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Volumn 11, Issue 2, 1997, Pages 147-153

Helical epitopes determined by low-stringency antibody screening of a combinatorial peptide library

Author keywords

AIDS; monoclonal antibodies; phage display libraries; protein secondary structure; vaccine

Indexed keywords

EPITOPE; GLYCOPROTEIN GP 120; MONOCLONAL ANTIBODY; PEPTIDE;

EID: 0031035358     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.2.9039957     Document Type: Article
Times cited : (20)

References (35)
  • 2
    • 0000557828 scopus 로고
    • X-ray crystallographic studies of proteins
    • Matthews, B. W. (1976) X-ray crystallographic studies of proteins. Annu. Rev. Phys. Chem. 27, 493-523
    • (1976) Annu. Rev. Phys. Chem. , vol.27 , pp. 493-523
    • Matthews, B.W.1
  • 3
    • 0024587230 scopus 로고
    • Protein structure determination in solution by nuclear magnetic resonance spectroscopy
    • Wuthrich, K. (1989) Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243, 45-50
    • (1989) Science , vol.243 , pp. 45-50
    • Wuthrich, K.1
  • 4
    • 0028112295 scopus 로고
    • Protein structure determination with three- and four-dimensional NMR spectroscopy
    • Oschkinat, H., Muller, T., and Dieckmann, T. (1994) Protein structure determination with three- and four-dimensional NMR spectroscopy. Chem. Int. Ed. Engl. 33, 277-293
    • (1994) Chem. Int. Ed. Engl. , vol.33 , pp. 277-293
    • Oschkinat, H.1    Muller, T.2    Dieckmann, T.3
  • 5
    • 0002608849 scopus 로고
    • Applications of three- and four-dimentional heteronuclear NMR spectroscopy to protein structure determination
    • Clore, G. M., and Gronenborn, M. (1991) Applications of three- and four-dimentional heteronuclear NMR spectroscopy to protein structure determination. Prog. NMR Spectrosc. 23, 43-92
    • (1991) Prog. NMR Spectrosc. , vol.23 , pp. 43-92
    • Clore, G.M.1    Gronenborn, M.2
  • 6
    • 0028355519 scopus 로고
    • NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus
    • De Lorimer, R., Moody, M. A., Haynes, B. F., and Spicer, L. D. (1994) NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus. Biochemistry 33, 2055-2062
    • (1994) Biochemistry , vol.33 , pp. 2055-2062
    • De Lorimer, R.1    Moody, M.A.2    Haynes, B.F.3    Spicer, L.D.4
  • 7
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms S., and Brahms, J. (1980) Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138, 149-178
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 8
    • 0026484855 scopus 로고
    • Generation of substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlation in Fourier transform infrared spectroscopy
    • Prestrelski, S. J., Byler, D. M., and Liebman, M. N. (1992) Generation of substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlation in Fourier transform infrared spectroscopy. Proteins 14, 440-450
    • (1992) Proteins , vol.14 , pp. 440-450
    • Prestrelski, S.J.1    Byler, D.M.2    Liebman, M.N.3
  • 9
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P. Y., and Fasman G. D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47, 45-148
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 10
    • 0020186244 scopus 로고
    • Identification of secondary structure in globular proteins: A new algorithm
    • Ramakrishnan, C., and Soman, K. V. (1982) Identification of secondary structure in globular proteins: A new algorithm. Int. J. Pept. Protein Res. 20, 218-237
    • (1982) Int. J. Pept. Protein Res. , vol.20 , pp. 218-237
    • Ramakrishnan, C.1    Soman, K.V.2
  • 11
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in proteins
    • Levitt, M., and Greer, J. (1977) Automatic identification of secondary structure in proteins. J. Mol. Biol. 114, 181-293
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-293
    • Levitt, M.1    Greer, J.2
  • 12
    • 0024395940 scopus 로고
    • A 3D building blocks approach to analyzing and predicting structure of proteins
    • Unger, R., Harel, D., and Sussman, J. L. (1989) A 3D building blocks approach to analyzing and predicting structure of proteins. Proteins 5, 355-373
    • (1989) Proteins , vol.5 , pp. 355-373
    • Unger, R.1    Harel, D.2    Sussman, J.L.3
  • 13
    • 0023555768 scopus 로고
    • Further development of protein secondary structure prediction using information theory: New parameters and consideration of residue pairs
    • Gilbrat, J.-F., Garnier, J., and Robson, B. (1987) Further development of protein secondary structure prediction using information theory: New parameters and consideration of residue pairs J. Mol. Biol. 198, 425-443
    • (1987) J. Mol. Biol. , vol.198 , pp. 425-443
    • Gilbrat, J.-F.1    Garnier, J.2    Robson, B.3
  • 14
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 15
    • 0021097529 scopus 로고
    • How good are predictions of protein secondary structure?
    • Kabsch, W., and Sander, C. (1983) How good are predictions of protein secondary structure? FEBS Lett. 155, 179-182
    • (1983) FEBS Lett. , vol.155 , pp. 179-182
    • Kabsch, W.1    Sander, C.2
  • 17
    • 0041170983 scopus 로고
    • Antibodies
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Harlow E., and Lan, D. (1988) Antibodies. A laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1988) A Laboratory Manual
    • Harlow, E.1    Lan, D.2
  • 18
    • 0015452895 scopus 로고
    • Staphylococcal protease: A proteolytic enzyme specific for glutamoyl bonds
