메뉴 건너뛰기




Volumn 12, Issue 12, 2013, Pages 5791-5800

Site-specific glycan-peptide analysis for determination of N-glycoproteome heterogeneity

Author keywords

glycomics; glycopeptide; glycoproteomics; mass spectrometry; N linked glycosylation

Indexed keywords

GLYCAN; GLYCOPEPTIDASE; GLYCOPEPTIDE; GLYCOPROTEOME; PROTEOME; UNCLASSIFIED DRUG;

EID: 84890104706     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr400783j     Document Type: Article
Times cited : (143)

References (60)
  • 1
    • 0009755702 scopus 로고
    • Carbohydrates in protein. 3 the preparation and some of the properties of a glycopeptide from hen's-egg albumin
    • Johansen, P. G.; Marshall, R. D.; Neuberger, A. Carbohydrates in protein. 3 The preparation and some of the properties of a glycopeptide from hen's-egg albumin Biochem. J. 1961, 78, 518-27
    • (1961) Biochem. J. , vol.78 , pp. 518-527
    • Johansen, P.G.1    Marshall, R.D.2    Neuberger, A.3
  • 2
    • 0019934863 scopus 로고
    • Structural and numerical variations of the carbohydrate moiety of immunoglobulin G
    • Mizuochi, T.; Taniguchi, T.; Shimizu, A.; Kobata, A. Structural and numerical variations of the carbohydrate moiety of immunoglobulin G J. Immunol. 1982, 129 (5) 2016-20
    • (1982) J. Immunol. , vol.129 , Issue.5 , pp. 2016-2020
    • Mizuochi, T.1    Taniguchi, T.2    Shimizu, A.3    Kobata, A.4
  • 3
    • 0023092177 scopus 로고
    • Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G
    • Takahashi, N.; Ishii, I.; Ishihara, H.; Mori, M.; Tejima, S.; Jefferis, R.; Endo, S.; Arata, Y. Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G Biochemistry 1987, 26 (4) 1137-44
    • (1987) Biochemistry , vol.26 , Issue.4 , pp. 1137-1144
    • Takahashi, N.1    Ishii, I.2    Ishihara, H.3    Mori, M.4    Tejima, S.5    Jefferis, R.6    Endo, S.7    Arata, Y.8
  • 4
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R. L.; Lai, J.; Keck, R.; O'Connell, L. Y.; Hong, K.; Meng, Y. G.; Weikert, S. H.; Presta, L. G. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity J. Biol. Chem. 2002, 277 (30) 26733-40
    • (2002) J. Biol. Chem. , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7    Presta, L.G.8
  • 5
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T.; Nakamura, K.; Yamane, N.; Shoji-Hosaka, E.; Kanda, Y.; Sakurada, M.; Uchida, K.; Anazawa, H.; Satoh, M.; Yamasaki, M.; Hanai, N.; Shitara, K. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity J. Biol. Chem. 2003, 278 (5) 3466-73
    • (2003) J. Biol. Chem. , vol.278 , Issue.5 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 6
    • 0035937424 scopus 로고    scopus 로고
    • Glycosylation, immunity, and autoimmunity
    • Lowe, J. B. Glycosylation, immunity, and autoimmunity Cell 2001, 104 (6) 809-12
    • (2001) Cell , vol.104 , Issue.6 , pp. 809-812
    • Lowe, J.B.1
  • 7
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A.; Aebi, M. Intracellular functions of N-linked glycans Science 2001, 291 (5512) 2364-9
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 10
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: Glycan presentation and protein-fold stability
    • Wormald, M. R.; Dwek, R. A. Glycoproteins: glycan presentation and protein-fold stability Structure 1999, 7 (7) R155-60
    • (1999) Structure , vol.7 , Issue.7 , pp. 155-160
    • Wormald, M.R.1    Dwek, R.A.2
  • 11
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • Jakob, C. A.; Burda, P.; Roth, J.; Aebi, M. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure J. Cell Biol. 1998, 142 (5) 1223-33
    • (1998) J. Cell Biol. , vol.142 , Issue.5 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 12
    • 0035923524 scopus 로고    scopus 로고
    • Fringe modulation of Jagged1-induced Notch signaling requires the action of beta 4galactosyltransferase-1
    • Chen, J.; Moloney, D. J.; Stanley, P. Fringe modulation of Jagged1-induced Notch signaling requires the action of beta 4galactosyltransferase-1 Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (24) 13716-21
