메뉴 건너뛰기




Volumn 10, Issue 5, 2014, Pages

A New Class of Multimerization Selective Inhibitors of HIV-1 Integrase

Author keywords

[No Author keywords available]

Indexed keywords

ALLINI INHIBITOR; BI 1001; GS B; INTEGRASE INHIBITOR; KF 115; KF 116; NEVIRAPINE; RALTEGRAVIR; SAQUINAVIR; UNCLASSIFIED DRUG; ANTIVIRUS AGENT; INTEGRASE; LENS EPITHELIUM-DERIVED GROWTH FACTOR; P31 INTEGRASE PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTEIN BINDING; QUINOLINE; QUINOLINE DERIVATIVE; SIGNAL PEPTIDE;

EID: 84901657154     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004171     Document Type: Article
Times cited : (111)

References (84)
  • 1
    • 0001363865 scopus 로고    scopus 로고
    • Integration
    • In: Coffin JM, Hughes SH, Varmus HE, editors. Plainview, NY: Cold Spring Harbor Laboratory
    • Brown PO (1997) Integration. In: Coffin JM, Hughes SH, Varmus HE, editors. Retroviruses. Plainview, NY: Cold Spring Harbor Laboratory. pp. 161-204.
    • (1997) Retroviruses , pp. 161-204
    • Brown, P.O.1
  • 2
    • 79952070221 scopus 로고    scopus 로고
    • Structural biology of retroviral DNA integration
    • Li X, Krishnan L, Cherepanov P, Engelman A, (2011) Structural biology of retroviral DNA integration. Virology 411: 194-205.
    • (2011) Virology , vol.411 , pp. 194-205
    • Li, X.1    Krishnan, L.2    Cherepanov, P.3    Engelman, A.4
  • 3
    • 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. J Biol Chem 270: 29299-29306.
    • (1995) J Biol Chem , vol.270 , pp. 29299-29306
    • Andrake, M.D.1    Skalka, A.M.2
  • 4
    • 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. J Biol Chem 271: 7712-7718.
    • (1996) J Biol Chem , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 5
    • 0034682511 scopus 로고    scopus 로고
    • Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding
    • Chen JC, Krucinski J, Miercke LJ, Finer-Moore JS, Tang AH, et al. (2000) Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding. Proc Natl Acad Sci U S A 97: 8233-8238.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8233-8238
    • Chen, J.C.1    Krucinski, J.2    Miercke, L.J.3    Finer-Moore, J.S.4    Tang, A.H.5
  • 6
    • 0037126629 scopus 로고    scopus 로고
    • Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein
    • Wang JY, Ling H, Yang W, Craigie R, (2001) Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. Embo J 20: 7333-7343.
    • (2001) Embo J , vol.20 , pp. 7333-7343
    • Wang, J.Y.1    Ling, H.2    Yang, W.3    Craigie, R.4
  • 7
    • 0346036088 scopus 로고    scopus 로고
    • HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells
    • Cherepanov P, Maertens G, Proost P, Devreese B, Van Beeumen J, et al. (2003) HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells. J Biol Chem 278: 372-381.
    • (2003) J Biol Chem , vol.278 , pp. 372-381
    • Cherepanov, P.1    Maertens, G.2    Proost, P.3    Devreese, B.4    Van Beeumen, J.5
  • 8
    • 28644443483 scopus 로고    scopus 로고
    • A role for LEDGF/p75 in targeting HIV DNA integration
    • Ciuffi A, Llano M, Poeschla E, Hoffmann C, Leipzig J, et al. (2005) A role for LEDGF/p75 in targeting HIV DNA integration. Nat Med 11: 1287-1289.
    • (2005) Nat Med , vol.11 , pp. 1287-1289
    • Ciuffi, A.1    Llano, M.2    Poeschla, E.3    Hoffmann, C.4    Leipzig, J.5
  • 10
    • 34447513231 scopus 로고    scopus 로고
    • LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration
    • Shun MC, Raghavendra NK, Vandegraaff N, Daigle JE, Hughes S, et al. (2007) LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration. Genes Dev 21: 1767-1778.
