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Volumn 2, Issue 5, 2005, Pages 745-756

Determination of protein-derived epitopes by mass spectrometry

Author keywords

Chemical modification; Conformational; Discontinuous; Epitope extraction and excision; ESI MS; H D exchange; Immunosorption; Limited proteolysis; MALDI MS

Indexed keywords

AMINO ACID; ANTIGEN; DEUTERIUM; EPITOPE; HYDROGEN;

EID: 27144541763     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.2.5.745     Document Type: Review
Times cited : (69)

References (75)
  • 1
    • 0024438708 scopus 로고
    • Electrospray ionization for mass-spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass-spectrometry of large biomolecules. Science 246(4926), 64-71 (1989).
    • (1989) Science , vol.246 , Issue.4926 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 2
    • 0042318496 scopus 로고    scopus 로고
    • The origin of macromolecule ionization by laser irradiation (Nobel lecture)
    • Tanaka K. The origin of macromolecule ionization by laser irradiation (Nobel lecture). Angew Chem. Int. Ed. Engl. 42(33), 3860-3870 (2003).
    • (2003) Angew Chem. Int. Ed. Engl. , vol.42 , Issue.33 , pp. 3860-3870
    • Tanaka, K.1
  • 3
    • 0033533379 scopus 로고    scopus 로고
    • Characterization of the noncovalent complex of human immunodeficiency virus glycoprotein 120 with its cellular receptor CD4 by matrix-assisted laser desorption/ionization mass spectrometry
    • Borchers C, Tomer KB. Characterization of the noncovalent complex of human immunodeficiency virus glycoprotein 120 with its cellular receptor CD4 by matrix-assisted laser desorption/ionization mass spectrometry. Biochemistry 38(36), 11734-11740 (1999).
    • (1999) Biochemistry , vol.38 , Issue.36 , pp. 11734-11740
    • Borchers, C.1    Tomer, K.B.2
  • 4
    • 0034477744 scopus 로고    scopus 로고
    • Preservation and detection of specific antibody-peptide complexes by matrix-assisted laser desorption ionization mass spectrometry
    • Kiselar JG, Downard KM. Preservation and detection of specific antibody-peptide complexes by matrix-assisted laser desorption ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 11(8), 746-750 (2000).
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , Issue.8 , pp. 746-750
    • Kiselar, J.G.1    Downard, K.M.2
  • 5
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: A technology for studying noncovalent macromolecular complexes
    • Loo JA. Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes. Int. J. Mass Spectrom. 200(1-3), 175-186 (2000).
    • (2000) Int. J. Mass Spectrom. , vol.200 , Issue.1-3 , pp. 175-186
    • Loo, J.A.1
  • 7
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in cho cells
    • Zhu XG, Borchers C, Bienstock RJ, Tomer KB. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in cho cells. Biochemistry 39(37), 11194-11204 (2000).
    • (2000) Biochemistry , vol.39 , Issue.37 , pp. 11194-11204
    • Zhu, X.G.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 8
    • 2642578228 scopus 로고    scopus 로고
    • Immunoproteomics - mass spectrometry-based methods to study the targets of the immune response
    • Purcell AW, Gorman JJ. Immunoproteomics - mass spectrometry-based methods to study the targets of the immune response. Mol. Cell. Proteomics 3(3), 193-208 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.3 , pp. 193-208
    • Purcell, A.W.1    Gorman, J.J.2
  • 9
    • 0037366624 scopus 로고    scopus 로고
    • The use of HPLC-MS in T-cell epitope identification
    • Lemmel C, Stevanovic S. The use of HPLC-MS in T-cell epitope identification. Methods 29(3), 248-259 (2003).
    • (2003) Methods , vol.29 , Issue.3 , pp. 248-259
    • Lemmel, C.1    Stevanovic, S.2
  • 10
    • 0346776078 scopus 로고    scopus 로고
    • Tumor antigens and proteomics from the point of view of the major histocompatibility complex peptides
    • Admon A, Barnea E, Ziv T. Tumor antigens and proteomics from the point of view of the major histocompatibility complex peptides. Mol. Cell. Proteomics 2(6), 388-398 (2003).