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.24 , pp. 13716-13721
    • Chen, J.1    Moloney, D.J.2    Stanley, P.3
  • 13
    • 0035900637 scopus 로고    scopus 로고
    • Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding
    • Moody, A. M.; Chui, D.; Reche, P. A.; Priatel, J. J.; Marth, J. D.; Reinherz, E. L. Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding Cell 2001, 107 (4) 501-12
    • (2001) Cell , vol.107 , Issue.4 , pp. 501-512
    • Moody, A.M.1    Chui, D.2    Reche, P.A.3    Priatel, J.J.4    Marth, J.D.5    Reinherz, E.L.6
  • 15
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H.; Li, X. J.; Martin, D. B.; Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 2003, 21 (6) 660-6
    • (2003) Nat. Biotechnol. , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 16
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F.; Gnad, F.; Wisniewski, J. R.; Mann, M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints Cell 2010, 141 (5) 897-907
    • (2010) Cell , vol.141 , Issue.5 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 20
    • 68149158650 scopus 로고    scopus 로고
    • Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: Involvement of complex-type N-glycans in apical trafficking
    • Morelle, W.; Stechly, L.; Andre, S.; Van Seuningen, I.; Porchet, N.; Gabius, H. J.; Michalski, J. C.; Huet, G. Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking Biol. Chem. 2009, 390 (7) 529-44
    • (2009) Biol. Chem. , vol.390 , Issue.7 , pp. 529-544
    • Morelle, W.1    Stechly, L.2    Andre, S.3    Van Seuningen, I.4    Porchet, N.5    Gabius, H.J.6    Michalski, J.C.7    Huet, G.8
  • 22
    • 80555136756 scopus 로고    scopus 로고
    • Identification of glycan structure alterations on cell membrane proteins in desoxyepothilone B resistant leukemia cells
    • 009001
    • Nakano, M.; Saldanha, R.; Gobel, A.; Kavallaris, M.; Packer, N. H. Identification of glycan structure alterations on cell membrane proteins in desoxyepothilone B resistant leukemia cells Mol. Cell. Proteomics 2011, 10 (11) M111 009001
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.11 , pp. 111
    • Nakano, M.1    Saldanha, R.2    Gobel, A.3    Kavallaris, M.4    Packer, N.H.5
  • 23
    • 76849083068 scopus 로고    scopus 로고
    • Enhanced detection of sialylated and sulfated glycans with negative ion mode nanoliquid chromatography/mass spectrometry at high pH
    • Thomsson, K. A.; Backstrom, M.; Holmen Larsson, J. M.; Hansson, G. C.; Karlsson, H. Enhanced detection of sialylated and sulfated glycans with negative ion mode nanoliquid chromatography/mass spectrometry at high pH Anal. Chem. 2010, 82 (4) 1470-7
    • (2010) Anal. Chem. , vol.82 , Issue.4 , pp. 1470-1477
    • Thomsson, K.A.1    Backstrom, M.2    Holmen Larsson, J.M.3    Hansson, G.C.4    Karlsson, H.5
  • 24
    • 79951561182 scopus 로고    scopus 로고
    • Glycomics analysis of mammalian heparan sulfates modified by the human extracellular sulfatase HSulf2
    • Staples, G. O.; Shi, X.; Zaia, J. Glycomics analysis of mammalian heparan sulfates modified by the human extracellular sulfatase HSulf2 PLoS One 2011, 6 (2) e16689
    • (2011) PLoS One , vol.6 , Issue.2 , pp. 16689
    • Staples, G.O.1    Shi, X.2    Zaia, J.3
  • 25
    • 84862870851 scopus 로고    scopus 로고
    • Mass spectrometric O-glycan analysis after combined O-glycan release by beta-elimination and 1-phenyl-3-methyl-5-pyrazolone labeling
    • Zauner, G.; Koeleman, C. A.; Deelder, A. M.; Wuhrer, M. Mass spectrometric O-glycan analysis after combined O-glycan release by beta-elimination and 1-phenyl-3-methyl-5-pyrazolone labeling Biochim. Biophys. Acta 2012, 1820 (9) 1420-8
    • (2012) Biochim. Biophys. Acta , vol.1820 , Issue.9 , pp. 1420-1428
    • Zauner, G.1    Koeleman, C.A.2    Deelder, A.M.3    Wuhrer, M.4
  • 27
