메뉴 건너뛰기




Volumn 402, Issue 1-2, 2014, Pages 35-42

Optimization of peptide arrays for studying antibodies to hepatitis C virus continuous epitopes

Author keywords

E1E2 glycoprotein; HCV; Peptide array

Indexed keywords

BIOLOGICAL MARKER; BUFFER; E1 PROTEIN, HEPATITIS C VIRUS; EPITOPE; ESTER; GLYCOPROTEIN E2, HEPATITIS C VIRUS; HEPATITIS C ANTIBODY; N HYDROXYSUCCINIMIDE; N-HYDROXYSUCCINIMIDE; POLYVINYL ALCOHOL; SUCCINIMIDE DERIVATIVE; VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 84888324178     PISSN: 00221759     EISSN: 18727905     Source Type: Journal    
DOI: 10.1016/j.jim.2013.11.005     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0035083184 scopus 로고    scopus 로고
    • A chemoselective method for site-specific immobilization of peptides via aminooxy group
    • Adamczyk M., Gebler J.C., Reddy R.E., Yu Z. A chemoselective method for site-specific immobilization of peptides via aminooxy group. Bioconjug. Chem. 2001, 12:139.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 139
    • Adamczyk, M.1    Gebler, J.C.2    Reddy, R.E.3    Yu, Z.4
  • 2
    • 62449321935 scopus 로고    scopus 로고
    • Peptide microarrays for serum antibody diagnostics
    • Andresen H., Bier F.F. Peptide microarrays for serum antibody diagnostics. Methods Mol. Biol. 2009, 509:123.
    • (2009) Methods Mol. Biol. , vol.509 , pp. 123
    • Andresen, H.1    Bier, F.F.2
  • 6
    • 33645381298 scopus 로고    scopus 로고
    • Protein and peptide arrays: recent trends and new directions
    • Cretich M., Damin F., Pirri G., Chiari M. Protein and peptide arrays: recent trends and new directions. Biomol. Eng. 2006, 23:77.
    • (2006) Biomol. Eng. , vol.23 , pp. 77
    • Cretich, M.1    Damin, F.2    Pirri, G.3    Chiari, M.4
  • 8
    • 0028021952 scopus 로고
    • Formation and intracellular-localization of hepatitis-C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses
    • Dubuisson J., Hsu H.H., Cheung R.C., Greenberg H.B., Russell D.G., Rice C.M. Formation and intracellular-localization of hepatitis-C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses. J. Virol. 1994, 68:6147.
    • (1994) J. Virol. , vol.68 , pp. 6147
    • Dubuisson, J.1    Hsu, H.H.2    Cheung, R.C.3    Greenberg, H.B.4    Russell, D.G.5    Rice, C.M.6
  • 9
    • 0043158700 scopus 로고    scopus 로고
    • Increased resistance of peptides to serum proteases by modification of their amino groups
    • Galati R., Verdina A., Falasca G., Chersi A. Increased resistance of peptides to serum proteases by modification of their amino groups. Z. Naturforsch. C. 2003, 58:558.
    • (2003) Z. Naturforsch. C. , vol.58 , pp. 558
    • Galati, R.1    Verdina, A.2    Falasca, G.3    Chersi, A.4
  • 12
    • 84857308609 scopus 로고    scopus 로고
    • Increased affinity and solubility of peptides used for direct peptide ELISA on polystyrene surfaces through fusion with a polystyrene-binding peptide tag
    • Kogot J.M., Sarkes D.A., Val-Addo I., Pellegrino P.M., Stratis-Cullum D.N. Increased affinity and solubility of peptides used for direct peptide ELISA on polystyrene surfaces through fusion with a polystyrene-binding peptide tag. BioTechniques 2012, 52:95.
    • (2012) BioTechniques , vol.52 , pp. 95
    • Kogot, J.M.1    Sarkes, D.A.2    Val-Addo, I.3    Pellegrino, P.M.4    Stratis-Cullum, D.N.5
  • 13
    • 84869229723 scopus 로고    scopus 로고
    • Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33
    • Kong L., Giang E., Nieusma T., Robbins J.B., Deller M.C., Stanfield R.L., Wilson I.A., Law M. Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33. J. Virol. 2012, 86:13085.
    • (2012) J. Virol. , vol.86 , pp. 13085
    • Kong, L.1    Giang, E.2    Nieusma, T.3    Robbins, J.B.4    Deller, M.C.5    Stanfield, R.L.6    Wilson, I.A.7    Law, M.8
  • 15
    • 61549118827 scopus 로고    scopus 로고
    • Nomenclature and numbering of the hepatitis C virus
    • Kuiken C., Simmonds P. Nomenclature and numbering of the hepatitis C virus. Methods Mol. Biol. 2009, 510:33.
    • (2009) Methods Mol. Biol. , vol.510 , pp. 33
    • Kuiken, C.1    Simmonds, P.2
  • 17
    • 32044456461 scopus 로고    scopus 로고
    • Versatile and efficient synthesis of protein-polysaccharide conjugate vaccines using aminooxy reagents and oxime chemistry
    • Lees A., Sen G., LopezAcosta A. Versatile and efficient synthesis of protein-polysaccharide conjugate vaccines using aminooxy reagents and oxime chemistry. Vaccine 2006, 24:716.
    • (2006) Vaccine , vol.24 , pp. 716
    • Lees, A.1    Sen, G.2    LopezAcosta, A.3
  • 18
    • 0036898579 scopus 로고    scopus 로고
    • Protein microarrays and proteomics
