메뉴 건너뛰기




Volumn 9, Issue 5-6, 1996, Pages 631-638

Epitope Contiguous Chains and Antibody Recognition in HIV-1 Synthetic Peptide Antigens

Author keywords

Antibody recognition; Conformation; Contiguous chains; Enzyme linked immunosorbent assay HIV 1; Synthetic peptides

Indexed keywords

EPITOPE; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; PEPTIDE; POLYSTYRENE DERIVATIVE;

EID: 0030224320     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(199634/12)9:5/6<631::AID-JMR312>3.0.CO;2-N     Document Type: Article
Times cited : (5)

References (24)
  • 1
    • 0003423124 scopus 로고
    • Solid phase peptide synthesis. A practical approach
    • ed. by D. Richwood and B. D. Hames, IRL Press
    • Atherton, E. and Sheppard, R. (1989). Solid phase peptide synthesis. A practical approach. In Practical Approach Series, ed. by D. Richwood and B. D. Hames, p. 203. IRL Press.
    • (1989) Practical Approach Series , pp. 203
    • Atherton, E.1    Sheppard, R.2
  • 2
    • 49149144747 scopus 로고
    • The adsorptive characteristics of proteins for polystyrene and their significance in solid phase immunoassays
    • Cantarero, I. A., Butler, J. E. and Osborne, J. W. (1980). The adsorptive characteristics of proteins for polystyrene and their significance in solid phase immunoassays. Analytical Biochemistry 105, 375.
    • (1980) Analytical Biochemistry , vol.105 , pp. 375
    • Cantarero, I.A.1    Butler, J.E.2    Osborne, J.W.3
  • 3
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B. and Noble, R. L. (1990). Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Peptide Protein Res. 35, 161.
    • (1990) Int. J. Peptide Protein Res. , vol.35 , pp. 161
    • Fields, G.B.1    Noble, R.L.2
  • 4
    • 0021964141 scopus 로고
    • Measurement of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet, B., Chaffotte, A. F., Djavadi-Ohaniance, L. and Goldberg, M. E. (1985). Measurement of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 37, 305.
    • (1985) J. Immunol. Methods , vol.37 , pp. 305
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 5
    • 0025893762 scopus 로고
    • General method for rapid synthesis of multicomponent peptide mixtures
    • Furka, Á., Sebestyén, F., Asgedom, M. and Dibó, G. (1991). General method for rapid synthesis of multicomponent peptide mixtures. Int. J. Protein. Res. 37, 487.
    • (1991) Int. J. Protein. Res. , vol.37 , pp. 487
    • Furka, Á.1    Sebestyén, F.2    Asgedom, M.3    Dibó, G.4
  • 6
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp, T. P. and Woods, K. R. (1981). Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. U.S.A. 78, 3824.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 3824
    • Hopp, T.P.1    Woods, K.R.2
  • 7
    • 0025910214 scopus 로고
    • Specificity of new peptide immunoassays versus other immunoassays and agglutination tests for detection of HIV antibody in African sera
    • Léonard, G., Verdier, M., Sangaré, A., Rey, J. L. and Denis, F. (1991). Specificity of new peptide immunoassays versus other immunoassays and agglutination tests for detection of HIV antibody in African sera. Eur. J. Clin. Microbiol. Infect. Dis. 10, 636.
    • (1991) Eur. J. Clin. Microbiol. Infect. Dis. , vol.10 , pp. 636
    • Léonard, G.1    Verdier, M.2    Sangaré, A.3    Rey, J.L.4    Denis, F.5
  • 8
    • 0021266325 scopus 로고
    • The effect of epitope density and antibody affinity on the ELISA as analyzed by monoclonal antibodies
    • Lew, A. M. (1984). The effect of epitope density and antibody affinity on the ELISA as analyzed by monoclonal antibodies. J. Immunol. Methods 72, 171.
    • (1984) J. Immunol. Methods , vol.72 , pp. 171
    • Lew, A.M.1
  • 9
    • 0024787957 scopus 로고
    • Structure and function of the HIV envelope
    • McKeating, J. and Willey, R. (1989). Structure and function of the HIV envelope. AIDS 3 (supl. 1), S35.
    • (1989) AIDS , vol.3 , Issue.1 SUPL
    • McKeating, J.1    Willey, R.2
  • 10
    • 0025087191 scopus 로고
    • Search for epitope-specific antibody repose to the signifying resistance to disease development
    • Neurath, R., Strick, N., Taylor, R, Rubinstein, P. and Stevens, C. (1990). Search for epitope-specific antibody repose to the signifying resistance to disease development. AIDS Res. and Hum. Retroviruses 6, 1183.
    • (1990) AIDS Res. and Hum. Retroviruses , vol.6 , pp. 1183
    • Neurath, R.1    Strick, N.2    Taylor, R.3    Rubinstein, P.4    Stevens, C.5
  • 11
    • 0024362184 scopus 로고
    • Epitope mapping of monoclonal antibodies against human immunodeficiency virus type 1 structural proteins by using peptides
    • Niedrig, M., Hinkula, J., Weigelt, W., L'Age-Sterhr, J., Pauli, G., Rosen, J. and Wahren, B. (1989). Epitope mapping of monoclonal antibodies against human immunodeficiency virus type 1 structural proteins by using peptides. J. Virol. 6, 3525.
