, 874-882.
    • (2001) J. Nat. Prod. , vol.64 , pp. 874-882
    • Singh, S.B.1    Jayasuriya, H.2    Salituro, G.M.3    Zink, D.L.4    Shafiee, A.5
  • 69
    • 0037170622 scopus 로고    scopus 로고
    • Integrastatins: Structure and HIV-1 integrase inhibitory activities of two novel racemic tetracyclic aromatic heterocycles produced by two fungal species
    • Singh, S. B.; Zink, D. L.; Quamina, D. S.; Pelaez, F.; Teran, A.; Felock, P.; Hazuda, D. Integrastatins: structure and HIV-1 integrase inhibitory activities of two novel racemic tetracyclic aromatic heterocycles produced by two fungal species. Tetrahedron Letters 2002, 43, 2351-2354.
    • (2002) Tetrahedron Letters , vol.43 , pp. 2351-2354
    • Singh, S.B.1    Zink, D.L.2    Quamina, D.S.3    Pelaez, F.4    Teran, A.5    Felock, P.6    Hazuda, D.7
  • 70
  • 71
    • 0018834106 scopus 로고
    • Inhibition of the alternative pathway of human complement in vitro by a natural microbial product, complestatin
    • Kaneko, I.; Fearon, D. T.; Austen, K. F. Inhibition of the alternative pathway of human complement in vitro by a natural microbial product, complestatin. J. Immunol. 1980, 124, 1194-1198.
    • (1980) J. Immunol. , vol.124 , pp. 1194-1198
    • Kaneko, I.1    Fearon, D.T.2    Austen, K.F.3
  • 72
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow, S. A.; Vincent, K. A.; Ellison, V.; Brown, P. O. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 1992, 255, 723-726.
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 73
    • 0036728958 scopus 로고    scopus 로고
    • Sesquiterpenes and alkaloids from Lindera chunii and their inhibitory activities against HIV-1 integrase
    • Zhang, C. F.; Nakamura, N.; Tewtrakul, S.; Hattori, M.; Sun, Q. S. et al. Sesquiterpenes and alkaloids from Lindera chunii and their inhibitory activities against HIV-1 integrase. Chem. Pharm. Bull. (Tokyo) 2002, 50, 1195-1200.
    • (2002) Chem. Pharm. Bull. (Tokyo) , vol.50 , pp. 1195-1200
    • Zhang, C.F.1    Nakamura, N.2    Tewtrakul, S.3    Hattori, M.4    Sun, Q.S.5
  • 74
    • 0036836956 scopus 로고    scopus 로고
    • Thalassiolins A-C: New marine-derived inhibitors of HIV cDNA integrase
    • Rowley, D. C.; Hansen, M. S.; Rhodes, D.; Sotriffer, C. A.; Ni, H. et al. Thalassiolins A-C: new marine-derived inhibitors of HIV cDNA integrase. Bioorg. Med. Chem. 2002, 10, 3619-3625.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3619-3625
    • Rowley, D.C.1    Hansen, M.S.2    Rhodes, D.3    Sotriffer, C.A.4    Ni, H.5
  • 75
    • 0035997934 scopus 로고    scopus 로고
    • Isolation of two highly potent and non-toxic inhibitors of human immunodeficiency virus type 1 (HIV-1) integrase from Salvia miltiorrhiza
    • Abd-Elazem, I. S.; Chen, H. S.; Bates, R. B.; Huang, R. C. C. Isolation of two highly potent and non-toxic inhibitors of human immunodeficiency virus type 1 (HIV-1) integrase from Salvia miltiorrhiza. Antiviral Res. 2002, 55, 91-106.