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An, H. J.; Peavy, T. R.; Hedrick, J. L.; Lebrilla, C. B. Determination of N-glycosylation sites and site heterogeneity in glycoproteins Anal. Chem. 2003, 75 (20) 5628-37
    • (2003) Anal. Chem. , vol.75 , Issue.20 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 28
    • 33646159287 scopus 로고    scopus 로고
    • Site-specific glycosylation analysis of the bovine lysosomal alpha-mannosidase
    • Faid, V.; Evjen, G.; Tollersrud, O. K.; Michalski, J. C.; Morelle, W. Site-specific glycosylation analysis of the bovine lysosomal alpha-mannosidase Glycobiology 2006, 16 (5) 440-61
    • (2006) Glycobiology , vol.16 , Issue.5 , pp. 440-461
    • Faid, V.1    Evjen, G.2    Tollersrud, O.K.3    Michalski, J.C.4    Morelle, W.5
  • 29
    • 33645100367 scopus 로고    scopus 로고
    • Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms
    • Kolarich, D.; Weber, A.; Turecek, P. L.; Schwarz, H. P.; Altmann, F. Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms Proteomics 2006, 6 (11) 3369-80
    • (2006) Proteomics , vol.6 , Issue.11 , pp. 3369-3380
    • Kolarich, D.1    Weber, A.2    Turecek, P.L.3    Schwarz, H.P.4    Altmann, F.5
  • 30
    • 66149104552 scopus 로고    scopus 로고
    • Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system
    • Kuzmanov, U.; Jiang, N.; Smith, C. R.; Soosaipillai, A.; Diamandis, E. P. Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system Mol. Cell. Proteomics 2009, 8 (4) 791-8
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.4 , pp. 791-798
    • Kuzmanov, U.1    Jiang, N.2    Smith, C.R.3    Soosaipillai, A.4    Diamandis, E.P.5
  • 32
    • 79951996840 scopus 로고    scopus 로고
    • Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle
    • Yu, T.; Guo, C.; Wang, J.; Hao, P.; Sui, S.; Chen, X.; Zhang, R.; Wang, P.; Yu, G.; Zhang, L.; Dai, Y.; Li, N. Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle Glycobiology 2011, 21 (2) 206-24
    • (2011) Glycobiology , vol.21 , Issue.2 , pp. 206-224
    • Yu, T.1    Guo, C.2    Wang, J.3    Hao, P.4    Sui, S.5    Chen, X.6    Zhang, R.7    Wang, P.8    Yu, G.9    Zhang, L.10    Dai, Y.11    Li, N.12
  • 36
    • 84868029522 scopus 로고    scopus 로고
    • Site-specific glycoproteomics confirms that protein structure dictates formation of N-glycan type, core fucosylation and branching
    • Thaysen-Andersen, M.; Packer, N. H. Site-specific glycoproteomics confirms that protein structure dictates formation of N-glycan type, core fucosylation and branching Glycobiology 2012, 22 (11) 1440-52
    • (2012) Glycobiology , vol.22 , Issue.11 , pp. 1440-1452
    • Thaysen-Andersen, M.1    Packer, N.H.2
  • 37
    • 29244474601 scopus 로고    scopus 로고
    • High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis
    • Uematsu, R.; Furukawa, J.; Nakagawa, H.; Shinohara, Y.; Deguchi, K.; Monde, K.; Nishimura, S. High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis Mol Cell Proteomics 2005, 4 (12) 1977-89
    • (2005) Mol Cell Proteomics , vol.4 , Issue.12 , pp. 1977-1989
    • Uematsu, R.1    Furukawa, J.2    Nakagawa, H.3    Shinohara, Y.4    Deguchi, K.5    Monde, K.6    Nishimura, S.7
  • 38
  • 40
    • 84859862380 scopus 로고    scopus 로고
    • Human urinary glycoproteomics; Attachment site specific analysis of N- and O-linked glycosylations by CID and ECD
    • Halim, A.; Nilsson, J.; Ruetschi, U.; Hesse, C.; Larson, G. Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD Mol. Cell. Proteomics 2012, 11 (4) 013649
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.4 , pp. 013649
    • Halim, A.1    Nilsson, J.2    Ruetschi, U.3    Hesse, C.4    Larson, G.5
  • 41
    • 84863789621 scopus 로고    scopus 로고
    • How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides
    • 016774
    • Darula, Z.; Sherman, J.; Medzihradszky, K. F. How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides Mol. Cell. Proteomics 2012, 11 (7) O111 016774
