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Volumn 36, Issue 3, 1997, Pages 139-156

Molecular mechanisms in retrovirus DNA integration

Author keywords

Integrase; Integration; Retrovirus

Indexed keywords

1,3 BIS(5,7 HYDROXY 2 NAPHTHALENECARBOXAMIDO)PROPANE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIVIRUS AGENT; AROMATIC AMIDE; AURINTRICARBOXYLIC ACID; BETA CONINDENDROL; BIS NAPHTHOYLAMIDE DERIVATIVE; CAFFEIC ACID DERIVATIVE; CAFFEIC ACID PHENETHYL ESTER; CATECHOL DERIVATIVE; CICHORIC ACID; CURCUMIN; CYNARINE; FLAVONE DERIVATIVE; INTEGRASE; INTEGRASE INHIBITOR; INTERCALATING AGENT; LIGNAN; MONOCLONAL ANTIBODY; QUERCETAGENIN; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS ENZYME;

EID: 0031434606     PISSN: 01663542     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-3542(97)00046-6     Document Type: Article
Times cited : (148)

References (127)
  • 1
    • 0029974222 scopus 로고    scopus 로고
    • Concerted integration of linear retroviral DNA by the avian sarcoma virus integrase in vitro: Dependence on both long terminal repeat termini
    • Aiyar A., Hindmarsh P., Skalka A.M., Leis J. Concerted integration of linear retroviral DNA by the avian sarcoma virus integrase in vitro: dependence on both long terminal repeat termini. J. Virol. 70:1996;3571-3580.
    • (1996) J. Virol. , vol.70 , pp. 3571-3580
    • Aiyar, A.1    Hindmarsh, P.2    Skalka, A.M.3    Leis, J.4
  • 2
    • 0029055551 scopus 로고
    • Isolation of high-affinity RNA ligands to HIV-1 integrase from a random pool
    • Allen P., Worland S., Gold L. Isolation of high-affinity RNA ligands to HIV-1 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
  • 3
    • 0028863151 scopus 로고
    • Multimerization determinants reside in both the catalytic core and C-terminus of avian sarcoma virus integrase
    • Andrake M., Skalka A.M. Multimerization determinants reside in both the catalytic core and C-terminus of avian sarcoma virus integrase. J. Biol. Chem. 270:1995;29299-29306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29299-29306
    • Andrake, M.1    Skalka, A.M.2
  • 4
    • 0029814410 scopus 로고    scopus 로고
    • Retroviral integrases: Putting the pieces together
    • Andrake M., Skalka A.M. Retroviral integrases: putting the pieces together. J. Biol. Chem. 271:1996;19633-19636.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19633-19636
    • Andrake, M.1    Skalka, A.M.2
  • 5
    • 0030922072 scopus 로고    scopus 로고
    • A metal-induced conformational change and activation in HIV-1 integrase
    • Asante-Appiah E., Skalka A.M. A metal-induced conformational change and activation in 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
  • 6
    • 0028120546 scopus 로고
    • Atomic structure of Ruv C resolvase: A Holliday junction-specific endonuclease from E. coli
    • Ariyoshi M., Vassylyev D.G., Iwasaki H., Nakamura H., Shinagawa H., Morikawa K. Atomic structure of Ruv C resolvase: a Holliday junction-specific endonuclease from E. coli. Cell. 78:1994;1063-1072.
    • (1994) Cell , vol.78 , pp. 1063-1072
    • Ariyoshi, M.1    Vassylyev, D.G.2    Iwasaki, H.3    Nakamura, H.4    Shinagawa, H.5    Morikawa, K.6
  • 7
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two-metal ion mechanism
    • Beese L.S., Steitz T.A. Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two-metal ion mechanism. EMBO J. 10:1991;25-33.
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 8
    • 0024654338 scopus 로고
    • A nucleoprotein complex mediates the integration of retroviral DNA
    • Bowerman B., Brown P.O., Bishop J.M., Varmus H.E. A nucleoprotein complex mediates the integration of retroviral DNA. Genes Dev. 3:1989;469-478.
    • (1989) Genes Dev. , vol.3 , pp. 469-478
    • Bowerman, B.1    Brown, P.O.2    Bishop, J.M.3    Varmus, H.E.4
  • 9
    • 0023647997 scopus 로고
    • Correct integration of retroviral DNA in vitro
    • Brown P.O., Bowerman B., Varmus H.E., Bishop J.M. Correct integration of retroviral DNA in vitro. Cell. 49:1987;347-356.
    • (1987) Cell , vol.49 , pp. 347-356
    • Brown, P.O.1    Bowerman, B.2    Varmus, H.E.3    Bishop, J.M.4
  • 11
    • 0029643858 scopus 로고
    • The catalytic domain of avian sarcoma virus integrase: Confirmation of the active site residues in the presence of divalent cations
    • Bujacz G., Jaskólski M., Alexandratos J., Wlodawer A., Merkel G., Katz R.A., Skalka A.M. The catalytic domain of avian sarcoma virus integrase: confirmation of the active site residues in the presence of divalent cations. Structure. 4:1995;89-96.