    • (2003) Mol. Cell. Proteomics , vol.2 , Issue.6 , pp. 388-398
    • Admon, A.1    Barnea, E.2    Ziv, T.3
  • 11
    • 0036537938 scopus 로고    scopus 로고
    • Electrospray mass spectrometry for the identification of MHC class I-associated peptides expressed on cancer cells
    • Bonner PLR, Lill JR, Hill S, Creaser CS, Rees RC. Electrospray mass spectrometry for the identification of MHC class I-associated peptides expressed on cancer cells. J. Immunol. Methods 262(1-2), 5-19 (2002).
    • (2002) J. Immunol. Methods , vol.262 , Issue.1-2 , pp. 5-19
    • Bonner, P.L.R.1    Lill, J.R.2    Hill, S.3    Creaser, C.S.4    Rees, R.C.5
  • 12
    • 0034100284 scopus 로고    scopus 로고
    • Contributions of mass spectrometry to structural immunology
    • Downard KM. Contributions of mass spectrometry to structural immunology. J. Mass Spectrom. 35(4), 493-503 (2000).
    • (2000) J. Mass Spectrom. , vol.35 , Issue.4 , pp. 493-503
    • Downard, K.M.1
  • 13
    • 0032152437 scopus 로고    scopus 로고
    • Contribution of mass spectrometry to contemporary immunology
    • de Jong A. Contribution of mass spectrometry to contemporary immunology. Mass Spectrom. Rev. 17(5), 311-335 (1998).
    • (1998) Mass Spectrom. Rev. , vol.17 , Issue.5 , pp. 311-335
    • De Jong, A.1
  • 14
    • 0033563266 scopus 로고    scopus 로고
    • Lack of significant differences in association rates and affinities of antibodies from short-term and long-term responses to hen egg lysozyme
    • Goldbaum FA, Cauerhff A, Velikovsky CA, Llera AS, Riottot MM, Poljak RJ. Lack of significant differences in association rates and affinities of antibodies from short-term and long-term responses to hen egg lysozyme. J. Immunol. 162(10), 6040-6045 (1999).
    • (1999) J. Immunol. , vol.162 , Issue.10 , pp. 6040-6045
    • Goldbaum, F.A.1    Cauerhff, A.2    Velikovsky, C.A.3    Llera, A.S.4    Riottot, M.M.5    Poljak, R.J.6
  • 15
    • 0034429848 scopus 로고    scopus 로고
    • Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays
    • Butler JE. Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays. Methods 22(1), 4-23 (2000).
    • (2000) Methods , vol.22 , Issue.1 , pp. 4-23
    • Butler, J.E.1
  • 16
    • 0034431122 scopus 로고    scopus 로고
    • Surface plasmon resonance-based immunoassays
    • Mullett WM, Lai EPC, Yeung JM. Surface plasmon resonance-based immunoassays. Methods 22(1), 77-91 (2000).
    • (2000) Methods , vol.22 , Issue.1 , pp. 77-91
    • Mullett, W.M.1    Lai, E.P.C.2    Yeung, J.M.3
  • 17
    • 0037342411 scopus 로고    scopus 로고
    • Spying on HIV with SPR
    • Rich RL, Myszka DG. Spying on HIV with SPR. Trends Microbiol. 11(3), 124-133 (2003).
    • (2003) Trends Microbiol. , vol.11 , Issue.3 , pp. 124-133
    • Rich, R.L.1    Myszka, D.G.2
  • 18
    • 0034426852 scopus 로고    scopus 로고
    • Experimental design for analysis of complex kinetics using surface plasmon resonance
    • Lipschultz CA, Li YL, Smith-Gill S. Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20(3), 310-318 (2000).
    • (2000) Methods , vol.20 , Issue.3 , pp. 310-318
    • Lipschultz, C.A.1    Li, Y.L.2    Smith-Gill, S.3
  • 19
    • 0030174343 scopus 로고    scopus 로고
    • Epitope mapping by label-free biomolecular interaction analysis
    • Malmqvist M. Epitope mapping by label-free biomolecular interaction analysis. Methods 9(3), 525-532 (1996).