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.7 , pp. 111
    • Darula, Z.1    Sherman, J.2    Medzihradszky, K.F.3
  • 42
    • 84876009601 scopus 로고    scopus 로고
    • Glycoproteomic analysis of the secretome of human endothelial cells
    • Yin, X.; Bern, M.; Xing, Q.; Ho, J.; Viner, R.; Mayr, M. Glycoproteomic analysis of the secretome of human endothelial cells Mol. Cell. Proteomics 2013, 12 (4) 956-78
    • (2013) Mol. Cell. Proteomics , vol.12 , Issue.4 , pp. 956-978
    • Yin, X.1    Bern, M.2    Xing, Q.3    Ho, J.4    Viner, R.5    Mayr, M.6
  • 44
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N- and O-glycans released from glycoproteins
    • Jensen, P. H.; Karlsson, N. G.; Kolarich, D.; Packer, N. H. Structural analysis of N- and O-glycans released from glycoproteins Nat. Protoc. 2012, 7 (7) 1299-310
    • (2012) Nat. Protoc. , vol.7 , Issue.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3    Packer, N.H.4
  • 45
    • 80054030914 scopus 로고    scopus 로고
    • Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation
    • 009381
    • Hao, P.; Ren, Y.; Alpert, A. J.; Sze, S. K. Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation Mol. Cell. Proteomics 2011, 10 (10) O111 009381
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.10 , pp. 111
    • Hao, P.1    Ren, Y.2    Alpert, A.J.3    Sze, S.K.4
  • 46
    • 84857873715 scopus 로고    scopus 로고
    • Chemical deamidation: A common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses
    • Palmisano, G.; Melo-Braga, M. N.; Engholm-Keller, K.; Parker, B. L.; Larsen, M. R. Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses J. Proteome Res. 2012, 11 (3) 1949-57
    • (2012) J. Proteome Res. , vol.11 , Issue.3 , pp. 1949-1957
    • Palmisano, G.1    Melo-Braga, M.N.2    Engholm-Keller, K.3    Parker, B.L.4    Larsen, M.R.5
  • 47
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall, L.; Canterbury, J. D.; Weston, J.; Noble, W. S.; MacCoss, M. J. Semi-supervised learning for peptide identification from shotgun proteomics datasets Nat. Methods 2007, 4 (11) 923-5
    • (2007) Nat. Methods , vol.4 , Issue.11 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 48
    • 84875521318 scopus 로고    scopus 로고
    • Byonic: Advanced Peptide and protein identification software
    • Wiley: New York, Chapter 13, Unit 13.20.
    • Bern, M.; Kil, Y. J.; Becker, C. Byonic: advanced Peptide and protein identification software. In Current Protocols in Bioinformatics; Wiley: New York, 2012; Chapter 13, Unit 13.20.
    • (2012) Current Protocols in Bioinformatics
    • Bern, M.1    Kil, Y.J.2    Becker, C.3
  • 49
    • 84868336980 scopus 로고    scopus 로고
    • Expert System for Computer Assisted Annotation of MS/MS Spectra
    • Neuhauser, N.; Michalski, A.; Cox, J.; Mann, M. Expert System for Computer Assisted Annotation of MS/MS Spectra Mol Cell Proteomics 2012, 11, 1500-1509
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1500-1509
    • Neuhauser, N.1    Michalski, A.2    Cox, J.3    Mann, M.4
  • 50
    • 78149391462 scopus 로고    scopus 로고
    • H-score, a mass accuracy driven rescoring approach for improved peptide identification in modification rich samples
    • Savitski, M. M.; Mathieson, T.; Becher, I.; Bantscheff, M. H-score, a mass accuracy driven rescoring approach for improved peptide identification in modification rich samples J. Proteome Res. 2010, 9 (11) 5511-6
    • (2010) J. Proteome Res. , vol.9 , Issue.11 , pp. 5511-5516
    • Savitski, M.M.1    Mathieson, T.2    Becher, I.3    Bantscheff, M.4
  • 51
    • 26444539668 scopus 로고    scopus 로고
    • Orthogonality of separation in two-dimensional liquid chromatography
    • Gilar, M.; Olivova, P.; Daly, A. E.; Gebler, J. C. Orthogonality of separation in two-dimensional liquid chromatography Anal. Chem. 2005, 77 (19) 6426-34
    • (2005) Anal. Chem. , vol.77 , Issue.19 , pp. 6426-6434
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 52