    • (2002) Antiviral Res. , vol.55 , pp. 91-106
    • Abd-Elazem, I.S.1    Chen, H.S.2    Bates, R.B.3    Huang, R.C.C.4
  • 76
    • 0037294186 scopus 로고    scopus 로고
    • Four novel bis-(naphtho-gamma-pyrones) isolated from Fusarium species as inhibitors of HIV-1 integrase
    • Singh, S. B.; Zink, D. L.; Bills, G. F.; Teran, A.; Silverman, K. C. et al. Four novel bis-(naphtho-gamma-pyrones) isolated from Fusarium species as inhibitors of HIV-1 integrase. Bioorg. Med. Chem. Lett. 2003, 13, 713-717.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 713-717
    • Singh, S.B.1    Zink, D.L.2    Bills, G.F.3    Teran, A.4    Silverman, K.C.5
  • 77
    • 0029557124 scopus 로고
    • Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library
    • Puras Lutzke, R. A.; Eppens, N. A.; Weber, P. A.; Houghten, R. A.; Plasterk, R. H. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. Proc. Natl. Acad. Sci. USA 1995, 92, 11456-11460.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11456-11460
    • Puras Lutzke, R.A.1    Eppens, N.A.2    Weber, P.A.3    Houghten, R.A.4    Plasterk, R.H.5
  • 78
    • 3042800435 scopus 로고    scopus 로고
    • Tryptophan-rich integrase inhibitory peptides and peptidomimetics
    • EDK: Paris
    • Roller, P. P.; Long, Y.-Q.; Lung, F.-D. T.; Pommier, Y.; Neamati, N. Tryptophan-rich integrase inhibitory peptides and peptidomimetics. Peptides 2000; EDK: Paris, 2001; pp 725-726.
    • (2001) Peptides 2000 , pp. 725-726
    • Roller, P.P.1    Long, Y.-Q.2    Lung, F.-D.T.3    Pommier, Y.4    Neamati, N.5
  • 79
    • 0035923394 scopus 로고    scopus 로고
    • Peptide inhibitors of HIV-1 integrase dissociate the enzyme oligomers
    • Maroun, R. G.; Gayet, S.; Benleulmi, M. S.; Porumb, H.; Zargarian, L. et al. Peptide inhibitors of HIV-1 integrase dissociate the enzyme oligomers. Biochemistry 2001, 40, 13840-13848.
    • (2001) Biochemistry , vol.40 , pp. 13840-13848
    • Maroun, R.G.1    Gayet, S.2    Benleulmi, M.S.3    Porumb, H.4    Zargarian, L.5
  • 80
    • 0029743107 scopus 로고    scopus 로고
    • A synthetic peptide from the human immunodeficiency virus type-1 integrase exhibits coiled-coil properties and interferes with the in vitro integration activity of the enzyme. Correlated biochemical and spectroscopic results
    • Sourgen, F.; Maroun, R. G.; Frere, V.; Bouziane, M.; Auclair, C. et al. A synthetic peptide from the human immunodeficiency virus type-1 integrase exhibits coiled-coil properties and interferes with the in vitro integration activity of the enzyme. Correlated biochemical and spectroscopic results. Eur. J. Biochem. 1996, 240, 765-773.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 765-773
    • Sourgen, F.1    Maroun, R.G.2    Frere, V.3    Bouziane, M.4    Auclair, C.5
  • 81
    • 0035106282 scopus 로고    scopus 로고
    • Self-association of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by electro spray ionization mass spectrometry in trifluoroethanol/water mixtures
    • Fermandjian, S.; Maroun, R. S.; Amekraz, B.; Jankowski, C. K. Self-association of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by electro spray ionization mass spectrometry in trifluoroethanol/water mixtures. Rapid Commun. Mass Spectrom. 2001, 15, 320-324.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 320-324
    • Fermandjian, S.1    Maroun, R.S.2    Amekraz, B.3    Jankowski, C.K.4
  • 82
    • 0033557819 scopus 로고    scopus 로고
    • Conformational aspects of HIV-1 integrase inhibition by a peptide derived from the enzyme central domain and by antibodies raised against this peptide
    • Maroun, R. G.; Krebs, D.; Roshani, M.; Porumb, H.; Auclair, C. et al. Conformational aspects of HIV-1 integrase inhibition by a peptide derived from the enzyme central domain and by antibodies raised against this peptide. Eur. J. Biochem. 1999, 260, 145-155.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 145-155
    • Maroun, R.G.1    Krebs, D.2    Roshani, M.3    Porumb, H.4    Auclair, C.5
  • 84
    • 0028097285 scopus 로고
    • Monoclonal antibodies against HIV type 1 integrase: Clues to molecular structure
    • Bizub-Bender, D.; Kulkosky, J.; Skalka, A. M. Monoclonal antibodies against HIV type 1 integrase: clues to molecular structure. AIDS. Res. Hum. Retrov. 1994, 10, 1105-1115.
