메뉴 건너뛰기




Volumn 17, Issue 3, 2013, Pages 339-345

Allosteric inhibition of HIV-1 integrase activity

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; HIV 1 INTEGRASE; INTEGRASE INHIBITOR; INTEGRASE STRAND TRANSFER INHIBITOR; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 84878869428     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2013.04.010     Document Type: Review
Times cited : (64)

References (41)
  • 1
    • 84858409977 scopus 로고    scopus 로고
    • The structural biology of HIV-1: mechanistic and therapeutic insights
    • Engelman A., Cherepanov P. The structural biology of HIV-1: mechanistic and therapeutic insights. Nat Rev Microbiol 2012, 10:279-290.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 279-290
    • Engelman, A.1    Cherepanov, P.2
  • 2
    • 84858988089 scopus 로고    scopus 로고
    • Temporal changes in the epidemiology of transmission of drug-resistant HIV-1 across the world
    • Frentz D., Boucher C.A., van de Vijver D.A. Temporal changes in the epidemiology of transmission of drug-resistant HIV-1 across the world. AIDS Rev 2012, 14:17-27.
    • (2012) AIDS Rev , vol.14 , pp. 17-27
    • Frentz, D.1    Boucher, C.A.2    van de Vijver, D.A.3
  • 3
    • 84870324937 scopus 로고    scopus 로고
    • Retroviral integrase proteins and HIV-1 DNA integration
    • Krishnan L., Engelman A. Retroviral integrase proteins and HIV-1 DNA integration. J Biol Chem 2012, 287:40858-40866.
    • (2012) J Biol Chem , vol.287 , pp. 40858-40866
    • Krishnan, L.1    Engelman, A.2
  • 6
    • 79251545504 scopus 로고    scopus 로고
    • Allosteric inhibitor development targeting HIV-1 integrase
    • Al-Mawsawi L.Q., Neamati N. Allosteric inhibitor development targeting HIV-1 integrase. ChemMedChem 2011, 6:228-241.
    • (2011) ChemMedChem , vol.6 , pp. 228-241
    • Al-Mawsawi, L.Q.1    Neamati, N.2
  • 7
    • 84875545671 scopus 로고    scopus 로고
    • Non-enzymatic functions of retroviral integrase: the next target for novel anti-HIV drug development
    • Masuda T. Non-enzymatic functions of retroviral integrase: the next target for novel anti-HIV drug development. Front Microbiol 2011, 2:210.
    • (2011) Front Microbiol , vol.2 , pp. 210
    • Masuda, T.1
  • 8
    • 84859641222 scopus 로고    scopus 로고
    • Novel therapeutic strategies targeting HIV integrase
    • Quashie P.K., Sloan R.D., Wainberg M.A. Novel therapeutic strategies targeting HIV integrase. BMC Med 2012, 10:34.
    • (2012) BMC Med , vol.10 , pp. 34
    • Quashie, P.K.1    Sloan, R.D.2    Wainberg, M.A.3
  • 10
    • 10344221084 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase
    • Cherepanov P., Devroe E., Silver P.A., Engelman A. Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase. J Biol Chem 2004, 279:48883-48892.
    • (2004) J Biol Chem , vol.279 , pp. 48883-48892
    • Cherepanov, P.1    Devroe, E.2    Silver, P.A.3    Engelman, A.4
  • 11
    • 84871220094 scopus 로고    scopus 로고
    • HRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor
    • Wang H., Jurado K.A., Wu X., Shun M.-C., Li X., Ferris A.L., Smith S.J., Patel P.A., Fuchs J.R., Cherepanov P., et al. HRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor. Nucleic Acids Res 2012, 40:11518-11530.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11518-11530
    • Wang, H.1    Jurado, K.A.2    Wu, X.3    Shun, M.-C.4    Li, X.5    Ferris, A.L.6    Smith, S.J.7    Patel, P.A.8    Fuchs, J.R.9    Cherepanov, P.10
  • 14
    • 84871962937 scopus 로고    scopus 로고
    • Differential effects of human immunodeficiency virus type 1 capsid and cellular factors nucleoporin 153 and LEDGF/p75 on the efficiency and specificity of viral DNA integration
    • Koh Y., Wu X., Ferris A.L., Matreyek K.A., Smith S.J., Lee K., KewalRamani V.N., Hughes S.H., Engelman A. Differential effects of human immunodeficiency virus type 1 capsid and cellular factors nucleoporin 153 and LEDGF/p75 on the efficiency and specificity of viral DNA integration. J Virol 2013, 87:648-658.
    • (2013) J Virol , vol.87 , pp. 648-658
    • Koh, Y.1    Wu, X.2    Ferris, A.L.3    Matreyek, K.A.4    Smith, S.J.5    Lee, K.6    KewalRamani, V.N.7    Hughes, S.H.8    Engelman, A.9
  • 15
    • 79952070221 scopus 로고    scopus 로고
    • Structural biology of retroviral DNA integration
    • Li X., Krishnan L., Cherepanov P., Engelman A. Structural biology of retroviral DNA integration. Virology 2011, 411:194-205.
    • (2011) Virology , vol.411 , pp. 194-205
    • Li, X.1    Krishnan, L.2    Cherepanov, P.3    Engelman, A.4
  • 16
    • 84863823336 scopus 로고    scopus 로고
    • Cherepanov P: 3'-processing and strand transfer catalysed by retroviral integrase in crystallo
