메뉴 건너뛰기




Volumn 15, Issue 7, 2016, Pages 2217-2226

Recent advances in clinical glycoproteomics of immunoglobulins (Igs)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; IMMUNOGLOBULIN A; IMMUNOGLOBULIN E; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; ANTIGEN; GLYCOSYLATED IGA; GLYCOSYLATED IGG; IMMUNOGLOBULIN G;

EID: 84977265438     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.O116.058503     Document Type: Review
Times cited : (50)

References (121)
  • 3
    • 84944684515 scopus 로고    scopus 로고
    • Pathways responsible for human autoantibody and therapeutic intravenous IgG activity in humanized mice
    • Schwab, I., Lux, A., and Nimmerjahn, F. (2015) Pathways responsible for human autoantibody and therapeutic intravenous IgG activity in humanized mice. Cell Rep 13, 610-620
    • (2015) Cell Rep , vol.13 , pp. 610-620
    • Schwab, I.1    Lux, A.2    Nimmerjahn, F.3
  • 4
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., and Dwek, R. A. (2007) The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21-50
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 6
    • 84910647104 scopus 로고    scopus 로고
    • Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
    • Bondt, A., Rombouts, Y., Selman, M. H., Hensbergen, P. J., Reiding, K. R., Hazes, J. M., Dolhain, R. J., and Wuhrer, M. (2014) Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol. Cell. Proteomics 13, 3029-3039
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3029-3039
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.3    Hensbergen, P.J.4    Reiding, K.R.5    Hazes, J.M.6    Dolhain, R.J.7    Wuhrer, M.8
  • 8
    • 0034095724 scopus 로고    scopus 로고
    • Effect of somatic hypermutation on potential N-glycosylation sites in human immuno-globulin heavy chain variable regions
    • Dunn-Walters, D., Boursier, L., and Spencer, J. (2000) Effect of somatic hypermutation on potential N-glycosylation sites in human immuno-globulin heavy chain variable regions. Mol. Immunol. 37, 107-113
    • (2000) Mol. Immunol. , vol.37 , pp. 107-113
    • Dunn-Walters, D.1    Boursier, L.2    Spencer, J.3
  • 11
    • 84961938333 scopus 로고    scopus 로고
    • Fc-receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions
    • DiLillo, D. J., and Ravetch, J. V. (2015) Fc-receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions. Cancer Immunol. Res. 3, 704-713
    • (2015) Cancer Immunol. Res. , vol.3 , pp. 704-713
    • DiLillo, D.J.1    Ravetch, J.V.2
  • 12
    • 78751608551 scopus 로고    scopus 로고
    • The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo
    • Anthony, R. M., and Nimmerjahn, F. (2011) The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo. Curr. Opin. Organ Transplant 16, 7-14
    • (2011) Curr. Opin. Organ Transplant , vol.16 , pp. 7-14
    • Anthony, R.M.1    Nimmerjahn, F.2
  • 13
  • 15
    • 0034017259 scopus 로고    scopus 로고
    • Increased N-linked glycosylation leading to oversialylation of monomeric immunoglobulin A1 from patients with Sjogren's syndrome
    • Basset, C., Durand, V., Jamin, C., Clement, J., Pennec, Y., Youinou, P., Dueymes, M., and Roitt, I. M. (2000) Increased N-linked glycosylation leading to oversialylation of monomeric immunoglobulin A1 from patients with Sjogren's syndrome. Scand. J. Immunol. 51, 300-306
    • (2000) Scand. J. Immunol. , vol.51 , pp. 300-306
    • Basset, C.1    Durand, V.2    Jamin, C.3    Clement, J.4    Pennec, Y.5    Youinou, P.6    Dueymes, M.7    Roitt, I.M.8
  • 20
    • 84885204309 scopus 로고    scopus 로고
    • Association between galactosy-lation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation
    • Bondt, A., Selman, M. H., Deelder, A. M., Hazes, J. M., Willemsen, S. P., Wuhrer, M., and Dolhain, R. J. (2013) Association between galactosy-lation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation. J. Proteome Res. 12, 4522-4531
