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Volumn 78, Issue 14, 2004, Pages 7582-7589

Determinants of human immunodeficiency virus type 1 baseline susceptibility to the fusion inhibitors enfuvirtide and T-649 reside outside the peptide interaction site

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; PEPTIDE FUSION INHIBITOR; PROTEIN INHIBITOR; T 1249; T 649; UNCLASSIFIED DRUG;

EID: 3142779320     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.14.7582-7589.2004     Document Type: Article
Times cited : (55)

References (33)
  • 2
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan, D. C., C. T. Chutkowski, and P. S. Kim. 1998. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. USA 95:15613-15617.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 3
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 4
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y., and G. D. Fasman. 1978. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:251-276.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 5
    • 0035873517 scopus 로고    scopus 로고
    • Thermodynamics of peptide inhibitor binding to HIV-1 gp41
    • Cole, J. L., and V. M. Garsky. 2001. Thermodynamics of peptide inhibitor binding to HIV-1 gp41. Biochemistry 40:5633-5641.
    • (2001) Biochemistry , vol.40 , pp. 5633-5641
    • Cole, J.L.1    Garsky, V.M.2
  • 6
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120
    • Derdeyn, C. A., J. M. Decker, J. N. Sfakianos, X. Wu, W. A. O'Brien, L. Ratner, J. C. Kappes, G. M. Shaw, and E. Hunter. 2000. Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120. J. Virol. 74:8358-8367.
    • (2000) J. Virol. , vol.74 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Wu, X.4    O'Brien, W.A.5    Ratner, L.6    Kappes, J.C.7    Shaw, G.M.8    Hunter, E.9
  • 7
    • 0034890660 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor
    • Derdeyn, C. A., J. M. Decker, J. N. Sfakianos, Z. Zhang, W. A. O'Brien, L. Ratner, G. M. Shaw, and E. Hunter. 2001. Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor. J. Virol. 75:8605-8614.
    • (2001) J. Virol. , vol.75 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Zhang, Z.4    O'Brien, W.A.5    Ratner, L.6    Shaw, G.M.7    Hunter, E.8
  • 8
    • 0028077123 scopus 로고
    • Genetic variation of HIV type 1 in four World Health Organization- sponsored vaccine evaluation sites: Generation of functional envelope (glycoprotein 160) clones representative of sequence subtypes A, B, C, and E
    • Gao, F., L. Yue, S. Craig, C. L. Thornton, D. L. Robertson, F. E. McCutchan, J. A. Bradac, P. M. Sharp, B. H. Hahn, et al. 1994. Genetic variation of HIV type 1 in four World Health Organization-sponsored vaccine evaluation sites: generation of functional envelope (glycoprotein 160) clones representative of sequence subtypes A, B, C, and E. AIDS Res. Hum. Retrovir. 10:1359-1368.
    • (1994) AIDS Res. Hum. Retrovir. , vol.10 , pp. 1359-1368
    • Gao, F.1    Yue, L.2    Craig, S.3    Thornton, C.L.4    Robertson, D.L.5    McCutchan, F.E.6    Bradac, J.A.7    Sharp, P.M.8    Hahn, B.H.9
  • 9
    • 0037301373 scopus 로고    scopus 로고
    • Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites
    • He, Y., R. Vassell, M. Zaitseva, N. Nguyen, Z. Yang, Y. Weng, and C. D. Weiss. 2003. Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites. J. Virol. 77:1666-1671.
    • (2003) J. Virol. , vol.77 , pp. 1666-1671
    • He, Y.1    Vassell, R.2    Zaitseva, M.3    Nguyen, N.4    Yang, Z.5    Weng, Y.6    Weiss, C.D.7
  • 10
    • 0032904012 scopus 로고    scopus 로고
    • HIV-1 envelope determinants for cell tropism and chemokine receptor use
    • Hoffman, T. L., and R. W. Doms. 1999. HIV-1 envelope determinants for cell tropism and chemokine receptor use. Mol. Membr. Biol. 16:57-65.
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 57-65
    • Hoffman, T.L.1    Doms, R.W.2
  • 11
    • 0032883082 scopus 로고    scopus 로고
    • Analysis of the critical domain in the V3 loop of human immunodeficiency virus type 1 gp120 involved in CCR5 utilization
    • Hung, C. S., N. Vander Heyden, and L. Ratner. 1999. Analysis of the critical domain in the V3 loop of human immunodeficiency virus type 1 gp120 involved in CCR5 utilization. J. Virol. 73:8216-8226.
    • (1999) J. Virol. , vol.73 , pp. 8216-8226