    • (1994) AIDS Res. Hum. Retrov. , vol.10 , pp. 1105-1115
    • Bizub-Bender, D.1    Kulkosky, J.2    Skalka, A.M.3
  • 85
    • 0030922072 scopus 로고    scopus 로고
    • A metal-induced conformational change and activation of HIV-1 integrase
    • Asante-Appiah, E.; Skalka, A. M. A metal-induced conformational change and activation of HIV-1 integrase. J. Biol. Chem. 1997, 272, 16196-16205.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16196-16205
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 86
    • 0034623997 scopus 로고    scopus 로고
    • An inhibitory monoclonal antibody binds at the turn of the helix-turn-helix motif in the N-terminal domain of HIV-1 integrase
    • Yi, J.; Arthur, J. W.; Dunbrack, R. L., Jr.; Skalka, A. M. An inhibitory monoclonal antibody binds at the turn of the helix-turn-helix motif in the N-terminal domain of HIV-1 integrase. J. Biol. Chem. 2000, 275, 38739-38748.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38739-38748
    • Yi, J.1    Arthur, J.W.2    Dunbrack Jr., R.L.3    Skalka, A.M.4
  • 87
    • 0037023718 scopus 로고    scopus 로고
    • Mapping the epitope of an inhibitory monoclonal antibody to the C- terminal DNA-binding domain of HIV-1 integrase
    • Yi, J.; Cheng, H.; Andrake, M. D.; Dunbrack, R. L., Jr.; Roder, H. et al. Mapping the epitope of an inhibitory monoclonal antibody to the C- terminal DNA-binding domain of HIV-1 integrase. J. Biol. Chem. 2002, 277, 12164-12174.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12164-12174
    • Yi, J.1    Cheng, H.2    Andrake, M.D.3    Dunbrack Jr., R.L.4    Roder, H.5
  • 88
    • 0032938325 scopus 로고    scopus 로고
    • Inhibition of HIV-1 by an anti-integrase single-chain variable fragment [SFv]: Delivery by SV40 provides durable protection against HIV-1 and does not require selection
    • BouHamdan, M.; Duan, L. X.; Pomerantz, R. J.; Strayer, D. S. Inhibition of HIV-1 by an anti-integrase single-chain variable fragment [SFv]: delivery by SV40 provides durable protection against HIV-1 and does not require selection. Gene Ther. 1999, 6, 660-666.
    • (1999) Gene Ther. , vol.6 , pp. 660-666
    • BouHamdan, M.1    Duan, L.X.2    Pomerantz, R.J.3    Strayer, D.S.4
  • 89
    • 0033925327 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication and infectivity by expression of a fusion protein, VPR-anti-integrase single-chain variable fragment [SFv]: Intravirion molecular therapies
    • BouHamdan, M.; Kulkosky, J.; Duan, L. X.; Pomerantz, R. J. Inhibition of HIV-1 replication and infectivity by expression of a fusion protein, VPR-anti-integrase single-chain variable fragment [SFv]: intravirion molecular therapies. J. Hum. Virol. 2000, 3, 6-15.
    • (2000) J. Hum. Virol. , vol.3 , pp. 6-15
    • BouHamdan, M.1    Kulkosky, J.2    Duan, L.X.3    Pomerantz, R.J.4
  • 90
    • 10344256143 scopus 로고    scopus 로고
    • Intracellular expression of single-chain variable fragments to inhibit early stages of the viral life cycle by targeting human immunodeficiency virus type 1 integrase
    • Levy-Mintz, P.; Duan, L.; Zhang, H.; Hu, B.; Dornadula, G. et al. Intracellular expression of single-chain variable fragments to inhibit early stages of the viral life cycle by targeting human immunodeficiency virus type 1 integrase. J. Virol. 1996, 70, 8821-8832.