    • (2013) J. Proteome Res. , vol.12 , pp. 4522-4531
    • Bondt, A.1    Selman, M.H.2    Deelder, A.M.3    Hazes, J.M.4    Willemsen, S.P.5    Wuhrer, M.6    Dolhain, R.J.7
  • 23
    • 84983656017 scopus 로고    scopus 로고
    • Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 2: Mass spectrometric methods
    • Reusch, D., Haberger, M., Falck, D., Peter, B., Maier, B., Gassner, J., Hook, M., Wagner, K., Bonnington, L., Bulau, P., and Wuhrer, M. (2015) Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 2: Mass spectrometric methods. MAbs 7, 732-742
    • (2015) MAbs , vol.7 , pp. 732-742
    • Reusch, D.1    Haberger, M.2    Falck, D.3    Peter, B.4    Maier, B.5    Gassner, J.6    Hook, M.7    Wagner, K.8    Bonnington, L.9    Bulau, P.10    Wuhrer, M.11
  • 25
    • 84977274111 scopus 로고    scopus 로고
    • IMGT® [last updated 20/12/2012; accessed 01/2016]
    • IMGT® (2001) Protein display: Human IGH C-REGIONs [last updated 20/12/2012; accessed 01/2016] http://www.imgt.org/IMGTrepertoire/Proteins/protein/human/IGH/IGHC/Hu-IGHCallgenes.html
    • (2001) Protein Display: Human IGH C-REGIONs
  • 26
    • 84977271558 scopus 로고    scopus 로고
    • UniProt 2003 [last updated 28/08/2016; accessed 01/2016]
    • UniProt 2003 [last updated 28/08/2016; accessed 01/2016] http://uniprot.org
  • 27
    • 84911909440 scopus 로고    scopus 로고
    • Next-generation sequencing and protein mass spectrometry for the comprehensive analysis of human cellular and serum antibody repertoires
    • Lavinder, J. J., Horton, A. P., Georgiou, G., and Ippolito, G. C. (2015) Next-generation sequencing and protein mass spectrometry for the comprehensive analysis of human cellular and serum antibody repertoires. Curr. Opin. Chem. Biol. 24, 112-120
    • (2015) Curr. Opin. Chem. Biol. , vol.24 , pp. 112-120
    • Lavinder, J.J.1    Horton, A.P.2    Georgiou, G.3    Ippolito, G.C.4
  • 29
    • 84939865371 scopus 로고    scopus 로고
    • Linkage-specific sialic acid derivatization for MALDI-TOF-MS profiling of IgG glycopeptides
    • de Haan, N., Reiding, K. R., Haberger, M., Reusch, D., Falck, D., and Wuhrer, M. (2015) Linkage-specific sialic acid derivatization for MALDI-TOF-MS profiling of IgG glycopeptides. Anal. Chem. 87, 8284-8291
    • (2015) Anal. Chem. , vol.87 , pp. 8284-8291
    • De Haan, N.1    Reiding, K.R.2    Haberger, M.3    Reusch, D.4    Falck, D.5    Wuhrer, M.6
  • 34
  • 37
    • 84922464116 scopus 로고    scopus 로고
    • Aberrant serum immunoglobulin G glycosylation in chronic hepatitis B is associated with histological liver damage and reversible by antiviral therapy
    • Ho, C. H., Chien, R. N., Cheng, P. N., Liu, J. H., Liu, C. K., Su, C. S., Wu, I. C., Li, I. C., Tsai, H. W., Wu, S. L., Liu, W. C., Chen, S. H., and Chang, T. T. (2015) Aberrant serum immunoglobulin G glycosylation in chronic hepatitis B is associated with histological liver damage and reversible by antiviral therapy. J. Infect. Dis. 211, 115-124
    • (2015) J. Infect. Dis. , vol.211 , pp. 115-124
    • Ho, C.H.1    Chien, R.N.2    Cheng, P.N.3    Liu, J.H.4    Liu, C.K.5    Su, C.S.6    Wu, I.C.7    Li, I.C.8    Tsai, H.W.9    Wu, S.L.10    Liu, W.C.11    Chen, S.H.12    Chang, T.T.13
  • 43
    • 74049141466 scopus 로고    scopus 로고
    • Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 microm sorbent
    • Ahn, J., Bones, J., Yu, Y. Q., Rudd, P. M., and Gilar, M. (2010) Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 microm sorbent. J. Chro-matogr. B 878, 403-408
    • (2010) J. Chro-matogr. B , vol.878 , pp. 403-408
    • Ahn, J.1    Bones, J.2    Yu, Y.Q.3    Rudd, P.M.4    Gilar, M.5
  • 45
    • 84939865360 scopus 로고    scopus 로고
    • Ultrahigh throughput, ultrafiltration-based n-glycomics platform for ul-traperformance liquid chromatography (ULTRA(3))
    • Stockmann, H., Duke, R. M., Millan Martin, S., and Rudd, P. M. (2015) Ultrahigh throughput, ultrafiltration-based n-glycomics platform for ul-traperformance liquid chromatography (ULTRA(3)). Anal. Chem. 87, 8316-8322
