메뉴 건너뛰기




Volumn 73, Issue 7, 1999, Pages 5795-5802

Peptide ligands to human immunodeficiency virus type 1 gp120 identified from phage display libraries

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120; LIGAND; MONOCLONAL ANTIBODY 17B; NEUTRALIZING ANTIBODY; PEPTIDE; PEPTIDE LIBRARY; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 0033027065     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.7.5795-5802.1999     Document Type: Article
Times cited : (85)

References (40)
  • 1
    • 0025278031 scopus 로고
    • Analysis of the site in CD4 that binds to the HIV envelope glycoprotein
    • Brodsky, M. H., M. Warton, R. M. Myers, and D. R. Littman. 1990. Analysis of the site in CD4 that binds to the HIV envelope glycoprotein. J. Immunol. 144:3078-3086.
    • (1990) J. Immunol. , vol.144 , pp. 3078-3086
    • Brodsky, M.H.1    Warton, M.2    Myers, R.M.3    Littman, D.R.4
  • 2
    • 0028023726 scopus 로고
    • Structure of influenza haemaglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemaglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 3
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 4
    • 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
  • 5
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dormán, G., and G. D. Prestwich. 1994. Benzophenone photophores in biochemistry. Biochemistry 33:5661-5673.
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dormán, G.1    Prestwich, G.D.2
  • 8
    • 0345366076 scopus 로고    scopus 로고
    • Unpublished results
    • Ferrer, M. Unpublished results.
    • Ferrer, M.1
  • 9
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R A., C. T. Wild, Y. Weng, and C. D. Weiss. 1998. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5:276-279.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 11
    • 0031240001 scopus 로고    scopus 로고
    • Enveloped viruses: A common mode of membrane fusion?
    • Hughson, F. M. 1997. Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7:565-569.
    • (1997) Curr. Biol. , vol.7 , pp. 565-569
    • Hughson, F.M.1
  • 12
    • 0023890869 scopus 로고
    • Location and chemical synthesis of a binding site for HIV-1 on the CD4 protein
    • Jameson, B. A., P. E. Rao, L. I. Kong, B. H. Hahn, G. M. Shaw, L. E. Hood, and S. B. H. Kent. 1988. Location and chemical synthesis of a binding site for HIV-1 on the CD4 protein. Science 240:1335-1339.
    • (1988) Science , vol.240 , pp. 1335-1339
    • Jameson, B.A.1    Rao, P.E.2    Kong, L.I.3    Hahn, B.H.4    Shaw, G.M.5    Hood, L.E.6    Kent, S.B.H.7
  • 14
    • 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
  • 15
    • 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, 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.5    Merutka, G.6
  • 17
    • 0032577581 scopus 로고    scopus 로고
    • Chemokine receptors: Keys to AIDS pathogenesis?
    • Littman, D. R. 1998. Chemokine receptors: keys to AIDS pathogenesis? Cell 93:677-680.
    • (1998) Cell , vol.93 , pp. 677-680
    • Littman, D.R.1
  • 18
    • 0027049402 scopus 로고
    • Human immunodeficiency virus gp120 binding C′C″ ridge of CD4 domain 1 is also involved in interactions with class II major histocompatibility complex molecules
    • Moebius, U., L. K. Clayton, S. Abraham, A. Diener, J. J. Yunis, S. C. Harrison, and E. L. Reinherz. 1992. Human immunodeficiency virus gp120 binding C′C″ ridge of CD4 domain 1 is also involved in interactions with class II major histocompatibility complex molecules. Proc. Natl. Acad. Sci. USA 89:12008-12012.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12008-12012
    • Moebius, U.1    Clayton, L.K.2    Abraham, S.3    Diener, A.4    Yunis, J.J.5    Harrison, S.C.6    Reinherz, E.L.7
  • 19
    • 0026650992 scopus 로고
    • The human immunodeficiency virus gp120 binding site on CD4: Delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure
    • Moebius, U., L. K. Clayton, S. Abraham, S. C. Harrison, and E. L. Reinherz. 1992. The human immunodeficiency virus gp120 binding site on CD4: delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure. J. Exp. Med. 176:507-517.
