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Volumn 52, Issue C, 1999, Pages 427-458

Inhibitors of Human Immunodeficiency Virus Integrase

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRASE; INTEGRASE INHIBITOR; VIRUS DNA;

EID: 0032611358     PISSN: 00653527     EISSN: 15578399     Source Type: Book Series    
DOI: 10.1016/S0065-3527(08)60310-3     Document Type: Article
Times cited : (105)

References (150)
  • 1
    • 0002915381 scopus 로고
    • Retroviruses.
    • D. Berg M. Howe Am. Soc. Microbiol. Washington, DC
    • Varmus, H., Brown, P., Retroviruses. Berg, D., Howe, M., (eds.) Mobile DNA, 1989, Am. Soc. Microbiol., Washington, DC, 53–108.
    • (1989) Mobile DNA , pp. 53-108
    • Varmus, H.1    Brown, P.2
  • 3
    • 0001363865 scopus 로고    scopus 로고
    • Integration.
    • J.M. Coffin S.H. Hughes H.E. Varmus Cold Spring Harbor Press Cold Spring Harbor, N.Y.
    • Brown, P.O., Integration. Coffin, J.M., Hughes, S.H., Varmus, H.E., (eds.) Retroviruses, 1998, Cold Spring Harbor Press, Cold Spring Harbor, N.Y., 161–203.
    • (1998) Retroviruses , pp. 161-203
    • Brown, P.O.1
  • 4
    • 0031214288 scopus 로고    scopus 로고
    • In vitro assays for activities of retroviral integrase.
    • Chow, S.A., In vitro assays for activities of retroviral integrase. Methods: Companion to Methods Enzymol. 12 (1997), 306–317.
    • (1997) Methods: Companion to Methods Enzymol. , vol.12 , pp. 306-317
    • Chow, S.A.1
  • 5
    • 0008293521 scopus 로고    scopus 로고
    • Retroviral integrase: A novel target in antiviral development; basic in vitro assays with the purified enzyme.
    • D. Kinchington R. Schinazi Humana Press Totowa, NJ
    • Mazumder, A., Neamati, N., Sunder, S., Owen, J., Pommier, Y., Retroviral integrase: A novel target in antiviral development; basic in vitro assays with the purified enzyme. Kinchington, D., Schinazi, R., (eds.) Methods in Cellular and Molecular Biology: Antiviral Evaluation, 1998, Humana Press, Totowa, NJ.
    • (1998) Methods in Cellular and Molecular Biology: Antiviral Evaluation
    • Mazumder, A.1    Neamati, N.2    Sunder, S.3    Owen, J.4    Pommier, Y.5
  • 6
    • 0031434606 scopus 로고    scopus 로고
    • Molecular mechanisms in retrovirus DNA integration.
    • Asante-Appiah, E., Skalka, A.M., Molecular mechanisms in retrovirus DNA integration. Antiviral Res. 36 (1997), 139–156.
    • (1997) Antiviral Res. , vol.36 , pp. 139-156
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 8
    • 0030855938 scopus 로고    scopus 로고
    • Design and discovery of HIV-1 integrase inhibitors.
    • Neamati, N., Sunder, S., Pommier, Y., Design and discovery of HIV-1 integrase inhibitors. Drug Discovery Today 2 (1997), 487–498.
    • (1997) Drug Discovery Today , vol.2 , pp. 487-498
    • Neamati, N.1    Sunder, S.2    Pommier, Y.3
  • 10
    • 0029166510 scopus 로고
    • Processing of deoxyuridine mismatches and abasic sites by human immunodeficiency virus type I integrase.
    • Mazumder, A., Pommier, Y., Processing of deoxyuridine mismatches and abasic sites by human immunodeficiency virus type I integrase. Nucleic Acids Res. 23 (1995), 2865–2871.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2865-2871
    • Mazumder, A.1    Pommier, Y.2
  • 11
    • 0026095906 scopus 로고
    • Human immunodeficiency virus integrase protein requires a subterminal position for its viral DNA recognition sequence for efficient cleavage.
    • Vink, C, van Gent, D.C., Elgersma, Y., Plasterk, R.H.A., Human immunodeficiency virus integrase protein requires a subterminal position for its viral DNA recognition sequence for efficient cleavage. J. Virol. 65 (1991), 4636–4644.
    • (1991) J. Virol. , vol.65 , pp. 4636-4644
    • Vink, C.1    van Gent, D.C.2    Elgersma, Y.3    Plasterk, R.H.A.4
  • 12
    • 0031935582 scopus 로고    scopus 로고
    • Mapping viral DNA specificity to the central region of integrase by using functional human immunodeficiency virus type 1/Visna virus chimeric proteins.
    • Katzman, M., Sudol, M., Mapping viral DNA specificity to the central region of integrase by using functional human immunodeficiency virus type 1/Visna virus chimeric proteins. J. Virol. 72 (1998), 1744–1753.
    • (1998) J. Virol. , vol.72 , pp. 1744-1753
    • Katzman, M.1    Sudol, M.2
  • 13
    • 0029861955 scopus 로고    scopus 로고
    • Influence of subterminal viral DNA nucleotide on differential susceptibility to cleavage by human immunodeficiency virus type 1 and visna virus integrases.
    • Katzman, M., Sudol, M., Influence of subterminal viral DNA nucleotide on differential susceptibility to cleavage by human immunodeficiency virus type 1 and visna virus integrases. J. Virol. 70 (1996), 9069–9073.
    • (1996) J. Virol. , vol.70 , pp. 9069-9073
    • Katzman, M.1    Sudol, M.2
  • 14
    • 0032576722 scopus 로고    scopus 로고
    • Recognition of the four Watson-Crick base pairs in the DNA minor groove by synthetic ligands.
    • White, S., Szewczyk, J.W., Turner, J.M., Baird, E.E., Dervan, P.B., Recognition of the four Watson-Crick base pairs in the DNA minor groove by synthetic ligands. Nature (London) 391 (1998), 468–470.
    • (1998) Nature (London) , vol.391 , pp. 468-470
    • White, S.1    Szewczyk, J.W.2    Turner, J.M.3    Baird, E.E.4    Dervan, P.B.5
  • 15
    • 0031820936 scopus 로고    scopus 로고
    • Highly potent synthetic polyamines, bisdistamycins and lexitropsins as inhibitors of human immunodeficiency virus type 1 integrase.
    • Neamati, N., Mazumder, A., Sunder, S., Owen, J.M., Tandon, M., Lown, J.W., Pommier, Y., Highly potent synthetic polyamines, bisdistamycins and lexitropsins as inhibitors of human immunodeficiency virus type 1 integrase. Mol. Pharmacol. 54 (1998), 280–290.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 280-290
    • Neamati, N.1    Mazumder, A.2    Sunder, S.3    Owen, J.M.4    Tandon, M.5    Lown, J.W.6    Pommier, Y.7
  • 17
    • 0028288222 scopus 로고
    • Triple helix formation with short oligonucleotide-intercalator conjugates matching the HIV-1 U3 LTR end sequence.