    • (2015) Anal. Chem. , vol.87 , pp. 8316-8322
    • Stockmann, H.1    Duke, R.M.2    Millan Martin, S.3    Rudd, P.M.4
  • 47
    • 0034750593 scopus 로고    scopus 로고
    • DNA sequence variability of IGHG3 alleles associated to the main G3m haplotypes in human populations
    • Dard, P., Lefranc, M. P., Osipova, L., and Sanchez-Mazas, A. (2001) DNA sequence variability of IGHG3 alleles associated to the main G3m haplotypes in human populations. Eur. J. Hum. Genet. 9, 765-772
    • (2001) Eur. J. Hum. Genet. , vol.9 , pp. 765-772
    • Dard, P.1    Lefranc, M.P.2    Osipova, L.3    Sanchez-Mazas, A.4
  • 48
    • 84941057683 scopus 로고    scopus 로고
    • Glycoforms of immunoglobulin G based biopharmaceuticals are differentially cleaved by trypsin due to the glycoform influence on higher-order structure
    • Falck, D., Jansen, B. C., Plomp, R., Reusch, D., Haberger, M., and Wuhrer, M. (2015) Glycoforms of immunoglobulin G based biopharmaceuticals are differentially cleaved by trypsin due to the glycoform influence on higher-order structure. J. Proteome Res. 14, 4019-4028
    • (2015) J. Proteome Res. , vol.14 , pp. 4019-4028
    • Falck, D.1    Jansen, B.C.2    Plomp, R.3    Reusch, D.4    Haberger, M.5    Wuhrer, M.6
  • 49
    • 84905448970 scopus 로고    scopus 로고
    • One-pot synthesis of magnetic colloidal nanocrystal clusters coated with chitosan for selective enrichment of glycopeptides
    • Fang, C., Xiong, Z., Qin, H., Huang, G., Liu, J., Ye, M., Feng, S., and Zou, H. (2014) One-pot synthesis of magnetic colloidal nanocrystal clusters coated with chitosan for selective enrichment of glycopeptides. Anal. Chim. Acta. 841, 99-105
    • (2014) Anal. Chim. Acta. , vol.841 , pp. 99-105
    • Fang, C.1    Xiong, Z.2    Qin, H.3    Huang, G.4    Liu, J.5    Ye, M.6    Feng, S.7    Zou, H.8
  • 50
    • 84899951266 scopus 로고    scopus 로고
    • A dextran-bonded stationary phase for saccharide separation
    • Sheng, Q., Su, X., Li, X., Ke, Y., and Liang, X. (2014) A dextran-bonded stationary phase for saccharide separation. J. Chromatogr. A 1345, 57-67
    • (2014) J. Chromatogr. A , vol.1345 , pp. 57-67
    • Sheng, Q.1    Su, X.2    Li, X.3    Ke, Y.4    Liang, X.5
  • 51
    • 84906708081 scopus 로고    scopus 로고
    • Efficient enrichment of glycopeptides using metal-organic frameworks by hydrophilic interaction chromatography
    • Ji, Y., Xiong, Z., Huang, G., Liu, J., Zhang, Z., Liu, Z., Ou, J., Ye, M., and Zou, H. (2014) Efficient enrichment of glycopeptides using metal-organic frameworks by hydrophilic interaction chromatography. Analyst 139, 4987-4993
    • (2014) Analyst , vol.139 , pp. 4987-4993
    • Ji, Y.1    Xiong, Z.2    Huang, G.3    Liu, J.4    Zhang, Z.5    Liu, Z.6    Ou, J.7    Ye, M.8    Zou, H.9
  • 52
    • 84947732292 scopus 로고    scopus 로고
    • Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing pep-tides
    • Li, S., Wang, L., Zhao, S., Lin, J., Zheng, J., and Lin, Z. (2015) Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing pep-tides. J. Sep. Sci. 38, 3954-3960
    • (2015) J. Sep. Sci. , vol.38 , pp. 3954-3960
    • Li, S.1    Wang, L.2    Zhao, S.3    Lin, J.4    Zheng, J.5    Lin, Z.6
  • 53
    • 84940571582 scopus 로고    scopus 로고
    • Preparation of hydrophilic monolithic capillary column by in situ photo-polymerization of N-vinyl-2-pyrrolidi-none and acrylamide for highly selective and sensitive enrichment of N-linked glycopeptides
    • Jiang, H., Yuan, H., Qu, Y., Liang, Y., Jiang, B., Wu, Q., Deng, N., Liang, Z., Zhang, L., and Zhang, Y. (2016) Preparation of hydrophilic monolithic capillary column by in situ photo-polymerization of N-vinyl-2-pyrrolidi-none and acrylamide for highly selective and sensitive enrichment of N-linked glycopeptides. Talanta 146, 225-230
    • (2016) Talanta , vol.146 , pp. 225-230