    • (1989) J. Virol. , vol.6 , pp. 3525
    • Niedrig, M.1    Hinkula, J.2    Weigelt, W.3    L'Age-Sterhr, J.4    Pauli, G.5    Rosen, J.6    Wahren, B.7
  • 12
    • 0024605425 scopus 로고
    • Immunochemistry at interfaces
    • Nygren, H. and Stenberg, M. (1989). Immunochemistry at interfaces. Immunology 66, 321.
    • (1989) Immunology , vol.66 , pp. 321
    • Nygren, H.1    Stenberg, M.2
  • 13
    • 0025968853 scopus 로고
    • Mapping the anatomy of the immunodominant domain of the human immunodeficiency virus gp41 transmembrane protein: Peptide conformation analysis using monoclonal antibodies and proton nuclear magnetic resonance spectroscopy
    • Oldstone, M. B., Tishon, A., Lewicki, H., Dyson, H. J., Feher, V. A., Assa-Munt, N. and Wright, P. E. (1991). Mapping the anatomy of the immunodominant domain of the human immunodeficiency virus gp41 transmembrane protein: peptide conformation analysis using monoclonal antibodies and proton nuclear magnetic resonance spectroscopy. J. Virol. 65, 1727.
    • (1991) J. Virol. , vol.65 , pp. 1727
    • Oldstone, M.B.1    Tishon, A.2    Lewicki, H.3    Dyson, H.J.4    Feher, V.A.5    Assa-Munt, N.6    Wright, P.E.7
  • 14
    • 0025737588 scopus 로고
    • Epitope mapping employing immobilized synthetic peptides. How specific is the reactivity of these peptides with antiserum raised against the parent protein?
    • Savoca, R., Schwab, C. and Bossahard, H. R. (1991). Epitope mapping employing immobilized synthetic peptides. How specific is the reactivity of these peptides with antiserum raised against the parent protein? J. Immunol. Methods 141, 245.
    • (1991) J. Immunol. Methods , vol.141 , pp. 245
    • Savoca, R.1    Schwab, C.2    Bossahard, H.R.3
  • 15
    • 0028012508 scopus 로고
    • Influence of solid-phase antigen in competition enzyme-linked immunosorbent assays (ELISAs) on calculated antigen-antibody dissociation constants
    • Seligman, S. J. (1994). Influence of solid-phase antigen in competition enzyme-linked immunosorbent assays (ELISAs) on calculated antigen-antibody dissociation constants. J. Immunol. Methods 168, 101.
    • (1994) J. Immunol. Methods , vol.168 , pp. 101
    • Seligman, S.J.1
  • 16
    • 0022839477 scopus 로고
    • Assessment of coating-efficiency in ELISA plates by direct protein determination
    • Sorensen, K. and Brodbeck, U. (1986). Assessment of coating-efficiency in ELISA plates by direct protein determination. J. Immunol. Methods 93, 291.
    • (1986) J. Immunol. Methods , vol.93 , pp. 291
    • Sorensen, K.1    Brodbeck, U.2
  • 17
    • 0023718403 scopus 로고
    • Kinetics of antigen-antibody reactions at solid-liquid interfaces
    • Stenberg, M. and Nygren, H. (1988). Kinetics of antigen-antibody reactions at solid-liquid interfaces. J. Immunol. Methods 113, 3.
    • (1988) J. Immunol. Methods , vol.113 , pp. 3
    • Stenberg, M.1    Nygren, H.2
  • 18
    • 0023250991 scopus 로고
    • Modification of an ELISA-based procedure for affinity determination: Correction necessary for use with bivalent antibody
    • Stevens, F. (1987). Modification of an ELISA-based procedure for affinity determination: Correction necessary for use with bivalent antibody. Mol. Immunol. 24, 1055.
    • (1987) Mol. Immunol. , vol.24 , pp. 1055
    • Stevens, F.1
  • 19
    • 0025996335 scopus 로고
    • Role of conserved gp41 cysteine residues in the processing of human immunodeficiency virus envelope precursor and viral infectivity
    • Syu, W. J., Lee, E. R., Du, B., Yu, Q. C., Essex, M. and Lee, T. H. (1991). Role of conserved gp41 cysteine residues in the processing of human immunodeficiency virus envelope precursor and viral infectivity. J. Virol. 65, 6349.
    • (1991) J. Virol. , vol.65 , pp. 6349
    • Syu, W.J.1    Lee, E.R.2    Du, B.3    Yu, Q.C.4    Essex, M.5    Lee, T.H.6
  • 20
    • 0000237623 scopus 로고
    • Antigenic cross-reactivity between proteins and peptides: New insights and applications
    • Van Regenmortel, M. H. V. (1987). Antigenic cross-reactivity between proteins and peptides: new insights and applications. Trends Biochem. Sci. 12, 237.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 237
    • Van Regenmortel, M.H.V.1
  • 21
    • 0027401004 scopus 로고
    • Synthetic peptides versus natural antigens in immunoassays
    • Van Regenmortel, M. H. V. (1993). Synthetic peptides versus natural antigens in immunoassays. Ann. Biol. Clin. 52, 39.
    • (1993) Ann. Biol. Clin. , vol.52 , pp. 39
    • Van Regenmortel, M.H.V.1
  • 23
    • 0003918423 scopus 로고
    • Chapman and Hall, New York
    • Weber, G. (1992). Protein Interactions p. 293. Chapman and Hall, New York.
    • (1992) Protein Interactions , pp. 293
    • Weber, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.