    • (1996) Methods , vol.9 , Issue.3 , pp. 525-532
    • Malmqvist, M.1
  • 20
    • 0346494733 scopus 로고    scopus 로고
    • Epitope identification and discovery using phage display libraries: Applications in vaccine development and diagnostics
    • Wang LF, Yu M. Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics. Curr. Drug Targets 5(1), 1-15 (2004).
    • (2004) Curr. Drug Targets , vol.5 , Issue.1 , pp. 1-15
    • Wang, L.F.1    Yu, M.2
  • 21
    • 0035358814 scopus 로고    scopus 로고
    • Random-peptide libraries and antigen-fragment libraries for epitope mapping and the development of vaccines and diagnostics
    • Irving MB, Pan O, Scott JK. Random-peptide libraries and antigen-fragment libraries for epitope mapping and the development of vaccines and diagnostics. Curr. Opin. Chem. Biol. 5(3), 314-324 (2001).
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , Issue.3 , pp. 314-324
    • Irving, M.B.1    Pan, O.2    Scott, J.K.3
  • 22
    • 11144227042 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1
    • Zwick MB, Jensen R, Church S et al. Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1 J. Virol. 79(2), 1252-1261 (2005).
    • (2005) J. Virol. , vol.79 , Issue.2 , pp. 1252-1261
    • Zwick, M.B.1    Jensen, R.2    Church, S.3
  • 23
    • 18344385532 scopus 로고    scopus 로고
    • NMR spectroscopy and protein structure determination: Applications to drug discovery and development
    • Wishart D. NMR spectroscopy and protein structure determination: applications to drug discovery and development. Curr. Pharm. Biotechnol. 6(2), 105-120 (2005).
    • (2005) Curr. Pharm. Biotechnol. , vol.6 , Issue.2 , pp. 105-120
    • Wishart, D.1
  • 24
    • 20044390069 scopus 로고    scopus 로고
    • Recent developments in structural proteomics for protein structure determination
    • Liu HL, Hsu JP. Recent developments in structural proteomics for protein structure determination. Proteomics 5(8), 2056-2068 (2005). Excellent review of structural analysis of proteins by nuclear magnetic resonance, x-ray crystallography and computer modeling for proteomics studies.
    • (2005) Proteomics , vol.5 , Issue.8 , pp. 2056-2068
    • Liu, H.L.1    Hsu, J.P.2
  • 25
    • 11844260128 scopus 로고    scopus 로고
    • Life in the fast lane for protein crystallization and x-ray crystallography
    • Pusey ML, Liu ZJ, Tempel W et al. Life in the fast lane for protein crystallization and x-ray crystallography. Prog. Biophys. Mol. Biol. 88(3), 359-386 (2005).
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , Issue.3 , pp. 359-386
    • Pusey, M.L.1    Liu, Z.J.2    Tempel, W.3
  • 26
    • 7644220670 scopus 로고    scopus 로고
    • Physical methods for structure, dynamics and binding in immunological research
    • Morikis D, Lambris JD. Physical methods for structure, dynamics and binding in immunological research. Trends Immunol. 25(12), 700-707 (2004).
    • (2004) Trends Immunol. , vol.25 , Issue.12 , pp. 700-707
    • Morikis, D.1    Lambris, J.D.2
  • 27
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • Hunte C, Michel H. Crystallisation of membrane proteins mediated by antibody fragments. Curr. Opin. Struct. Biol. 12(4), 503-508 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , Issue.4 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 28
    • 0029646090 scopus 로고
    • The use of antibody fragments for crystallization and structure determinations
    • Kovari LC, Momany C, Rossmann MG. The use of antibody fragments for crystallization and structure determinations. Structure 3(12), 1291-1293 (1995).
    • (1995) Structure , vol.3 , Issue.12 , pp. 1291-1293
    • Kovari, L.C.1    Momany, C.2    Rossmann, M.G.3
  • 29
    • 3543072396 scopus 로고    scopus 로고
    • 'Affinity-proteomics': Direct protein identification from biological material using mass spectrometric epitope mapping
    • Macht M, Marquardt A, Deininger SO, Damoc E, Kohlmann M, Przybylski M. 'Affinity-proteomics': direct protein identification from biological material using mass spectrometric epitope mapping. Anal. Bioanal. Chem. 378(4), 1102-1111 (2004). Affinity isolation of proteins from a cell lysate that have a 'joint epitope motif' in combination with mass spectrometry (MS) analysis for targeted proteomics.