    • Jiang, H.1    Yuan, H.2    Qu, Y.3    Liang, Y.4    Jiang, B.5    Wu, Q.6    Deng, N.7    Liang, Z.8    Zhang, L.9    Zhang, Y.10
  • 54
    • 84879462715 scopus 로고    scopus 로고
    • Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides
    • Cao, L., Yu, L., Guo, Z., Li, X., Xue, X., and Liang, X. (2013) Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides. J. Chromatogr. A 1299, 18-24
    • (2013) J. Chromatogr. A , vol.1299 , pp. 18-24
    • Cao, L.1    Yu, L.2    Guo, Z.3    Li, X.4    Xue, X.5    Liang, X.6
  • 55
    • 70349784960 scopus 로고    scopus 로고
    • Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies
    • Wohlgemuth, J., Karas, M., Eichhorn, T., Hendriks, R., and Andrecht, S. (2009) Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies. Anal. Biochem. 395, 178-188
    • (2009) Anal. Biochem. , vol.395 , pp. 178-188
    • Wohlgemuth, J.1    Karas, M.2    Eichhorn, T.3    Hendriks, R.4    Andrecht, S.5
  • 56
    • 79955009170 scopus 로고    scopus 로고
    • A novel zwitterionic HILIC stationary phase based on "thiol-ene" click chemistry between cysteine and vinyl silica
    • Shen, A., Guo, Z., Yu, L., Cao, L., and Liang, X. (2011) A novel zwitterionic HILIC stationary phase based on "thiol-ene" click chemistry between cysteine and vinyl silica. Chem. Commun. 47, 4550-4552
    • (2011) Chem. Commun. , vol.47 , pp. 4550-4552
    • Shen, A.1    Guo, Z.2    Yu, L.3    Cao, L.4    Liang, X.5
  • 57
    • 84891946484 scopus 로고    scopus 로고
    • Synthesis of zwitterionic polymer brushes hybrid silica nanoparticles via controlled polymerization for highly efficient enrichment of glycopeptides
    • Huang, G., Xiong, Z., Qin, H., Zhu, J., Sun, Z., Zhang, Y., Peng, X., ou, J., and Zou, H. (2014) Synthesis of zwitterionic polymer brushes hybrid silica nanoparticles via controlled polymerization for highly efficient enrichment of glycopeptides. Anal. Chim. Acta 809, 61-68
    • (2014) Anal. Chim. Acta , vol.809 , pp. 61-68
    • Huang, G.1    Xiong, Z.2    Qin, H.3    Zhu, J.4    Sun, Z.5    Zhang, Y.6    Peng, X.7    Ou, J.8    Zou, H.9
  • 58
    • 84922797889 scopus 로고    scopus 로고
    • Facile synthesis of zwitterionic polymer-coated core-shell magnetic nanoparticles for highly specific capture of N-linked glycopeptides
    • Chen, Y., Xiong, Z., Zhang, L., Zhao, J., Zhang, Q., Peng, L., Zhang, W., Ye, M., and Zou, H. (2015) Facile synthesis of zwitterionic polymer-coated core-shell magnetic nanoparticles for highly specific capture of N-linked glycopeptides. Nanoscale 7, 3100-3108
    • (2015) Nanoscale , vol.7 , pp. 3100-3108
    • Chen, Y.1    Xiong, Z.2    Zhang, L.3    Zhao, J.4    Zhang, Q.5    Peng, L.6    Zhang, W.7    Ye, M.8    Zou, H.9
  • 59
    • 84925486059 scopus 로고    scopus 로고
    • Applications of multiple reaction monitoring to clinical glycomics
    • Ruhaak, L. R., and Lebrilla, C. B. (2015) Applications of multiple reaction monitoring to clinical glycomics. Chromatographia 78, 335-342
    • (2015) Chromatographia , vol.78 , pp. 335-342
    • Ruhaak, L.R.1    Lebrilla, C.B.2
  • 60
    • 84949034098 scopus 로고    scopus 로고
    • A method for comprehensive glycosite-map-ping and direct quantitation of serum glycoproteins
    • Hong, Q., Ruhaak, L. R., Stroble, C., Parker, E., Huang, J., Maverakis, E., and Lebrilla, C. B. (2015) A method for comprehensive glycosite-map-ping and direct quantitation of serum glycoproteins. J. Proteome Res. 14, 5179-5192
    • (2015) J. Proteome Res. , vol.14 , pp. 5179-5192
    • Hong, Q.1    Ruhaak, L.R.2    Stroble, C.3    Parker, E.4    Huang, J.5    Maverakis, E.6    Lebrilla, C.B.7
  • 61
    • 84884273245 scopus 로고    scopus 로고
    • Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring
    • Hong, Q., Lebrilla, C. B., Miyamoto, S., and Ruhaak, L. R. (2013) Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring. Anal. Chem. 85, 8585-8593
