메뉴 건너뛰기




Volumn 8, Issue 6, 1997, Pages 463-483

HIV-1 integrase as a target for antiviral drugs

Author keywords

AIDS; Chemotherapy; Drug design; Hydroxylated aromatics; Inhibitors; Integrase; Nucleotides

Indexed keywords

ENZYME INHIBITOR; INTEGRASE;

EID: 0030865411     PISSN: 09563202     EISSN: None     Source Type: Journal    
DOI: 10.1177/095632029700800601     Document Type: Article
Times cited : (78)

References (180)
  • 1
    • 0029055551 scopus 로고
    • Isolation of high-affinity RNA ligands to HIV1 integrase from a random pool
    • Allen P, Worland S & Gold L (1995) Isolation of high-affinity RNA ligands to HIV1 integrase from a random pool. Virology 209: 327-336.
    • (1995) Virology , vol.209 , pp. 327-336
    • Allen, P.1    Worland, S.2    Gold, L.3
  • 2
    • 0028863151 scopus 로고
    • Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase
    • Andrake MD & Skalka AM (1995) Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase. Journal of Biological Chemistry 270: 29299-23006.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 29299-123006
    • Andrake, M.D.1    Skalka, A.M.2
  • 3
    • 0029814410 scopus 로고    scopus 로고
    • Retroviral integrase, putting the pieces together
    • Andrake MD & Skalka AM (1996) Retroviral integrase, putting the pieces together. Journal of Biological Chemistry 271: 19633-19636.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 19633-19636
    • Andrake, M.D.1    Skalka, A.M.2
  • 4
    • 0030922072 scopus 로고    scopus 로고
    • A metal-induced conformational change and activation of HIV-1 integrase
    • Asante-Appiah E & Skalka AM (1997) A metal-induced conformational change and activation of HIV-1 integrase. Journal of Biological Chemistry 272: 16196-16205.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 16196-16205
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 5
    • 0031028292 scopus 로고    scopus 로고
    • Functional identification of nucleotides conferring substrate specificity to retroviral integrase reactions
    • Balakrishnan M & Jonsson CB (1997) Functional identification of nucleotides conferring substrate specificity to retroviral integrase reactions. Journal of Virology 71: 1025-1035.
    • (1997) Journal of Virology , vol.71 , pp. 1025-1035
    • Balakrishnan, M.1    Jonsson, C.B.2
  • 6
    • 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 EV, Huber WE, Marcotrigiano J, Clark PK, Clark AD, Arnold E & Hughes SH (1996) 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. Journal of Virology 70: 4484-4494.
    • (1996) Journal of Virology , 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
  • 7
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese LS, Derbyshire V & Steitz TA (1993) Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science 260: 352-355.
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 9
  • 10
    • 0030219760 scopus 로고    scopus 로고
    • Target-sequence preferences of HIV-1 integration complexes in vitro
    • Bor YC, Miller MD, Bushman FD & Orgel LE (1996) Target-sequence preferences of HIV-1 integration complexes in vitro. Virology 222: 283-288.
    • (1996) Virology , vol.222 , pp. 283-288
    • Bor, Y.C.1    Miller, M.D.2    Bushman, F.D.3    Orgel, L.E.4
  • 11
    • 0029008475 scopus 로고
    • Impairment of Moloney murine leukemia virus integration in a cell line underexpressing DNA topoisomerase II
    • Bouillé P, Subra F, Goulaouic H, Carteau S & Auclair C (1995) Impairment of Moloney murine leukemia virus integration in a cell line underexpressing DNA topoisomerase II. Cancer Research 55: 3211-3217.
    • (1995) Cancer Research , vol.55 , pp. 3211-3217
    • Bouillé, P.1    Subra, F.2    Goulaouic, H.3    Carteau, S.4    Auclair, C.5
  • 12
    • 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 DI, Mouscadet J-F & Auclair C (1996) Alternate strand DNA triple helix-mediated inhibition of HIV-1 U5 long terminal repeat integration in vitro. Journal of Biological Chemistry 271: 10359-10364.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 10359-10364
    • Bouziane, M.1    Cherny, D.I.2    Mouscadet, J.-F.3    Auclair, C.4
  • 15
    • 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 ZL, Clement-Mella C & Wlodawer A (1996a) The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant. FEBS Letters 398: 175-178.
    • (1996) FEBS Letters , vol.398 , pp. 175-178
    • Bujacz, G.1    Alexandratos, J.2    Qing, Z.L.3    Clement-Mella, C.4    Wlodawer, A.5
  • 16
    • 0029643858 scopus 로고    scopus 로고
    • The catalytic domain of avian sarcoma virus integrase: Conformation of the active-site residues in the presence of divalent cations
    • Bujacz G, Jaskolski M, Alexandratos J, Wlodawer A, Merkel G, Katz RA & Skalka AM (1996b) The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Current Biology 4: 89-96.
    • (1996) Current Biology , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5    Katz, R.A.6    Skalka, A.M.7
  • 24
    • 0026034790 scopus 로고
    • Activities of human immunodeficiency virus (HIV) integration protein in vitro: Specific cleavage and integration of HIV DNA
    • Bushman FD & Craigie R (1991) Activities of human immunodeficiency virus (HIV) integration protein in vitro: specific cleavage and integration of HIV DNA. Proceedings of the National Academy of Sciences, USA 88: 1339-1343.
    • (1991) Proceedings of the National Academy of Sciences, USA , vol.88 , pp. 1339-1343
    • Bushman, F.D.1    Craigie, R.2
  • 25
    • 0026568640 scopus 로고
    • Integration of human immunodeficiency virus DNA: Adduct interference analysis of required DNA sites
    • Bushman FD & Craigie R (1992) Integration of human immunodeficiency virus DNA: adduct interference analysis of required DNA sites. Proceedings of the National Academy of Sciences, USA 89: 3458-3462.
    • (1992) Proceedings of the National Academy of Sciences, USA , vol.89 , pp. 3458-3462
    • Bushman, F.D.1    Craigie, R.2
  • 26
    • 0025133394 scopus 로고
    • Retroviral DNA integration directed by HIV integration protein in vitro
    • Bushman FD, Fujiwara T & Craigie R (1990) Retroviral DNA integration directed by HIV integration protein in vitro. Science 249: 1555-1558.