    • (2007) Genes Dev , vol.21 , pp. 1767-1778
    • Shun, M.C.1    Raghavendra, N.K.2    Vandegraaff, N.3    Daigle, J.E.4    Hughes, S.5
  • 11
    • 77649259825 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor fusion proteins redirect HIV-1 DNA integration
    • Ferris AL, Wu X, Hughes CM, Stewart C, Smith SJ, et al. (2010) Lens epithelium-derived growth factor fusion proteins redirect HIV-1 DNA integration. Proc Natl Acad Sci U S A 107: 3135-3140.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3135-3140
    • Ferris, A.L.1    Wu, X.2    Hughes, C.M.3    Stewart, C.4    Smith, S.J.5
  • 12
    • 24044489892 scopus 로고    scopus 로고
    • The interaction of LEDGF/p75 with integrase is lentivirus-specific and promotes DNA binding
    • Busschots K, Vercammen J, Emiliani S, Benarous R, Engelborghs Y, et al. (2005) The interaction of LEDGF/p75 with integrase is lentivirus-specific and promotes DNA binding. J Biol Chem 280: 17841-17847.
    • (2005) J Biol Chem , vol.280 , pp. 17841-17847
    • Busschots, K.1    Vercammen, J.2    Emiliani, S.3    Benarous, R.4    Engelborghs, Y.5
  • 13
    • 28444445583 scopus 로고    scopus 로고
    • Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75
    • Cherepanov P, Ambrosio AL, Rahman S, Ellenberger T, Engelman A, (2005) Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75. Proc Natl Acad Sci U S A 102: 17308-17313.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17308-17313
    • Cherepanov, P.1    Ambrosio, A.L.2    Rahman, S.3    Ellenberger, T.4    Engelman, A.5
  • 14
    • 0041856142 scopus 로고    scopus 로고
    • LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells
    • Maertens G, Cherepanov P, Pluymers W, Busschots K, De Clercq E, et al. (2003) LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells. J Biol Chem 278: 33528-33539.
    • (2003) J Biol Chem , vol.278 , pp. 33528-33539
    • Maertens, G.1    Cherepanov, P.2    Pluymers, W.3    Busschots, K.4    De Clercq, E.5
  • 15
    • 59249089461 scopus 로고    scopus 로고
    • A novel co-crystal structure affords the design of gain-of-function lentiviral integrase mutants in the presence of modified PSIP1/LEDGF/p75
    • Hare S, Shun MC, Gupta SS, Valkov E, Engelman A, et al. (2009) A novel co-crystal structure affords the design of gain-of-function lentiviral integrase mutants in the presence of modified PSIP1/LEDGF/p75. PLoS Pathog 5: e1000259.
    • (2009) PLoS Pathog , vol.5
    • Hare, S.1    Shun, M.C.2    Gupta, S.S.3    Valkov, E.4    Engelman, A.5
  • 16
    • 57649116082 scopus 로고    scopus 로고
    • Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein
    • McKee CJ, Kessl JJ, Shkriabai N, Dar MJ, Engelman A, et al. (2008) Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein. J Biol Chem 283: 31802-31812.
    • (2008) J Biol Chem , vol.283 , pp. 31802-31812
    • McKee, C.J.1    Kessl, J.J.2    Shkriabai, N.3    Dar, M.J.4    Engelman, A.5
  • 17
    • 84876027348 scopus 로고    scopus 로고
    • Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes
    • Eidahl JO, Crowe BL, North JA, McKee CJ, Shkriabai N, et al. (2013) Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes. Nucleic Acids Res 41: 3924-3936.
    • (2013) Nucleic Acids Res , vol.41 , pp. 3924-3936
    • Eidahl, J.O.1    Crowe, B.L.2    North, J.A.3    McKee, C.J.4    Shkriabai, N.5
  • 18
    • 84863654457 scopus 로고    scopus 로고
    • Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing
    • Pradeepa MM, Sutherland HG, Ule J, Grimes GR, Bickmore WA, (2012) Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. PLoS Genet 8: e1002717.
