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Volumn 77, Issue 6, 2003, Pages 3724-3733

Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; OCTAPEPTIDE; PEPTIDE 59; UNCLASSIFIED DRUG;

EID: 0037334588     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.6.3724-3733.2003     Document Type: Article
Times cited : (37)

References (71)
  • 1
    • 0000551005 scopus 로고
    • Viscosity as a conformational sieve. NOE of linear peptides in cryoprotective mixtures
    • Amodeo, P., A. Motta, D. Picone, G. Saviano, T. Tancredi, and P. A. Temussi. 1991. Viscosity as a conformational sieve. NOE of linear peptides in cryoprotective mixtures. J. Magn. Reson. 95:201-207.
    • (1991) J. Magn. Reson. , vol.95 , pp. 201-207
    • Amodeo, P.1    Motta, A.2    Picone, D.3    Saviano, G.4    Tancredi, T.5    Temussi, P.A.6
  • 3
    • 0028357377 scopus 로고
    • Serum neutralization of feline immunodeficiency virus is markedly dependent on passage history of the virus and host system
    • Baldinotti, F., D. Matteucci, P. Mazzetti, C. Giannelli, P. Bandecchi, F. Tozzini, and M. Bendinelli. 1994. Serum neutralization of feline immunodeficiency virus is markedly dependent on passage history of the virus and host system. J. Virol. 68:4572-4579.
    • (1994) J. Virol. , vol.68 , pp. 4572-4579
    • Baldinotti, F.1    Matteucci, D.2    Mazzetti, P.3    Giannelli, C.4    Bandecchi, P.5    Tozzini, F.6    Bendinelli, M.7
  • 4
    • 5144233105 scopus 로고
    • Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and D. G. Davis. 1985. Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 6
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0029072191 scopus 로고
    • A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen, C.-H., T. J. Matthews, C. B. McDanal, D. P. Bolognesi, and M. L. Greenberg. 1995. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69:3771-3777.
    • (1995) J. Virol. , vol.69 , pp. 3771-3777
    • Chen, C.-H.1    Matthews, T.J.2    McDanal, C.B.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 10
    • 2642611131 scopus 로고    scopus 로고
    • Autologous and heterologous neutralization analyses of primary feline immunodeficiency virus isolates
    • Del Mauro, D., D. Matteucci, S. Giannecchini, F. Maggi, M. Pistello, and M. Bendinelli. 1998. Autologous and heterologous neutralization analyses of primary feline immunodeficiency virus isolates. J. Virol. 72:2199-2207.
    • (1998) J. Virol. , vol.72 , pp. 2199-2207
    • Del Mauro, D.1    Matteucci, D.2    Giannecchini, S.3    Maggi, F.4    Pistello, M.5    Bendinelli, M.6
  • 11
    • 0035040022 scopus 로고    scopus 로고
    • Binding of recombinant feline immunodeficiency virus surface glycoprotein to feline cells: Role of CXCR4, cell-surface heparans, and an unidentified non-CXCR4 receptor
    • de Parseval, A., and J. H. Elder. 2001. Binding of recombinant feline immunodeficiency virus surface glycoprotein to feline cells: role of CXCR4, cell-surface heparans, and an unidentified non-CXCR4 receptor. J. Virol. 75: 4528-4539.
    • (2001) J. Virol. , vol.75 , pp. 4528-4539
    • De Parseval, A.1    Elder, J.H.2
  • 12
    • 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
  • 13
    • 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
  • 15
    • 0034675998 scopus 로고    scopus 로고
    • HIV-1 membrane fusion: Targets of opportunity
    • Doms, R. W., and J. P. Moore. 2000. HIV-1 membrane fusion: targets of opportunity. J. Cell Biol. 151:F9-F13.
    • (2000) J. Cell Biol. , vol.151
    • Doms, R.W.1    Moore, J.P.2
  • 16
    • 0021187796 scopus 로고
    • Proteins at work: "Stop-action" pictures at subzero temperatures
    • Douzou, P., and G. A. Petsko. 1984. Proteins at work: "stop-action" pictures at subzero temperatures. Adv. Protein Chem. 36:245-361.