    • (1990) Science , vol.249 , pp. 1555-1558
    • Bushman, F.D.1    Fujiwara, T.2    Craigie, R.3
  • 28
    • 0028225959 scopus 로고
    • Human immunodeficiency virus type 1 integrase: Effect on viral replication of mutation at highly conserved residues
    • Cannon PM, Wilson W, Byles E, Kingsman SM & Kingsman AJK (1994) Human immunodeficiency virus type 1 integrase: effect on viral replication of mutation at highly conserved residues. Journal of Virology 68: 4768-4775.
    • (1994) Journal of Virology , vol.68 , pp. 4768-4775
    • Cannon, P.M.1    Wilson, W.2    Byles, E.3    Kingsman, S.M.4    Kingsman, A.J.K.5
  • 29
    • 0029655459 scopus 로고    scopus 로고
    • Conserved sequences in the carboxyl terminus of integrase that are essential for human immunodeficiency virus type 1 replication
    • Cannon PM, Byles ED, Kingsman SM & Kingsman AJ (1996) Conserved sequences in the carboxyl terminus of integrase that are essential for human immunodeficiency virus type 1 replication. Journal of Virology 70: 651-657.
    • (1996) Journal of Virology , vol.70 , pp. 651-657
    • Cannon, P.M.1    Byles, E.D.2    Kingsman, S.M.3    Kingsman, A.J.4
  • 32
    • 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 JF, Goulaouic H, Subra F & Auclair C (1994) Inhibition of the in vitro integration of Moloney murine leukemia virus DNA by the DNA minor groove binder netropsin. Biochemical Pharmacology 47: 1821-1826.
    • (1994) Biochemical Pharmacology , vol.47 , pp. 1821-1826
    • Carteau, S.1    Mouscadet, J.F.2    Goulaouic, H.3    Subra, F.4    Auclair, C.5
  • 33
    • 0029938801 scopus 로고    scopus 로고
    • Assaying the activity of HIV-1 integrase with DNA-coated plates
    • Chang YC, Ching TT & Syu WJ (1996) Assaying the activity of HIV-1 integrase with DNA-coated plates. Journal of Virological Methods 59: 135-140.
    • (1996) Journal of Virological Methods , vol.59 , pp. 135-140
    • Chang, Y.C.1    Ching, T.T.2    Syu, W.J.3
  • 34
    • 0027971617 scopus 로고
    • Juxtaposition of two viral DNa ends in a bimolecular disintegration reaction mediated by multimers of human immunodeficiency virus type 1 or murine leukemia virus integrase
    • Chow SA & Brown PO (1994) Juxtaposition of two viral DNA ends in a bimolecular disintegration reaction mediated by multimers of human immunodeficiency virus type 1 or murine leukemia virus integrase. Journal of Virology 68: 7869-7878.
    • (1994) Journal of Virology , vol.68 , pp. 7869-7878
    • Chow, S.A.1    Brown, P.O.2
  • 35
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow SA, Vincent KA, Ellison V & Brown PO (1992) Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 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
  • 37
    • 0026659014 scopus 로고
    • Inhibition of HIV-1 integration protein by aurintricarboxylic acid monomers, monomer analogs, and polymer fractions
    • Cushman M & Sherman P (1992) Inhibition of HIV-1 integration protein by aurintricarboxylic acid monomers, monomer analogs, and polymer fractions. Biochemical and Biophysical Research Communications 185: 85-90.
    • (1992) Biochemical and Biophysical Research Communications , vol.185 , pp. 85-90
    • Cushman, M.1    Sherman, P.2
  • 40
    • 0027489647 scopus 로고
    • Influence of substrate structure on disintegration activity of Moloney murine leukemia virus integrase
    • Donzella GA, Jonsson CB & Roth MJ (1993) Influence of substrate structure on disintegration activity of Moloney murine leukemia virus integrase. Journal of Virology 67: 7077-7087.
    • (1993) Journal of Virology , vol.67 , pp. 7077-7087
    • Donzella, G.A.1    Jonsson, C.B.2    Roth, M.J.3
  • 41
    • 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 (1997) Identification of the antiviral nucleoside drug binding site of HIV-1 integrase by proteolytic peptide mapping. Antiviral Research 34: A42.
    • (1997) Antiviral Research , vol.34
    • Drake, R.1    Neamati, N.2    Sunthankar, P.3    Mazumder, A.4    Pommier, Y.5
  • 42
    • 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 (1992) Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 protein in vitro. Virology 188: 459-468.
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 43
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity of other polynucleotide transferases
    • Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R & Davies DR (1994) Crystal structure of the catalytic domain of HIV-1 integrase: similarity of other polynucleotide transferases. Science 266: 1981-1986.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 46
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison V & Brown PO (1994) A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proceedings of the National Academy of Sciences, USA 91: 7316-7320.
    • (1994) Proceedings of the National Academy of Sciences, USA , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 48
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type I integrase function in vino
    • Engelman A & Craigie R (1992) Identification of conserved amino acid residues critical for human immunodeficiency virus type I integrase function in vino. Journal of Virology 66: 6361-6169.
    • (1992) Journal of Virology , vol.66 , pp. 6361-16169
    • Engelman, A.1    Craigie, R.2
  • 49
    • 0029083428 scopus 로고
    • Efficient magnesium-dependent human immunodeficiency virus type 1 integrase activity
    • Engelman A & Craigie R (1995) Efficient magnesium-dependent human immunodeficiency virus type 1 integrase activity. Journal of Virology 69: 5908-5911.
    • (1995) Journal of Virology , vol.69 , pp. 5908-5911
    • Engelman, A.1    Craigie, R.2
  • 50
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
    • Engelman A, Mizuuchi K & Craigie R (1991) HIV-1 DNA integration: mechanism of viral DNA cleavage and DNA strand transfer. Cell 67: 1211-1221.
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 51
    • 0027179694 scopus 로고
    • Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman A, Bushman FD & Craigie R (1993) Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO Journal 12: 3269-3275.
    • (1993) EMBO Journal , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 52
    • 0028067324 scopus 로고
    • The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding
    • Engelman A, Hickman AB & Craigie R (1994) The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding. Journal of Virology 68: 5911-5917.