    • (1995) Structure , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskólski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5    Katz, R.A.6    Skalka, A.M.7
  • 12
    • 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
  • 17
    • 0027199982 scopus 로고
    • Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection
    • Bukrinsky M.I., Sharova N., McDonald T.L., Pusharskaya T., Stevenson M. Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection. Proc. Natl. Acad. Sci. USA. 90:1993;6125-6129.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6125-6129
    • Bukrinsky, M.I.1    Sharova, N.2    McDonald, T.L.3    Pusharskaya, T.4    Stevenson, M.5
  • 19
    • 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. USA. 88:1991;1339-1343.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1339-1343
    • Bushman, F.D.1    Craigie, R.2
  • 20
    • 0028205117 scopus 로고
    • Rous sarcoma virus integrase: Mapping functions for catalysis and substrate binding
    • Bushman F.D., Wang B. Rous sarcoma virus integrase: mapping functions for catalysis and substrate binding. J. Virol. 68:1994;2215-2223.
    • (1994) J. Virol. , vol.68 , pp. 2215-2223
    • Bushman, F.D.1    Wang, B.2
  • 21
    • 0030986376 scopus 로고    scopus 로고
    • Solution structure of the N-terminal zinc binding domain of HIV-1 integrase
    • Cai M., Zheng R., Caffrey R., Clove M., Gronenborn A.M. Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nature Struct. Biol. 4:1997;567-577.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 567-577
    • Cai, M.1    Zheng, R.2    Caffrey, R.3    Clove, M.4    Gronenborn, A.M.5
  • 23
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus type
    • Chow S.A., Vincent K.A., Ellison V., Brown P.O. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus type. Science. 25:1992;723-726.
    • (1992) Science , vol.25 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 24
    • 0022318818 scopus 로고
    • Mutants and pseudorevertants of Moloney murine leukemia virus with alterations at the integration site
    • Colicelli J., Goff S.P. Mutants and pseudorevertants of Moloney murine leukemia virus with alterations at the integration site. Cell. 42:1985;573-580.
    • (1985) Cell , vol.42 , pp. 573-580
    • Colicelli, J.1    Goff, S.P.2
  • 25
    • 0028008793 scopus 로고
    • Combinative interactions of a human immunodeficiency virus (HIV) tat antagonist with reverse transcriptase inhibitors and HIV protease inhibitor
    • Connell E.V., Hsu M.-C., Richman D.D. Combinative interactions of a human immunodeficiency virus (HIV) tat antagonist with reverse transcriptase inhibitors and HIV protease inhibitor. Antimicrob. Agents Chemother. 38:1994;348-352.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 348-352
    • Connell, E.V.1    Hsu, M.-C.2    Richman, D.D.3
  • 26
    • 0027302144 scopus 로고
    • Antiviral synergy between inhibitors of HIV proteinase and reverse transcriptase
    • Craig J.C., Duncan J.B., Whitakker L., Roberts N.A. Antiviral synergy between inhibitors of HIV proteinase and reverse transcriptase. Antivir. Chem. Chemother. 4:1993;161-166.
    • (1993) Antivir. Chem. Chemother. , vol.4 , pp. 161-166
    • Craig, J.C.1    Duncan, J.B.2    Whitakker, L.3    Roberts, N.A.4
  • 27
    • 0025031786 scopus 로고
    • The IN protein of Moloney murine leukemia virus processes the viral DNA ends and accomplishes their integration in vitro
    • Craigie R., Fujiwara T., Bushman F. The IN protein of Moloney murine leukemia virus processes the viral DNA ends and accomplishes their integration in vitro. Cell. 62:1990;829-837.
    • (1990) Cell , vol.62 , pp. 829-837
    • Craigie, R.1    Fujiwara, T.2    Bushman, F.3
  • 28
    • 0026637378 scopus 로고
    • Hotspots and warm spots: Integration specificity of retroelements
    • Craigie R. Hotspots and warm spots: integration specificity of retroelements. Trends Genet. 8:1992;187-190.
    • (1992) Trends Genet. , vol.8 , pp. 187-190
    • Craigie, R.1
  • 29
    • 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
  • 31
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies J.F. II, Hostomska Z., Hostomsky Z., Jordan S.R., Matthews D.A. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science. 252:1991;88-95.