    • (1984) Adv. Protein Chem. , vol.36 , pp. 245-361
    • Douzou, P.1    Petsko, G.A.2
  • 17
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • Eckert, D. M., and P. S. Kim. 2001. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc. Natl. Acad. Sci. USA 98:11187-11192.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 18
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D. M., V. N. Malashkevich, L. H. Hong, P. A. Carr, and P. S. Kim. 1999. Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99:103-115.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 19
    • 0032775435 scopus 로고    scopus 로고
    • Bicyclams, selective antagonists of the human chemokine receptor CXCR4, potently inhibit feline immunodeficiency virus replication
    • Egberink, H. F., E. De Clercq, A. L. van Vliet, J. Balzarini, G. J. Bridger, G. Henson, M. C. Horzinek, and D. Schols. 1999. Bicyclams, selective antagonists of the human chemokine receptor CXCR4, potently inhibit feline immunodeficiency virus replication. J. Virol. 73:6346-6352.
    • (1999) J. Virol. , vol.73 , pp. 6346-6352
    • Egberink, H.F.1    De Clercq, E.2    Van Vliet, A.L.3    Balzarini, J.4    Bridger, G.J.5    Henson, G.6    Horzinek, M.C.7    Schols, D.8
  • 21
    • 0029138450 scopus 로고
    • Feline immunodeficiency virus as a model for development of molecular approaches to intervention strategies against lentivirus infections
    • Elder, J. H., and T. R. Phillips. 1995. Feline immunodeficiency virus as a model for development of molecular approaches to intervention strategies against lentivirus infections. Adv. Virus Res. 45:225-247.
    • (1995) Adv. Virus Res. , vol.45 , pp. 225-247
    • Elder, J.H.1    Phillips, T.R.2
  • 23
    • 0035039605 scopus 로고    scopus 로고
    • Feline immunodeficiency virus cell entry
    • Frey, S. C. S., E. A. Hoover, and J. I. Mullins. 2001. Feline immunodeficiency virus cell entry. J. Virol. 75:5433-5440.
    • (2001) J. Virol. , vol.75 , pp. 5433-5440
    • Frey, S.C.S.1    Hoover, E.A.2    Mullins, J.I.3
  • 24
    • 0036631775 scopus 로고    scopus 로고
    • AIDS vaccination studies using an ex vivo feline immunodeficiency virus model: Failure to protect and possible enhancement of challenge infection by four cell-based vaccines prepared with autologous lymphoblasts
    • Giannecchini, S., P. Isola, O. Sichi, D. Matteucci, M. Pistello, L. Zaccaro, D. Del Mauro, and M. Bendinelli. 2002. AIDS vaccination studies using an ex vivo feline immunodeficiency virus model: failure to protect and possible enhancement of challenge infection by four cell-based vaccines prepared with autologous lymphoblasts. J. Virol. 76:6882-6892.
    • (2002) J. Virol. , vol.76 , pp. 6882-6892
    • Giannecchini, S.1    Isola, P.2    Sichi, O.3    Matteucci, D.4    Pistello, M.5    Zaccaro, L.6    Del Mauro, D.7    Bendinelli, M.8
  • 25
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., C. Mumenthaler, and K. Wüthrich. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 27
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., B. H. Meyer, P. Bachman, and R. R. Ernst. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meyer, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 28
    • 0032850583 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: Role of a conserved hydrophobic cavity in membrane fusion
    • Ji, H., W. Shu, F. T. Burling, S. Jiang, and M. Lu. 1999. Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusion. J. Virol. 73:8578-8586.
    • (1999) J. Virol. , vol.73 , pp. 8578-8586
    • Ji, H.1    Shu, W.2    Burling, F.T.3    Jiang, S.4    Lu, M.5
  • 30
    • 0033041322 scopus 로고    scopus 로고
    • A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody
    • Jiang, S., K. Lin, L. Zhang, and A. K. Debnath. 1999. A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods 80:85-96.