    • (1994) Journal of Virology , vol.68 , pp. 5911-5917
    • Engelman, A.1    Hickman, A.B.2    Craigie, R.3
  • 53
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication
    • Engelman A, Englund G, Orenstein JM, Martin MA & Craigie R (1995) Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication. Journal of Virology 69: 2729-2736.
    • (1995) Journal of Virology , vol.69 , pp. 2729-2736
    • Engelman, A.1    Englund, G.2    Orenstein, J.M.3    Martin, M.A.4    Craigie, R.5
  • 54
    • 0030988998 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the catalytic domain of human immunodeficiency virus type 1 integrase
    • Engelman A, Liu Y, Chen H, Farzan M & Dyda F (1997) Structure-based mutagenesis of the catalytic domain of human immunodeficiency virus type 1 integrase. Journal of Virology 71: 3507-3514.
    • (1997) Journal of Virology , vol.71 , pp. 3507-3514
    • Engelman, A.1    Liu, Y.2    Chen, H.3    Farzan, M.4    Dyda, F.5
  • 55
    • 0025968854 scopus 로고
    • Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex
    • Farnet CM & Haseltine WA (1991) Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex. Journal of Virology 65: 1910-1915.
    • (1991) Journal of Virology , vol.65 , pp. 1910-1915
    • Farnet, C.M.1    Haseltine, W.A.2
  • 57
    • 0001996953 scopus 로고    scopus 로고
    • HIV cDNA integration: Molecular biology and inhibitor development
    • Farnet CM & Bushman FD (1996b) HIV cDNA integration: molecular biology and inhibitor development. AIDS 10 (supplement A) 53-511.
    • (1996) AIDS , vol.10 , Issue.SUPPL. A , pp. 53-511
    • Farnet, C.M.1    Bushman, F.D.2
  • 58
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet O, Ramond P, Polard P, Prère MF & Chandler M (1990) Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences? Molecular Microbiology 4: 1771-1777.
    • (1990) Molecular Microbiology , vol.4 , pp. 1771-1777
    • Fayet, O.1    Ramond, P.2    Polard, P.3    Prère, M.F.4    Chandler, M.5
  • 60
  • 61
    • 0026760582 scopus 로고
    • Concerted integration of viral DNA termini by purified avian mveloblastosis virus integrase
    • Fitzgerald ML, Vora AC, Zeh WG & Grandgenett DP (1992) Concerted integration of viral DNA termini by purified avian mveloblastosis virus integrase. Journal of Virology 66: 6257-6263.
    • (1992) Journal of Virology , vol.66 , pp. 6257-6263
    • Fitzgerald, M.L.1    Vora, A.C.2    Zeh, W.G.3    Grandgenett, D.P.4
  • 63
    • 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 (1995) HIV nuclear import is governed by the phophotyrosine-mediated binding of the matrix to the core domain of integrase. Cell 83: 569-576.
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 64
    • 0027102597 scopus 로고
    • Genetic of retroviral integration
    • Goff SP (1992) Genetic of retroviral integration. Annual Review of Genetics 26: 527-544.
    • (1992) Annual Review of Genetics , vol.26 , pp. 527-544
    • Goff, S.P.1
  • 65
    • 0029094543 scopus 로고
    • Concerted integration of retrovirus-like DNA by human immunodeficiency virus type 1 integrase
    • Goodarzi G, Im G-J, Brackmann K & Grandgenett D (1995) Concerted integration of retrovirus-like DNA by human immunodeficiency virus type 1 integrase. Journal of Virology 69: 1090-1097.
    • (1995) Journal of Virology , vol.69 , pp. 1090-1097
    • Goodarzi, G.1    Im, G.-J.2    Brackmann, K.3    Grandgenett, D.4
  • 66
    • 0030908147 scopus 로고    scopus 로고
    • Host site selection for concerted integration by human immunodeficiency virus type 1 virions in vitro
    • Goodarzi G, Chiu R, Brackmann K, Kohn KW, Pommier Y & Grandgenett DP (1997) Host site selection for concerted integration by human immunodeficiency virus type 1 virions in vitro. Virology 231: 210-217.
    • (1997) Virology , vol.231 , pp. 210-217
    • Goodarzi, G.1    Chiu, R.2    Brackmann, K.3    Kohn, K.W.4    Pommier, Y.5    Grandgenett, D.P.6
  • 72
    • 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 TM, Engelman A, Ghirlando R & Craigie R (1996) A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxyl-terminal domains in multimerization. Journal of Biological Chemistry 271: 7712-7718.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 73
    • 0027404102 scopus 로고
    • Characterization of the forward and reverse integration reactions of the Moloney murine leukemia virus integrase protein purified from Escherichia coli
    • Jonsson CB, Donzella GA & Roth MJ (1993) Characterization of the forward and reverse integration reactions of the Moloney murine leukemia virus integrase protein purified from Escherichia coli. Journal of Biological Chemistry 268: 1462-1469.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 1462-1469
    • Jonsson, C.B.1    Donzella, G.A.2    Roth, M.J.3
  • 74
    • 1842302312 scopus 로고
    • Protein-protein interactions of HIV-1 IN: INI-1 (IN Interactor-1), a novel human gene with sequence similarity to yeast transcription factor SNF5
    • Kalpana GV & Goff SP (1994) Protein-protein interactions of HIV-1 IN: INI-1 (IN Interactor-1), a novel human gene with sequence similarity to yeast transcription factor SNF5. Journal of Cellular Biochemistry 18B: 27.
    • (1994) Journal of Cellular Biochemistry , vol.18 B , pp. 27
    • Kalpana, G.V.1    Goff, S.P.2
  • 75
    • 0028566214 scopus 로고
    • Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5
    • Kalpana GV, Marmon S, Wang W, Crabtree GR & Goff SP (1994) Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5. Science 266: 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
  • 76
    • 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 (1996) Influence of subterminal viral DNA nucleotide on differential susceptibility to cleavage by human immunodeficiency virus type 1 and visna virus integrases. Journal of Virology 70: 9069-9073.
    • (1996) Journal of Virology , vol.70 , pp. 9069-9073
    • Katzman, M.1    Sudol, M.2
  • 77
    • 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 RA, Skalka AM & Leis J (1989) The avian retroviral integration protein cleaves the terminal sequences of linear viral DNA at the in vivo sites of integration. Journal of Virology 63: 5319-5327.