    • (1991) Science , vol.252 , pp. 88-95
    • Davies J.F. II1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 32
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda F., Hickman A.B., Jenkins T.M., Engelman A., Craigie R., Davies D.R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science. 266:1994;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
  • 33
    • 0030041593 scopus 로고    scopus 로고
    • (-)-Arctigenin as a lead structure for inhibitors of human immunodeficiency virus type 1 integrase
    • Eich E., Pietz H., Kaloga M., Schultz 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    Pietz, H.2    Kaloga, M.3    Schultz, J.4    Fesen, M.R.5    Mazumder, A.6    Pommier, Y.7
  • 35
    • 0025337327 scopus 로고
    • Human immunodeficiency virus integration in a cell-free system
    • Ellison V., Abrams H., Roe T., Lifson J., Brown P.O. Human immunodeficiency virus integration 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.O.5
  • 36
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison V., Brown P.O. A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc. Natl. Acad. Sci. USA. 91:1994;7316-7320.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 37
    • 0028888455 scopus 로고
    • An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer
    • Ellison V., Gerton J., Vincent K.A., Brown P.O. An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer. J. Biol. Chem. 270:1995;3320-3326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3320-3326
    • Ellison, V.1    Gerton, J.2    Vincent, K.A.3    Brown, P.O.4
  • 38
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro
    • Engelman A., Craigie R. Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro. J. Virol. 66:1992;6361-6369.
    • (1992) J. Virol. , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 39
    • 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. 67:1992;1211-1221.
    • (1992) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 40
    • 0027179694 scopus 로고
    • Identification of discreet functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman A., Bushman F.D., Craigie R. Identification of discreet functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO J. 12:1993;3269-3275.
    • (1993) EMBO J. , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 41
    • 0028067324 scopus 로고
    • The core and C-terminal domains of the integrase from human immunodeficiency virus type 1 each contribute to nonspecific DNA binding
    • Engelman A., Hickman A.B., Craigie R. The core and C-terminal domains of the integrase from human immunodeficiency virus type 1 each contribute to nonspecific DNA binding. J. Virol. 68:1994;5911-5917.
    • (1994) J. Virol. , vol.68 , pp. 5911-5917
    • Engelman, A.1    Hickman, A.B.2    Craigie, R.3
  • 42
    • 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
  • 43
    • 0030988998 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the catalytic domain of human immunodeficiency type 1 integrase
    • Engelman A., Ying L., Chen H., Farzan M., Dyda F. Structure-based mutagenesis of the catalytic domain of human immunodeficiency type 1 integrase. J. Virol. 71:1997;3507-3514.
    • (1997) J. Virol. , vol.71 , pp. 3507-3514
    • Engelman, A.1    Ying, L.2    Chen, H.3    Farzan, M.4    Dyda, F.5
  • 44
    • 0025968854 scopus 로고
    • Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex
    • Farnet C.M., Haseltine W.A. Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex. J. Virol. 65:1991;1910-1915.
    • (1991) J. Virol. , vol.65 , pp. 1910-1915
    • Farnet, C.M.1    Haseltine, W.A.2
  • 45
    • 0031004162 scopus 로고    scopus 로고
    • HIV-1 cDNA integration: Requirement of HMG I(Y) protein for function of preintegration complexes in vitro
    • Farnet C.M., Bushman F.D. HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro. Cell. 88:1997;483-492.
    • (1997) Cell , vol.88 , pp. 483-492
    • Farnet, C.M.1    Bushman, F.D.2
  • 46
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet O., Ramond P., Polard P., Prére M.F., Chandler M. Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences? Mol. Microbiol. 4:1990;1771-1777.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1771-1777
    • Fayet, O.1    Ramond, P.2    Polard, P.3    Prére, M.F.4    Chandler, M.5
  • 48
    • 0028070994 scopus 로고
    • Inhibition of HIV-1 integrase by flavones, caffeic acid phenthyl ester (CAPE) and related compounds
    • Fesen M.R., Pommier Y., Leteurtre F., Hiroguchi S., Yung J., Kohn K. Inhibition of HIV-1 integrase by flavones, caffeic acid phenthyl ester (CAPE) and related compounds. Biochem. Pharm. 48:1994;595-608.
    • (1994) Biochem. Pharm. , vol.48 , pp. 595-608
    • Fesen, M.R.1    Pommier, Y.2    Leteurtre, F.3    Hiroguchi, S.4    Yung, J.5    Kohn, K.6
  • 49
    • 0026760582 scopus 로고
    • Concerted integration of viral DNA termini by purified avian myeloblastosis virus integrase
    • Fitzgerald M.L., Vora A.C., Zeh W.G., Grandgenett D.P. Concerted integration of viral DNA termini by purified avian myeloblastosis virus integrase. J. Virol. 66:1992;6257-6263.
    • (1992) J. Virol. , vol.66 , pp. 6257-6263
    • Fitzgerald, M.L.1    Vora, A.C.2    Zeh, W.G.3    Grandgenett, D.P.4
  • 50
    • 0028283854 scopus 로고
    • HIV-1 infection of non-dividing cells
    • Freed E.O., Martin M.A. HIV-1 infection of non-dividing cells. Nature. 369:1994;107-108.
    • (1994) Nature , vol.369 , pp. 107-108
    • Freed, E.O.1    Martin, M.A.2
  • 51
    • 0029062117 scopus 로고
    • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection
    • Freed E.O., Englund G., Martin M.A. Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection. J. Virol. 69:1995;3949-3954.