    • (1999) J. Virol. Methods , vol.80 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.4
  • 31
    • 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
  • 32
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implications for the viral fusion mechanism
    • Judice, J. K., J. Y. K. Tom, W. Huang, T. Wrin, J. Vennari, C. J. Petropoulos, and R. S. McDowell. 1997. Inhibition of HIV type 1 infectivity by constrained α-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.K.2    Huang, W.3    Wrin, T.4    Vennari, J.5    Petropoulos, C.J.6    McDowell, R.S.7
  • 36
    • 0029926552 scopus 로고    scopus 로고
    • HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41
    • Lawless, M. K., S. Barney, K. I. Guthrie, T. B. Bucy, S. R. Petteway, Jr., and G. Merutka. 1996. HIV-1 membrane fusion mechanism: structural studies of the interactions between biologically-active peptides from gp41. Biochemistry 35:13697-13708.
    • (1996) Biochemistry , vol.35 , pp. 13697-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3    Bucy, T.B.4    Petteway S.R., Jr.5    Merutka, G.6
  • 38
    • 0034759947 scopus 로고    scopus 로고
    • Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis
    • Lu, M., M. O. Stoller, S. Wang, J. Liu, M. B. Fagan, and J. H. Numberg. 2001. Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis. J. Virol. 75:11146-11156.
    • (2001) J. Virol. , vol.75 , pp. 11146-11156
    • Lu, M.1    Stoller, M.O.2    Wang, S.3    Liu, J.4    Fagan, M.B.5    Numberg, J.H.6
  • 39
    • 0032483021 scopus 로고    scopus 로고
    • Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides
    • Malashkevich, V. N., D. C. Chan, C. T. Chutkowski, and P. S. Kim. 1998. Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl. Acad. Sci. USA 95:9134-9139.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9134-9139
    • Malashkevich, V.N.1    Chan, D.C.2    Chutkowski, C.T.3    Kim, P.S.4
  • 41
    • 0030841372 scopus 로고    scopus 로고
    • Most potential linear B cell epitopes of Env glycoproteins of feline immunodeficiency virus are immunogenically silent in infected cats
    • Massi, C., S. Lombardi, E. Indino, D. Matteucci, C. La Rosa, F. Esposito, C. Garzelli, and M. Bendinelli. 1997. Most potential linear B cell epitopes of Env glycoproteins of feline immunodeficiency virus are immunogenically silent in infected cats. AIDS Res. Hum. Retrovir. 13:1121-1129.
    • (1997) AIDS Res. Hum. Retrovir. , vol.13 , pp. 1121-1129
    • Massi, C.1    Lombardi, S.2    Indino, E.3    Matteucci, D.4    La Rosa, C.5    Esposito, F.6    Garzelli, C.7    Bendinelli, M.8
  • 42
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 43
    • 0034978733 scopus 로고    scopus 로고
    • Genetic subtypes, humoral immunity, and human immunodeficiency virus type vaccine development
    • Moore, J. P., P. W. H. I. Parren, and D. Burton. 2001. Genetic subtypes, humoral immunity, and human immunodeficiency virus type vaccine development. J. Virol. 75:5721-5729.
    • (2001) J. Virol. , vol.75 , pp. 5721-5729
    • Moore, J.P.1    Parren, P.W.H.I.2    Burton, D.3
  • 44
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Muñoz-Barroso, I., S. Durell, K. Sakaguchi, E. Appella, and R. Blumenthal. 1998. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell Biol. 140:315-323.
    • (1998) J. Cell Biol. , vol.140 , pp. 315-323
    • Muñoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 45
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Muñoz-Barroso, I., K. Salzwedel, E. Hunter, and R. Blumenthal. 1999. Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J. Virol. 73:6089-6092.