    • (2012) PLoS Genet , vol.8
    • Pradeepa, M.M.1    Sutherland, H.G.2    Ule, J.3    Grimes, G.R.4    Bickmore, W.A.5
  • 19
    • 84878309032 scopus 로고    scopus 로고
    • Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain
    • van Nuland R, van Schaik FM, Simonis M, van Heesch S, Cuppen E, et al. (2013) Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain. Epigenetics Chromatin 6: 12.
    • (2013) Epigenetics Chromatin , vol.6 , pp. 12
    • van Nuland, R.1    van Schaik, F.M.2    Simonis, M.3    van Heesch, S.4    Cuppen, E.5
  • 20
    • 79960404187 scopus 로고    scopus 로고
    • Gammaretroviral integration into nucleosomal target DNA in vivo
    • Roth SL, Malani N, Bushman FD, (2011) Gammaretroviral integration into nucleosomal target DNA in vivo. J Virol 85: 7393-7401.
    • (2011) J Virol , vol.85 , pp. 7393-7401
    • Roth, S.L.1    Malani, N.2    Bushman, F.D.3
  • 21
    • 3042843657 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors: a decade of research and two drugs in clinical trial
    • Johnson AA, Marchand C, Pommier Y, (2004) HIV-1 integrase inhibitors: a decade of research and two drugs in clinical trial. Curr Top Med Chem 4: 1059-1077.
    • (2004) Curr Top Med Chem , vol.4 , pp. 1059-1077
    • Johnson, A.A.1    Marchand, C.2    Pommier, Y.3
  • 22
    • 84865663948 scopus 로고    scopus 로고
    • HIV integrase as a target for antiretroviral therapy
    • Hazuda DJ, (2012) HIV integrase as a target for antiretroviral therapy. Curr Opin HIV AIDS 7: 383-389.
    • (2012) Curr Opin HIV AIDS , vol.7 , pp. 383-389
    • Hazuda, D.J.1
  • 24
    • 47949120697 scopus 로고    scopus 로고
    • Raltegravir with optimized background therapy for resistant HIV-1 infection
    • Steigbigel RT, Cooper DA, Kumar PN, Eron JE, Schechter M, et al. (2008) Raltegravir with optimized background therapy for resistant HIV-1 infection. N Engl J Med 359: 339-354.
    • (2008) N Engl J Med , vol.359 , pp. 339-354
    • Steigbigel, R.T.1    Cooper, D.A.2    Kumar, P.N.3    Eron, J.E.4    Schechter, M.5
  • 25
    • 79957668616 scopus 로고    scopus 로고
    • Elvitegravir overcomes resistance to raltegravir induced by integrase mutation Y143
    • Metifiot M, Vandegraaff N, Maddali K, Naumova A, Zhang X, et al. (2011) Elvitegravir overcomes resistance to raltegravir induced by integrase mutation Y143. AIDS 25: 1175-1178.
    • (2011) AIDS , vol.25 , pp. 1175-1178
    • Metifiot, M.1    Vandegraaff, N.2    Maddali, K.3    Naumova, A.4    Zhang, X.5
  • 26
    • 84892453291 scopus 로고    scopus 로고
    • The M50I polymorphic substitution in association with the R263K mutation in HIV-1 subtype B integrase increases drug resistance but does not restore viral replicative fitness
    • Wares M, Mesplede T, Quashie PK, Osman N, Han Y, et al. (2014) The M50I polymorphic substitution in association with the R263K mutation in HIV-1 subtype B integrase increases drug resistance but does not restore viral replicative fitness. Retrovirology 11: 7.
    • (2014) Retrovirology , vol.11 , pp. 7
    • Wares, M.1    Mesplede, T.2    Quashie, P.K.3    Osman, N.4    Han, Y.5
  • 27
    • 80455178762 scopus 로고    scopus 로고
    • FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75
    • Kessl JJ, Li M, Ignatov M, Shkriabai N, Eidahl JO, et al. (2011) FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75. Nucleic Acids Res 39: 9009-9022.