    • Houmard, J., and Drapeau, G. R. (1972) Staphylococcal protease: A proteolytic enzyme specific for glutamoyl bonds. Proc. Nat. Acad. Sci. USA 69, 3506-3509
    • (1972) Proc. Nat. Acad. Sci. USA , vol.69 , pp. 3506-3509
    • Houmard, J.1    Drapeau, G.R.2
  • 19
    • 0023814393 scopus 로고
    • 95- and 25-kDa fragments of the human immunodeficiency virus envelope glycoprotein gp120 bind to the CD4 receptor
    • Nygren, A., Bergman, T., Matthews, T., Jornval, H., and Wigzell, H. (1988) 95- and 25-kDa fragments of the human immunodeficiency virus envelope glycoprotein gp120 bind to the CD4 receptor. Proc. Natl. Acad. Sci. USA 85, 6543-6546
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6543-6546
    • Nygren, A.1    Bergman, T.2    Matthews, T.3    Jornval, H.4    Wigzell, H.5
  • 20
    • 0023739598 scopus 로고
    • Protein blotting: A manual
    • Glick, D., ed, John Wiley & Sons, New York
    • Gershoni, J. M. (1988) Protein blotting: A manual. In Methods of Biochemical Analysis (Glick, D., ed) Vol. 33, pp. 1-58, John Wiley & Sons, New York
    • (1988) Methods of Biochemical Analysis , vol.33 , pp. 1-58
    • Gershoni, J.M.1
  • 21
    • 0024991625 scopus 로고
    • Peptides on phages: A vast library of peptides for identifying ligands
    • Cwirla, S. E., Peters, E. A., Barrett, R. W., and Dower, W. J. (1990) Peptides on phages: a vast library of peptides for identifying ligands. Proc. Natl. Acad. Sci. USA 87, 6378-6382
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6378-6382
    • Cwirla, S.E.1    Peters, E.A.2    Barrett, R.W.3    Dower, W.J.4
  • 22
    • 1842291330 scopus 로고    scopus 로고
    • Construction and use of 20mer phage display epitope library
    • Humana Press, Totowa, N.J. In press
    • Stern, B., and Gershoni, J. M. (1997) Construction and use of 20mer phage display epitope library. In Methods in Molecular Biology, Humana Press, Totowa, N.J. In press
    • (1997) Methods in Molecular Biology
    • Stern, B.1    Gershoni, J.M.2
  • 23
    • 0027266779 scopus 로고
    • Libraries of peptides and proteins displayed on filamentous phage
    • Smith, G. P., and Scott, J. K. (1993) Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol. 217, 228-257
    • (1993) Methods Enzymol. , vol.217 , pp. 228-257
    • Smith, G.P.1    Scott, J.K.2
  • 24
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and Cohen, S. N. 1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179-207
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 25
    • 84969001783 scopus 로고
    • The attraction of the proteins for small molecules and ions
    • Scatchard, G. (1949) The attraction of the proteins for small molecules and ions. Ann. N.Y., Sci. 51, 600-672
    • (1949) Ann. N.Y., Sci. , vol.51 , pp. 600-672
    • Scatchard, G.1
  • 28
    • 0028979185 scopus 로고
    • Direct interaction of compliment factor H with the Cl domain of HIV type 1 glycoprotein 120
    • Pinter, C., Siccardi, A. G., Longhi, R., and Clivio, A. (1995) Direct interaction of compliment factor H with the Cl domain of HIV type 1 glycoprotein 120. AIDS Res. Hum. Retroviruses 11, 577-588
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 577-588
    • Pinter, C.1    Siccardi, A.G.2    Longhi, R.3    Clivio, A.4
  • 30
    • 0027273332 scopus 로고
    • Secondary structure of gp160 and gp120 envelope glycoproteins of human immunodeficiency virus type 1: A Fourier transform infrared spectroscopic study
    • DeCroly, E., Cornet, B., Martin, I., Ruysschaert, J.-M., and Vandenbranden, M. (1993) Secondary structure of gp160 and gp120 envelope glycoproteins of human immunodeficiency virus type 1: a Fourier transform infrared spectroscopic study. J. Virol. 67, 3552-3560
    • (1993) J. Virol. , vol.67 , pp. 3552-3560
    • Decroly, E.1    Cornet, B.2    Martin, I.3    Ruysschaert, J.-M.4    Vandenbranden, M.5
  • 32
    • 0028107685 scopus 로고
    • Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies
    • Moore, J. P., Sattentau, Q. J., Wyatt, R., and Sodroski, J. (1994) Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies. J. Virol. 68, 469-484
    • (1994) J. Virol. , vol.68 , pp. 469-484
    • Moore, J.P.1    Sattentau, Q.J.2    Wyatt, R.3    Sodroski, J.4
  • 33
    • 0028034993 scopus 로고
    • Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1
    • Moore, J. P., Willey, R. L., Lewis, G. K., Robinson, J., and Sodroski, J. (1994) Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol. 68, 6836-6847
    • (1994) J. Virol. , vol.68 , pp. 6836-6847
    • Moore, J.P.1    Willey, R.L.2    Lewis, G.K.3    Robinson, J.4    Sodroski, J.5
  • 34
    • 0025253819 scopus 로고
    • Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding
    • Olshevsky, U., Heleseth, E., Furman, C., Li, J., Haseltine, W., and Sodroski, J. (1990) Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding. J. Virol. 64, 5701-5707
    • (1990) J. Virol. , vol.64 , pp. 5701-5707
    • Olshevsky, U.1    Heleseth, E.2    Furman, C.3    Li, J.4    Haseltine, W.5    Sodroski, J.6
  • 35
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth, E., Olshevski, U., Furman, C., and Sodroski, J. (1991) Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J. Virol. 65, 2119-2123
    • (1991) J. Virol. , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevski, U.2    Furman, C.3    Sodroski, J.4


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