    • (1989) Journal of Virology , vol.63 , pp. 5319-5327
    • Katzman, M.1    Katz, R.A.2    Skalka, A.M.3    Leis, J.4
  • 78
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Erratum 19: 1358
    • Khan E, Mack JP, Katz RA, Kulkosky J & Skalka AM (1991) Retroviral integrase domains: DNA binding and the recognition of LTR sequences. Nucleic Acids Research 19: 851-860; Erratum 19: 1358.
    • (1991) Nucleic Acids Research , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 80
    • 0028790504 scopus 로고
    • Enhanced and coordinated processing of synapsed viral DNA ends by retroviral integrases in vitro
    • Kukolj G & Skalka AM (1995) Enhanced and coordinated processing of synapsed viral DNA ends by retroviral integrases in vitro. Genes and Development 9: 2556-2567.
    • (1995) Genes and Development , vol.9 , pp. 2556-2567
    • Kukolj, G.1    Skalka, A.M.2
  • 81
    • 0031060369 scopus 로고    scopus 로고
    • Subcellular localization of avian sarcoma virus and human immunodeficiency virus type 1 integrases
    • Kukolj G, Jones KS & Skalka AM (1997) Subcellular localization of avian sarcoma virus and human immunodeficiency virus type 1 integrases. Journal of Virology 71: 843-847.
    • (1997) Journal of Virology , vol.71 , pp. 843-847
    • Kukolj, G.1    Jones, K.S.2    Skalka, A.M.3
  • 83
    • 0026719238 scopus 로고
    • Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases
    • Kulkosky J, Jones KS, Katz RA, Mack JP & Skalka AM (1992) Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Molecular and Cellular Biology 12: 2331-2338.
    • (1992) Molecular and Cellular Biology , vol.12 , pp. 2331-2338
    • Kulkosky, J.1    Jones, K.S.2    Katz, R.A.3    Mack, J.P.4    Skalka, A.M.5
  • 84
    • 0026072804 scopus 로고
    • Substrate specificity of recombinant human immunodeficiency virus integrase protein
    • LaFemina RL, Callahan PL & Cordingley MG (1991) Substrate specificity of recombinant human immunodeficiency virus integrase protein. Journal of Virology 65: 5624-5630.
    • (1991) Journal of Virology , vol.65 , pp. 5624-5630
    • LaFemina, R.L.1    Callahan, P.L.2    Cordingley, M.G.3
  • 88
    • 0026537415 scopus 로고
    • Both substrate and target oligonucleotide sequences affect in vitro integration mediated by human immunodeficiency virus type 1 integrase protein produced in Saccharomyces cerevisiae
    • Leavitt AD, Rose RB & Varmus HE (1992) Both substrate and target oligonucleotide sequences affect in vitro integration mediated by human immunodeficiency virus type 1 integrase protein produced in Saccharomyces cerevisiae. Journal of Virology 66: 2359-2368.
    • (1992) Journal of Virology , vol.66 , pp. 2359-2368
    • Leavitt, A.D.1    Rose, R.B.2    Varmus, H.E.3
  • 89
    • 0027470432 scopus 로고
    • Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro
    • Leavitt AD, Shiue L & Varmus HE (1993) Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro. Journal of Biological Chemistry 268: 2113-2119.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 2113-2119
    • Leavitt, A.D.1    Shiue, L.2    Varmus, H.E.3
  • 90
    • 0028077096 scopus 로고
    • Protection of retroviral DNa from autointegration: Involvement of a cellular factor
    • Lee MS & Craigie R (1994) Protection of retroviral DNA from autointegration: involvement of a cellular factor. Proceedings of the National Academy of Sciences, USA 91: 9823-9827.
    • (1994) Proceedings of the National Academy of Sciences, USA , vol.91 , pp. 9823-9827
    • Lee, M.S.1    Craigie, R.2
  • 91
    • 0029670473 scopus 로고    scopus 로고
    • Zinc stimulates Mg2+-dependent 3′-processing activity of human immunodeficiency virus type 1 integrase in vitro
    • Lee SP & Han MK (1996) Zinc stimulates Mg2+-dependent 3′-processing activity of human immunodeficiency virus type 1 integrase in vitro. Biochemistry 35: 3837-3844.
    • (1996) Biochemistry , vol.35 , pp. 3837-3844
    • Lee, S.P.1    Han, M.K.2
  • 92
    • 0028984923 scopus 로고
    • Characterization of Mg2+-dependent 3′-processing activity for human immunodeficiency virus typel integrase in vitro: Real-time kinetic studies using fluorescence resonance energy transfer
    • Lee SP, Kim HG, Censullo ML & Han MK (1995a) Characterization of Mg2+-dependent 3′-processing activity for human immunodeficiency virus typel integrase in vitro: real-time kinetic studies using fluorescence resonance energy transfer. Biochemistry 34: 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
  • 93
    • 0029091789 scopus 로고
    • Substrate-length-dependent activities of human immunodeficiency type 1 integrase in vitro: Differential DNA binding affinities associated with different lengths of substrates
    • Lee SP, Censullo ML, Kim HG & Han MK (1995b) Substrate-length-dependent activities of human immunodeficiency type 1 integrase in vitro: differential DNA binding affinities associated with different lengths of substrates. Biochemistry 34: 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
  • 94
    • 0030614408 scopus 로고    scopus 로고
    • Zn2+ promotes the self-association of human immunodeficiency virus type-1 integrase in vitro
    • Lee SP, Xiao J, Knutson JR, Lewis MS & Han MK (1997) Zn2+ promotes the self-association of human immunodeficiency virus type-1 integrase in vitro. Biochemistry 36: 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
  • 96
    • 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
    • Lew-Mintz P, Duan L, Zhang H, Hu B, Dornadula G, Zhu M, Kulkosky J, Bizub-Bender D, Skalka AM & Pomerantz RJ (1996) Intracellular expression of single-chain variable fragments to inhibit early stages of the viral life cycle by targeting human immunodeficiency virus type 1 integrase. Journal of Virology 70: 8821-8832.
    • (1996) Journal of Virology , vol.70 , pp. 8821-8832
    • Lew-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
  • 97
    • 0028171531 scopus 로고
    • Nucleotide binding bv the HIV-1 integrase protein in vitro
    • Lipford JR, Worland ST & Farnet CM (1994) Nucleotide binding bv the HIV-1 integrase protein in vitro. Journal of AIDS 7: 1215-1223.