    • (1999) J. Virol. , vol.73 , pp. 6089-6092
    • Muñoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 46
    • 0034834565 scopus 로고    scopus 로고
    • Receptors and entry cofactors for retroviruses include single and multiple transmembrane-spanning proteins as well as newly described glycophosphatidylinositol-anchored and secreted proteins
    • Overbaugh, J., A. D. Miller, and M. V. Eiden. 2001. Receptors and entry cofactors for retroviruses include single and multiple transmembrane-spanning proteins as well as newly described glycophosphatidylinositol-anchored and secreted proteins. Microbiol. Mol. Biol. Rev. 65:371-389.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 371-389
    • Overbaugh, J.1    Miller, A.D.2    Eiden, M.V.3
  • 47
    • 0028903355 scopus 로고
    • Structural analysis of the principal immunodominant domain of the feline immunodeficiency virus transmembrane glycoprotein
    • Pancino, G., L. Camoin, and P. Sonigo. 1995. Structural analysis of the principal immunodominant domain of the feline immunodeficiency virus transmembrane glycoprotein. J. Virol. 69:2110-2118.
    • (1995) J. Virol. , vol.69 , pp. 2110-2118
    • Pancino, G.1    Camoin, L.2    Sonigo, P.3
  • 49
    • 0034755554 scopus 로고    scopus 로고
    • Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5
    • Parker, C. E., L. J. Deterding, C. Hager-braun, J. M. Binley, N. Schülke, H. Katinger, J. P. Moore, and K. B. Tomer. 2001. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J. Virol. 75:10906-10911.
    • (2001) J. Virol. , vol.75 , pp. 10906-10911
    • Parker, C.E.1    Deterding, L.J.2    Hager-braun, C.3    Binley, J.M.4    Schülke, N.5    Katinger, H.6    Moore, J.P.7    Tomer, K.B.8
  • 50
    • 0023137671 scopus 로고
    • Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome
    • Pedersen, N. C., E. W. Ho, M. L. Brown, and J. K. Yamamoto. 1987. Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome. Science 235:790-793.
    • (1987) Science , vol.235 , pp. 790-793
    • Pedersen, N.C.1    Ho, E.W.2    Brown, M.L.3    Yamamoto, J.K.4
  • 51
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., O. W. Sørensen, and R. R. Ernst. 1982. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104:6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 52
    • 0029985950 scopus 로고    scopus 로고
    • Neutralization sensitivity and accessibility of continuous B cell epitopes of the feline immunodeficiency virus envelope
    • Richardson, J., I. Fossati, A. Moraillon, S. Castelot, P. Sonigo, and G. Pancino. 1996. Neutralization sensitivity and accessibility of continuous B cell epitopes of the feline immunodeficiency virus envelope. J. Gen. Virol. 77:759-777.
    • (1996) J. Gen. Virol. , vol.77 , pp. 759-777
    • Richardson, J.1    Fossati, I.2    Moraillon, A.3    Castelot, S.4    Sonigo, P.5    Pancino, G.6
  • 53
    • 0031935144 scopus 로고    scopus 로고
    • Delayed infection after immunization with a peptide from the transmembrane glycoprotein of the feline immunodeficiency virus
    • Richardson, J., A. Moraillon, F. Crespeau, S. Baud, P. Sonigo, and G. Pancino. 1998. Delayed infection after immunization with a peptide from the transmembrane glycoprotein of the feline immunodeficiency virus. J. Virol. 72:2406-2415.
    • (1998) J. Virol. , vol.72 , pp. 2406-2415
    • Richardson, J.1    Moraillon, A.2    Crespeau, F.3    Baud, S.4    Sonigo, P.5    Pancino, G.6
  • 55
    • 0027420109 scopus 로고
    • Evolution of structural proteins of feline immunodeficiency virus: Molecular epidemiology and evidence of selection for change
    • Rigby, M. A., E. C. Holmes, M. Pistello, A. Mackay, A. J. L. Brown, and J. C. Neil. 1993. Evolution of structural proteins of feline immunodeficiency virus: molecular epidemiology and evidence of selection for change. J. Gen. Virol. 74:425-436.
    • (1993) J. Gen. Virol. , vol.74 , pp. 425-436
    • Rigby, M.A.1    Holmes, E.C.2    Pistello, M.3    Mackay, A.4    Brown, A.J.L.5    Neil, J.C.6
  • 56
    • 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
  • 57
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., M. S. Kay, and P. S. Kim. 2001. Protein design of an HIV-1 entry inhibitor. Science 291:884-888.