    • (2013) Anal. Chem. , vol.85 , pp. 8585-8593
    • Hong, Q.1    Lebrilla, C.B.2    Miyamoto, S.3    Ruhaak, L.R.4
  • 62
    • 84921535104 scopus 로고    scopus 로고
    • Quan-titative analysis of immunoglobulin subclasses and subclass specific glycosylation by LC-MS-MRM in liver disease
    • Yuan, W., Sanda, M., Wu, J., Koomen, J., and Goldman, R. (2015) Quan-titative analysis of immunoglobulin subclasses and subclass specific glycosylation by LC-MS-MRM in liver disease. J. Proteomics 116, 24-33
    • (2015) J. Proteomics , vol.116 , pp. 24-33
    • Yuan, W.1    Sanda, M.2    Wu, J.3    Koomen, J.4    Goldman, R.5
  • 64
    • 84901800096 scopus 로고    scopus 로고
    • In-depth structural characterization of N-linked glycopeptides using complete derivatiza-tion for carboxyl groups followed by positive-and negative-ion tandem mass spectrometry
    • Nishikaze, T., Kawabata, S., and Tanaka, K. (2014) In-depth structural characterization of N-linked glycopeptides using complete derivatiza-tion for carboxyl groups followed by positive-and negative-ion tandem mass spectrometry. Anal. Chem. 86, 5360-5369
    • (2014) Anal. Chem. , vol.86 , pp. 5360-5369
    • Nishikaze, T.1    Kawabata, S.2    Tanaka, K.3
  • 66
    • 84902814201 scopus 로고    scopus 로고
    • High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification
    • Reiding, K. R., Blank, D., Kuijper, D. M., Deelder, A. M., and Wuhrer, M. (2014) High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification. Anal. Chem. 86, 5784-5793
    • (2014) Anal. Chem. , vol.86 , pp. 5784-5793
    • Reiding, K.R.1    Blank, D.2    Kuijper, D.M.3    Deelder, A.M.4    Wuhrer, M.5
  • 67
    • 77958033642 scopus 로고    scopus 로고
    • Derivatization with 1-pyrenyldiazomethane enhances ionization of glycopeptides but not peptides in matrix-assisted laser desorption/ionization mass spec-trometry
    • Amano, J., Nishikaze, T., Tougasaki, F., Jinmei, H., Sugimoto, I., Sug-awara, S., Fujita, M., Osumi, K., and Mizuno, M. (2010) Derivatization with 1-pyrenyldiazomethane enhances ionization of glycopeptides but not peptides in matrix-assisted laser desorption/ionization mass spec-trometry. Anal. Chem. 82, 8738-8743
    • (2010) Anal. Chem. , vol.82 , pp. 8738-8743
    • Amano, J.1    Nishikaze, T.2    Tougasaki, F.3    Jinmei, H.4    Sugimoto, I.5    Sugawara, S.6    Fujita, M.7    Osumi, K.8    Mizuno, M.9
  • 68
    • 79955629718 scopus 로고    scopus 로고
    • Negative-ion MALDI-MS2 for discrimination of alpha2, 3-and alpha2, 6-sialylation on glycopeptides labeled with a pyrene derivative
    • Nishikaze, T., Nakamura, T., Jinmei, H., and Amano, J. (2011) Negative-ion MALDI-MS2 for discrimination of alpha2, 3-and alpha2, 6-sialylation on glycopeptides labeled with a pyrene derivative. J. Chromatogr. B 879, 1419-1428
    • (2011) J. Chromatogr. B , vol.879 , pp. 1419-1428
    • Nishikaze, T.1    Nakamura, T.2    Jinmei, H.3    Amano, J.4
  • 70
    • 84938750181 scopus 로고    scopus 로고
    • Lysine conjugation properties in human IgGs studied by integrating high-resolution native mass spectrometry and bottom-up proteomics
    • Gautier, V., Boumeester, A. J., Lossl, P., and Heck, A. J. (2015) Lysine conjugation properties in human IgGs studied by integrating high-resolution native mass spectrometry and bottom-up proteomics. Proteom-ics 15, 2756-2765
    • (2015) Proteom-ics , vol.15 , pp. 2756-2765
    • Gautier, V.1    Boumeester, A.J.2    Lossl, P.3    Heck, A.J.4
  • 71
    • 84903756237 scopus 로고    scopus 로고
    • A new tool for monoclonal antibody analysis: Application of IdeS proteol-ysis in IgG domain-specific characterization
    • An, Y., Zhang, Y., Mueller, H. M., Shameem, M., and Chen, X. (2014) A new tool for monoclonal antibody analysis: application of IdeS proteol-ysis in IgG domain-specific characterization. MAbs 6, 879-893
    • (2014) MAbs , vol.6 , pp. 879-893
    • An, Y.1    Zhang, Y.2    Mueller, H.M.3    Shameem, M.4    Chen, X.5