    • (1995) J. Virol. , vol.69 , pp. 3949-3954
    • Freed, E.O.1    Englund, G.2    Martin, M.A.3
  • 52
    • 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. 88:1997;171-174.
    • (1997) Cell , vol.88 , pp. 171-174
    • Freed, E.O.1    Englund, G.2    Maldarelli, F.3    Martin, M.A.4
  • 53
    • 0028821383 scopus 로고
    • HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator
    • Gallay P., Swingler S., Aiken C., Trono D. HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator. Cell. 80:1995;379-388.
    • (1995) Cell , vol.80 , pp. 379-388
    • Gallay, P.1    Swingler, S.2    Aiken, C.3    Trono, D.4
  • 54
    • 0028839344 scopus 로고
    • HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase
    • Gallay P., Swingler S., Song J., Bushman F., Trono D. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase. Cell. 83:1995;569-576.
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 55
    • 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.P. Concerted integration of retrovirus-like DNA by human immunodeficiency virus type 1 integrase. J. Virol. 69:1995;6090-6097.
    • (1995) J. Virol. , vol.69 , pp. 6090-6097
    • Goodarzi, G.1    Im, G.-J.2    Brackmann, K.3    Grandgenett, D.P.4
  • 56
    • 0029655849 scopus 로고    scopus 로고
    • Directed integration of viral DNA mediated by fusion proteins consisting of human immunodeficiency virus type 1 integrase and E. coli Lex A protein
    • Goulaouic H., Chow S.A. Directed integration of viral DNA mediated by fusion proteins consisting of human immunodeficiency virus type 1 integrase and E. coli Lex A protein. J. Virol. 70:1996;37-46.
    • (1996) J. Virol. , vol.70 , pp. 37-46
    • Goulaouic, H.1    Chow, S.A.2
  • 58
    • 0027973067 scopus 로고
    • Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase
    • Hickman A.B., Palmer A., Engelman R., Craigie R., Wingfield P. Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase. J. Biol. Chem. 46:1994;29279-29287.
    • (1994) J. Biol. Chem. , vol.46 , pp. 29279-29287
    • Hickman, A.B.1    Palmer, A.2    Engelman, R.3    Craigie, R.4    Wingfield, P.5
  • 59
    • 0027404369 scopus 로고
    • Human immunodeficiency virus type 1 DNA integration: Fine structure target analysis using synthetic oligonucleotides
    • Hong T., Murphy E., Groarke J., Drlica K. Human immunodeficiency virus type 1 DNA integration: Fine structure target analysis using synthetic oligonucleotides. J. Virol. 67:1993;1127-1131.
    • (1993) J. Virol. , vol.67 , pp. 1127-1131
    • Hong, T.1    Murphy, E.2    Groarke, J.3    Drlica, K.4
  • 60
    • 0029980485 scopus 로고    scopus 로고
    • A soluble active mutant of HIV-1 integrase: Multimerization involves the core and C-terminal domains
    • Jenkins T.M., Engelman A., Ghirlando R., Craigie R. A soluble active mutant of HIV-1 integrase: multimerization involves the core and C-terminal domains. J. Biol. Chem. 271:1996;7712-7718.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 61
    • 2642604727 scopus 로고
    • Computer analysis of retroviral pol genes: Assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes
    • Johnson M.S., McClure M.A., Feng D.-F., Gray J., Doolittle R.F. Computer analysis of retroviral pol genes: assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes. Proc. Natl. Acad. Sci. USA. 83:1986;7648-7652.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7648-7652
    • Johnson, M.S.1    McClure, M.A.2    Feng, D.-F.3    Gray, J.4    Doolittle, R.F.5
  • 62
    • 0024491687 scopus 로고
    • Synergistic inhibition of human immunodeficiency virus type 1 and type 2 replication in vitro by castanospermine and 3′-azido-3′-deoxythymidine
    • Johnson V.A., Walker B.D., Barhus M.A., Paradis T.J., Chou T.-C., Hirsch M.S. Synergistic inhibition of human immunodeficiency virus type 1 and type 2 replication in vitro by castanospermine and 3′-azido-3′-deoxythymidine. Antimicrob. Agents Chemother. 33:1989;53-57.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 53-57
    • Johnson, V.A.1    Walker, B.D.2    Barhus, M.A.3    Paradis, T.J.4    Chou, T.-C.5    Hirsch, M.S.6
  • 63
    • 0026665238 scopus 로고
    • Retroviral integrase functions as a multimer and can turn over catalytically
    • Jones K.S., Coleman J., Merkel G.W., Laue T.M., Skalka A.M. Retroviral integrase functions as a multimer and can turn over catalytically. J. Biol. Chem. 267:1992;16037-16040.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16037-16040
    • Jones, K.S.1    Coleman, J.2    Merkel, G.W.3    Laue, T.M.4    Skalka, A.M.5
  • 64
    • 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
  • 65
    • 0027377121 scopus 로고
    • Crystal structure of Escherichia coli RNase H1 in complex with Mg at 2.8 A resolution: Proof of a single Mg-binding site
    • Katayanagi K., Okumura M., Morikawa K. Crystal structure of Escherichia coli RNase H1 in complex with Mg at 2.8 A resolution: proof of a single Mg-binding site. Prot. Struct. Func. Genet. 17:1993;337-346.