    • (2001) Science. , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 59
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel, K., J. T. West, and E. Hunter. 1999. A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J. Virol. 73:2469-2480.
    • (1999) J. Virol. , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 60
    • 0033678611 scopus 로고    scopus 로고
    • Molecular mimicry between the trimeric ectodomain of the transmembrane protein of immunosuppressive lentiviruses (HIV-SIV-FIV) and interleukin 2
    • Serres, P. F. 2000. Molecular mimicry between the trimeric ectodomain of the transmembrane protein of immunosuppressive lentiviruses (HIV-SIV-FIV) and interleukin 2. C. R. Acad. Sci. Ser. III 323:1019-1029.
    • (2000) C. R. Acad. Sci. Ser. III , vol.323 , pp. 1019-1029
    • Serres, P.F.1
  • 61
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez, T., W. R. Gallaher, A. Agirre, F. M. Goni, and J. L. Nieva. 2000. Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J. Virol. 74:8038-8047.
    • (2000) J. Virol. , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 64
    • 0028953212 scopus 로고
    • The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure
    • Wild, C., T. Greenwell, D. Shugars, L. Rimsky-Clarke, and T. J. Matthews. 1995. The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Hum. Retrovir. 11:323-325.
    • (1995) AIDS Res. Hum. Retrovir. , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.J.5
  • 65
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 66
    • 0030937655 scopus 로고    scopus 로고
    • FIV infection of the domestic cat: An animal model for AIDS
    • Willett, B. J., J. N. Flynn, and M. J. Hosie. 1997. FIV infection of the domestic cat: an animal model for AIDS. Immunol. Today 18:182-189.
    • (1997) Immunol. Today , vol.18 , pp. 182-189
    • Willett, B.J.1    Flynn, J.N.2    Hosie, M.J.3
  • 67
    • 0030816181 scopus 로고    scopus 로고
    • Shared usage of the chemokine receptor CXCR4 by the feline and human immunodeficiency viruses
    • Willett, B. J., L. Picard, M. J. Hosie, J. D. Turner, K. Adema, and P. R. Clapham. 1997. Shared usage of the chemokine receptor CXCR4 by the feline and human immunodeficiency viruses. J. Virol. 71:6407-6415.
    • (1997) J. Virol. , vol.71 , pp. 6407-6415
    • Willett, B.J.1    Picard, L.2    Hosie, M.J.3    Turner, J.D.4    Adema, K.5    Clapham, P.R.6
  • 68
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt, R., and J. Sodroski. 1998. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 69
    • 0035339989 scopus 로고    scopus 로고
    • Epitope-vaccine as a new strategy against HIV-1 mutation
    • Xiao, Y., Y. Lu, and Y.-H. Chen. 2001. Epitope-vaccine as a new strategy against HIV-1 mutation. Immunol. Lett. 77:3-6.
    • (2001) Immunol. Lett. , vol.77 , pp. 3-6
    • Xiao, Y.1    Lu, Y.2    Chen, Y.-H.3
  • 70
    • 0025916440 scopus 로고
    • Development of IL-2-independent feline lymphoid cell lines chronically infected with feline immunodeficiency virus: Importance for diagnostic reagents and vaccines
    • Yamamoto, J. K., C. D. Ackley, H. Zochlinski, H. Louie, E. Pembroke, M. Torten, H. Hansen, R. Munn, and T. Okuda. 1991. Development of IL-2-independent feline lymphoid cell lines chronically infected with feline immunodeficiency virus: importance for diagnostic reagents and vaccines. Intervirology 32:361-375.
    • (1991) Intervirology , vol.32 , pp. 361-375
    • Yamamoto, J.K.1    Ackley, C.D.2    Zochlinski, H.3    Louie, H.4    Pembroke, E.5    Torten, M.6    Hansen, H.7    Munn, R.8    Okuda, T.9


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