    • Mouscadet, J.-F., Ketterlé, C., Goulaouic, H., Carteau, S., Subra, F., Le Bret, M., Auclair, C., Triple helix formation with short oligonucleotide-intercalator conjugates matching the HIV-1 U3 LTR end sequence. Biochemistry 33 (1994), 4187–4196.
    • (1994) Biochemistry , vol.33 , pp. 4187-4196
    • Mouscadet, J.-F.1    Ketterlé, C.2    Goulaouic, H.3    Carteau, S.4    Subra, F.5    Le Bret, M.6    Auclair, C.7
  • 18
    • 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. U.S.A. 91 (1994), 7316–7320.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 19
    • 0032562165 scopus 로고    scopus 로고
    • Displacement of viral DNA termini from stable HIV-1 integrase nucleoprotein complexes induced by secondary DNA-binding interactions.
    • Pemberton, I.K., Buc, H., Buckle, M., Displacement of viral DNA termini from stable HIV-1 integrase nucleoprotein complexes induced by secondary DNA-binding interactions. Biochemistry 37 (1998), 2682–2690.
    • (1998) Biochemistry , vol.37 , pp. 2682-2690
    • Pemberton, I.K.1    Buc, H.2    Buckle, M.3
  • 20
    • 0030051081 scopus 로고    scopus 로고
    • The role of manganese in promoting multimerization and assembly of human immunodeficiency type 1 integrase as a catalytically active complex on immobilized long terminal repeat substrates.
    • Wolfe, A.L., Felock, P.J., Hastings, H.C., Uncapher Blau, C., Hazuda, D., The role of manganese in promoting multimerization and assembly of human immunodeficiency type 1 integrase as a catalytically active complex on immobilized long terminal repeat substrates. J. Virol. 70 (1996), 1424–1432.
    • (1996) J. Virol. , vol.70 , pp. 1424-1432
    • Wolfe, A.L.1    Felock, P.J.2    Hastings, H.C.3    Uncapher Blau, C.4    Hazuda, D.5
  • 21
    • 85023063958 scopus 로고
    • Characterization of a stable HIV integrase-viral DNA complex: an early intermediate in the integration pathway.
    • Ellison, V., Vincent, K.A., Brown, P.O., Characterization of a stable HIV integrase-viral DNA complex: an early intermediate in the integration pathway. J. Cell. Biochem., 18B, 1994, 19.
    • (1994) J. Cell. Biochem. , vol.18B , pp. 19
    • Ellison, V.1    Vincent, K.A.2    Brown, P.O.3
  • 22
    • 0025337327 scopus 로고
    • Human immunodeficiency in a cell-free system.
    • Ellison, V., Abrams, H., Roe, T., Lifson, J., Brown, P., Human immunodeficiency in a cell-free system. J. Virol. 64 (1990), 2711–2715.
    • (1990) J. Virol. , vol.64 , pp. 2711-2715
    • Ellison, V.1    Abrams, H.2    Roe, T.3    Lifson, J.4    Brown, P.5
  • 23
    • 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 36 (1997), 10655–10665.
    • (1997) Biochemistry , vol.36 , pp. 10655-10665
    • Heuer, T.S.1    Brown, P.O.2
  • 24
    • 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. 16 (1997), 6849–6859.
    • (1997) EMBO J. , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 26
    • 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., Pommier, Y., Inhibition of human immunodeficiency virus type 1 integrase by guanosine quartet structures. Biochemistry 43 (1996), 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    Pommier, Y.6
  • 28
    • 0028242724 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by 3′-azido-3′-deoxythymi-dylate.
    • Mazumder, A., Cooney, D., Agbaria, R., Gupta, M., Pommier, Y., Inhibition of human immunodeficiency virus type 1 integrase by 3′-azido-3′-deoxythymi-dylate. Proc. Natl. Acad. Sci. U.S.A. 91 (1994), 5771–5775.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5771-5775
    • Mazumder, A.1    Cooney, D.2    Agbaria, R.3    Gupta, M.4    Pommier, Y.5
  • 29
    • 0028171531 scopus 로고
    • Nucleotide binding by the HIV-1 integrase protein in vitro.
    • Lipford, J.R., Worland, S.T., Farnet, C.M., Nucleotide binding by the HIV-1 integrase protein in vitro. J. AIDS 7 (1994), 1215–1223.
    • (1994) J. AIDS , vol.7 , pp. 1215-1223
    • Lipford, J.R.1    Worland, S.T.2    Farnet, C.M.3
  • 32
    • 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. 185 (1992), 85–90.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 85-90
    • Cushman, M.1    Sherman, P.2
  • 34
    • 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. 305 (1993), 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
  • 36
    • 0031060473 scopus 로고    scopus 로고
    • Equivalent inhibition of half-site and full-site retroviral strand transfer reactions by structurally diverse compounds.
    • Hazuda, D., Felock, P., Hastings, J., Pramanik, B., Wolfe, A., Goodarzi, G., Vora, A., Brackmann, K., Grandgenett, D., Equivalent inhibition of half-site and full-site retroviral strand transfer reactions by structurally diverse compounds. J. Virol. 71 (1997), 807–811.
    • (1997) J. Virol. , vol.71 , pp. 807-811
    • Hazuda, D.1    Felock, P.2    Hastings, J.3    Pramanik, B.4    Wolfe, A.5    Goodarzi, G.6    Vora, A.7    Brackmann, K.8    Grandgenett, D.9
  • 37
    • 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 (Cambridge, Mass.) 67 (1991), 1211–1221.
    • (1991) Cell (Cambridge, Mass.) , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 38
    • 0026348879 scopus 로고
    • Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein.
    • Vink, C., Yeheskiely, E., van der Marel, G.A., Van Boom, J.H., Plasterk, R.H.A., Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein. Nucleic Acids Res. 19 (1991), 6691–6698.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6691-6698
    • Vink, C.1    Yeheskiely, E.2    van der Marel, G.A.3    Van Boom, J.H.4    Plasterk, R.H.A.5
  • 39
    • 0029993527 scopus 로고    scopus 로고
    • Nonspecific alcoholysis, a novel endonuclease activity of human immunodeficiency virus type 1 and other retroviral integrases.
    • Katzman, M., Sudol, M., Nonspecific alcoholysis, a novel endonuclease activity of human immunodeficiency virus type 1 and other retroviral integrases. J. Virol. 70 (1996), 2598–2604.