    • (2011) Nucleic Acids Res , vol.39 , pp. 9009-9022
    • Kessl, J.J.1    Li, M.2    Ignatov, M.3    Shkriabai, N.4    Eidahl, J.O.5
  • 28
    • 0035068122 scopus 로고    scopus 로고
    • Identification of a small-molecule binding site at the dimer interface of the HIV integrase catalytic domain
    • Molteni V, Greenwald J, Rhodes D, Hwang Y, Kwiatkowski W, et al. (2001) Identification of a small-molecule binding site at the dimer interface of the HIV integrase catalytic domain. Acta Crystallogr D Biol Crystallogr 57: 536-544.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 536-544
    • Molteni, V.1    Greenwald, J.2    Rhodes, D.3    Hwang, Y.4    Kwiatkowski, W.5
  • 29
    • 2342569518 scopus 로고    scopus 로고
    • Identification of an inhibitor-binding site to HIV-1 integrase with affinity acetylation and mass spectrometry
    • Shkriabai N, Patil SS, Hess S, Budihas SR, Craigie R, et al. (2004) Identification of an inhibitor-binding site to HIV-1 integrase with affinity acetylation and mass spectrometry. Proc Natl Acad Sci U S A 101: 6894-6899.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6894-6899
    • Shkriabai, N.1    Patil, S.S.2    Hess, S.3    Budihas, S.R.4    Craigie, R.5
  • 30
    • 70349331248 scopus 로고    scopus 로고
    • An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule
    • Kessl JJ, Eidahl JO, Shkriabai N, Zhao Z, McKee CJ, et al. (2009) An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule. Mol Pharmacol 76: 824-832.
    • (2009) Mol Pharmacol , vol.76 , pp. 824-832
    • Kessl, J.J.1    Eidahl, J.O.2    Shkriabai, N.3    Zhao, Z.4    McKee, C.J.5
  • 32
    • 77952553431 scopus 로고    scopus 로고
    • Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
    • Christ F, Voet A, Marchand A, Nicolet S, Desimmie BA, et al. (2010) Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication. Nat Chem Biol 6: 442-448.
    • (2010) Nat Chem Biol , vol.6 , pp. 442-448
    • Christ, F.1    Voet, A.2    Marchand, A.3    Nicolet, S.4    Desimmie, B.A.5
  • 33
    • 84860871902 scopus 로고    scopus 로고
    • A multimode, cooperative mechanism of action of allosteric HIV-1 integrase inhibitors
    • Kessl JJ, Jena N, Koh Y, Taskent-Sezgin H, Slaughter A, et al. (2012) A multimode, cooperative mechanism of action of allosteric HIV-1 integrase inhibitors. J Biol Chem 287: 16801-16811.
    • (2012) J Biol Chem , vol.287 , pp. 16801-16811
    • Kessl, J.J.1    Jena, N.2    Koh, Y.3    Taskent-Sezgin, H.4    Slaughter, A.5
  • 34
    • 84864387134 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the LEDGF/p75 binding site of integrase block HIV replication and modulate integrase multimerization
    • Christ F, Shaw S, Demeulemeester J, Desimmie BA, Marchand A, et al. (2012) Small-molecule inhibitors of the LEDGF/p75 binding site of integrase block HIV replication and modulate integrase multimerization. Antimicrob Agents Chemother 56: 4365-4374.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 4365-4374
    • Christ, F.1    Shaw, S.2    Demeulemeester, J.3    Desimmie, B.A.4    Marchand, A.5
  • 35
    • 84862271587 scopus 로고    scopus 로고
    • New class of HIV-1 integrase (IN) inhibitors with a dual mode of action
    • Tsiang M, Jones GS, Niedziela-Majka A, Kan E, Lansdon EB, et al. (2012) New class of HIV-1 integrase (IN) inhibitors with a dual mode of action. J Biol Chem 287: 21189-21203.
    • (2012) J Biol Chem , vol.287 , pp. 21189-21203
    • Tsiang, M.1    Jones, G.S.2    Niedziela-Majka, A.3    Kan, E.4    Lansdon, E.B.5
  • 37
    • 84895852851 scopus 로고    scopus 로고
    • Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors
    • Jurado KA, Engelman A, (2013) Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors. Expert Rev Mol Med 15: e14.