    • (1993) Prot. Struct. Func. Genet. , vol.17 , pp. 337-346
    • Katayanagi, K.1    Okumura, M.2    Morikawa, K.3
  • 66
    • 0025011051 scopus 로고
    • The avian retroviral IN protein is both necessary and sufficient for integration recombination in vitro
    • Katz R.A., Merkel G., Kulkosky J., Leis J., Skalka A.M. The avian retroviral IN protein is both necessary and sufficient for integration recombination in vitro. Cell. 63:1990;87-95.
    • (1990) Cell , vol.63 , pp. 87-95
    • Katz, R.A.1    Merkel, G.2    Kulkosky, J.3    Leis, J.4    Skalka, A.M.5
  • 67
    • 0029862622 scopus 로고    scopus 로고
    • Targeting of retroviral integrase by a fusion to a heterologous DNA binding domain: Ln vitro activities and incorporation of a fusion protein into viral particles
    • Katz R.A., Merkel G., Skalka A.M. Targeting of retroviral integrase by a fusion to a heterologous DNA binding domain: ln vitro activities and incorporation of a fusion protein into viral particles. Virology. 217:1996;178-190.
    • (1996) Virology , vol.217 , pp. 178-190
    • Katz, R.A.1    Merkel, G.2    Skalka, A.M.3
  • 68
    • 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
  • 69
    • 0029861955 scopus 로고    scopus 로고
    • Influence of subterminal viral DNA nucleotides on differential susceptibility to cleavage by human immunodeficiency virus type 1 and visna virus integrases
    • Katzman M., Sudol M. Influence of subterminal viral DNA nucleotides 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
  • 70
    • 0026651815 scopus 로고
    • Nonrandom integration of retroviral DNA in vitro: Effect of CpG methylation
    • Kitamura Y., Lee Y.M., Coffin J.M. Nonrandom integration of retroviral DNA in vitro: effect of CpG methylation. Proc. Natl. Acad. Sci. USA. 89:1992;5532-5536.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5532-5536
    • Kitamura, Y.1    Lee, Y.M.2    Coffin, J.M.3
  • 71
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Khan E., Mack J.P.G., 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.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.G.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 72
    • 0028790504 scopus 로고
    • Enhanced and coordinated processing of viral DNA ends by retroviral integrates in vitro
    • Kukolj G., Skalka A.M. Enhanced and coordinated processing of viral DNA ends by retroviral integrates in vitro. Genes Dev. 9:1995;2556-2567.
    • (1995) Genes Dev. , vol.9 , pp. 2556-2567
    • Kukolj, G.1    Skalka, A.M.2
  • 73
    • 0031060369 scopus 로고    scopus 로고
    • Subcellular localization of avian sarcoma virus and human immunodeficiency virus type 1 integrases
    • Kukolj G., Jones K.S., Skalka A.M. Subcellular localization of avian sarcoma virus and human immunodeficiency virus type 1 integrases. J. Virol. 71:1997;843-847.
    • (1997) J. Virol. , vol.71 , pp. 843-847
    • Kukolj, G.1    Jones, K.S.2    Skalka, A.M.3
  • 74
    • 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 K.S., Katz R.A., Mack J.P.G., Skalka A.M. Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Mol. Cell. Biol. 12:1992;2331-2338.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2331-2338
    • Kulkosky, J.1    Jones, K.S.2    Katz, R.A.3    Mack, J.P.G.4    Skalka, A.M.5
  • 75
    • 0028850802 scopus 로고
    • Activities and substrate specificity of the evolutionarily conserved central domain of retroviral integrase
    • Kulkosky J., Katz R.A., Merkel G., Skalka A.M. Activities and substrate specificity of the evolutionarily conserved central domain of retroviral integrase. Virology. 206:1995;448-456.
    • (1995) Virology , vol.206 , pp. 448-456
    • Kulkosky, J.1    Katz, R.A.2    Merkel, G.3    Skalka, A.M.4
  • 76
    • 0026072804 scopus 로고
    • Substrate specificity of recombinant human immunodeficiency virus type 1 integrase protein
    • LaFemina R.L., Callahan P.L., Cordingley M.G. Substrate specificity of recombinant human immunodeficiency virus type 1 integrase protein. J. Virol. 65:1991;5624-5630.