    • (1996) J. Virol. , vol.70 , pp. 2598-2604
    • Katzman, M.1    Sudol, M.2
  • 41
    • 0028070994 scopus 로고
    • Inhibition of HIV-1 integrase by flavones, caffeic acid phenethyl ester (CAPE) and related compounds.
    • Fesen, M.R., Pommier, Y., Leteurtre, F., Hiroguchi, S., Yung, J., Kohn, K.W., Inhibition of HIV-1 integrase by flavones, caffeic acid phenethyl ester (CAPE) and related compounds. Biochem. Pharmacol. 48 (1994), 595–608.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 595-608
    • Fesen, M.R.1    Pommier, Y.2    Leteurtre, F.3    Hiroguchi, S.4    Yung, J.5    Kohn, K.W.6
  • 42
    • 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 255 (1992), 723–726.
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 43
    • 0031032592 scopus 로고    scopus 로고
    • 3′-End processing and kinetics of 5′-end joining during retroviral integration in vivo.
    • Roe, T., Chow, S.A., Brown, P.O., 3′-End processing and kinetics of 5′-end joining during retroviral integration in vivo. J. Virol. 71 (1997), 1334–1340.
    • (1997) J. Virol. , vol.71 , pp. 1334-1340
    • Roe, T.1    Chow, S.A.2    Brown, P.O.3
  • 44
    • 0031887358 scopus 로고    scopus 로고
    • Efficient gap repair catalyzed in vitro by an intrinsic DNA polymerase activity of human immunodeficiency virus type 1 integrase.
    • Acel, A., Udashkin, B.E., Wainberg, M.A., Faust, E.A., Efficient gap repair catalyzed in vitro by an intrinsic DNA polymerase activity of human immunodeficiency virus type 1 integrase. J. Virol. 72 (1998), 2062–2071.
    • (1998) J. Virol. , vol.72 , pp. 2062-2071
    • Acel, A.1    Udashkin, B.E.2    Wainberg, M.A.3    Faust, E.A.4
  • 45
    • 0029845980 scopus 로고    scopus 로고
    • Differential inhibition of HIV-1 preintegration complexes and purified integrase protein by small molecules.
    • Farnet, C.M., Wang, B., Lipford, J.R., Bushman, F.D., Differential inhibition of HIV-1 preintegration complexes and purified integrase protein by small molecules. Proc. Natl. Acad. Sci. U.S.A. 93 (1996), 9742–9747.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9742-9747
    • Farnet, C.M.1    Wang, B.2    Lipford, J.R.3    Bushman, F.D.4
  • 46
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition.
    • Miller, M.D., Farnet, C.M., Bushman, F.D., Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J. Virol. 71 (1997), 5382–5390.
    • (1997) J. Virol. , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 48
    • 0028283854 scopus 로고
    • HIV-1 infection ofnon-dividing cells.
    • Freed, E.O., Martin, M.A., HIV-1 infection ofnon-dividing cells. Nature (London) 369 (1994), 107–108.
    • (1994) Nature (London) , vol.369 , pp. 107-108
    • Freed, E.O.1    Martin, M.A.2
  • 49
    • 0031472241 scopus 로고    scopus 로고
    • Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection.
    • Freed, E.O., Englund, G., Maldarelli, F., Martin, M.A., Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection. Cell (Cambridge, Mass.) 88 (1997), 171–174.
    • (1997) Cell (Cambridge, Mass.) , vol.88 , pp. 171-174
    • Freed, E.O.1    Englund, G.2    Maldarelli, F.3    Martin, M.A.4
  • 50
    • 0028851734 scopus 로고
    • Interface peptides as structure-based human immunodeficiency virus reverse transcriptase inhibitors.
    • Divita, G., Baillon, J.G., Rittinger, K., Chermann, J.-C., Goody, R.S., Interface peptides as structure-based human immunodeficiency virus reverse transcriptase inhibitors. J. Biol. Chem. 270 (1995), 28642–28646.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28642-28646
    • Divita, G.1    Baillon, J.G.2    Rittinger, K.3    Chermann, J.-C.4    Goody, R.S.5
  • 51
    • 0030662656 scopus 로고    scopus 로고
    • Inhibitors of the nuclear translocation of the HIV-1 preintegration complex.
    • Bukrinsky, M., Inhibitors of the nuclear translocation of the HIV-1 preintegration complex. Drugs Future 22 (1997), 875–883.
    • (1997) Drugs Future , vol.22 , pp. 875-883
    • Bukrinsky, M.1
  • 52
    • 0029171804 scopus 로고
    • Nuclear localization signal of HIV-1 as a novel target for therapeutic intervention.
    • Dubrovsky, L., Ulrich, P., Nuovo, G.J., Manogue, K.R., Cerami, A., Bukrinsky, M., Nuclear localization signal of HIV-1 as a novel target for therapeutic intervention. Mol. Med. 1 (1995), 217–230.
    • (1995) Mol. Med. , vol.1 , pp. 217-230
    • Dubrovsky, L.1    Ulrich, P.2    Nuovo, G.J.3    Manogue, K.R.4    Cerami, A.5    Bukrinsky, M.6
  • 54
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA.
    • Wolff, B., Sanglier, J.J., Wang, Y., Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem. Biol. 4 (1997), 139–147.
    • (1997) Chem. Biol. , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 55
    • 85023026963 scopus 로고    scopus 로고
    • 2+-dependent 3′-processing activity of human immunodeficiency virus type 1 integrase in vitro.
    • 2+-dependent 3′-processing activity of human immunodeficiency virus type 1 integrase in vitro. Biochemistry 36 (1996), 173–180.
    • (1996) Biochemistry , vol.36 , pp. 173-180
    • Lee, S.P.1    Han, M.K.2
  • 56
    • 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. U.S.A. 93 (1996), 13659–13664.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3
  • 57
    • 0030614408 scopus 로고    scopus 로고
    • 2+ promotes the self-association of human immunodeficiency virus type-1 integrase in vitro.
    • 2+ promotes the self-association of human immunodeficiency virus type-1 integrase in vitro. Biochemistry 36 (1997), 173–180.
    • (1997) Biochemistry , vol.36 , pp. 173-180
    • Lee, S.P.1    Xiao, J.2    Knutson, J.R.3    Lewis, M.S.4    Han, M.K.5
  • 58
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding.
    • Bushman, F.D., Engelman, A., Palmer, I., Wingfield, P., Craigie, R., Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. Sci. U.S.A. 90 (1993), 3428–3432.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 59
    • 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.A.M., Plasterk, R.H.A., Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein. Nucleic Acids Res. 21 (1993), 1419–1425.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.A.M.2    Plasterk, R.H.A.3
  • 60
    • 0029954581 scopus 로고    scopus 로고
    • Virus-encoded zinc fingers as targets for antiviral chemotherapy.
    • Rice, W.G., Turpin, J.A., Virus-encoded zinc fingers as targets for antiviral chemotherapy. Rev. Med. Virol. 6 (1996), 187–199.