    • Hare S., Maertens G.N. Cherepanov P: 3'-processing and strand transfer catalysed by retroviral integrase in crystallo. EMBO J 2012, 31:3020-3028.
    • (2012) EMBO J , vol.31 , pp. 3020-3028
    • Hare, S.1    Maertens, G.N.2
  • 17
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare S., Gupta S.S., Valkov E., Engelman A., Cherepanov P. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 2010, 464:232-236.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 18
    • 78149434355 scopus 로고    scopus 로고
    • The mechanism of retroviral integration through X-ray structures of its key intermediates
    • Maertens G.N., Hare S., Cherepanov P. The mechanism of retroviral integration through X-ray structures of its key intermediates. Nature 2010, 468:326-329.
    • (2010) Nature , vol.468 , pp. 326-329
    • Maertens, G.N.1    Hare, S.2    Cherepanov, P.3
  • 21
    • 84868535547 scopus 로고    scopus 로고
    • Solution conformations of prototype foamy virus integrase and its stable synaptic complex with u5 viral DNA
    • Gupta K., Curtis J.E., Krueger S., Hwang Y., Cherepanov P., Bushman F.D., Van Duyne G.D. Solution conformations of prototype foamy virus integrase and its stable synaptic complex with u5 viral DNA. Structure 2012, 20:1918-1928.
    • (2012) Structure , vol.20 , pp. 1918-1928
    • Gupta, K.1    Curtis, J.E.2    Krueger, S.3    Hwang, Y.4    Cherepanov, P.5    Bushman, F.D.6    Van Duyne, G.D.7
  • 22
    • 28444445583 scopus 로고    scopus 로고
    • Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75
    • Cherepanov P., Ambrosio A.L.B., Rahman S., Ellenberger T., Engelman A. Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75. Proc Natl Acad Sci U S A 2005, 102:17308-17313.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17308-17313
    • Cherepanov, P.1    Ambrosio, A.L.B.2    Rahman, S.3    Ellenberger, T.4    Engelman, A.5
  • 23
    • 33847279490 scopus 로고    scopus 로고
    • LEDGF/p75 interferes with the formation of synaptic nucleoprotein complexes that catalyze full-site HIV-1 DNA integration in vitro: implications for the mechanism of viral cDNA integration
    • Raghavendra N.K., Engelman A. LEDGF/p75 interferes with the formation of synaptic nucleoprotein complexes that catalyze full-site HIV-1 DNA integration in vitro: implications for the mechanism of viral cDNA integration. Virology 2007, 360:1-5.
    • (2007) Virology , vol.360 , pp. 1-5
    • Raghavendra, N.K.1    Engelman, A.2
  • 24
    • 57649116082 scopus 로고    scopus 로고
    • Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein
    • McKee C.J., Kessl J.J., Shkriabai N., Dar M.J., Engelman A., Kvaratskhelia M. Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein. J Biol Chem 2008, 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    Kvaratskhelia, M.6
  • 26
    • 33751242046 scopus 로고    scopus 로고
    • Overexpression of the lens epithelium-derived growth factor/p75 integrase binding domain inhibits human immunodeficiency virus replication
    • De Rijck J., Vandekerckhove L., Gijsbers R., Hombrouck A., Hendrix J., Vercammen J., Engelborghs Y., Christ F., Debyser Z. Overexpression of the lens epithelium-derived growth factor/p75 integrase binding domain inhibits human immunodeficiency virus replication. J Virol 2006, 80:11498-11509.
    • (2006) J Virol , vol.80 , pp. 11498-11509
    • De Rijck, J.1    Vandekerckhove, L.2    Gijsbers, R.3    Hombrouck, A.4    Hendrix, J.5    Vercammen, J.6    Engelborghs, Y.7    Christ, F.8    Debyser, Z.9
  • 30
    • 42149180682 scopus 로고    scopus 로고
    • Inhibitory profile of a LEDGF/p75 peptide against HIV-1 integrase: insight into integrase-DNA complex formation and catalysis
    • Al-Mawsawi L.Q., Christ F., Dayam R., Debyser Z., Neamati N. Inhibitory profile of a LEDGF/p75 peptide against HIV-1 integrase: insight into integrase-DNA complex formation and catalysis. FEBS Lett 2008, 582:1425-1430.
    • (2008) FEBS Lett , vol.582 , pp. 1425-1430
    • Al-Mawsawi, L.Q.1    Christ, F.2    Dayam, R.3    Debyser, Z.4    Neamati, N.5
  • 41
    • 84878137599 scopus 로고    scopus 로고
    • Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation. Proc Natl Acad Sci U S A 2013, .
    • Jurado KA, Wang H, Slaughter A, Feng L, Kessl JJ, Koh Y, Wang W, Ballandras-Colas A, Pater PA, Fuchs JR, et al.: Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation. Proc Natl Acad Sci U S A 2013, . doi:10.1073/pnas.1300703110.
    • Jurado, K.A.1    Wang, H.2    Slaughter, A.3    Feng, L.4    Kessl, J.J.5    Koh, Y.6    Wang, W.7    Ballandras-Colas, A.8    Pater, P.A.9    Fuchs, J.R.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.