    • (1994) Journal of AIDS , vol.7 , pp. 1215-1223
    • Lipford, J.R.1    Worland, S.T.2    Farnet, C.M.3
  • 99
    • 0028034050 scopus 로고
    • Characterization of the minimal DNA-binding domain of the HIV integrase protein
    • Lutzke RAP, Vink C & Plasterk RHA (1994) Characterization of the minimal DNA-binding domain of the HIV integrase protein. Nucleic Acids Research 22: 4125-4131.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4125-4131
    • Rap, L.1    Vink, C.2    Plasterk, R.H.A.3
  • 101
    • 0029166510 scopus 로고
    • Processing of deoxyuridine mismatches and abasic sites by human immunodeficiency virus type I integrase
    • Mazumder A & Pommier Y (1995) Processing of deoxyuridine mismatches and abasic sites by human immunodeficiency virus type I integrase. Nucleic Acids Research 23: 2865-2871.
    • (1995) Nucleic Acids Research , vol.23 , pp. 2865-2871
    • Mazumder, A.1    Pommier, Y.2
  • 102
    • 0028352363 scopus 로고
    • Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase
    • Mazumder A, Engelman A, Craigie R, Fesen M & Pommier Y (1994a) Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase. Nucleic Acids Research 22: 1037-1043.
    • (1994) Nucleic Acids Research , vol.22 , pp. 1037-1043
    • Mazumder, A.1    Engelman, A.2    Craigie, R.3    Fesen, M.4    Pommier, Y.5
  • 103
    • 0028020102 scopus 로고
    • Methylphosphonodiester substitution near the conserved CA dinucleotide in the HIV LTR alters both the extent of 3′-processing and choice of nucleophile by HIV-1 integrase
    • Mazumder A, Gupta M & Pommier Y (1994b) Methylphosphonodiester substitution near the conserved CA dinucleotide in the HIV LTR alters both the extent of 3′-processing and choice of nucleophile by HIV-1 integrase. Nucleic Acids Research 22: 4441-4448.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4441-4448
    • Mazumder, A.1    Gupta, M.2    Pommier, Y.3
  • 106
    • 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 (1995b) Effects of tyrphostins, protein kinase inhibitors, on human immunodeficiency virus type 1 integrase. Biochemistry 34: 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
  • 108
    • 0029964978 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by guanosine quartet structures
    • Mazumder A, Neamati N, Ojwang JO, Sunder S, Rando RF & Pommier Y (1996a) Inhibition of human immunodeficiency virus type 1 integrase by guanosine quartet structures. Biochemistry 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    Pommier, Y.6
  • 109
    • 0029864507 scopus 로고    scopus 로고
    • Chemical trapping of ternary complexes of human immunodeficiency virus type 1 integrase, divalent metal, and DNA substrates containing an abasic site
    • Mazumder A, Neamati N, Pilon A, Sunder S & Pommier Y (1996b) Chemical trapping of ternary complexes of human immunodeficiency virus type 1 integrase, divalent metal, and DNA substrates containing an abasic site. Journal of Biological Chemistry 271: 27330-27338.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 27330-27338
    • Mazumder, A.1    Neamati, N.2    Pilon, A.3    Sunder, S.4    Pommier, Y.5
  • 112
    • 1842285050 scopus 로고    scopus 로고
    • Retroviral integrase: A novel target in antiviral drug development: basic in vitro assays with the purified enzyme
    • Edited by D Kinchington and R Schinazi. Totowa, NJ: Humana Press (in press)
    • Mazumder A, Neamati N, Sunder S, Owen J & Pommier Y (1997a) Retroviral integrase: a novel target in antiviral drug development: basic in vitro assays with the purified enzyme. In Methods in Cellular and Molecular Biology: Antiviral Evaluation. Edited by D Kinchington and R Schinazi. Totowa, NJ: Humana Press (in press).
    • (1997) Methods in Cellular and Molecular Biology: Antiviral Evaluation
    • Mazumder, A.1    Neamati, N.2    Sunder, S.3    Owen, J.4    Pommier, Y.5
  • 114
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: Studies of organization and composition
    • Miller MD, Farnet CM & Bushman FD (1997) Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. Journal of Virology 71: 5382-5390.
    • (1997) Journal of Virology , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 115
    • 0026799383 scopus 로고
    • Polynucleotidyl transfer reactions in transpositional DNA recombination
    • Mizuuchi K (1992) Polynucleotidyl transfer reactions in transpositional DNA recombination. Cell 267: 21273-21276.
    • (1992) Cell , vol.267 , pp. 21273-21276
    • Mizuuchi, K.1
  • 117
    • 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 (1994b) Triple helix formation with short oligonucleotide-intercalator conjugates matching the HIV-1 U3 LTR end sequence. Biochemistry 33: 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
  • 118
    • 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 KS, Merkel GW & Skalka AM (1993) Rapid solution assays for retroviral integration reactions and their use in kinetic analyses of wild-type and mutant Rous sarcoma virus integrases. Proceedings of the National Academy of Sciences, USA 90: 11633-11637.
    • (1993) Proceedings of the National Academy of Sciences, USA , vol.90 , pp. 11633-11637
    • Müller, B.1    Jones, K.S.2    Merkel, G.W.3    Skalka, A.M.4
  • 119
    • 0028067639 scopus 로고
    • DNA bending creates favored sites for retroviral integration: An explanation for preferred insertion sites in nucleosomes
    • Müller H-P & Varmus HE (1994) DNA bending creates favored sites for retroviral integration: an explanation for preferred insertion sites in nucleosomes. EMBO Journal 13: 4704-4714.
    • (1994) EMBO Journal , vol.13 , pp. 4704-4714
    • Müller, H.-P.1    Varmus, H.E.2
  • 120
    • 0026652466 scopus 로고
    • A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the viral integrase in vivo
    • Murphy JE & Goff SP (1992) A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the viral integrase in vivo. Journal of Virology 66: 5092-5095.
    • (1992) Journal of Virology , vol.66 , pp. 5092-5095
    • Murphy, J.E.1    Goff, S.P.2
  • 122
    • 0030855938 scopus 로고    scopus 로고
    • Design and discovery of HIV-1 integrase inhibitors
    • Neamati N, Sunder S & Pommier Y (1997a) Design and discovery of HIV-1 integrase inhibitors. Drug Discovery Today 2: 487-498..