  • 72
    • 84883859087 scopus 로고    scopus 로고
    • Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry
    • Lynaugh, H., Li, H., and Gong, B. (2013) Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry. MAbs 5, 641-645
    • (2013) MAbs , vol.5 , pp. 641-645
    • Lynaugh, H.1    Li, H.2    Gong, B.3
  • 74
    • 84939785399 scopus 로고    scopus 로고
    • Direct identification of rituximab main isoforms and subunit analysis by online selective comprehensive two-dimensional liquid chromatography-mass spectrometry
    • Stoll, D. R., Harmes, D. C., Danforth, J., Wagner, E., Guillarme, D., Fekete, S., and Beck, A. (2015) Direct identification of rituximab main isoforms and subunit analysis by online selective comprehensive two-dimensional liquid chromatography-mass spectrometry. Anal. Chem. 87, 8307-8315
    • (2015) Anal. Chem. , vol.87 , pp. 8307-8315
    • Stoll, D.R.1    Harmes, D.C.2    Danforth, J.3    Wagner, E.4    Guillarme, D.5    Fekete, S.6    Beck, A.7
  • 75
    • 84901816364 scopus 로고    scopus 로고
    • Structural analysis of an intact monoclonal antibody by online electrochemical reduction of disulfide bonds and Fourier transform ion cyclotron resonance mass spectrometry
    • Nicolardi, S., Deelder, A. M., Palmblad, M., and van der Burgt, Y. E. (2014) Structural analysis of an intact monoclonal antibody by online electrochemical reduction of disulfide bonds and Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 86, 5376-5382
    • (2014) Anal. Chem. , vol.86 , pp. 5376-5382
    • Nicolardi, S.1    Deelder, A.M.2    Palmblad, M.3    Van Der Burgt, Y.E.4
  • 76
    • 84897142414 scopus 로고    scopus 로고
    • Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry
    • Rosati, S., Yang, Y., Barendregt, A., and Heck, A. J. (2014) Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry. Nat. Protoc. 9, 967-976
    • (2014) Nat. Protoc. , vol.9 , pp. 967-976
    • Rosati, S.1    Yang, Y.2    Barendregt, A.3    Heck, A.J.4
  • 77
    • 84892367060 scopus 로고    scopus 로고
    • Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies
    • Zhang, H., Cui, W., and Gross, M. L. (2014) Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies. FEBS Lett. 588, 308-317
    • (2014) FEBS Lett. , vol.588 , pp. 308-317
    • Zhang, H.1    Cui, W.2    Gross, M.L.3
  • 78
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis
    • Holland, M., Yagi, H., Takahashi, N., Kato, K., Savage, C. O., Goodall, D. M., and Jefferis, R. (2006) Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis. Biochim. Biophys. Acta 1760, 669-677
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 669-677
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.5    Goodall, D.M.6    Jefferis, R.7
  • 79
    • 77956187222 scopus 로고    scopus 로고
    • Analytical and functional aspects of antibody sialylation
    • Stadlmann, J., Pabst, M., and Altmann, F. (2010) Analytical and functional aspects of antibody sialylation. J. Clin. Immunol. 30, S15-19
    • (2010) J. Clin. Immunol. , vol.30 , pp. S15-19
    • Stadlmann, J.1    Pabst, M.2    Altmann, F.3
  • 85
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: Evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • Raju, T. S., Briggs, J. B., Borge, S. M., and Jones, A. J. (2000) Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 10, 477-486
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 86
    • 84948469789 scopus 로고    scopus 로고
    • Site-specific protein N-and O-glycosylation analysis by a C18-porous graphitized carbon-liquid chromatography-electrospray ionization mass spectrometry approach using pronase treated glycopeptides
    • Stavenhagen, K., Plomp, R., and Wuhrer, M. (2015) Site-specific protein N-and O-glycosylation analysis by a C18-porous graphitized carbon-liquid chromatography-electrospray ionization mass spectrometry approach using pronase treated glycopeptides. Anal. Chem. 87, 11691-11699
