메뉴 건너뛰기




Volumn 55, Issue 9, 2011, Pages 4251-4260

Novel postentry inhibitor of human immunodeficiency virus type 1 replication screened by yeast membrane-associated two-hybrid system

Author keywords

[No Author keywords available]

Indexed keywords

2 (BENZOTHIAZOL 2 YLMETHYLTHIO) 4 METHYLPYRIMIDINE; CAPSID PROTEIN; GAG PROTEIN; LUCIFERASE; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 80051813979     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00299-11     Document Type: Article
Times cited : (13)

References (38)
  • 2
    • 65349162716 scopus 로고    scopus 로고
    • Impact of human immunodeficiency virus type 1 resistance to protease inhibitors on evolution of resistance to the maturation inhibitor bevirimat (PA-457)
    • Adamson, C S, K. Waki, S D Ablan, K. Salzwedel, and E O Freed. 2009. Impact of human immunodeficiency virus type 1 resistance to protease inhibitors on evolution of resistance to the maturation inhibitor bevirimat (PA-457). J. Virol. 83:4884-4894.
    • (2009) J. Virol. , vol.83 , pp. 4884-4894
    • Adamson, C.S.1    Waki, K.2    Ablan, S.D.3    Salzwedel, K.4    Freed, E.O.5
  • 3
    • 60349111092 scopus 로고    scopus 로고
    • Cell-free assays for HIV-1 uncoating
    • Aiken, C. 2009. Cell-free assays for HIV-1 uncoating. Methods Mol. Biol. 485:41-53.
    • (2009) Methods Mol. Biol. , vol.485 , pp. 41-53
    • Aiken, C.1
  • 4
    • 0027931640 scopus 로고
    • Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
    • DOI 10.1016/0092-8674(94)90271-2
    • Aronheim, A., et al. 1994. Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway. Cell 78:949-961. (Pubitemid 24292324)
    • (1994) Cell , vol.78 , Issue.6 , pp. 949-961
    • Aronheim, A.1    Engelberg, D.2    Li, N.3    Ai-Alawi, N.4    Schlessinger, J.5    Karin, M.6
  • 5
    • 57649116079 scopus 로고    scopus 로고
    • Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein
    • Bartonova, V., et al. 2008. Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein. J. Biol. Chem. 283:32024-32033.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32024-32033
    • Bartonova, V.1
  • 6
    • 13544273297 scopus 로고    scopus 로고
    • A novel HIV-1 antiviral high throughput screening approach for the discovery of HIV-1 inhibitors
    • DOI 10.1016/j.antiviral.2004.11.001
    • Blair, W S, et al. 2005. A novel HIV-1 antiviral high throughput screening approach for the discovery of HIV-1 inhibitors. Antiviral Res. 65:107-116. (Pubitemid 40222287)
    • (2005) Antiviral Research , vol.65 , Issue.2 , pp. 107-116
    • Blair, W.S.1    Isaacson, J.2    Li, X.3    Cao, J.4    Peng, Q.5    Kong, G.F.Z.6    Patick, A.K.7
  • 7
    • 71249123121 scopus 로고    scopus 로고
    • New small-molecule inhibitor class targeting human immunodeficiency virus type 1 virion maturation
    • Blair, W S, et al. 2009. New small-molecule inhibitor class targeting human immunodeficiency virus type 1 virion maturation. Antimicrob. Agents Chemother. 53:5080-5087.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 5080-5087
    • Blair, W.S.1
  • 8
    • 0030768919 scopus 로고    scopus 로고
    • Yeast as a model organism
    • DOI 10.1126/science.277.5330.1259
    • Botstein, D. 1997. Yeast as a model organism. Science 277:1259-1260. (Pubitemid 27449069)
    • (1997) Science , vol.277 , Issue.5330 , pp. 1259-1260
    • Botstein, D.1    Chervitz, S.A.2    Cherry, J.M.3
  • 9
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription
    • Braaten, D., E K Franke, and J. Luban. 1996. Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J. Virol. 70:3551-3560. (Pubitemid 26157335)
    • (1996) Journal of Virology , vol.70 , Issue.6 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 10
    • 73549103358 scopus 로고    scopus 로고
    • The development of antiretroviral therapy and its impact on the HIV-1/AIDS pandemic
    • Broder, S. 2010. The development of antiretroviral therapy and its impact on the HIV-1/AIDS pandemic. Antiviral Res. 85:1-18.
    • (2010) Antiviral Res. , vol.85 , pp. 1-18
    • Broder, S.1
  • 11
    • 0030885353 scopus 로고    scopus 로고
    • Transfer of the HIV-1 cyclophilin-binding site to simian immunodeficiency virus from Macaca mulatta can confer both cyclosporin sensitivity and cyclosporin dependence
    • DOI 10.1073/pnas.94.20.10943
    • Bukovsky, A A, A. Weimann, M A Accola, and H G Gottlinger. 1997. Transfer of the HIV-1 cyclophilin-binding site to simian immunodeficiency virus from Macaca mulatta can confer both cyclosporin sensitivity and cyclosporin dependence. Proc. Natl. Acad. Sci. U. S. A. 94:10943-10948. (Pubitemid 27430840)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.20 , pp. 10943-10948
    • Bukovsky, A.A.1    Weimann, A.2    Accola, M.A.3    Gottlinger, H.G.4
  • 12
    • 0035025888 scopus 로고    scopus 로고
    • A quantitative assay for HIV DNA integration in vivo
    • DOI 10.1038/87979
    • Butler, S L, M S T Hansen, and F D Bushman. 2001. A quantitative assay for HIV DNA integration in vivo. Nat. Med. 7:631-634. (Pubitemid 32448333)
    • (2001) Nature Medicine , vol.7 , Issue.5 , pp. 631-634
    • Butler, S.L.1    Hansen, M.S.T.2    Bushman, F.D.3