    • (1997) Drug Discovery Today , vol.2 , pp. 487-498
    • Neamati, N.1    Sunder, S.2    Pommier, Y.3
  • 126
    • 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 BM, Haugan IR, Berg K, Olsen L, Brown PO & Helland DE (1996) Monoclonal antibodies against human immunodeficiency virus type 1 integrase: epitope mapping and differential effects on integrase activities in vitro. Journal of Virology 70: 1580-1587.
    • (1996) Journal of Virology , 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
  • 128
    • 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 (1996) 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. Journal of Biomolecular Structure and Dynamics 13: 835-853.
    • (1996) Journal of Biomolecular Structure and Dynamics , 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
  • 129
    • 0030026836 scopus 로고    scopus 로고
    • The metal ion-induced cooperative binding of HIV-1 integrase to DNa exhibits a marked preference for Mn(II) rather than Mg(II)
    • Pemberton IK, Buckle M & Buc H (1996) The metal ion-induced cooperative binding of HIV-1 integrase to DNA exhibits a marked preference for Mn(II) rather than Mg(II). Journal of Biological Chemistry 271: 1498-1506.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 1498-1506
    • Pemberton, I.K.1    Buckle, M.2    Buc, H.3
  • 130
    • 0000420523 scopus 로고    scopus 로고
    • DNA topoisomerase II inhibitors
    • Edited by BA Teicher. Totowa, NJ: Humana Press
    • Pommier Y (1997) DNA topoisomerase II inhibitors. In Cancer Therapeutics: Experimental and Clinical Agents. Edited by BA Teicher. Totowa, NJ: Humana Press, pp. 153-174.
    • (1997) Cancer Therapeutics: Experimental and Clinical Agents , pp. 153-174
    • Pommier, Y.1
  • 131
    • 0028264042 scopus 로고
    • Human immunodeficiency virus integrase directs integration to sites of severe DNA distortion within the nucleosome core
    • Pruss D, Bushman FD & Wolffe AP (1994a) Human immunodeficiency virus integrase directs integration to sites of severe DNA distortion within the nucleosome core. Proceedings of the National Academy of Sciences, USA 91: 5913-5917.
    • (1994) Proceedings of the National Academy of Sciences, USA , vol.91 , pp. 5913-5917
    • Pruss, D.1    Bushman, F.D.2    Wolffe, A.P.3
  • 132
    • 0028125005 scopus 로고
    • The influence of DNA and nucleosome structure on integration events directed by HIV integrase
    • Pruss D, Reeves R, Bushman FD & Wolffe AP (1994b) The influence of DNA and nucleosome structure on integration events directed by HIV integrase. Journal of Biological Chemistry 269: 25031-25041.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 25031-25041
    • Pruss, D.1    Reeves, R.2    Bushman, F.D.3    Wolffe, A.P.4
  • 133
    • 0026696624 scopus 로고
    • Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection
    • Pryciak PM & Varmus HE (1992) Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection. Cell 69: 769-780.
    • (1992) Cell , vol.69 , pp. 769-780
    • Pryciak, P.M.1    Varmus, H.E.2
  • 134
    • 0026567862 scopus 로고
    • Retroviral integration into minichromosomes in vitro
    • Pryciak PM, Sil A & Varmus HE (1992) Retroviral integration into minichromosomes in vitro. EMBO Journal 11: 291-303.
    • (1992) EMBO Journal , vol.11 , pp. 291-303
    • Pryciak, P.M.1    Sil, A.2    Varmus, H.E.3
  • 135
    • 0029122532 scopus 로고
    • Sequences in the human immunodeficiency virus type 1 U3 region required for in vivo and in vitro integration
    • Reicin AS, Kalpana G, Paik S, Marmon S & Goff S (1995) Sequences in the human immunodeficiency virus type 1 U3 region required for in vivo and in vitro integration. Journal of Virology 69: 5904-5907.
    • (1995) Journal of Virology , vol.69 , pp. 5904-5907
    • Reicin, A.S.1    Kalpana, G.2    Paik, S.3    Marmon, S.4    Goff, S.5
  • 137
    • 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 WE, Cordeiro M, Abdel-Malek S, Jia Q, Chow SA, Reinecke MG & Mitchell WM (1996a) Dicaffeoylquinic acid inhibitors of human immunodeficiency virus integrase: inhibition of the core catalytic domain of human immunodeficiency virus integrase. Molecular Pharmacology 50: 846-855.
    • (1996) Molecular Pharmacology , 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
  • 139
    • 0027158091 scopus 로고
    • Integration of murine leukemia virus DNA depends on mitosis
    • Roe T, Reynolds TC, Yu G & Brown PO (1993) Integration of murine leukemia virus DNA depends on mitosis. EMBO Journal 12: 2099-2108.
    • (1993) EMBO Journal , vol.12 , pp. 2099-2108
    • Roe, T.1    Reynolds, T.C.2    Yu, G.3    Brown, P.O.4
  • 140
    • 0031032592 scopus 로고    scopus 로고
    • 3′-End processing and kinetics of 5′-end joining during retroviral integration in vivo
    • Roe T, Chow SA & Brown PO (1997) 3′-End processing and kinetics of 5′-end joining during retroviral integration in vivo. Journal of Virology 71: 1334-1340.
    • (1997) Journal of Virology , vol.71 , pp. 1334-1340
    • Roe, T.1    Chow, S.A.2    Brown, P.O.3
  • 141
    • 0026634793 scopus 로고
    • The N-terminal region of HIV-1 integrase is required for integration activity, but not for DNA-binding
    • Schauer M & Billich A (1992) The N-terminal region of HIV-1 integrase is required for integration activity, but not for DNA-binding. Biochemical and Biophysical Research Communications 185: 874-880.
    • (1992) Biochemical and Biophysical Research Communications , vol.185 , pp. 874-880
    • Schauer, M.1    Billich, A.2
  • 142
    • 0018069786 scopus 로고
    • Virus-coded origin of a 32,000-dalton protein from avian retrovirus cores: Structural relatedness of p32 and the beta polypeptide of the avian retrovirus DNa polymerase
    • Schiff RD & Grandgenett DP (1978) Virus-coded origin of a 32,000-dalton protein from avian retrovirus cores: structural relatedness of p32 and the beta polypeptide of the avian retrovirus DNA polymerase. Journal of Virology 28: 279-291.