    • (2004) Anal. Bioanal. Chem. , vol.378 , Issue.4 , pp. 1102-1111
    • Macht, M.1    Marquardt, A.2    Deininger, S.O.3    Damoc, E.4    Kohlmann, M.5    Przybylski, M.6
  • 30
  • 31
    • 0033867592 scopus 로고    scopus 로고
    • With the benefit of hindsight
    • Milstein C. With the benefit of hindsight. Immunol. Today 21(8), 359-364 (2000).
    • (2000) Immunol. Today , vol.21 , Issue.8 , pp. 359-364
    • Milstein, C.1
  • 33
    • 0021042615 scopus 로고
    • On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB-c mice
    • Parham P. On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB-c mice. J. Immunol. 131(6), 2895-2902 (1983).
    • (1983) J. Immunol. , vol.131 , Issue.6 , pp. 2895-2902
    • Parham, P.1
  • 34
    • 0022497692 scopus 로고
    • Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes
    • Jemmerson R, Paterson Y. Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes. Science 232(4753), 1001-1004 (1986).
    • (1986) Science , vol.232 , Issue.4753 , pp. 1001-1004
    • Jemmerson, R.1    Paterson, Y.2
  • 35
    • 0025630449 scopus 로고
    • Molecular epitope identification by limited proteolysis of an immobilized antigen-antibody complex and mass spectrometric peptide mapping
    • Suckau D, Kohl J, Karwath G et al. Molecular epitope identification by limited proteolysis of an immobilized antigen-antibody complex and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. USA 87(24), 9848-9852 (1990). First report of epitope excision in conjunction with MS analysis using fast atom bombardment MS and plasma desorption MS.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.24 , pp. 9848-9852
    • Suckau, D.1    Kohl, J.2    Karwath, G.3
  • 36
    • 0034129705 scopus 로고    scopus 로고
    • Characterization of an anti-Borrelia burgdorferi OspA conformational epitope by limited proteolysis of monoclonal antibody-bound antigen and mass spectrometric peptide mapping
    • Legros V, Jolivet-Reynaud C, Battail-Poirot N, Saint-Pierre C, Forest E. Characterization of an anti-Borrelia burgdorferi OspA conformational epitope by limited proteolysis of monoclonal antibody-bound antigen and mass spectrometric peptide mapping. Protein Sci. 9(5), 1002-1010 (2000).
    • (2000) Protein Sci. , vol.9 , Issue.5 , pp. 1002-1010
    • Legros, V.1    Jolivet-Reynaud, C.2    Battail-Poirot, N.3    Saint-Pierre, C.4    Forest, E.5
  • 38
    • 0033135224 scopus 로고    scopus 로고
    • Direct identification of protein epitopes by mass spectrometry without immobilization of antibody and isolation of antibody-peptide complexes
    • Kiselar JG, Downard KM. Direct identification of protein epitopes by mass spectrometry without immobilization of antibody and isolation of antibody-peptide complexes. Anal. Chem. 71(9), 1792-1801 (1999).
    • (1999) Anal. Chem. , vol.71 , Issue.9 , pp. 1792-1801
    • Kiselar, J.G.1    Downard, K.M.2
  • 39
    • 0036852750 scopus 로고    scopus 로고
    • Therapeutically effective antibodies against amyloid-β peptide target amyloid-β residues 4-10 and inhibit cytotoxicity and fibrillogenesis
    • McLaurin J, Cecal R, Kierstead ME et al. Therapeutically effective antibodies against amyloid-β peptide target amyloid-β residues 4-10 and inhibit cytotoxicity and fibrillogenesis. Nature Med. 8(11), 1263-1269 (2002).