    • (1996) Rev. Med. Virol. , vol.6 , pp. 187-199
    • Rice, W.G.1    Turpin, J.A.2
  • 61
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences.
    • errata: Nucleic Acids Res., p. 1358
    • Khan, E., Mack, J.P., Katz, R.A., Kulkosky, J., Skalka, A.M., Retroviral integrase domains: DNA binding and the recognition of LTR sequences. Nucleic Acids Res. 19 (1991), 851–860 errata: Nucleic Acids Res., p. 1358.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 62
    • 0026459411 scopus 로고
    • Requirement of active human immunodeficiency virus type 1 integrase enzyme for productive infection of human T-lymphoid cells.
    • La Femina, R.L., Schneider, C.L., Robbins, H.L., Callahan, P.L., Le Grow, K., Roth, E., Schleif, W.A., Emini, E.A., Requirement of active human immunodeficiency virus type 1 integrase enzyme for productive infection of human T-lymphoid cells. J. Virol. 66 (1992), 7414–7419.
    • (1992) J. Virol. , vol.66 , pp. 7414-7419
    • La Femina, R.L.1    Schneider, C.L.2    Robbins, H.L.3    Callahan, P.L.4    Le Grow, K.5    Roth, E.6    Schleif, W.A.7    Emini, E.A.8
  • 63
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type I integrase function in vitro.
    • Engelman, A., Craigie, R., Identification of conserved amino acid residues critical for human immunodeficiency virus type I integrase function in vitro. J. Virol. 66 (1992), 6361–6369.
    • (1992) J. Virol. , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 64
  • 65
    • 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. Retrovirus 10 (1994), 1105–1115.
    • (1994) AIDS Res. Hum. Retrovirus , vol.10 , pp. 1105-1115
    • Bizub-Bender, D.1    Kulkosky, J.2    Skalka, A.M.3
  • 66
    • 0029670765 scopus 로고    scopus 로고
    • Monoclonal antibodies against human immunodeficiency virus type 1 integrase: Epitope mapping and differential effects on integrase activities in vitro.
    • Nilsen, B.M., Haugan, I.R., Berg, K., Olsen, L., Brown, P.O., Helland, D.E., Monoclonal antibodies against human immunodeficiency virus type 1 integrase: Epitope mapping and differential effects on integrase activities in vitro. J. Virol. 70 (1996), 1580–1587.
    • (1996) J. Virol. , vol.70 , pp. 1580-1587
    • Nilsen, B.M.1    Haugan, I.R.2    Berg, K.3    Olsen, L.4    Brown, P.O.5    Helland, D.E.6
  • 67
    • 0030003130 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by the Fab fragment of a specific monoclonal antibody suggests that different multimerization states are required for different enzymatic functions.
    • Barsov, E.V., Huber, W.E., Marcotrigiano, J., Clark, P.K., Clark, A.D., Arnold, E., Hughes, S.H., Inhibition of human immunodeficiency virus type 1 integrase by the Fab fragment of a specific monoclonal antibody suggests that different multimerization states are required for different enzymatic functions. J. Virol. 70 (1996), 4484–4494.
    • (1996) J. Virol. , vol.70 , pp. 4484-4494
    • Barsov, E.V.1    Huber, W.E.2    Marcotrigiano, J.3    Clark, P.K.4    Clark, A.D.5    Arnold, E.6    Hughes, S.H.7
  • 68
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins.
    • Koch, C.A., Anderson, D., Moran, M.F., Ellis, C., Pawson, T., SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252 (1991), 668–674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 69
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase.
    • Grzesiek, S., Bax, A., Clore, M., Gronenborn, A.M., Hu, J.-S., Kaufman, J., Palmer, I., Stahl, S.J., Wingfield, P.T., The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nat. Struct. Biol. 3 (1996), 340–345.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, M.3    Gronenborn, A.M.4    Hu, J.-S.5    Kaufman, J.6    Palmer, I.7    Stahl, S.J.8    Wingfield, P.T.9
  • 70
    • 0028895156 scopus 로고
    • SH2 and SH3 domains: Potential targets for anti-cancer drug design.
    • Smithgall, T.E., SH2 and SH3 domains: Potential targets for anti-cancer drug design. J. Pharmacol. Toxicol. Methods 34 (1995), 125–132.
    • (1995) J. Pharmacol. Toxicol. Methods , vol.34 , pp. 125-132
    • Smithgall, T.E.1
  • 71
    • 0032515399 scopus 로고    scopus 로고
    • Exploring the leucine-proline binding pocket of the src SH3 domain using structure-based, split-pool synthesis and affinity-based selection.
    • Morken, J.P., Kapoor, T.M., Feng, S., Shirai, F., Schreiber, S.L., Exploring the leucine-proline binding pocket of the src SH3 domain using structure-based, split-pool synthesis and affinity-based selection. J. Am. Chem. Soc. 120 (1998), 30–36.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 30-36
    • Morken, J.P.1    Kapoor, T.M.2    Feng, S.3    Shirai, F.4    Schreiber, S.L.5
  • 72
    • 0032515410 scopus 로고    scopus 로고
    • Exploring the specificity pockets of two homologous SH3 domains using structure-based, split-pool synthesis and affinity-based selection.
    • Kapoor, T.M., Andreotti, A.H., Schreiber, S.L., Exploring the specificity pockets of two homologous SH3 domains using structure-based, split-pool synthesis and affinity-based selection. J. Am. Chem. Soc. 120 (1998), 23–29.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 23-29
    • Kapoor, T.M.1    Andreotti, A.H.2    Schreiber, S.L.3
  • 73
    • 0028125329 scopus 로고
    • Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA.
    • Vink, C., Lutzke, R.A.P., Plasterk, R.H.A., Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA. Nucleic Acids Res. 22 (1994), 4103–4110.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4103-4110
    • Vink, C.1    Lutzke, R.A.P.2    Plasterk, R.H.A.3
  • 74
    • 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. 272 (1997), 16196–16205.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16196-16205
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 75
    • 0028984923 scopus 로고
    • 2+-dependent 3′-processing activity for human immunodeficiency virus type 1 integrase in vitro: Real-time kinetic studies using fluorescence resonance energy transfer.
    • 2+-dependent 3′-processing activity for human immunodeficiency virus type 1 integrase in vitro: Real-time kinetic studies using fluorescence resonance energy transfer. Biochemistry 34 (1995), 10205–10214.
    • (1995) Biochemistry , vol.34 , pp. 10205-10214
    • Lee, S.P.1    Kim, H.G.2    Censullo, M.L.3    Han, M.K.4
  • 76
    • 0029083428 scopus 로고
    • Efficient magnesium-dependent human immunodeficiency virus type 1 integrase activity.