    • (1978) Journal of Virology , vol.28 , pp. 279-291
    • Schiff, R.D.1    Grandgenett, D.P.2
  • 143
    • 0031050297 scopus 로고    scopus 로고
    • Disruption of the terminal base pairs of retroviral DNA during integration
    • Scottoline BP, Chow S, Effison V & Brown PO (1997) Disruption of the terminal base pairs of retroviral DNA during integration. Genes and Development 11: 371-382.
    • (1997) Genes and Development , vol.11 , pp. 371-382
    • Scottoline, B.P.1    Chow, S.2    Effison, V.3    Brown, P.O.4
  • 144
    • 0025366844 scopus 로고
    • Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity
    • Sherman PA & Fyfe JA (1990) Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity. Proceedings of the National Academy of Sciences, USA 87: 5119-5123.
    • (1990) Proceedings of the National Academy of Sciences, USA , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 145
    • 0026693410 scopus 로고
    • Human immunodeficiency virus type 1 integration protein: DNA sequence requirements for cleaving and joining reactions
    • Sherman PA, Dickson ML & Fyfe JA (1992) Human immunodeficiency virus type 1 integration protein: DNA sequence requirements for cleaving and joining reactions. Journal of Virology 66: 3593-3601.
    • (1992) Journal of Virology , vol.66 , pp. 3593-3601
    • Sherman, P.A.1    Dickson, M.L.2    Fyfe, J.A.3
  • 146
    • 0024292602 scopus 로고
    • Highly preferred targets for retrovirus integration
    • Shih C-C, Stoye JF & Coffin JM (1988) Highly preferred targets for retrovirus integration. Cell 53: 531-538.
    • (1988) Cell , vol.53 , pp. 531-538
    • Shih, C.-C.1    Stoye, J.F.2    Coffin, J.M.3
  • 147
    • 0028006533 scopus 로고
    • Genetic analysis of the human immunodeficiency virus type 1 integrase protein
    • Shin C-C, Taddeo WA, Haseltine WA & Farnet CM (1994) Genetic analysis of the human immunodeficiency virus type 1 integrase protein. Journal of Virology 68: 1633-1642.
    • (1994) Journal of Virology , vol.68 , pp. 1633-1642
    • Shin, C.-C.1    Taddeo, W.A.2    Haseltine, W.A.3    Farnet, C.M.4
  • 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 RG, Frere V, Bouziane M, Auclair C, Troalen F & Fermandjian S (1996) 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. European Journal of Biochemistry 240: 765-773.
    • (1996) European Journal of Biochemistry , 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
    • 0028846457 scopus 로고
    • Erbstatin analogue methyl 2,5-dihydroxycinnamate cross-links proteins and is cytotoxic to normal and neoplastic epithelial cells by a mechanism independent of tyrosine kinase inhibition
    • Stanwell C, Burke TR & Yuspa SH (1995) Erbstatin analogue methyl 2,5-dihydroxycinnamate cross-links proteins and is cytotoxic to normal and neoplastic epithelial cells by a mechanism independent of tyrosine kinase inhibition. Cancer Research 55: 4950-4956.
    • (1995) Cancer Research , vol.55 , pp. 4950-4956
    • Stanwell, C.1    Burke, T.R.2    Yuspa, S.H.3
  • 151
    • 0029838374 scopus 로고    scopus 로고
    • Sequence analysis of the human DNA flanking sites of human immunodeficiency virus type 1 integration
    • Stevens SW & Griffith JD (1996) Sequence analysis of the human DNA flanking sites of human immunodeficiency virus type 1 integration. Journal of Virology 70: 6459-6462.
    • (1996) Journal of Virology , vol.70 , pp. 6459-6462
    • Stevens, S.W.1    Griffith, J.D.2
  • 152
    • 0028131189 scopus 로고
    • Identification of factors that govern HIV-1 replication in non-dividing cells
    • Stevenson M (1994) Identification of factors that govern HIV-1 replication in non-dividing cells. AIDS Research and Human Retroviruses 10: S11-S15.
    • (1994) AIDS Research and Human Retroviruses , vol.10
    • Stevenson, M.1
  • 153
    • 0025238945 scopus 로고
    • HIV-1 replication is controlled at the level of T cell activation and proviral integration
    • Stevenson M, Stanwick TL, Dempsey MP & Lamonica CA (1990) HIV-1 replication is controlled at the level of T cell activation and proviral integration. EMBO Journal 9: 1551-1560.
    • (1990) EMBO Journal , vol.9 , pp. 1551-1560
    • Stevenson, M.1    Stanwick, T.L.2    Dempsey, M.P.3    Lamonica, C.A.4
  • 154
    • 0029861757 scopus 로고    scopus 로고
    • Reversion of a human immunodeficiency virus type 1 integrase mutant at a second site restores enzyme function and virus infectivity
    • Taddeo B, Carlini F, Verani P & Engelman A (1996) Reversion of a human immunodeficiency virus type 1 integrase mutant at a second site restores enzyme function and virus infectivity. Journal of Virology 12: 8277-8284.
    • (1996) Journal of Virology , vol.12 , pp. 8277-8284
    • Taddeo, B.1    Carlini, F.2    Verani, P.3    Engelman, A.4
  • 155
    • 0028089732 scopus 로고
    • DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein
    • van den Ent FMI, Vink C & Plasterk RHA (1994) DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein. Journal of Virology 68: 7825-7832.
    • (1994) Journal of Virology , vol.68 , pp. 7825-7832
    • Van Den Ent, F.M.I.1    Vink, C.2    Plasterk, R.H.A.3
  • 156
    • 0025775488 scopus 로고
    • DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2
    • van Gent DC, Elgersma Y, Bolk MW, Vink C & Plasterk RHA (1991) DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2. Nucleic Acids Research 19: 3821-3827.
    • (1991) Nucleic Acids Research , 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
  • 159
    • 0023038804 scopus 로고
    • Acceptor sites for retroviral integrations map near DNase I-hypersensitive sites in chromatin
    • Vijaya S, Steffen DL & Robinson HL (1986) Acceptor sites for retroviral integrations map near DNase I-hypersensitive sites in chromatin. Journal of Virology 60: 665-697.