    • (2002) Nature Med. , vol.8 , Issue.11 , pp. 1263-1269
    • McLaurin, J.1    Cecal, R.2    Kierstead, M.E.3
  • 40
    • 0000399445 scopus 로고
    • Direct analysis of affinity-bound analytes by MALDI/TOF MS
    • Papac DI, Hoyes J, Tomer KB. Direct analysis of affinity-bound analytes by MALDI/TOF MS. Anal. Chem. 66(17), 2609-2613 (1994).
    • (1994) Anal. Chem. , vol.66 , Issue.17 , pp. 2609-2613
    • Papac, D.I.1    Hoyes, J.2    Tomer, K.B.3
  • 41
    • 0028004403 scopus 로고
    • Epitope mapping of the gastrin-releasing peptide antibombesin monoclonal-antibody complex by proteolysis followed by matrix-assisted laser-desorption ionization mass-spectrometry
    • Papac DI, Hoyes J, Tomer KB. Epitope mapping of the gastrin-releasing peptide antibombesin monoclonal-antibody complex by proteolysis followed by matrix-assisted laser-desorption ionization mass-spectrometry. Protein Sci. 3(9), 1485-1492 (1994).
    • (1994) Protein Sci. , vol.3 , Issue.9 , pp. 1485-1492
    • Papac, D.I.1    Hoyes, J.2    Tomer, K.B.3
  • 42
    • 0032231990 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization mass spectrometry mapping of human immunodeficiency virus-gp120 epitopes recognized by a limited polyclonal antibody
    • Jeyarajah S, Parker CE, Sumner MT, Tomer KB. Matrix-assisted laser desorption ionization mass spectrometry mapping of human immunodeficiency virus-gp120 epitopes recognized by a limited polyclonal antibody. J. Am. Soc. Mass Spectrom. 9(2), 157-165 (1998).
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , Issue.2 , pp. 157-165
    • Jeyarajah, S.1    Parker, C.E.2    Sumner, M.T.3    Tomer, K.B.4
  • 43
    • 0029898211 scopus 로고    scopus 로고
    • Epitope mapping by mass spectrometry - Determination of an epitope on HIV-1(IIIb) p26 recognized by a monoclonal antibody
    • Parker CE, Papac DI, Trojak SK, Tomer KB. Epitope mapping by mass spectrometry - determination of an epitope on HIV-1(IIIb) p26 recognized by a monoclonal antibody. J. Immunol. 157(1), 198-206 (1996).
    • (1996) J. Immunol. , vol.157 , Issue.1 , pp. 198-206
    • Parker, C.E.1    Papac, D.I.2    Trojak, S.K.3    Tomer, K.B.4
  • 44
    • 0035880528 scopus 로고    scopus 로고
    • A general strategy for epitope mapping by direct MALDI-TOF mass spectrometry using secondary antibodies and cross-linking
    • Peter JF, Tomer KB. A general strategy for epitope mapping by direct MALDI-TOF mass spectrometry using secondary antibodies and cross-linking. Anal. Chem. 73(16), 4012-4019 (2001). Development of indirect immunosorption for selective enrichment and oriented exposure of an antibody of interest for epitope mapping.
    • (2001) Anal. Chem. , vol.73 , Issue.16 , pp. 4012-4019
    • Peter, J.F.1    Tomer, K.B.2
  • 45
    • 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 CE, Deterding LJ, Hager-Braun C et al. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus Type 1 for the neutralizing monoclonal antibody 2f5. J. Virol. 75(22), 10906-10911 (2001).
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 10906-10911
    • Parker, C.E.1    Deterding, L.J.2    Hager-Braun, C.3
  • 46
    • 0034467604 scopus 로고    scopus 로고
    • Mapping epitopes of monoclonal antibodies against HIV-1 integrase with limited proteolysis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • Yi J, Skalka AM. Mapping epitopes of monoclonal antibodies against HIV-1 integrase with limited proteolysis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Biopolymers 55(4), 308-318 (2000).