    • Hung, C.S.1    Vander Heyden, N.2    Ratner, L.3
  • 12
    • 0002614837 scopus 로고    scopus 로고
    • Viral entry and receptors
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.). Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Hunter, E. 1997. Viral entry and receptors, p. 71-121. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1997) Retroviruses , pp. 71-121
    • Hunter, E.1
  • 13
    • 0034693932 scopus 로고    scopus 로고
    • Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1
    • Jin, B. S., J. R. Ryu, K. Ahn, and Y. G. Yu. 2000. Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir. 16:1797-1804.
    • (2000) AIDS Res. Hum. Retrovir. , vol.16 , pp. 1797-1804
    • Jin, B.S.1    Ryu, J.R.2    Ahn, K.3    Yu, Y.G.4
  • 14
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 infectivity by constrained alpha-helical peptides: Implications for the viral fusion mechanism
    • Judice, J. K., J. Y. Tom, W. Huang, T. Wrin, J. Vennari, C. J. Petropoulos, and R. S. McDowell. 1997. Inhibition of HIV type 1 infectivity by constrained alpha-helical peptides: implications for the viral fusion mechanism. Proc. Natl. Acad. Sci. USA 94:13426-13430.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13426-13430
    • Judice, J.K.1    Tom, J.Y.2    Huang, W.3    Wrin, T.4    Vennari, J.5    Petropoulos, C.J.6    McDowell, R.S.7
  • 15
    • 0037321703 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 attachment, coreceptor, and fusion inhibitors are active against both direct and trans infection of primary cells
    • Ketas, T. J., I. Frank, P. J. Klasse, B. M. Sullivan, J. P. Gardner, C. Spenlehauer, M. Nesin, W. C. Olson, J. P. Moore, and M. Pope. 2003. Human immunodeficiency virus type 1 attachment, coreceptor, and fusion inhibitors are active against both direct and trans infection of primary cells. J. Virol. 77:2762-2767.
    • (2003) J. Virol. , vol.77 , pp. 2762-2767
    • Ketas, T.J.1    Frank, I.2    Klasse, P.J.3    Sullivan, B.M.4    Gardner, J.P.5    Spenlehauer, C.6    Nesin, M.7    Olson, W.C.8    Moore, J.P.9    Pope, M.10
  • 19
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D., R. Wyatt, J. Robinson, R. W. Sweet, J. Sodroski, and W. A. Hendrickson. 1998. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 21
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 22
    • 0023829903 scopus 로고
    • 'DNA Strider': A 'C' program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers
    • Marck, C. 1988. 'DNA Strider': a 'C' program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers. Nucleic Acids Res. 16:1829-1836.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1829-1836
    • Marck, C.1
  • 24
    • 0037183892 scopus 로고    scopus 로고
    • Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor
    • Poveda, E., B. Rodes, C. Toro, L. Martin-Carbonero, J. Gonzalez-Lahoz, and V. Soriano. 2002. Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor. AIDS 16:1959-1961.
    • (2002) AIDS , vol.16 , pp. 1959-1961
    • Poveda, E.1    Rodes, B.2    Toro, C.3    Martin-Carbonero, L.4    Gonzalez-Lahoz, J.5    Soriano, V.6
  • 26
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., D. C. Shugars, and T. J. Matthews. 1998. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72:986-993.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., J. W. Dubay, T. Greenwell, T. Baird, Jr., T. G. Oas, C. McDanal, E. Hunter, and T. Matthews. 1994. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA 91:12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 32
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C., T. Oas, C. McDanal, D. Bolognesi, and T. Matthews. 1992. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 89:10537-10541.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 33
    • 0037119027 scopus 로고    scopus 로고
    • Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients
    • Xu, L., S. Hue, S. Taylor, D. Ratcliffe, J. A. Workman, S. Jackson, P. A. Cane, and D. Pillay. 2002. Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients. AIDS 16:1684-1686.
    • (2002) AIDS , vol.16 , pp. 1684-1686
    • Xu, L.1    Hue, S.2    Taylor, S.3    Ratcliffe, D.4    Workman, J.A.5    Jackson, S.6    Cane, P.A.7    Pillay, D.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.