    • Engelman, A., Craigie, R., Efficient magnesium-dependent human immunodeficiency virus type 1 integrase activity. J. Virol. 69 (1995), 5908–5911.
    • (1995) J. Virol. , vol.69 , pp. 5908-5911
    • Engelman, A.1    Craigie, R.2
  • 77
    • 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., Katz, R.A., Skalka, A.M., Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity. J. Biol. Chem. 272 (1997), 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    Katz, R.A.6    Skalka, A.M.7
  • 78
    • 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. 398 (1996), 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
  • 79
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H.
    • Yang, W., Steitz, T.A., Recombining the structures of HIV integrase, RuvC and RNase H. Curr. Biol. 3 (1995), 131–134.
    • (1995) Curr. Biol. , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 81
    • 0028566214 scopus 로고
    • Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5.
    • Kalpana, G.V., Marmon, S., Wang, W., Crabtree, G.R., Goff, S.P., Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5. Science 266 (1994), 2002–2006.
    • (1994) Science , vol.266 , pp. 2002-2006
    • Kalpana, G.V.1    Marmon, S.2    Wang, W.3    Crabtree, G.R.4    Goff, S.P.5
  • 82
    • 0032477738 scopus 로고    scopus 로고
    • Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region.
    • Morozov, A., Yung, E., Kalpana, G.V., Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region. Proc. Natl. Acad. Sci. U.S.A. 95 (1998), 1120–1125.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 1120-1125
    • Morozov, A.1    Yung, E.2    Kalpana, G.V.3
  • 83
    • 0028839344 scopus 로고
    • HIV nuclear import is governed by the phophotyrosine-mediated binding of the matrix to the core domain of integrase.
    • Gallay, P., Swingler, S., Song, J., Bushman, F., Trono, D., HIV nuclear import is governed by the phophotyrosine-mediated binding of the matrix to the core domain of integrase. Cell (Cambridge, Mass.) 83 (1995), 569–576.
    • (1995) Cell (Cambridge, Mass.) , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 85
    • 0030583586 scopus 로고    scopus 로고
    • Triterpenes as potential dimerization inhibitoon of HIV-1 protease.
    • Quere, L., Wenger, T., Schramm, H.J., Triterpenes as potential dimerization inhibitoon of HIV-1 protease. Biochem. Biophys. Res. Commun. 227 (1996), 484–488.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 484-488
    • Quere, L.1    Wenger, T.2    Schramm, H.J.3
  • 86
    • 0029966228 scopus 로고    scopus 로고
    • Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation.
    • McPhee, F., Good, A.C., Kuntz, I.D., Craik, C.S., Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation. Proc. Natl. Acad. Sci. U.S.A. 93 (1996), 11477–11481.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11477-11481
    • McPhee, F.1    Good, A.C.2    Kuntz, I.D.3    Craik, C.S.4
  • 87
    • 0026720467 scopus 로고
    • Intracellular immunization-transdominant mutants of HIV gene-products as tools for the study and interruption of viral replication.
    • Feinberg, M.B., Trono, D., Intracellular immunization-transdominant mutants of HIV gene-products as tools for the study and interruption of viral replication. AIDS Res. Hum. Retroviruses 8 (1992), 1013–1022.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 1013-1022
    • Feinberg, M.B.1    Trono, D.2
  • 88
    • 0028842828 scopus 로고
    • Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation.
    • Babe, L.M., Rose, J., Craik, C.S., Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation. Proc. Natl. Acad. Sci. U.S.A. 92 (1995), 10069–10073.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10069-10073
    • Babe, L.M.1    Rose, J.2    Craik, C.S.3
  • 89
    • 0029839487 scopus 로고    scopus 로고
    • Intracellular expression of human immunodeficiency virus type 1(HIV-1) protease variants inhibits replication of wild-type and protease inhibitor-resistant HIV-1 strains in human T-cell lines.
    • Junker, U., Escaich, S., Plavec, I., Baker, J., McPhee, F., Rose, J.R., Craik, C.S., Bohnlein, E., Intracellular expression of human immunodeficiency virus type 1(HIV-1) protease variants inhibits replication of wild-type and protease inhibitor-resistant HIV-1 strains in human T-cell lines. J. Virol. 70 (1996), 7765–7772.
    • (1996) J. Virol. , vol.70 , pp. 7765-7772
    • Junker, U.1    Escaich, S.2    Plavec, I.3    Baker, J.4    McPhee, F.5    Rose, J.R.6    Craik, C.S.7    Bohnlein, E.8
  • 90
    • 0028213920 scopus 로고
    • A Rev-inducible mutant gag gene stably transferred into T lymphocytes: An approach to gene therapy against human immunodeficiency virus type 1 infection.
    • Smythe, J., Sun, D., Thomson, M., Markham, P., Reitz, M.S.J., Gallo, R.C., Lisziewicz, J., A Rev-inducible mutant gag gene stably transferred into T lymphocytes: An approach to gene therapy against human immunodeficiency virus type 1 infection. Proc. Natl. Acad. Sci. U.S.A. 91 (1994), 3657–3661.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 3657-3661
    • Smythe, J.1    Sun, D.2    Thomson, M.3    Markham, P.4    Reitz, M.S.J.5    Gallo, R.C.6    Lisziewicz, J.7
  • 91
    • 0025986843 scopus 로고
    • Dissociative inhibition of dimeric enzymes: Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide.
    • Zhang, Z.Y., Poorman, R.A., Maggiora, L.L., Heinrikson, R.L., Kezdy, F.J., Dissociative inhibition of dimeric enzymes: Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide. J. Biol. Chem. 266 (1991), 15591–15594.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15591-15594
    • Zhang, Z.Y.1    Poorman, R.A.2    Maggiora, L.L.3    Heinrikson, R.L.4    Kezdy, F.J.5
  • 92
    • 0027087479 scopus 로고
    • Synthetic “interface” peptides alter dimeric assembly of the HIV 1 and 2 proteases.
    • Babe, L.M., Rose, J., Craik, C.S., Synthetic “interface” peptides alter dimeric assembly of the HIV 1 and 2 proteases. Protein Sci. 1 (1992), 1244–1253.
    • (1992) Protein Sci. , vol.1 , pp. 1244-1253
    • Babe, L.M.1    Rose, J.2    Craik, C.S.3
  • 94
    • 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. 87 (1990), 5119–5123.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 96
    • 0024431589 scopus 로고
    • The avian retroviral integration protein cleaves the terminal sequences of linear viral DNA at the in vivo sites of integration.
    • Katzman, M., Katz, R.A., Skalka, A.M., Leis, J., The avian retroviral integration protein cleaves the terminal sequences of linear viral DNA at the in vivo sites of integration. J. Virol. 63 (1989), 5319–5327.