    • (2015) Anal. Chem. , vol.87 , pp. 11691-11699
    • Stavenhagen, K.1    Plomp, R.2    Wuhrer, M.3
  • 87
    • 84872593638 scopus 로고    scopus 로고
    • In-gel nonspecific proteolysis for elucidating glycoproteins: A method for targeted protein-specific glycosyla-tion analysis in complex protein mixtures
    • Nwosu, C. C., Huang, J., Aldredge, D. L., Strum, J. S., Hua, S., Seipert, R. R., and Lebrilla, C. B. (2013) In-gel nonspecific proteolysis for elucidating glycoproteins: a method for targeted protein-specific glycosyla-tion analysis in complex protein mixtures. Anal. Chem. 85, 956-963
    • (2013) Anal. Chem. , vol.85 , pp. 956-963
    • Nwosu, C.C.1    Huang, J.2    Aldredge, D.L.3    Strum, J.S.4    Hua, S.5    Seipert, R.R.6    Lebrilla, C.B.7
  • 88
    • 61849103543 scopus 로고    scopus 로고
    • Analytical performance of immobilized pronase for glyco-peptide footprinting and implications for surpassing reductionist glyco-proteomics
    • Dodds, E. D., Seipert, R. R., Clowers, B. H., German, J. B., and Lebrilla, C. B. (2009) Analytical performance of immobilized pronase for glyco-peptide footprinting and implications for surpassing reductionist glyco-proteomics. J. Proteome Res. 8, 502-512
    • (2009) J. Proteome Res. , vol.8 , pp. 502-512
    • Dodds, E.D.1    Seipert, R.R.2    Clowers, B.H.3    German, J.B.4    Lebrilla, C.B.5
  • 96
    • 84926432276 scopus 로고    scopus 로고
    • Skewed Fc glycosylation profiles of anti-proteinase 3 immu-noglobulin G1 autoantibodies from granulomatosis with polyangiitis patients show low levels of bisection, galactosylation, and sialylation
    • Wuhrer, M., Stavenhagen, K., Koeleman, C. A., Selman, M. H., Harper, L., Jacobs, B. C., Savage, C. O., Jefferis, R., Deelder, A. M., and Morgan, M. (2015) Skewed Fc glycosylation profiles of anti-proteinase 3 immu-noglobulin G1 autoantibodies from granulomatosis with polyangiitis patients show low levels of bisection, galactosylation, and sialylation. J. Proteome Res. 14, 1657-1665
    • (2015) J. Proteome Res. , vol.14 , pp. 1657-1665
    • Wuhrer, M.1    Stavenhagen, K.2    Koeleman, C.A.3    Selman, M.H.4    Harper, L.5    Jacobs, B.C.6    Savage, C.O.7    Jefferis, R.8    Deelder, A.M.9    Morgan, M.10
  • 102
    • 84881553777 scopus 로고    scopus 로고
    • Defective immunoglobulin A (IgA) glycosylation and IgA deposits in patients with IgA nephropathy
    • Kolka, R., Valdimarsson, H., Bodvarsson, M., Hardarson, S., and Jonsson, T. (2013) Defective immunoglobulin A (IgA) glycosylation and IgA deposits in patients with IgA nephropathy. APMIS 121, 890-897
    • (2013) APMIS , vol.121 , pp. 890-897
    • Kolka, R.1    Valdimarsson, H.2    Bodvarsson, M.3    Hardarson, S.4    Jonsson, T.5
  • 105
    • 76149084829 scopus 로고    scopus 로고
    • GlycoSpectrumScan: Fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA
    • Deshpande, N., Jensen, P. H., Packer, N. H., and Kolarich, D. (2010) GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA. J. Proteome Res. 9, 1063-1075
    • (2010) J. Proteome Res. , vol.9 , pp. 1063-1075
    • Deshpande, N.1    Jensen, P.H.2    Packer, N.H.3    Kolarich, D.4
  • 106
    • 84886950647 scopus 로고    scopus 로고
    • Elucidating heterogeneity of IgA1 hinge-region O-gly-cosylation by use of MALDI-TOF/TOF mass spectrometry: Role of cys-teine alkylation during sample processing
    • Franc, V., Rehulka, P., Raus, M., Stulik, J., Novak, J., Renfrow, M. B., and Sebela, M. (2013) Elucidating heterogeneity of IgA1 hinge-region O-gly-cosylation by use of MALDI-TOF/TOF mass spectrometry: role of cys-teine alkylation during sample processing. J. Proteomics 92, 299-312
    • (2013) J. Proteomics , vol.92 , pp. 299-312
    • Franc, V.1    Rehulka, P.2    Raus, M.3    Stulik, J.4    Novak, J.5    Renfrow, M.B.6    Sebela, M.7
  • 107
    • 84870510055 scopus 로고    scopus 로고