    • (2000) Biopolymers , vol.55 , Issue.4 , pp. 308-318
    • Yi, J.1    Skalka, A.M.2
  • 47
    • 0034655261 scopus 로고    scopus 로고
    • Mass spectrometric characterization of a discontinuous epitope of the HIV envelope protein HIV-gp120 recognized by the human monoclonal antibody 1331A
    • Hochleitner EO, Gorny MK, Zolla-Pazner S, Tomer KB. Mass spectrometric characterization of a discontinuous epitope of the HIV envelope protein HIV-gp120 recognized by the human monoclonal antibody 1331A. J. Immunol. 164(8), 4156-4161 (2000).
    • (2000) J. Immunol. , vol.164 , Issue.8 , pp. 4156-4161
    • Hochleitner, E.O.1    Gorny, M.K.2    Zolla-Pazner, S.3    Tomer, K.B.4
  • 48
    • 0029731189 scopus 로고    scopus 로고
    • Mass spectrometric mapping of protein epitope structures of myocardial infarct markers myoglobin and troponin T
    • Macht M, Fiedler W, Kurzinger K, Przybylski M. Mass spectrometric mapping of protein epitope structures of myocardial infarct markers myoglobin and troponin T. Biochemistry 35(49), 15633-15639 (1996).
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15633-15639
    • Macht, M.1    Fiedler, W.2    Kurzinger, K.3    Przybylski, M.4
  • 49
    • 0028541590 scopus 로고
    • Protein epitope mapping by mass-spectrometry
    • Zhao YM, Chait BT. Protein epitope mapping by mass-spectrometry. Anal. Chem. 66(21), 3723-3726 (1994).
    • (1994) Anal. Chem. , vol.66 , Issue.21 , pp. 3723-3726
    • Zhao, Y.M.1    Chait, B.T.2
  • 50
    • 1842863941 scopus 로고    scopus 로고
    • Determination of epitopes by mass spectrometry
    • Hager-Braun C, Tomer KB. Determination of epitopes by mass spectrometry. Methods Mol. Med. 94, 109-120 (2004). Step-by-step protocol for the immobilization of antibodies for indirect immunosorption, epitope excision and epitope fine definition by matrix-assisted laser desorption/ionization MS.
    • (2004) Methods Mol. Med. , vol.94 , pp. 109-120
    • Hager-Braun, C.1    Tomer, K.B.2
  • 51
    • 0023153676 scopus 로고
    • Epitope mapping by chemical modification of free and antibody-bound protein antigen
    • Burnens A, Demotz S, Corradin G, Binz H, Bosshard HR. Epitope mapping by chemical modification of free and antibody-bound protein antigen. Science 235(4790), 780-783 (1987).
    • (1987) Science , vol.235 , Issue.4790 , pp. 780-783
    • Burnens, A.1    Demotz, S.2    Corradin, G.3    Binz, H.4    Bosshard, H.R.5
  • 52
    • 0028183497 scopus 로고
    • Molecular characterization of surface-topology in protein tertiary structures by amino-acylation and mass-spectrometric peptide-mapping
    • Glocker MO, Borchers C, Fiedler W, Suckau D, Przybylski M. Molecular characterization of surface-topology in protein tertiary structures by amino-acylation and mass-spectrometric peptide-mapping. Bioconjug. Chem. 5(6), 583-590 (1994).
    • (1994) Bioconjug. Chem. , vol.5 , Issue.6 , pp. 583-590
    • Glocker, M.O.1    Borchers, C.2    Fiedler, W.3    Suckau, D.4    Przybylski, M.5
  • 53
    • 0032584106 scopus 로고    scopus 로고
    • Creatine kinase: Essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry
    • Wood TD, Guan ZQ, Borders CL, Chen LH, Kenyon GL, McLafferty FW. Creatine kinase: essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry. Proc. Natl Acad. Sci. USA 95(7), 3362-3365 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.7 , pp. 3362-3365
    • Wood, T.D.1    Guan, Z.Q.2    Borders, C.L.3    Chen, L.H.4    Kenyon, G.L.5    McLafferty, F.W.6
  • 54
    • 0025879057 scopus 로고
    • A mass-spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system
    • Steiner RF, Albaugh S, Fenselau C, Murphy C, Vestling M. A mass-spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system. Anal. Biochem. 196(1), 120-125 (1991).