    • (1989) J. Virol. , vol.63 , pp. 5319-5327
    • Katzman, M.1    Katz, R.A.2    Skalka, A.M.3    Leis, J.4
  • 97
  • 98
    • 0026072804 scopus 로고
    • Substrate specificity of recombinant human immunodeficiency virus integrase protein.
    • La Femina, R.L., Callahan, P.L., Cordingley, M.G., Substrate specificity of recombinant human immunodeficiency virus integrase protein. J. Virol. 65 (1991), 5624–5630.
    • (1991) J. Virol. , vol.65 , pp. 5624-5630
    • La Femina, R.L.1    Callahan, P.L.2    Cordingley, M.G.3
  • 99
    • 0026537415 scopus 로고
    • Both substrate and target oligonucleotide sequences affect in vitro integration mediated by human immunodeficiency virus type 1 integrase protein produced in
    • Leavitt, A.D., Rose, R.B., Varmus, H.E., Both substrate and target oligonucleotide sequences affect in vitro integration mediated by human immunodeficiency virus type 1 integrase protein produced in. Saccharomyces cerevisiae. J. Virol. 66 (1992), 2359–2368.
    • (1992) Saccharomyces cerevisiae. J. Virol. , vol.66 , pp. 2359-2368
    • Leavitt, A.D.1    Rose, R.B.2    Varmus, H.E.3
  • 100
    • 0025775488 scopus 로고
    • DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2.
    • Van Gent, D.C., Elgersma, Y., Bolk, M.W., Vink, C., Plasterk, R.H.A., DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2. Nucleic Acids Res. 19 (1991), 3821–3827.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3821-3827
    • Van Gent, D.C.1    Elgersma, Y.2    Bolk, M.W.3    Vink, C.4    Plasterk, R.H.A.5
  • 101
    • 0027136287 scopus 로고
    • Rapid solution assays for retroviral integration reactions and their use in kinetic analyses of wild-type and mutant Rous sarcoma virus integrases.
    • Müller, B., Jones, K.S., Merkel, G.W., Skalka, A.M., Rapid solution assays for retroviral integration reactions and their use in kinetic analyses of wild-type and mutant Rous sarcoma virus integrases. Proc. Natl. Acad. Sci. U.S.A. 90 (1993), 11633–11637.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11633-11637
    • Müller, B.1    Jones, K.S.2    Merkel, G.W.3    Skalka, A.M.4
  • 102
    • 0028238134 scopus 로고
    • A high-throughput, non-radioactive microtiter plate assay for activity of the human immnodeficiency virus integrase protein.
    • Vink, C., Banks, M., Bethell, R., Plasterk, R.H.A., A high-throughput, non-radioactive microtiter plate assay for activity of the human immnodeficiency virus integrase protein. Nucleic Acids Res. 22 (1994), 2176–2177.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2176-2177
    • Vink, C.1    Banks, M.2    Bethell, R.3    Plasterk, R.H.A.4
  • 103
    • 0028303481 scopus 로고
    • A novel assay for the DNA strand-transfer reaction of HIV-1 integrase.
    • Hazuda, D.J., Hastings, J.C., Wolfe, A.L., Emini, E.A., A novel assay for the DNA strand-transfer reaction of HIV-1 integrase. Nucleic Acids Res. 22 (1994), 1121–1122.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1121-1122
    • Hazuda, D.J.1    Hastings, J.C.2    Wolfe, A.L.3    Emini, E.A.4
  • 104
    • 0029938801 scopus 로고    scopus 로고
    • Assaying the activity of HIV-1 integrase with DNA-coated plates.
    • Chang, Y.C., Ching, T.T., Syu, W.J., Assaying the activity of HIV-1 integrase with DNA-coated plates. J. Virol. Methods 59 (1996), 135–140.
    • (1996) J. Virol. Methods , vol.59 , pp. 135-140
    • Chang, Y.C.1    Ching, T.T.2    Syu, W.J.3
  • 105
    • 0025133394 scopus 로고
    • Retroviral DNA integration directed by HIV integration protein in vitro.
    • Bushman, F.D., Fujiwara, T., Craigie, R., Retroviral DNA integration directed by HIV integration protein in vitro. Science 249 (1990), 1555–1558.
    • (1990) Science , vol.249 , pp. 1555-1558
    • Bushman, F.D.1    Fujiwara, T.2    Craigie, R.3
  • 106
    • 0026034790 scopus 로고
    • Activities of human immunodeficiency virus (HIV) integration protein in vitro: Specific cleavage and integration of HIV DNA.
    • Bushman, F.D., Craigie, R., Activities of human immunodeficiency virus (HIV) integration protein in vitro: Specific cleavage and integration of HIV DNA. Proc. Natl. Acad. Sci. U.S.A. 88 (1991), 1339–1343.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1339-1343
    • Bushman, F.D.1    Craigie, R.2
  • 107
    • 0026740842 scopus 로고
    • Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 protein in vitro.
    • Drelich, M., Wilhelm, R., Mous, J., Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 protein in vitro. Virology 188 (1992), 459–468.
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 108
    • 0029091789 scopus 로고
    • Substrate-length-dependent activities of human immunodeficiency type 1 integrase in vitro: Differential DNA binding affinities associated with different lenghths of substrates.
    • Lee, S.P., Censullo, M.L., Kim, H.G., Han, M.K., Substrate-length-dependent activities of human immunodeficiency type 1 integrase in vitro: Differential DNA binding affinities associated with different lenghths of substrates. Biochemistry 34 (1995), 10215–10223.
    • (1995) Biochemistry , vol.34 , pp. 10215-10223
    • Lee, S.P.1    Censullo, M.L.2    Kim, H.G.3    Han, M.K.4
  • 109
    • 0028924311 scopus 로고
    • Three-dimensional quantitative structure-activity relationship (QSAR) of HIV integrase inhibitors: A comparative molecular field analysis (CoMFA) study.
    • Raghavan, K., Buolamwini, J.K., Fesen, M.R., Pommier, Y., Kohn, K.W., Weinstein, J.N., Three-dimensional quantitative structure-activity relationship (QSAR) of HIV integrase inhibitors: A comparative molecular field analysis (CoMFA) study. J. Med. Chem. 38 (1995), 890–897.
    • (1995) J. Med. Chem. , vol.38 , pp. 890-897
    • Raghavan, K.1    Buolamwini, J.K.2    Fesen, M.R.3    Pommier, Y.4    Kohn, K.W.5    Weinstein, J.N.6
  • 110
    • 0031469396 scopus 로고    scopus 로고
    • Potent inhibitors of human immunodeficiency virus type 1 integrase: Identification of a novel four-point pharmacophore and tetracyclines as novel inhibitors.