    • (1986) Journal of Virology , vol.60 , pp. 665-697
    • Vijaya, S.1    Steffen, D.L.2    Robinson, H.L.3
  • 160
    • 0027508068 scopus 로고
    • The human immunodeficiency virus integrase protein
    • Vink C & Plasterk RHA (1993) The human immunodeficiency virus integrase protein. Trends in Genetics 9: 433-437.
    • (1993) Trends in Genetics , vol.9 , pp. 433-437
    • Vink, C.1    Plasterk, R.H.A.2
  • 161
    • 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 GA, van Boom JH & Plasterk RHA (1991a) Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein. Nucleic Acids Research 19: 6691-6698.
    • (1991) Nucleic Acids Research , 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
  • 162
    • 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 DC, Elgersma Y & Plasterk RHA (1991b) Human immunodeficiency virus integrase protein requires a subterminal position for its viral DNA recognition sequence for efficient cleavage. Journal of Virology 65: 4636-4644.
    • (1991) Journal of Virology , vol.65 , pp. 4636-4644
    • Vink, C.1    Van Gent, D.C.2    Elgersma, Y.3    Plasterk, R.H.A.4
  • 163
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein
    • Vink C, Oude Groeninger AAM & Plasterk RHA (1993) Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein. Nucleic Acids Research 21: 1419-1425.
    • (1993) Nucleic Acids Research , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeninger, A.A.M.2    Plasterk, R.H.A.3
  • 164
    • 0028125329 scopus 로고
    • Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA
    • Vink C, Lutzke RAP & Plasterk RHA (1994a) Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA. Nucleic Acids Research 22: 4103-4110.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4103-4110
    • Vink, C.1    Lutzke, R.A.P.2    Plasterk, R.H.A.3
  • 165
    • 0028238134 scopus 로고
    • A high-throughput, non-radioactive microtiter plate assay for activity of the human immunodeficiency virus integrase protein
    • Vink C, Banks M, Bethell R & Plasterk RHA (1994b) A high-throughput, non-radioactive microtiter plate assay for activity of the human immunodeficiency virus integrase protein. Nucleic Acids Research 22: 2176-2177.
    • (1994) Nucleic Acids Research , vol.22 , pp. 2176-2177
    • Vink, C.1    Banks, M.2    Bethell, R.3    Plasterk, R.H.A.4
  • 166
    • 0028234528 scopus 로고
    • The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allow the establishment of infection in macrophages and quiescent T lymphocytes
    • von Schwedler U, Kornbluth RS & Trono D (1994) The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allow the establishment of infection in macrophages and quiescent T lymphocytes. Proceedings of the National Academy of Sciences, USA 91: 6992-6996.
    • (1994) Proceedings of the National Academy of Sciences, USA , vol.91 , pp. 6992-6996
    • Von Schwedler, U.1    Kornbluth, R.S.2    Trono, D.3
  • 167
    • 0028784884 scopus 로고
    • Assembly and catalytic properties of retrovirus integrase-DNA complexes capable of efficiently performing concerted integration
    • Vora AC & Grandgenett DP (1995) Assembly and catalytic properties of retrovirus integrase-DNA complexes capable of efficiently performing concerted integration. Journal of Virology 69: 7483-7488.
    • (1995) Journal of Virology , vol.69 , pp. 7483-7488
    • Vora, A.C.1    Grandgenett, D.P.2
  • 169
    • 0028924020 scopus 로고
    • Human immunodeficiency virus type 1 integrase: Effects of mutations on viral ability to integrate, direct viral gene expression from unintegrated viral DNA templates, and sustain viral propagation in primary cells
    • Wiskerchen M & Muesing MA (1995a) Human immunodeficiency virus type 1 integrase: effects of mutations on viral ability to integrate, direct viral gene expression from unintegrated viral DNA templates, and sustain viral propagation in primary cells. Journal of Virology 69: 376-386.
    • (1995) Journal of Virology , vol.69 , pp. 376-386
    • Wiskerchen, M.1    Muesing, M.A.2
  • 170
    • 0028936208 scopus 로고
    • Identification and characterization of a temperature-sensitive mutant of human immunodeficiency virus type 1 by alanine scanning mutagenesis of the integrase gene
    • Wiskerchen M & Muesing MA (1995b) Identification and characterization of a temperature-sensitive mutant of human immunodeficiency virus type 1 by alanine scanning mutagenesis of the integrase gene. Journal of Virology 69: 597-601.
    • (1995) Journal of Virology , vol.69 , pp. 597-601
    • Wiskerchen, M.1    Muesing, M.A.2
  • 173
    • 0027205243 scopus 로고
    • Characterization of a DNa binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis
    • Woerner AM & Marcus-Sekura CJ (1993) Characterization of a DNA binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis. Nucleic Acids Research 21: 3507-3511.
    • (1993) Nucleic Acids Research , vol.21 , pp. 3507-3511
    • Woerner, A.M.1    Marcus-Sekura, C.J.2
  • 174
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang W & Steitz TA (1995) Recombining the structures of HIV integrase, RuvC and RNase H. Current Biology 3: 131-134.
    • (1995) Current Biology , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 175
    • 0028908038 scopus 로고
    • Different roles of bases within the integration signal sequence of human immunodeficiency virus type 1 in vitro
    • Yoshinaga T & Fujiwara T (1995) Different roles of bases within the integration signal sequence of human immunodeficiency virus type 1 in vitro. Journal of Virology 69: 3233-3236.
    • (1995) Journal of Virology , vol.69 , pp. 3233-3236
    • Yoshinaga, T.1    Fujiwara, T.2
  • 176
    • 0028087997 scopus 로고
    • Detection and characterization of a functional complex of human immunodeficiency virus type 1 intergrase and its substance by UV cross-linking
    • Yoshinaga T, Kimura-Ohtani Y & Fujiwara T (1994) Detection and characterization of a functional complex of human immunodeficiency virus type 1 intergrase and its substance by UV cross-linking. Journal of Virology 68: 5690-5697.
    • (1994) Journal of Virology , vol.68 , pp. 5690-5697
    • Yoshinaga, T.1    Kimura-Ohtani, Y.2    Fujiwara, T.3
  • 180
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng R, Jenkins TM & Craigie R (1996) Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proceedings of the National Academy of Sciences, USA 93: 13659-13664.
    • (1996) Proceedings of the National Academy of Sciences, USA , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.