    • (1991) Anal. Biochem. , vol.196 , Issue.1 , pp. 120-125
    • Steiner, R.F.1    Albaugh, S.2    Fenselau, C.3    Murphy, C.4    Vestling, M.5
  • 55
    • 0037065723 scopus 로고    scopus 로고
    • Characterization of the tertiary structure of soluble CD4 bound to glycosylated full-length HIVgp120 by chemical modification of arginine residues and mass spectrometric analysis
    • Hager-Braun C, Tomer KB. Characterization of the tertiary structure of soluble CD4 bound to glycosylated full-length HIVgp120 by chemical modification of arginine residues and mass spectrometric analysis. Biochemistry 41(6), 1759-1766 (2002).
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1759-1766
    • Hager-Braun, C.1    Tomer, K.B.2
  • 56
    • 4644231769 scopus 로고    scopus 로고
    • Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry
    • Strohalm M, Santrucek J, Hynek R, Kodicek M. Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry. Biochem. Biophys. Res. Commun. 323(4), 1134-1138 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , Issue.4 , pp. 1134-1138
    • Strohalm, M.1    Santrucek, J.2    Hynek, R.3    Kodicek, M.4
  • 58
    • 0141922884 scopus 로고    scopus 로고
    • Chemical modification of carboxylic residues in a cyclodextrin glucanotransferase and its implication in the hydrolysis/transglycosylation ratio of the α-amylase family
    • Alcalde M, Plou FJ, Perez-Boada M et al. Chemical modification of carboxylic residues in a cyclodextrin glucanotransferase and its implication in the hydrolysis/transglycosylation ratio of the α-amylase family. J. Mol. Catal. B Enzym. 26(1-2), 57-67 (2003).
    • (2003) J. Mol. Catal. B Enzym. , vol.26 , Issue.1-2 , pp. 57-67
    • Alcalde, M.1    Plou, F.J.2    Perez-Boada, M.3
  • 59
    • 0034067250 scopus 로고    scopus 로고
    • Characterization of a discontinuous epitope of the human immunodeficiency virus (HIV) core protein p24 by epitope excision and differential chemical modification followed by mass spectrometric peptide mapping analysis
    • Hochleitner EO, Borchers C, Parker C, Bienstock RJ, Tomer KB. Characterization of a discontinuous epitope of the human immunodeficiency virus (HIV) core protein p24 by epitope excision and differential chemical modification followed by mass spectrometric peptide mapping analysis. Protein Sci. 9(3), 487-496 (2000).
    • (2000) Protein Sci. , vol.9 , Issue.3 , pp. 487-496
    • Hochleitner, E.O.1    Borchers, C.2    Parker, C.3    Bienstock, R.J.4    Tomer, K.B.5
  • 60
    • 0032032551 scopus 로고    scopus 로고
    • Molecular characterization of a conformational epitope of hen egg white lysozyme by differential chemical modification of immune complexes and mass spectrometric peptide mapping
    • Fiedler W, Borchers C, Macht M, Deininger SO, Przybylski M. Molecular characterization of a conformational epitope of hen egg white lysozyme by differential chemical modification of immune complexes and mass spectrometric peptide mapping. Bioconjug. Chem. 9(2), 236-241 (1998).
    • (1998) Bioconjug. Chem. , vol.9 , Issue.2 , pp. 236-241
    • Fiedler, W.1    Borchers, C.2    Macht, M.3    Deininger, S.O.4    Przybylski, M.5
  • 61
    • 1842868694 scopus 로고    scopus 로고
    • Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes
    • Yan XG, Watson J, Ho PS, Deinzer ML. Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes. Mol. Cell. Proteomics 3(1), 10-23 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.1 , pp. 10-23
    • Yan, X.G.1    Watson, J.2    Ho, P.S.3    Deinzer, M.L.4
  • 62
    • 0031912073 scopus 로고    scopus 로고
    • Determinants of protein hydrogen exchange studied in equine cytochrome c
    • Milne JS, Mayne L, Roder H, Wand AJ, Englander SW. Determinants of protein hydrogen exchange studied in equine cytochrome c. Protein Sci. 7(3), 739-745 (1998).