    • (2013) Expert Rev Mol Med , vol.15
    • Jurado, K.A.1    Engelman, A.2
  • 38
    • 84878137599 scopus 로고    scopus 로고
    • Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation
    • Jurado KA, Wang H, Slaughter A, Feng L, Kessl JJ, et al. (2013) Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation. Proc Natl Acad Sci U S A 110: 8690-8695.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 8690-8695
    • Jurado, K.A.1    Wang, H.2    Slaughter, A.3    Feng, L.4    Kessl, J.J.5
  • 40
    • 84878408619 scopus 로고    scopus 로고
    • The A128T resistance mutation reveals aberrant protein multimerization as the primary mechanism of action of allosteric HIV-1 integrase inhibitors
    • Feng L, Sharma A, Slaughter A, Jena N, Koh Y, et al. (2013) The A128T resistance mutation reveals aberrant protein multimerization as the primary mechanism of action of allosteric HIV-1 integrase inhibitors. J Biol Chem 288: 15813-15820.
    • (2013) J Biol Chem , vol.288 , pp. 15813-15820
    • Feng, L.1    Sharma, A.2    Slaughter, A.3    Jena, N.4    Koh, Y.5
  • 41
    • 84883649897 scopus 로고    scopus 로고
    • Non-Catalytic Site HIV-1 Integrase Inhibitors Disrupt Core Maturation and Induce a Reverse Transcription Block in Target Cells
    • Balakrishnan M, Yant SR, Tsai L, O'Sullivan C, Bam RA, et al. (2013) Non-Catalytic Site HIV-1 Integrase Inhibitors Disrupt Core Maturation and Induce a Reverse Transcription Block in Target Cells. PLoS One 8: e74163.
    • (2013) PLoS One , vol.8
    • Balakrishnan, M.1    Yant, S.R.2    Tsai, L.3    O'Sullivan, C.4    Bam, R.A.5
  • 42
    • 84878214842 scopus 로고    scopus 로고
    • LEDGINs inhibit late stage HIV-1 replication by modulating integrase multimerization in the virions
    • Desimmie BA, Schrijvers R, Demeulemeester J, Borrenberghs D, Weydert C, et al. (2013) LEDGINs inhibit late stage HIV-1 replication by modulating integrase multimerization in the virions. Retrovirology 10: 57.
    • (2013) Retrovirology , vol.10 , pp. 57
    • Desimmie, B.A.1    Schrijvers, R.2    Demeulemeester, J.3    Borrenberghs, D.4    Weydert, C.5
  • 44
    • 0035026761 scopus 로고    scopus 로고
    • Construction and analysis of an infectious human Immunodeficiency virus type 1 subtype C molecular clone
    • Ndung'u T, Renjifo B, Essex M, (2001) Construction and analysis of an infectious human Immunodeficiency virus type 1 subtype C molecular clone. J Virol 75: 4964-4972.
    • (2001) J Virol , vol.75 , pp. 4964-4972
    • Ndung'u, T.1    Renjifo, B.2    Essex, M.3
  • 45
    • 62949153971 scopus 로고    scopus 로고
    • Preclinical evaluation of GS-9160, a novel inhibitor of human immunodeficiency virus type 1 integrase
    • Jones GS, Yu F, Zeynalzadegan A, Hesselgesser J, Chen X, et al. (2009) Preclinical evaluation of GS-9160, a novel inhibitor of human immunodeficiency virus type 1 integrase. Antimicrob Agents Chemother 53: 1194-1203.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 1194-1203
    • Jones, G.S.1    Yu, F.2    Zeynalzadegan, A.3    Hesselgesser, J.4    Chen, X.5
  • 46
    • 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. J Virol 69: 2729-2736.
    • (1995) J Virol , vol.69 , pp. 2729-2736
    • Engelman, A.1    Englund, G.2    Orenstein, J.M.3    Martin, M.A.4    Craigie, R.5
  • 47
    • 0032617446 scopus 로고    scopus 로고
    • In vivo analysis of retroviral integrase structure and function
    • Engelman A, (1999) In vivo analysis of retroviral integrase structure and function. Adv Virus Res 52: 411-426.
    • (1999) Adv Virus Res , vol.52 , pp. 411-426
    • Engelman, A.1
  • 48
    • 84878252974 scopus 로고    scopus 로고
    • A Homology Model of HIV-1 Integrase and Analysis of Mutations Designed to Test the Model
    • Johnson BC, Metifiot M, Ferris A, Pommier Y, Hughes SH, (2013) A Homology Model of HIV-1 Integrase and Analysis of Mutations Designed to Test the Model. J Mol Biol 425: 2133-2146.