    • MacBeath G. Protein microarrays and proteomics. Nat. Genet. 2002, 32(Suppl.):526.
    • (2002) Nat. Genet. , vol.32 , pp. 526
    • MacBeath, G.1
  • 21
    • 80051923476 scopus 로고    scopus 로고
    • A weak neutralizing antibody response to hepatitis C virus envelope glycoprotein enhances virus infection
    • Meyer K., Banerjee A., Frey S.E., Belshe R.B., Ray R. A weak neutralizing antibody response to hepatitis C virus envelope glycoprotein enhances virus infection. PLoS One 2011, 6:e23699.
    • (2011) PLoS One , vol.6 , pp. e23699
    • Meyer, K.1    Banerjee, A.2    Frey, S.E.3    Belshe, R.B.4    Ray, R.5
  • 25
    • 84869233037 scopus 로고    scopus 로고
    • Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody
    • Potter J.A., Owsianka A.M., Jeffery N., Matthews D.J., Keck Z.Y., Lau P., Foung S.K., Taylor G.L., Patel A.H. Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody. J. Virol. 2012, 86:12923.
    • (2012) J. Virol. , vol.86 , pp. 12923
    • Potter, J.A.1    Owsianka, A.M.2    Jeffery, N.3    Matthews, D.J.4    Keck, Z.Y.5    Lau, P.6    Foung, S.K.7    Taylor, G.L.8    Patel, A.H.9
  • 30
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • Schena M., Shalon D., Davis R.W., Brown P.O. Quantitative monitoring of gene expression patterns with a complementary DNA microarray. Science 1995, 270:467.
    • (1995) Science , vol.270 , pp. 467
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 31
    • 0030589816 scopus 로고    scopus 로고
    • Preferential labeling of alpha-amino N-terminal groups in peptides by biotin, application to the detection of specific anti-peptide antibodies by enzyme immunoassays
    • Selo I., Negroni L., Creminon C., Grassi J., Wal J.M. Preferential labeling of alpha-amino N-terminal groups in peptides by biotin, application to the detection of specific anti-peptide antibodies by enzyme immunoassays. J. Immunol. Methods 1996, 199:127.
    • (1996) J. Immunol. Methods , vol.199 , pp. 127
    • Selo, I.1    Negroni, L.2    Creminon, C.3    Grassi, J.4    Wal, J.M.5
  • 34
    • 4444365081 scopus 로고    scopus 로고
    • Producing peptide arrays for epitope mapping by intein-mediated protein ligation
    • (438, 440 passim)
    • Sun L., Rush J., Ghosh I., Maunus J.R., Xu M.Q. Producing peptide arrays for epitope mapping by intein-mediated protein ligation. BioTechniques 2004, 37:430. (438, 440 passim).
    • (2004) BioTechniques , vol.37 , pp. 430
    • Sun, L.1    Rush, J.2    Ghosh, I.3    Maunus, J.R.4    Xu, M.Q.5
  • 35
    • 84863229503 scopus 로고    scopus 로고
    • Naturally occurring antibodies that recognize linear epitopes in the amino terminus of the hepatitis C virus E2 protein confer noninterfering, additive neutralization
    • Tarr A.W., Urbanowicz R.A., Jayaraj D., Brown R.J., McKeating J.A., Irving W.L., Ball J.K. Naturally occurring antibodies that recognize linear epitopes in the amino terminus of the hepatitis C virus E2 protein confer noninterfering, additive neutralization. J. Virol. 2012, 86:2739.
    • (2012) J. Virol. , vol.86 , pp. 2739
    • Tarr, A.W.1    Urbanowicz, R.A.2    Jayaraj, D.3    Brown, R.J.4    McKeating, J.A.5    Irving, W.L.6    Ball, J.K.7
  • 36
    • 0036302087 scopus 로고    scopus 로고
    • Structural features of envelope proteins on hepatitis C virus-like particles as determined by anti-envelope monoclonal antibodies and CD81 binding
    • Triyatni M., Vergalla J., Davis A.R., Hadlock K.G., Foung S.K., Liang T.J. Structural features of envelope proteins on hepatitis C virus-like particles as determined by anti-envelope monoclonal antibodies and CD81 binding. Virology 2002, 298:124.
    • (2002) Virology , vol.298 , pp. 124
    • Triyatni, M.1    Vergalla, J.2    Davis, A.R.3    Hadlock, K.G.4    Foung, S.K.5    Liang, T.J.6
  • 39
    • 33751013270 scopus 로고    scopus 로고
    • Comparison of hydroxylated print additives on antibody microarray performance
    • Wu P., Grainger D.W. Comparison of hydroxylated print additives on antibody microarray performance. J. Proteome Res. 2006, 5:2956.
    • (2006) J. Proteome Res. , vol.5 , pp. 2956
    • Wu, P.1    Grainger, D.W.2
  • 41
    • 84870703991 scopus 로고    scopus 로고
    • Influenza virus neuraminidases with reduced enzymatic activity that avidly bind sialic acid receptors
    • Zhu X., McBride R., Nycholat C.M., Yu W., Paulson J.C., Wilson I.A. Influenza virus neuraminidases with reduced enzymatic activity that avidly bind sialic acid receptors. J. Virol. 2012, 86:13371.
    • (2012) J. Virol. , vol.86 , pp. 13371
    • Zhu, X.1    McBride, R.2    Nycholat, C.M.3    Yu, W.4    Paulson, J.C.5    Wilson, I.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.