    • Neamati, N., Hong, H., Sunder, S., Milne, G.W.A., Pommier, Y., Potent inhibitors of human immunodeficiency virus type 1 integrase: Identification of a novel four-point pharmacophore and tetracyclines as novel inhibitors. Mol. Pharmacol. 52 (1997), 1041–1055.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 1041-1055
    • Neamati, N.1    Hong, H.2    Sunder, S.3    Milne, G.W.A.4    Pommier, Y.5
  • 116
    • 0030805998 scopus 로고    scopus 로고
    • Curcumin analogs with altered potencies against HIV-1 integrase as probes for biochemical mechanisms of drug action.
    • Mazumder, A., Neamati, N., Sunder, S., Schulz, J., Pertz, H., Eich, E., Pommier, Y., Curcumin analogs with altered potencies against HIV-1 integrase as probes for biochemical mechanisms of drug action. J. Med. Chem. 40 (1997), 3057–3063.
    • (1997) J. Med. Chem. , vol.40 , pp. 3057-3063
    • Mazumder, A.1    Neamati, N.2    Sunder, S.3    Schulz, J.4    Pertz, H.5    Eich, E.6    Pommier, Y.7
  • 118
    • 0001996953 scopus 로고    scopus 로고
    • HIV cDNA integration: Molecular biology and inhibitor development.
    • Farnet, C.M., Bushman, F.D., HIV cDNA integration: Molecular biology and inhibitor development. AIDS 10:Suppl. A (1996), S3–S11.
    • (1996) AIDS , vol.10 , pp. S3-S11
    • Farnet, C.M.1    Bushman, F.D.2
  • 119
    • 0030902816 scopus 로고    scopus 로고
    • HIV integrase: A target for AIDS therapeutics.
    • Thomas, M., Brady, L., HIV integrase: A target for AIDS therapeutics. Trends Biotechnol. 15 (1997), 167–172.
    • (1997) Trends Biotechnol. , vol.15 , pp. 167-172
    • Thomas, M.1    Brady, L.2
  • 121
    • 0030969341 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 2 preintegration complexes: Activities in vitro and response to inhibitors.
    • Hansen, M.S.T., Bushman, F.D., Human immunodeficiency virus type 2 preintegration complexes: Activities in vitro and response to inhibitors. J. Virol. 71 (1997), 3351–3356.
    • (1997) J. Virol. , vol.71 , pp. 3351-3356
    • Hansen, M.S.T.1    Bushman, F.D.2
  • 122
    • 0029062402 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by a hydrophobic cation: The phenanthroline-cuprous complex.
    • Mazumder, A., Gupta, M., Perrin, D.M., Sigman, D.S., Rabinovitz, M., Pommier, Y., Inhibition of human immunodeficiency virus type 1 integrase by a hydrophobic cation: The phenanthroline-cuprous complex. AIDS Res. Hum. Retroviruses 11 (1995), 115–125.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 115-125
    • Mazumder, A.1    Gupta, M.2    Perrin, D.M.3    Sigman, D.S.4    Rabinovitz, M.5    Pommier, Y.6
  • 123
    • 0029990185 scopus 로고    scopus 로고
    • Alternate strand DNA triple helix-mediated inhibition of HIV-1 U5 long terminal repeat integration in vitro.
    • Bouziane, M., Cherny, D.I., Mouscadet, J.-F., Auclair, C., Alternate strand DNA triple helix-mediated inhibition of HIV-1 U5 long terminal repeat integration in vitro. J. Biol. Chem. 271 (1996), 10359–10364.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10359-10364
    • Bouziane, M.1    Cherny, D.I.2    Mouscadet, J.-F.3    Auclair, C.4
  • 124
    • 0029870911 scopus 로고    scopus 로고
    • A molecular mechanics and dynamics study of alternate triple-helices involving the integrase-binding site of the HIV-1 virus and oligonucleotides having a 3′-3′ internucleotide junction.
    • Ouali, M., Bouziane, M., Ketterle, C., Gabarro-Arpa, J., Auclair, C., Le Bret, M., A molecular mechanics and dynamics study of alternate triple-helices involving the integrase-binding site of the HIV-1 virus and oligonucleotides having a 3′-3′ internucleotide junction. J. Biomol. Struct. Dyn. 13 (1996), 835–853.
    • (1996) J. Biomol. Struct. Dyn. , vol.13 , pp. 835-853
    • Ouali, M.1    Bouziane, M.2    Ketterle, C.3    Gabarro-Arpa, J.4    Auclair, C.5    Le Bret, M.6
  • 125
    • 0028303604 scopus 로고
    • Inhibition of the in vitro integration of Moloney murine leukemia virus DNA by the DNA minor groove binder netropsin.
    • Carteau, S., Mouscadet, J.F., Goulaouic, H., Subra, F., Auclair, C., Inhibition of the in vitro integration of Moloney murine leukemia virus DNA by the DNA minor groove binder netropsin. Biochem. Pharmacol. 47 (1994), 1821–1826.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 1821-1826
    • Carteau, S.1    Mouscadet, J.F.2    Goulaouic, H.3    Subra, F.4    Auclair, C.5
  • 126
    • 0026637636 scopus 로고
    • Anti-HIV-1 activity of linked lexitropsins.
    • Wang, W., Lown, L., Anti-HIV-1 activity of linked lexitropsins. J. Med. Chem. 35 (1992), 2890–2897.
    • (1992) J. Med. Chem. , vol.35 , pp. 2890-2897
    • Wang, W.1    Lown, L.2
  • 127
    • 0006430045 scopus 로고    scopus 로고
    • Identification of the antiviral nucleoside drug binding site of HIV-1 integrase by proteolytic peptide mapping.
    • Drake, R., Neamati, N., Sunthankar, P., Mazumder, A., Pommier, Y., Identification of the antiviral nucleoside drug binding site of HIV-1 integrase by proteolytic peptide mapping. Antiviral Res., 34, 1997, A42.
    • (1997) Antiviral Res. , vol.34 , pp. A42
    • Drake, R.1    Neamati, N.2    Sunthankar, P.3    Mazumder, A.4    Pommier, Y.5
  • 128
    • 0029055551 scopus 로고
    • Isolation of high-affinity RNA ligands to HIV1 integrase from a random pool.
    • Allen, P., Worland, S., Gold, L., Isolation of high-affinity RNA ligands to HIV1 integrase from a random pool. Virology 209 (1995), 327–336.
    • (1995) Virology , vol.209 , pp. 327-336
    • Allen, P.1    Worland, S.2    Gold, L.3
  • 130
    • 0028820595 scopus 로고
    • Effects of tyrphostins, protein kinase inhibitors, on human immunodeficiency virus type 1 integrase.
    • Mazumder, A., Gazit, A., Levitzki, A., Nicklaus, M., Yung, J., Kohlhagen, G., Pommier, Y., Effects of tyrphostins, protein kinase inhibitors, on human immunodeficiency virus type 1 integrase. Biochemistry 34 (1995), 15111–15121.