    • (2013) J Mol Biol , vol.425 , pp. 2133-2146
    • Johnson, B.C.1    Metifiot, M.2    Ferris, A.3    Pommier, Y.4    Hughes, S.H.5
  • 49
    • 0036838711 scopus 로고    scopus 로고
    • Nuclear localization of human immunodeficiency virus type 1 preintegration complexes (PICs): V165A and R166A are pleiotropic integrase mutants primarily defective for integration, not PIC nuclear import
    • Limon A, Devroe E, Lu R, Ghory HZ, Silver PA, et al. (2002) Nuclear localization of human immunodeficiency virus type 1 preintegration complexes (PICs): V165A and R166A are pleiotropic integrase mutants primarily defective for integration, not PIC nuclear import. J Virol 76: 10598-10607.
    • (2002) J Virol , vol.76 , pp. 10598-10607
    • Limon, A.1    Devroe, E.2    Lu, R.3    Ghory, H.Z.4    Silver, P.A.5
  • 51
    • 0027969548 scopus 로고
    • Determination of diffusion coefficients of biological macromolecules by dynamic light scattering
    • Harding SE, (1994) Determination of diffusion coefficients of biological macromolecules by dynamic light scattering. Methods Mol Biol 22: 97-108.
    • (1994) Methods Mol Biol , vol.22 , pp. 97-108
    • Harding, S.E.1
  • 52
    • 0031022040 scopus 로고    scopus 로고
    • Static and dynamic light scattering of biological macromolecules: what can we learn?
    • Murphy RM, (1997) Static and dynamic light scattering of biological macromolecules: what can we learn? Curr Opin Biotechnol 8: 25-30.
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 25-30
    • Murphy, R.M.1
  • 53
    • 47349120456 scopus 로고    scopus 로고
    • Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements
    • Jachimska B, Wasilewska M, Adamczyk Z, (2008) Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements. Langmuir 24: 6866-6872.
    • (2008) Langmuir , vol.24 , pp. 6866-6872
    • Jachimska, B.1    Wasilewska, M.2    Adamczyk, Z.3
  • 54
    • 35648978159 scopus 로고    scopus 로고
    • Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies
    • Nobbmann U, Connah M, Fish B, Varley P, Gee C, et al. (2007) Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies. Biotechnol Genet Eng Rev 24: 117-128.
    • (2007) Biotechnol Genet Eng Rev , vol.24 , pp. 117-128
    • Nobbmann, U.1    Connah, M.2    Fish, B.3    Varley, P.4    Gee, C.5
  • 55
    • 77954761903 scopus 로고    scopus 로고
    • Nucleoprotein intermediates in HIV-1 DNA integration visualized by atomic force microscopy
    • Kotova S, Li M, Dimitriadis EK, Craigie R, (2010) Nucleoprotein intermediates in HIV-1 DNA integration visualized by atomic force microscopy. J Mol Biol 399: 491-500.
    • (2010) J Mol Biol , vol.399 , pp. 491-500
    • Kotova, S.1    Li, M.2    Dimitriadis, E.K.3    Craigie, R.4
  • 56
    • 0037428412 scopus 로고    scopus 로고
    • Functional oligomeric state of avian sarcoma virus integrase
    • Bao KK, Wang H, Miller JK, Erie DA, Skalka AM, et al. (2003) Functional oligomeric state of avian sarcoma virus integrase. J Biol Chem 278: 1323-1327.
    • (2003) J Biol Chem , vol.278 , pp. 1323-1327
    • Bao, K.K.1    Wang, H.2    Miller, J.K.3    Erie, D.A.4    Skalka, A.M.5
  • 58
    • 33745745419 scopus 로고    scopus 로고
    • Retroviral DNA integration: HIV and the role of LEDGF/p75
    • Ciuffi A, Bushman FD, (2006) Retroviral DNA integration: HIV and the role of LEDGF/p75. Trends Genet 22: 388-395.