    • (1996) J. Virol. , vol.70 , pp. 8821-8832
    • Levy-Mintz, P.1    Duan, L.2    Zhang, H.3    Hu, B.4    Dornadula, G.5
  • 91
    • 0032553365 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 replication in chronically infected monocytes and lymphocytes by retrovirus-mediated gene transfer of anti-Rev single- chain variable fragments
    • Ho, W. Z.; Lai, J. P.; Bouhamdan, M.; Duan, L.; Pomerantz, R. J. et al. Inhibition of HIV type 1 replication in chronically infected monocytes and lymphocytes by retrovirus-mediated gene transfer of anti-Rev single- chain variable fragments. AIDS Res. Hum. Retroviruses 1998, 14, 1573-1580.
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , pp. 1573-1580
    • Ho, W.Z.1    Lai, J.P.2    Bouhamdan, M.3    Duan, L.4    Pomerantz, R.J.5
  • 92
    • 0035078877 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infection by down-regulation of the CXCR4 co- receptor using an intracellular single chain variable fragment against CXCR4
    • BouHamdan, M.; Strayer, D. S.; Wei, D.; Mukhtar, M.; Duan, L. X. et al. Inhibition of HIV-1 infection by down-regulation of the CXCR4 co- receptor using an intracellular single chain variable fragment against CXCR4. Gene Ther. 2001, 8, 408-418.
    • (2001) Gene Ther. , vol.8 , pp. 408-418
    • BouHamdan, M.1    Strayer, D.S.2    Wei, D.3    Mukhtar, M.4    Duan, L.X.5
  • 94
    • 0037093953 scopus 로고    scopus 로고
    • Gene therapy using a simian virus 40-derived vector inhibits the development of in vivo human immunodeficiency virus type 1 infection of severe combined immunodeficiency mice implanted with human fetal thymic and liver tissue
    • Goldstein, H.; Pettoello-Mantovani, M.; Anderson, C. M.; Cordelier, P.; Pomerantz, R. J. et al. Gene therapy using a simian virus 40-derived vector inhibits the development of in vivo human immunodeficiency virus type 1 infection of severe combined immunodeficiency mice implanted with human fetal thymic and liver tissue. J. Infect. Dis. 2002, 185, 1425-1430.
    • (2002) J. Infect. Dis. , vol.185 , pp. 1425-1430
    • Goldstein, H.1    Pettoello-Mantovani, M.2    Anderson, C.M.3    Cordelier, P.4    Pomerantz, R.J.5
  • 96
    • 0037022202 scopus 로고    scopus 로고
    • Disruption of HIV-1 integrase-DNA complexes by short 6-oxocytosine-containing oligonucleotides
    • Brodin, P.; Pinskaya, M.; Buckle, M.; Parsch, U.; Romanova, E. et al. Disruption of HIV-1 integrase-DNA complexes by short 6-oxocytosine-containing oligonucleotides. Biochemistry 2002, 41, 1529-1538.
    • (2002) Biochemistry , vol.41 , pp. 1529-1538
    • Brodin, P.1    Pinskaya, M.2    Buckle, M.3    Parsch, U.4    Romanova, E.5
  • 97
    • 0036436802 scopus 로고    scopus 로고
    • DNA aptamers derived from HIV-1 RNase H inhibitors are strong anti-integrase agents
    • de Soultrait, V. R.; Lozach, P. Y.; Altmeyer, R.; Tarrago-Litvak, L.; Litvak, S. et al. DNA aptamers derived from HIV-1 RNase H inhibitors are strong anti-integrase agents. J. Mol. Biol. 2002, 324, 195-203.
    • (2002) J. Mol. Biol. , vol.324 , pp. 195-203
    • de Soultrait, V.R.1    Lozach, P.Y.2    Altmeyer, R.3    Tarrago-Litvak, L.4    Litvak, S.5
  • 98
    • 0029964978 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by guanosine quartet structures
    • Mazumder, A.; Neamati, N.; Ojwang, J. O.; Sunder, S.; Rando, R. F. et al. Inhibition of human immunodeficiency virus type 1 integrase by guanosine quartet structures. Biochemistry 1996, 43, 13762-13771.