    • (1992) J. Exp. Med. , vol.176 , pp. 507-517
    • Moebius, U.1    Clayton, L.K.2    Abraham, S.3    Harrison, S.C.4    Reinherz, E.L.5
  • 20
    • 0024599211 scopus 로고
    • An enzyme-linked immunosorbent assay for antibodies to the envelope glycoproteins of divergent strains of HIV-1
    • Moore, J. P., L. A. Wallace, E. A. C. Follett, and J. A. McKeating. 1989. An enzyme-linked immunosorbent assay for antibodies to the envelope glycoproteins of divergent strains of HIV-1. AIDS 3:155-163.
    • (1989) AIDS , vol.3 , pp. 155-163
    • Moore, J.P.1    Wallace, L.A.2    Follett, E.A.C.3    McKeating, J.A.4
  • 21
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport, I., Y. C. Chen, P. Cupers, S. E. Shoelson, and T. Kirchhausen. 1998. Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17:2148-2155.
    • (1998) EMBO J. , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 22
    • 0026707749 scopus 로고
    • Effects of CD4 synthetic peptides on HIV type 1 envelope glycoprotein function
    • Repke, H., D. Gabuzda, G. Palú, F. Emmrich, and J. Sodroski. 1992. Effects of CD4 synthetic peptides on HIV type 1 envelope glycoprotein function. J. Immunol. 149:1809-1816.
    • (1992) J. Immunol. , vol.149 , pp. 1809-1816
    • Repke, H.1    Gabuzda, D.2    Palú, G.3    Emmrich, F.4    Sodroski, J.5
  • 25
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau, Q. J., and J. P. Moore. 1993. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J. Virol. 67:7383-7393.
    • (1993) J. Virol. , vol.67 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2
  • 26
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau, Q. J, and J. P. Moore. 1991. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J. Exp. Med. 174:407-415.
    • (1991) J. Exp. Med. , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 27
    • 0026537562 scopus 로고
    • Construction of a binding site for human immunodeficiency virus type 1 gp12c0 in rat CD4
    • Schockmel, G. A., C. Somoza, S. J. Davis, A. F. Williams, and D. Healey. 1992. Construction of a binding site for human immunodeficiency virus Type 1 gp12c0 in rat CD4. J. Exp. Med. 175:301-304.
    • (1992) J. Exp. Med. , vol.175 , pp. 301-304
    • Schockmel, G.A.1    Somoza, C.2    Davis, S.J.3    Williams, A.F.4    Healey, D.5
  • 28
    • 0027405386 scopus 로고
    • A rat CD4 mutant containing the gp120-binding site mediates human immunodeficiency virus type 1 infection
    • Simon, J. H. M., C. Somoza, G. A. Schockmel, M. Collin, S. J. Davis, A. F. Williams, and W. James. 1993. A rat CD4 mutant containing the gp120-binding site mediates human immunodeficiency virus type 1 infection. J. Exp. Med. 177:949-954.
    • (1993) J. Exp. Med. , vol.177 , pp. 949-954
    • Simon, J.H.M.1    Somoza, C.2    Schockmel, G.A.3    Collin, M.4    Davis, S.J.5    Williams, A.F.6    James, W.7
  • 30
    • 0031902829 scopus 로고    scopus 로고
    • CD4-induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: Consequences for virus entry and neutralization
    • Sullivan, N., Y. Sun, Q. Sattentau, M. Thali, D. Wu, G. Denisova, J. Gershoni, J. Robinson, J. Moore, and J. Sodroski. 1998. CD4-induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization. J. Virol. 72:4694-4703.
    • (1998) J. Virol. , vol.72 , pp. 4694-4703
    • Sullivan, N.1    Sun, Y.2    Sattentau, Q.3    Thali, M.4    Wu, D.5    Denisova, G.6    Gershoni, J.7    Robinson, J.8    Moore, J.9    Sodroski, J.10
  • 31
  • 32
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali, M., J. P. Moore, C. Furman, M. Charles, D. D. Ho, J. Robinson, and J. Sodroski, 1993. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67:3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 35
    • 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, 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, T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 36
    • 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
  • 37
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.