    • (2006) Trends Genet , vol.22 , pp. 388-395
    • Ciuffi, A.1    Bushman, F.D.2
  • 59
    • 0037162715 scopus 로고    scopus 로고
    • HIV-1 integration in the human genome favors active genes and local hotspots
    • Schroder AR, Shinn P, Chen H, Berry C, Ecker JR, et al. (2002) HIV-1 integration in the human genome favors active genes and local hotspots. Cell 110: 521-529.
    • (2002) Cell , vol.110 , pp. 521-529
    • Schroder, A.R.1    Shinn, P.2    Chen, H.3    Berry, C.4    Ecker, J.R.5
  • 61
    • 84883400906 scopus 로고    scopus 로고
    • Treatment with suboptimal doses of raltegravir leads to aberrant HIV-1 integrations
    • Varadarajan J, McWilliams MJ, Hughes SH, (2013) Treatment with suboptimal doses of raltegravir leads to aberrant HIV-1 integrations. Proc Natl Acad Sci U S A 110: 14747-14752.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 14747-14752
    • Varadarajan, J.1    McWilliams, M.J.2    Hughes, S.H.3
  • 62
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases
    • Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, et al. (1994) Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl 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
  • 64
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 67
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62: 439-450.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 68
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi A, Gendelman HE, Koenig S, Folks T, Willey R, et al. (1986) Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J Virol 59: 284-291.
    • (1986) J Virol , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5
  • 69
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor RI, Chen BK, Choe S, Landau NR, (1995) Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206: 935-944.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 70
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini L, Blomer U, Gallay P, Ory D, Mulligan R, et al. (1996) In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272: 263-267.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5
  • 71
    • 35148886657 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 replication in immature and mature dendritic cells reveals dissociable cis- and trans-infection
    • Dong C, Janas AM, Wang JH, Olson WJ, Wu L, (2007) Characterization of human immunodeficiency virus type 1 replication in immature and mature dendritic cells reveals dissociable cis- and trans-infection. J Virol 81: 11352-11362.
    • (2007) J Virol , vol.81 , pp. 11352-11362
    • Dong, C.1    Janas, A.M.2    Wang, J.H.3    Olson, W.J.4    Wu, L.5
  • 72
    • 84871412468 scopus 로고    scopus 로고
    • SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+ T-lymphocytes cannot be upregulated by interferons
    • St Gelais C, de Silva S, Amie SM, Coleman CM, Hoy H, et al. (2012) SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+ T-lymphocytes cannot be upregulated by interferons. Retrovirology 9: 105.
    • (2012) Retrovirology , vol.9 , pp. 105
    • St Gelais, C.1    de Silva, S.2    Amie, S.M.3    Coleman, C.M.4    Hoy, H.5
  • 73
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 74
    • 80355146829 scopus 로고    scopus 로고
    • The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability
    • Jiang J, Ablan SD, Derebail S, Hercik K, Soheilian F, et al. (2011) The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability. Virology 421: 253-265.
    • (2011) Virology , vol.421 , pp. 253-265
    • Jiang, J.1    Ablan, S.D.2    Derebail, S.3    Hercik, K.4    Soheilian, F.5
  • 75
    • 79953288618 scopus 로고    scopus 로고
    • HIV integration targeting: a pathway involving Transportin-3 and the nuclear pore protein RanBP2
    • Ocwieja KE, Brady TL, Ronen K, Huegel A, Roth SL, et al. (2011) HIV integration targeting: a pathway involving Transportin-3 and the nuclear pore protein RanBP2. PLoS Pathog 7: e1001313.
    • (2011) PLoS Pathog , vol.7
    • Ocwieja, K.E.1    Brady, T.L.2    Ronen, K.3    Huegel, A.4    Roth, S.L.5
  • 76
    • 34547635063 scopus 로고    scopus 로고
    • HIV integration site selection: analysis by massively parallel pyrosequencing reveals association with epigenetic modifications
    • Wang GP, Ciuffi A, Leipzig J, Berry CC, Bushman FD, (2007) HIV integration site selection: analysis by massively parallel pyrosequencing reveals association with epigenetic modifications. Genome Res 17: 1186-1194.