    • (1991) J. Virol. , vol.65 , pp. 5624-5630
    • Lafemina, R.L.1    Callahan, P.L.2    Cordingley, M.G.3
  • 77
    • 0026459411 scopus 로고
    • Requirement of active human immunodeficiency virus type 1 integrase enzyme for proactive infection of human T-lymphoid cells
    • LaFemina R.L., Schneider C.L., Robbins H.L., Callahan P.L., LeGrow K., Roth E., Schleif W.A., Emini E.A. Requirement of active human immunodeficiency virus type 1 integrase enzyme for proactive infection of human T-lymphoid cells. J. Virol. 66:1992;7414-7419.
    • (1992) J. Virol. , vol.66 , pp. 7414-7419
    • Lafemina, R.L.1    Schneider, C.L.2    Robbins, H.L.3    Callahan, P.L.4    Legrow, K.5    Roth, E.6    Schleif, W.A.7    Emini, E.A.8
  • 79
    • 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 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) J. Virol. , vol.66 , pp. 2359-2368
    • Leavitt, A.D.1    Rose, R.B.2    Varmus, H.E.3
  • 80
    • 0025221829 scopus 로고
    • Efficient autointegration of avian retrovirus DNA in vitro
    • Lee Y.M.H., Coffin J.M. Efficient autointegration of avian retrovirus DNA in vitro. J. Virol. 64:1990;5624-5630.
    • (1990) J. Virol. , vol.64 , pp. 5624-5630
    • Lee, Y.M.H.1    Coffin, J.M.2
  • 81
    • 0344913991 scopus 로고
    • Protection of retroviral DNA from autointegration: Involvement of a cellular factor
    • Lee M.S., Craigie R. Protection of retroviral DNA from autointegration: involvement of a cellular factor. Proc. Natl. Acad. Sci. USA. 64:1994;5958-5965.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.64 , pp. 5958-5965
    • Lee, M.S.1    Craigie, R.2
  • 82
    • 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
  • 83
    • 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
  • 84
    • 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. 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.10
  • 85
    • 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
  • 87
    • 0028242724 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 by 3′-azido-3′-deoxythymidylate
    • Mazumder A., Cooney D., Agbaria R., Gupta M., Pommier Y. Inhibition of human immunodeficiency virus type 1 by 3′-azido-3′-deoxythymidylate. Proc. Natl. Acad. Sci. USA. 91:1994;5771-5775.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5771-5775
    • Mazumder, A.1    Cooney, D.2    Agbaria, R.3    Gupta, M.4    Pommier, Y.5
  • 89
    • 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
  • 91
    • 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
  • 92
    • 0028067639 scopus 로고
    • DNA bending creates favored sites for retroviral integration: An explanation for preferred insertion sites in nucleosomes
    • Müller H.-P., Varmus H.E. DNA bending creates favored sites for retroviral integration: an explanation for preferred insertion sites in nucleosomes. EMBO J. 13:1994;4704-4714.
    • (1994) EMBO J. , vol.13 , pp. 4704-4714
    • Müller, H.-P.1    Varmus, H.E.2
  • 93
    • 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 J.E., Goff S.P. A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the viral integrase in vivo. J. Virol. 66:1992;5092-5095.
    • (1992) J. Virol. , vol.66 , pp. 5092-5095
    • Murphy, J.E.1    Goff, S.P.2
  • 95
    • 0028814535 scopus 로고
    • Characterization of the human spuma retrovirus integrase by site-directed mutagenesis, by complementation, and by swapping the zinc finger domain of HIV-1
    • Pahl A., Flügel R.M. Characterization of the human spuma retrovirus integrase by site-directed mutagenesis, by complementation, and by swapping the zinc finger domain of HIV-1. J. Biol. Chem. 270:1995;2957-2966.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2957-2966
    • Pahl, A.1    Flügel, R.M.2
  • 96
    • 0021022185 scopus 로고
    • The terminal nucleotides of retrovirus DNA are required for integration but not virus production
    • Panganiban A.T., Temin H.M. The terminal nucleotides of retrovirus DNA are required for integration but not virus production. Nature. 306:1983;155-160.
    • (1983) Nature , vol.306 , pp. 155-160
    • Panganiban, A.T.1    Temin, H.M.2
  • 97
    • 0030026836 scopus 로고    scopus 로고
    • The metal ion-induced cooperative binding of HIV-1 integrase to DNA exhibits preference for Mn(II) rather than Mg(II)
    • Pemberton I.K., Buckle M., Buc H. The metal ion-induced cooperative binding of HIV-1 integrase to DNA exhibits preference for Mn(II) rather than Mg(II). J. Biol. Chem. 271:1996;1498-1506.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1498-1506
    • Pemberton, I.K.1    Buckle, M.2    Buc, H.3
  • 98
    • 0026567862 scopus 로고
    • Retroviral integration into minichromosomes in vitro
    • Pryciak P.M., Sil A., Varmus H.E. Retroviral integration into minichromosomes in vitro. EMBO J. 11:1992;291-303.