    • (1996) Biochemistry , vol.43 , pp. 13762-13771
    • Mazumder, A.1    Neamati, N.2    Ojwang, J.O.3    Sunder, S.4    Rando, R.F.5
  • 99
    • 0030832691 scopus 로고    scopus 로고
    • Mode of interaction of G-quartets with the integrase of human immunodeficiency virus type 1
    • Cherepanov, P.; Este, J. A.; Rando, R. F.; Ojwang, J. O.; Reekmans, G. et al. Mode of interaction of G-quartets with the integrase of human immunodeficiency virus type 1. Mol. Pharmacol. 1997, 52, 771-780.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 771-780
    • Cherepanov, P.1    Este, J.A.2    Rando, R.F.3    Ojwang, J.O.4    Reekmans, G.5
  • 100
    • 0034647554 scopus 로고    scopus 로고
    • Mechanism of inhibition of HIV-1 integrase by G-tetrad-forming oligonucleotides in Vitro
    • Jing, N.; Marchand, C.; Liu, J.; Mitra, R.; Hogan, M. E. et al. Mechanism of inhibition of HIV-1 integrase by G-tetrad-forming oligonucleotides in Vitro. J. Biol. Chem. 2000, 275, 21460-21467.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21460-21467
    • Jing, N.1    Marchand, C.2    Liu, J.3    Mitra, R.4    Hogan, M.E.5
  • 101
    • 0037197675 scopus 로고    scopus 로고
    • Potassium-dependent folding: A key to intracellular delivery of G- quartet oligonucleotides as HIV inhibitors
    • Jing, N.; Xiong, W.; Guan, Y.; Pallansch, L.; Wang, S. Potassium-dependent folding: a key to intracellular delivery of G- quartet oligonucleotides as HIV inhibitors. Biochemistry 2002, 41, 5397-5403.
    • (2002) Biochemistry , vol.41 , pp. 5397-5403
    • Jing, N.1    Xiong, W.2    Guan, Y.3    Pallansch, L.4    Wang, S.5
  • 102
    • 0034120379 scopus 로고    scopus 로고
    • Modeling of the inhibition of retroviral integrases by styrylquinoline derivatives
    • Ouali, M.; Laboulais, C.; Leh, H.; Gill, D.; Desmaele, D. et al. Modeling of the inhibition of retroviral integrases by styrylquinoline derivatives. J. Med. Chem. 2000, 43, 1949-1957.
    • (2000) J. Med. Chem. , vol.43 , pp. 1949-1957
    • Ouali, M.1    Laboulais, C.2    Leh, H.3    Gill, D.4    Desmaele, D.5
  • 103
    • 0037162281 scopus 로고    scopus 로고
    • New class of HIV integrase inhibitors that block viral replication in cell culture
    • Pannecouque, C.; Pluymers, W.; Van Maele, B.; Tetz, V.; Cherepanov, P. et al. New class of HIV integrase inhibitors that block viral replication in cell culture. Curr. Biol. 2002, 12, 1169-1177.
    • (2002) Curr. Biol. , vol.12 , pp. 1169-1177
    • Pannecouque, C.1    Pluymers, W.2    Van Maele, B.3    Tetz, V.4    Cherepanov, P.5
  • 104
    • 0032054082 scopus 로고    scopus 로고
    • Helical and coiled-coil-forming properties of peptides derived from and inhibiting human immunodeficiency virus type 1 integrase assessed by 1H- NMR-use of NH temperature coefficients to probe coiled-coil structures
    • Krebs, D.; Maroun, R. G.; Sourgen, F.; Troalen, F.; Davoust, D. et al. Helical and coiled-coil-forming properties of peptides derived from and inhibiting human immunodeficiency virus type 1 integrase assessed by 1H- NMR-use of NH temperature coefficients to probe coiled-coil structures. Eur. J. Biochem. 1998, 253, 236-244.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 236-244
    • Krebs, D.1    Maroun, R.G.2    Sourgen, F.3    Troalen, F.4    Davoust, D.5


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