    • (2007) Genome Res , vol.17 , pp. 1186-1194
    • Wang, G.P.1    Ciuffi, A.2    Leipzig, J.3    Berry, C.C.4    Bushman, F.D.5
  • 77
  • 78
    • 61849143903 scopus 로고    scopus 로고
    • Integration target site selection by a resurrected human endogenous retrovirus
    • Brady T, Lee YN, Ronen K, Malani N, Berry CC, et al. (2009) Integration target site selection by a resurrected human endogenous retrovirus. Genes Dev 23: 633-642.
    • (2009) Genes Dev , vol.23 , pp. 633-642
    • Brady, T.1    Lee, Y.N.2    Ronen, K.3    Malani, N.4    Berry, C.C.5
  • 79
    • 84861216902 scopus 로고    scopus 로고
    • Thriving under stress: selective translation of HIV-1 structural protein mRNA during Vpr-mediated impairment of eIF4E translation activity
    • Sharma A, Yilmaz A, Marsh K, Cochrane A, Boris-Lawrie K, (2012) Thriving under stress: selective translation of HIV-1 structural protein mRNA during Vpr-mediated impairment of eIF4E translation activity. PLoS Pathog 8: e1002612.
    • (2012) PLoS Pathog , vol.8
    • Sharma, A.1    Yilmaz, A.2    Marsh, K.3    Cochrane, A.4    Boris-Lawrie, K.5
  • 80
    • 4644312883 scopus 로고    scopus 로고
    • Relationships between infectious titer, capsid protein levels, and reverse transcriptase activities of diverse human immunodeficiency virus type 1 isolates
    • Marozsan AJ, Fraundorf E, Abraha A, Baird H, Moore D, et al. (2004) Relationships between infectious titer, capsid protein levels, and reverse transcriptase activities of diverse human immunodeficiency virus type 1 isolates. J Virol 78: 11130-11141.
    • (2004) J Virol , vol.78 , pp. 11130-11141
    • Marozsan, A.J.1    Fraundorf, E.2    Abraha, A.3    Baird, H.4    Moore, D.5
  • 81
    • 0034004857 scopus 로고    scopus 로고
    • Variable sensitivity of CCR5-tropic human immunodeficiency virus type 1 isolates to inhibition by RANTES analogs
    • Torre VS, Marozsan AJ, Albright JL, Collins KR, Hartley O, et al. (2000) Variable sensitivity of CCR5-tropic human immunodeficiency virus type 1 isolates to inhibition by RANTES analogs. J Virol 74: 4868-4876.
    • (2000) J Virol , vol.74 , pp. 4868-4876
    • Torre, V.S.1    Marozsan, A.J.2    Albright, J.L.3    Collins, K.R.4    Hartley, O.5
  • 82
    • 67749147464 scopus 로고    scopus 로고
    • Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) Annealing to viral RNA in human immunodeficiency virus type 1
    • Guo F, Saadatmand J, Niu M, Kleiman L, (2009) Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) Annealing to viral RNA in human immunodeficiency virus type 1. J Virol 83: 8099-8107.
    • (2009) J Virol , vol.83 , pp. 8099-8107
    • Guo, F.1    Saadatmand, J.2    Niu, M.3    Kleiman, L.4
  • 83
    • 78951484220 scopus 로고    scopus 로고
    • Coordinate roles of Gag and RNA helicase A in promoting the annealing of formula to HIV-1 RNA
    • Xing L, Liang C, Kleiman L, (2011) Coordinate roles of Gag and RNA helicase A in promoting the annealing of formula to HIV-1 RNA. J Virol 85: 1847-1860.
    • (2011) J Virol , vol.85 , pp. 1847-1860
    • Xing, L.1    Liang, C.2    Kleiman, L.3
  • 84
    • 77958114725 scopus 로고    scopus 로고
    • The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1
    • Yan N, Regalado-Magdos AD, Stiggelbout B, Lee-Kirsch MA, Lieberman J, (2010) The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1. Nat Immunol 11: 1005-1013.
    • (2010) Nat Immunol , vol.11 , pp. 1005-1013
    • Yan, N.1    Regalado-Magdos, A.D.2    Stiggelbout, B.3    Lee-Kirsch, M.A.4    Lieberman, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.