    • (1992) EMBO J. , vol.11 , pp. 291-303
    • Pryciak, P.M.1    Sil, A.2    Varmus, H.E.3
  • 99
    • 0026696624 scopus 로고
    • Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection
    • Pryciak P.M., Varmus H.E. Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection. Cell. 69:1992;769-780.
    • (1992) Cell , vol.69 , pp. 769-780
    • Pryciak, P.M.1    Varmus, H.E.2
  • 100
    • 0028034050 scopus 로고
    • Characterization of the minimal DNA-binding domain of the HIV integrase protein
    • Puras-Lutzke R., Vink C., Plasterk R.H.A. Characterization of the minimal DNA-binding domain of the HIV integrase protein. Nucleic Acids Res. 22:1994;4125-4131.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4125-4131
    • Puras-Lutzke, R.1    Vink, C.2    Plasterk, R.H.A.3
  • 101
    • 0029557124 scopus 로고
    • Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library
    • Puras-Lutzke R.A., Eppens N.A., Weber P.A., Houghten R.A., Plasterk R.H.A. Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library. Proc. Natl. Acad. Sci. USA. 92:1995;11456-11460.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11456-11460
    • Puras-Lutzke, R.A.1    Eppens, N.A.2    Weber, P.A.3    Houghten, R.A.4    Plasterk, R.H.A.5
  • 102
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration
    • Rice P., Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell. 82:1995;209-220.
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.1    Mizuuchi, K.2
  • 105
    • 0027158091 scopus 로고
    • Integration of murine leukemia virus DNA depends on mitosis
    • Roe T., Reynolds T.C., Yu G., Brown P.O. Integration of murine leukemia virus DNA depends on mitosis. EMBO J. 12:1993;2099-2108.
    • (1993) EMBO J. , vol.12 , pp. 2099-2108
    • Roe, T.1    Reynolds, T.C.2    Yu, G.3    Brown, P.O.4
  • 106
    • 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
  • 107
    • 0024340289 scopus 로고
    • Structure of the termini of DNA intermediates in the integration of retroviral DNA: Dependence of IN function and terminal DNA sequence
    • Roth M.J., Schwartzenberg P.L., Goff S.P. Structure of the termini of DNA intermediates in the integration of retroviral DNA: dependence of IN function and terminal DNA sequence. Cell. 58:1989;47-54.
    • (1989) Cell , vol.58 , pp. 47-54
    • Roth, M.J.1    Schwartzenberg, P.L.2    Goff, S.P.3
  • 108
    • 0025001940 scopus 로고
    • Analysis of mutations in the integration reactions of Maloney murine leukemia virus: Effect on DNA binding and cutting
    • Roth M.J., Schwartzenberg P.L., Tanese N., Goff S.P. Analysis of mutations in the integration reactions of Maloney murine leukemia virus: effect on DNA binding and cutting. J. Virol. 64:1990;4709-4717.
    • (1990) J. Virol. , vol.64 , pp. 4709-4717
    • Roth, M.J.1    Schwartzenberg, P.L.2    Tanese, N.3    Goff, S.P.4
  • 109
    • 0031050297 scopus 로고    scopus 로고
    • Disruption of the terminal base pairs of retroviral DNA during integration
    • Scottoline B.P., Chow S.A., Ellison V., Brown P.O. Disruption of the terminal base pairs of retroviral DNA during integration. Genes Dev. 11:1997;371-382.
    • (1997) Genes Dev. , vol.11 , pp. 371-382
    • Scottoline, B.P.1    Chow, S.A.2    Ellison, V.3    Brown, P.O.4
  • 110
    • 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
    • Scourgen F., Maroun R.G., Frére V., Bouziane M., Anclair 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
    • Scourgen, F.1    Maroun, R.G.2    Frére, V.3    Bouziane, M.4    Anclair, C.5    Troalen, F.6    Fermandjian, S.7
  • 111
    • 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. USA. 87:1990;5119-5123.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 112
    • 0031592591 scopus 로고    scopus 로고
    • Characterization of feline immunodeficiency virus integrase and analysis of functional domains
    • Shibagaki Y., Holmes M.L., Appa R.S., Chow S.A. Characterization of feline immunodeficiency virus integrase and analysis of functional domains. Virology. 230:1997;1-10.
    • (1997) Virology , vol.230 , pp. 1-10
    • Shibagaki, Y.1    Holmes, M.L.2    Appa, R.S.3    Chow, S.A.4
  • 113
    • 0024292602 scopus 로고
    • Highly preferred targets for retrovirus integration
    • Shih C.-C., Stoye J.P., Coffin J.M. Highly preferred targets for retrovirus integration. Cell. 53:1988;531-537.