    • Inhibitory effect of HIV-specific neutralizing IgA on mucosal transmission of HIV in humanized mice
    • Hur, E. M., Patel, S. N., Shimizu, S., Rao, D. S., Gnanapragasam, P. N., An, D. S., Yang, L., and Baltimore, D. (2012) Inhibitory effect of HIV-specific neutralizing IgA on mucosal transmission of HIV in humanized mice. Blood 120, 4571-4582
    • (2012) Blood , vol.120 , pp. 4571-4582
    • Hur, E.M.1    Patel, S.N.2    Shimizu, S.3    Rao, D.S.4    Gnanapragasam, P.N.5    An, D.S.6    Yang, L.7    Baltimore, D.8
  • 108
    • 84871846348 scopus 로고    scopus 로고
    • Impact of IgA constant domain on HIV-1 neutralizing function of monoclonal antibody F425A1g8
    • Yu, X., Duval, M., Lewis, C., Gawron, M. A., Wang, R., Posner, M. R., and Cavacini, L. A. (2013) Impact of IgA constant domain on HIV-1 neutralizing function of monoclonal antibody F425A1g8. J. Immunol. 190, 205-210
    • (2013) J. Immunol. , vol.190 , pp. 205-210
    • Yu, X.1    Duval, M.2    Lewis, C.3    Gawron, M.A.4    Wang, R.5    Posner, M.R.6    Cavacini, L.A.7
  • 110
    • 84867774199 scopus 로고    scopus 로고
    • Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140
    • Pabst, M., Chang, M., Stadlmann, J., and Altmann, F. (2012) Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140. Biol. Chem. 393, 719-730
    • (2012) Biol. Chem. , vol.393 , pp. 719-730
    • Pabst, M.1    Chang, M.2    Stadlmann, J.3    Altmann, F.4
  • 112
    • 0031183917 scopus 로고    scopus 로고
    • Structural requirements for assembly of dimeric IgA probed by site-directed mu-tagenesis of J chain and a cysteine residue of the alpha-chain CH2 domain
    • Krugmann, S., Pleass, R. J., Atkin, J. D., and Woof, J. M. (1997) Structural requirements for assembly of dimeric IgA probed by site-directed mu-tagenesis of J chain and a cysteine residue of the alpha-chain CH2 domain. J. Immunol. 159, 244-249
    • (1997) J. Immunol. , vol.159 , pp. 244-249
    • Krugmann, S.1    Pleass, R.J.2    Atkin, J.D.3    Woof, J.M.4
  • 114
    • 84930438217 scopus 로고    scopus 로고
    • A microarray-matrix-assisted laser desorption/ionization-mass spectrometry approach for site-specific protein N-glycosylation analysis, as demonstrated for human serum immunoglobulin M (IgM)
    • Pabst, M., Kuster, S. K., Wahl, F., Krismer, J., Dittrich, P. S., and Zenobi, R. (2015) A microarray-matrix-assisted laser desorption/ionization-mass spectrometry approach for site-specific protein N-glycosylation analysis, as demonstrated for human serum immunoglobulin M (IgM). Mol. Cell. Proteomics 14, 1645-1656
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1645-1656
    • Pabst, M.1    Kuster, S.K.2    Wahl, F.3    Krismer, J.4    Dittrich, P.S.5    Zenobi, R.6
  • 119
    • 0014192793 scopus 로고
    • Raised levels of a new immunoglobulin class (IgND) in asthma
    • Johansson, S. G. (1967) Raised levels of a new immunoglobulin class (IgND) in asthma. Lancet 2, 951-953
    • (1967) Lancet , vol.2 , pp. 951-953
    • Johansson, S.G.1
  • 120
    • 0025969722 scopus 로고
    • Frequency analysis of IgE-secreting B lymphocytes in persons with normal or elevated serum IgE levels
    • King, C. L., Poindexter, R. W., Ragunathan, J., Fleisher, T. A., Ottesen, E. A., and Nutman, T. B. (1991) Frequency analysis of IgE-secreting B lymphocytes in persons with normal or elevated serum IgE levels. J. Immunol. 146, 1478-1483
    • (1991) J. Immunol. , vol.146 , pp. 1478-1483
    • King, C.L.1    Poindexter, R.W.2    Ragunathan, J.3    Fleisher, T.A.4    Ottesen, E.A.5    Nutman, T.B.6
  • 121
    • 0018199718 scopus 로고
    • Structure-function relation-ships in human immunoglobulin e
    • Dorrington, K. J., and Bennich, H. H. (1978) Structure-function relation-ships in human immunoglobulin E. Immunol. Rev. 41, 3-25
    • (1978) Immunol. Rev. , vol.41 , pp. 3-25
    • Dorrington, K.J.1    Bennich, H.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.