    • (1998) Protein Sci. , vol.7 , Issue.3 , pp. 739-745
    • Milne, J.S.1    Mayne, L.2    Roder, H.3    Wand, A.J.4    Englander, S.W.5
  • 63
    • 9744270012 scopus 로고    scopus 로고
    • Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry
    • Busenlehner LS, Armstrong RN. Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry. Arch. Biochem. Biophys. 433(1), 34-46 (2005).
    • (2005) Arch. Biochem. Biophys. , vol.433 , Issue.1 , pp. 34-46
    • Busenlehner, L.S.1    Armstrong, R.N.2
  • 65
    • 0036007555 scopus 로고    scopus 로고
    • Identification of the interface of a large protein-protein complex using H/D exchange and fourier transform ion cyclotron resonance mass spectrometry
    • Yamada N, Suzuki E, Hirayama K. Identification of the interface of a large protein-protein complex using H/D exchange and fourier transform ion cyclotron resonance mass spectrometry. Rapid Comm. Mass Spectrom. 16(4), 293-299 (2002).
    • (2002) Rapid Comm. Mass Spectrom. , vol.16 , Issue.4 , pp. 293-299
    • Yamada, N.1    Suzuki, E.2    Hirayama, K.3
  • 66
    • 0033557450 scopus 로고    scopus 로고
    • Hydrogen exchange electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions
    • Ehring H. Hydrogen exchange electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions. Anal. Biochem. 267(2), 252-259 (1999).
    • (1999) Anal. Biochem. , vol.267 , Issue.2 , pp. 252-259
    • Ehring, H.1
  • 67
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • Baerga-Ortiz A, Hughes CA, Mandell JG, Komives EA. Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci. 11(6), 1300-1308 (2002).
    • (2002) Protein Sci. , vol.11 , Issue.6 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C.A.2    Mandell, J.G.3    Komives, E.A.4
  • 68
    • 17844396912 scopus 로고    scopus 로고
    • Antibody-based proteomics for human tissue profiling
    • Uhlen M, Ponten F. Antibody-based proteomics for human tissue profiling. Mol. Cell. Proteomics 4(4), 384-393 (2005).
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.4 , pp. 384-393
    • Uhlen, M.1    Ponten, F.2
  • 70
  • 71
    • 0037350545 scopus 로고    scopus 로고
    • Immunotherapy: Past, present and future
    • Waldmann TA. Immunotherapy: past, present and future. Nature Med. 9(3), 269-277 (2003).
    • (2003) Nature Med. , vol.9 , Issue.3 , pp. 269-277
    • Waldmann, T.A.1
  • 72
    • 0036624291 scopus 로고    scopus 로고
    • Proteomics approaches towards antigen discovery and vaccine development
    • Klade CS. Proteomics approaches towards antigen discovery and vaccine development. Curr. Opin. Mol. Ther. 4(3), 216-223 (2002).
    • (2002) Curr. Opin. Mol. Ther. , vol.4 , Issue.3 , pp. 216-223
    • Klade, C.S.1
  • 73
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the antihuman immunodeficiency virus Type 1 antibody 2f5 in complex with its gp41 epitope
    • Ofek G, Tang M, Sambor A et al. Structure and mechanistic analysis of the antihuman immunodeficiency virus Type 1 antibody 2f5 in complex with its gp41 epitope. J. Virol. 78(19), 10724-10737 (2004).
    • (2004) J. Virol. , vol.78 , Issue.19 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3
  • 74
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing antiHIV antibody 4e10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso RMF, Zwick MB, Stanfield RL et al. Broadly neutralizing antiHIV antibody 4e10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 22(2), 163-173 (2005).
    • (2005) Immunity , vol.22 , Issue.2 , pp. 163-173
    • Cardoso, R.M.F.1    Zwick, M.B.2    Stanfield, R.L.3
  • 75
    • 0034482696 scopus 로고    scopus 로고
    • Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates
    • Kwong PD, Wyatt R, Majeed S et al. Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. Structure 8(12), 1329-1339 (2000).
    • (2000) Structure , vol.8 , Issue.12 , pp. 1329-1339
    • Kwong, P.D.1    Wyatt, R.2    Majeed, S.3


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