    • (1988) Cell , vol.53 , pp. 531-537
    • Shih, C.-C.1    Stoye, J.P.2    Coffin, J.M.3
  • 114
    • 0345345250 scopus 로고
    • Integrative recombination of retroviral DNA
    • In: Kucherlapati, R., Smith, R. (Eds.), American Society for Microbiology, Washington, DC
    • Skalka, A.M., 1988. Integrative recombination of retroviral DNA. In: Kucherlapati, R., Smith, R. (Eds.), Genetic recombination. American Society for Microbiology, Washington, DC, pp. 701-724.
    • (1988) Genetic Recombination , pp. 701-724
    • Skalka, A.M.1
  • 115
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • Steitz T.A., Smerdon S.J., Jager J., Joyce C.M. A unified polymerase mechanism for nonhomologous DNA and RNA polymerases. Science. 266:1994;2022-2025.
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1    Smerdon, S.J.2    Jager, J.3    Joyce, C.M.4
  • 116
    • 0030050591 scopus 로고    scopus 로고
    • Portals of entry: Uncovering HIV nuclear transport pathways
    • Stevenson M. Portals of entry: uncovering HIV nuclear transport pathways. Trends Cell Biol. 6:1996;9-15.
    • (1996) Trends Cell Biol. , vol.6 , pp. 9-15
    • Stevenson, M.1
  • 117
    • 0028089732 scopus 로고
    • DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein
    • van den Ent F.M., Vink C., Plasterk R.H. DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein. J. Virol. 68:1994;7825-7832.
    • (1994) J. Virol. , vol.68 , pp. 7825-7832
    • Van Den Ent, F.M.1    Vink, C.2    Plasterk, R.H.3
  • 118
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent D.C., Vink C., Oude Groeneger A.A.M., Plasterk R.H.A. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 12:1993;3261-3268.
    • (1993) EMBO J. , vol.12 , pp. 3261-3268
    • Van Gent, D.C.1    Vink, C.2    Oude Groeneger, A.A.M.3    Plasterk, R.H.A.4
  • 119
    • 0002915381 scopus 로고
    • Retroviruses
    • In: Berg, D.E., Howe, M.M. (Eds.), American Society for Microbiology, Washington, DC
    • Varmus, H.E., Brown, P.O., 1989. Retroviruses. In: Berg, D.E., Howe, M.M. (Eds.), Mobile DNA. American Society for Microbiology, Washington, DC, pp. 53-108.
    • (1989) Mobile DNA , pp. 53-108
    • Varmus, H.E.1    Brown, P.O.2
  • 120
    • 0027472085 scopus 로고
    • Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations
    • Vincent K.A., Ellison V., Chow S.A., Brown P.O. Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations. J. Virol. 67:1993;425-437.
    • (1993) J. Virol. , vol.67 , pp. 425-437
    • Vincent, K.A.1    Ellison, V.2    Chow, S.A.3    Brown, P.O.4
  • 121
    • 0026095906 scopus 로고
    • Human immunodeficiency virus type 1 integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage
    • Vink C., van Gent D.C., Elgersma Y., Plasterk R.H.A. Human immunodeficiency virus type 1 integrase protein requires a subterminal position of 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
  • 122
    • 0028234528 scopus 로고
    • The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescient T lymphocytes
    • Von Schwedler U., Kombluth R.S., Trono D. The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescient T lymphocytes. Proc. Natl. Acad. Sci USA. 91:1994;6992-6996.
    • (1994) Proc. Natl. Acad. Sci USA , vol.91 , pp. 6992-6996
    • Von Schwedler, U.1    Kombluth, R.S.2    Trono, D.3
  • 123
    • 0028116161 scopus 로고
    • Efficient concerted integration of retrovirus-like DNA in vitro by avian retrovirus integrase
    • Vora A.C., McCord M., Fitzgerald M.L., Inman R.B., Grandgenett D.P. Efficient concerted integration of retrovirus-like DNA in vitro by avian retrovirus integrase. Nucleic Acids Res. 22:1994;4454-4461.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4454-4461
    • Vora, A.C.1    McCord, M.2    Fitzgerald, M.L.3    Inman, R.B.4    Grandgenett, D.P.5
  • 124
    • 0030051081 scopus 로고    scopus 로고
    • The role of manganese in promoting multimerization and assembly of human immunodeficiency virus type 1 integrase as a catalytically active complex on immobilized long terminal repeat substrates
    • Wolfe A.L., Felock P.J., Hastings J.C., Blau C.U., Hazuda D.J. The role of manganese in promoting multimerization and assembly of human immunodeficiency virus 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, J.C.3    Blau, C.U.4    Hazuda, D.J.5
  • 125
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, Ruv C and RNase H
    • Yang W., Steitz T.A. Recombining the structures of HIV integrase, Ruv C and RNase H. Structure. 3:1995;88-95.
    • (1995) Structure , vol.3 , pp. 88-95
    • Yang, W.1    Steitz, T.A.2
  • 127
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization and enhances activity
    • Zheng R., Jenkins T.M., Craigie R. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization and enhances activity. Proc. Natl. Acad. Sci. USA. 93:1996;13644-13659.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13644-13659
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.