  • 14
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey, B M, U. Von Schwedler, W I Sundquist, and C. Aiken. 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76:5667-5677.
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 15
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • DOI 10.1038/372359a0
    • Franke, E K, H E Yuan, and J. Luban. 1994. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372:359-362. (Pubitemid 24363437)
    • (1994) Nature , vol.372 , Issue.6504 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 17
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • DOI 10.1126/science.283.5398.80
    • Ganser, B K, S. Li, V Y Klishko, J T Finch, and W I Sundquist. 1999. Assembly and analysis of conical models for the HIV-1 core. Science 283:80-83. (Pubitemid 29044851)
    • (1999) Science , vol.283 , Issue.5398 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 18
    • 34848866243 scopus 로고    scopus 로고
    • Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
    • DOI 10.1016/j.cell.2007.08.018, PII S0092867407010811
    • Ganser-Pornillos, B K, A. Cheng, and M. Yeager. 2007. Structure of full-length HIV-1 CA: A model for the mature capsid lattice. Cell 131:70-79. (Pubitemid 47498532)
    • (2007) Cell , vol.131 , Issue.1 , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 19
    • 0037097584 scopus 로고    scopus 로고
    • Deletion analysis of p16INKa and p15INKb in relapsed childhood acute lymphoblastic leukemia
    • INKb in relapsed childhood acute lymphoblastic leukemia. Blood 99:4629-4631.
    • (2002) Blood , vol.99 , pp. 4629-4631
    • Graf Einsiedel, H.1
  • 22
    • 0037651594 scopus 로고    scopus 로고
    • HIV capsid assembly
    • Morikawa, Y. 2003. HIV capsid assembly. Curr. HIV Res. 1:1-14.
    • (2003) Curr. HIV Res. , vol.1 , pp. 1-14
    • Morikawa, Y.1
  • 24
    • 67549109069 scopus 로고    scopus 로고
    • X-ray structures of the hexameric building block of the HIV capsid
    • Pornillos, O., et al. 2009. X-ray structures of the hexameric building block of the HIV capsid. Cell 137:1282-1292.
    • (2009) Cell , vol.137 , pp. 1282-1292
    • Pornillos, O.1
  • 25
    • 0025268321 scopus 로고
    • Rational design of peptide-based HIV proteinase inhibitors
    • Roberts, N A, et al. 1990. Rational design of peptide-based HIV proteinase inhibitors. Science 248:358-361.
    • (1990) Science , vol.248 , pp. 358-361
    • Roberts, N.A.1
  • 27
    • 78650064115 scopus 로고    scopus 로고
    • Small molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • Shi, J., J. Zhou, V B Shah, C. Aiken, and K. Whitby. 2011. Small molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. J. Virol. 85:542-549.
    • (2011) J. Virol. , vol.85 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 28
    • 33847205321 scopus 로고    scopus 로고
    • Inhibiting lentiviral replication by HEXIM1, a cellular negative regulator of the CDK9/cyclin T complex
    • Shimizu, S., et al. 2007. Inhibiting lentiviral replication by HEXIM1, a cellular negative regulator of the CDK9/cyclin T complex. AIDS 21:575-582.
    • (2007) AIDS , vol.21 , pp. 575-582
    • Shimizu, S.1
  • 30
    • 33645794537 scopus 로고    scopus 로고
    • Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor
    • Stremlau, M., et al. 2006. Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor. Proc. Natl. Acad. Sci. U. S. A. 103:5514-5519.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 5514-5519
    • Stremlau, M.1
  • 31
    • 77954748209 scopus 로고    scopus 로고
    • Peptide HIV-1 integrase inhibitors from HIV-1 gene products
    • Suzuki, S., et al. 2010. Peptide HIV-1 integrase inhibitors from HIV-1 gene products. J. Med. Chem. 53:5356-5360.
    • (2010) J. Med. Chem. , vol.53 , pp. 5356-5360
    • Suzuki, S.1
  • 35
    • 58149378581 scopus 로고    scopus 로고
    • Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-delta1 pleckstrin homology domain results in infectious pseudovirion production
    • Urano, E., et al. 2008. Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-delta1 pleckstrin homology domain results in infectious pseudovirion production. J. Gen. Virol. 89:3144-3149.
    • (2008) J. Gen. Virol. , vol.89 , pp. 3144-3149
    • Urano, E.1
  • 37
    • 24344470951 scopus 로고    scopus 로고
    • Cell-based and biochemical screening approaches for the discovery of novel HIV-1 inhibitors
    • DOI 10.1016/j.antiviral.2005.06.006, PII S0166354205001221
    • Westby, M., G R Nakayama, S L Butler, and W S Blair. 2005. Cell-based and biochemical screening approaches for the discovery of novel HIV-1 inhibitors. Antiviral Res. 67:121-140. (Pubitemid 41254196)
    • (2005) Antiviral Research , vol.67 , Issue.3 , pp. 121-140
    • Westby, M.1    Nakayama, G.R.2    Butler, S.L.3    Blair, W.S.4
  • 38
    • 42249105204 scopus 로고    scopus 로고
    • A cell-penetrating helical peptide as a potential HIV-1 inhibitor
    • Zhang, H., et al. 2008. A cell-penetrating helical peptide as a potential HIV-1 inhibitor. J. Mol. Biol. 378:565-580.
    • (2008) J. Mol. Biol. , vol.378 , pp. 565-580
    • Zhang, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.