    • (1995) Biochemistry , vol.34 , pp. 15111-15121
    • Mazumder, A.1    Gazit, A.2    Levitzki, A.3    Nicklaus, M.4    Yung, J.5    Kohlhagen, G.6    Pommier, Y.7
  • 131
    • 0030041593 scopus 로고    scopus 로고
    • (-)-Arctigenin as a lead structure for inhibitors of human immunodeficiency virus type-1 integrase.
    • Eich, E., Petz, H., Kaloga, M., Schulz, J., Fesen, M.R., Mazumder, A., Pommier, Y., (-)-Arctigenin as a lead structure for inhibitors of human immunodeficiency virus type-1 integrase. J. Med. Chem. 39 (1996), 86–95.
    • (1996) J. Med. Chem. , vol.39 , pp. 86-95
    • Eich, E.1    Petz, H.2    Kaloga, M.3    Schulz, J.4    Fesen, M.R.5    Mazumder, A.6    Pommier, Y.7
  • 133
    • 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., Reinecke, M.G., Mitchell, W.M., Dicaffeoylquinic acid inhibitors of human immunodeficiency virus integrase: Inhibition of the core catalytic domain of human immunodeficiency virus integrase. Mol. Pharmacol. 50 (1996), 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    Reinecke, M.G.6    Mitchell, W.M.7
  • 134
  • 136
    • 0030576651 scopus 로고    scopus 로고
    • Cell protein-crosslinking by erbstatin and related compounds.
    • Stanwell, C., Ye, B., Yuspa, S.H., Burke, T.R., Cell protein-crosslinking by erbstatin and related compounds. Biochem. Pharmacol. 52 (1996), 475–480.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 475-480
    • Stanwell, C.1    Ye, B.2    Yuspa, S.H.3    Burke, T.R.4
  • 137
    • 0029439547 scopus 로고
    • Plant polyphenols: Free radical scavenger or chain-breaking antioxidants?
    • Rice-Evans, C., Plant polyphenols: Free radical scavenger or chain-breaking antioxidants?. Biochem. Soc. Symp. 61 (1995), 103–116.
    • (1995) Biochem. Soc. Symp. , vol.61 , pp. 103-116
    • Rice-Evans, C.1
  • 138
    • 17744419436 scopus 로고    scopus 로고
    • The anti-HIV activity and mechanisms of action of pure compounds isolated from Rosa damascena.
    • Mahmood, N., Piacente, S., Pizza, C., Burke, A., Khan, A.I., Hay, A.J., The anti-HIV activity and mechanisms of action of pure compounds isolated from Rosa damascena. Biochem. Biophys. Res. Commun. 229 (1996), 73–79.
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 73-79
    • Mahmood, N.1    Piacente, S.2    Pizza, C.3    Burke, A.4    Khan, A.I.5    Hay, A.J.6
  • 139
    • 0030061391 scopus 로고    scopus 로고
    • Inhibition of HIV activation in latently infected cells by flavonoid compounds.
    • Critchfield, J.W., Butera, S.T., Folks, T.M., Inhibition of HIV activation in latently infected cells by flavonoid compounds. AIDS Res. Hum. Retroviruses 12 (1996), 39–46.
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , pp. 39-46
    • Critchfield, J.W.1    Butera, S.T.2    Folks, T.M.3
  • 142
    • 0006807931 scopus 로고    scopus 로고
    • Design and synthesis of photoactivatable coumarin-containing HIV-1 integrase inhibitors.
    • Zhao, H., Neamati, N., Pommier, Y., Burke, T.R., Design and synthesis of photoactivatable coumarin-containing HIV-1 integrase inhibitors. Heterocycles 45 (1997), 2277–2282.
    • (1997) Heterocycles , vol.45 , pp. 2277-2282
    • Zhao, H.1    Neamati, N.2    Pommier, Y.3    Burke, T.R.4
  • 144
    • 0026590931 scopus 로고
    • HIV-1 integrase: High-level production and screening assay for the endonucleolytic activity.
    • Billich, A., Schauer, M., Frank, S., Rosenwirth, B., Billich, S., HIV-1 integrase: High-level production and screening assay for the endonucleolytic activity. Antiviral Chem. Chemother. 3 (1992), 113–119.
    • (1992) Antiviral Chem. Chemother. , vol.3 , pp. 113-119
    • Billich, A.1    Schauer, M.2    Frank, S.3    Rosenwirth, B.4    Billich, S.5
  • 146
    • 0030867109 scopus 로고    scopus 로고
    • 2-Mercaptobenzenesulfonamides as novel inhibitors of human immunodeficiency virus type 1 integrase and replication.
    • Neamati, N., Mazumder, A., Sunder, S., Owen, J.M., Schultz, R.J., Pommier, Y., 2-Mercaptobenzenesulfonamides as novel inhibitors of human immunodeficiency virus type 1 integrase and replication. Antiviral Chem. Chemother. 8 (1997), 485–495.
    • (1997) Antiviral Chem. Chemother. , vol.8 , pp. 485-495
    • Neamati, N.1    Mazumder, A.2    Sunder, S.3    Owen, J.M.4    Schultz, R.J.5    Pommier, Y.6
  • 147
    • 0029557124 scopus 로고
    • Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library.
    • Lutzke, R.A.P., Eppens, N.A., Weber, P.A., Houghten, R.A., Plasterk, R.H.A., Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. Proc. Natl. Acad. Sci. U.S.A. 92 (1995), 11456–11460.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11456-11460
    • Lutzke, R.A.P.1    Eppens, N.A.2    Weber, P.A.3    Houghten, R.A.4    Plasterk, R.H.A.5
  • 148
    • 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., Troalen, F., Fermandjian, S., 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. 240 (1996), 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    Troalen, F.6    Fermandjian, S.7
  • 149
    • 0028225959 scopus 로고
    • Human immunodeficiency virus type 1 integrase: Effect on viral replication of mutation at hightly conserved residues.
    • Cannon, P.M., Wilson, W., Byles, E., Kingsman, S.M., Kingsman, A.J.K., Human immunodeficiency virus type 1 integrase: Effect on viral replication of mutation at hightly conserved residues. J. Virol. 68 (1994), 4768–4775.
    • (1994) J. Virol. , vol.68 , pp. 4768-4775
    • Cannon, P.M.1    Wilson, W.2    Byles, E.3    Kingsman, S.M.4    Kingsman, A.J.K.5
  • 150
    • 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., Zhu, M., Kulkosky, J., Bizub-Bender, D., Skalka, A.M., Pomerantz, R.J., 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. 70 (1996), 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    Zhu, M.6    Kulkosky, J.7    Bizub-Bender, D.8    Skalka, A.M.9    Pomerantz, R.J.10


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