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund, P.; Bunkenborg, J.; Elortza, F.; Jensen, O. N.; Roepstorff, P. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation J. Proteome Res. 2004, 3 (3) 556-66
    • (2004) J. Proteome Res. , vol.3 , Issue.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 53
    • 77954203412 scopus 로고    scopus 로고
    • Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics
    • Mysling, S.; Palmisano, G.; Hojrup, P.; Thaysen-Andersen, M. Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics Anal. Chem. 2010, 82 (13) 5598-609
    • (2010) Anal. Chem. , vol.82 , Issue.13 , pp. 5598-5609
    • Mysling, S.1    Palmisano, G.2    Hojrup, P.3    Thaysen-Andersen, M.4
  • 54
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • Scott, N. E.; Parker, B. L.; Connolly, A. M.; Paulech, J.; Edwards, A. V.; Crossett, B.; Falconer, L.; Kolarich, D.; Djordjevic, S. P.; Hojrup, P.; Packer, N. H.; Larsen, M. R.; Cordwell, S. J. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni Mol. Cell. Proteomics 2011, 10 (2) M000031-MCP201
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.2
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.5    Crossett, B.6    Falconer, L.7    Kolarich, D.8    Djordjevic, S.P.9    Hojrup, P.10    Packer, N.H.11    Larsen, M.R.12    Cordwell, S.J.13
  • 55
    • 84874584456 scopus 로고    scopus 로고
    • A proteomics search algorithm specifically designed for high-resolution tandem mass spectra
    • Wenger, C. D.; Coon, J. J. A proteomics search algorithm specifically designed for high-resolution tandem mass spectra J. Proteome Res. 2013, 12 (3) 1377-86
    • (2013) J. Proteome Res. , vol.12 , Issue.3 , pp. 1377-1386
    • Wenger, C.D.1    Coon, J.J.2
  • 56
    • 84869233177 scopus 로고    scopus 로고
    • Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics
    • Peterson, A. C.; Russell, J. D.; Bailey, D. J.; Westphall, M. S.; Coon, J. J. Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics Mol. Cell. Proteomics 2012, 11 (11) 1475-88
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.11 , pp. 1475-1488
    • Peterson, A.C.1    Russell, J.D.2    Bailey, D.J.3    Westphall, M.S.4    Coon, J.J.5
  • 57
    • 33646927292 scopus 로고    scopus 로고
    • Mass spectrometry of proton adducts of fucosylated N-glycans: Fucose transfer between antennae gives rise to misleading fragments
    • Wuhrer, M.; Koeleman, C. A.; Hokke, C. H.; Deelder, A. M. Mass spectrometry of proton adducts of fucosylated N-glycans: fucose transfer between antennae gives rise to misleading fragments Rapid Commun. Mass Spectrom. 2006, 20 (11) 1747-54
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , Issue.11 , pp. 1747-1754
    • Wuhrer, M.1    Koeleman, C.A.2    Hokke, C.H.3    Deelder, A.M.4
  • 58
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1
    • Parekh, R. B.; Tse, A. G.; Dwek, R. A.; Williams, A. F.; Rademacher, T. W. Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1 EMBO J. 1987, 6 (5) 1233-44
    • (1987) EMBO J. , vol.6 , Issue.5 , pp. 1233-1244
    • Parekh, R.B.1    Tse, A.G.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 59
    • 0027295706 scopus 로고
    • Comparative analysis of the N-glycans of rat, mouse and human Thy-1. Site-specific oligosaccharide patterns of neural Thy-1, a member of the immunoglobulin superfamily
    • Williams, A. F.; Parekh, R. B.; Wing, D. R.; Willis, A. C.; Barclay, A. N.; Dalchau, R.; Fabre, J. W.; Dwek, R. A.; Rademacher, T. W. Comparative analysis of the N-glycans of rat, mouse and human Thy-1. Site-specific oligosaccharide patterns of neural Thy-1, a member of the immunoglobulin superfamily Glycobiology 1993, 3 (4) 339-48
    • (1993) Glycobiology , vol.3 , Issue.4 , pp. 339-348
    • Williams, A.F.1    Parekh, R.B.2    Wing, D.R.3    Willis, A.C.4    Barclay, A.N.5    Dalchau, R.6    Fabre, J.W.7    Dwek, R.A.8    Rademacher, T.W.9
  • 60
    • 17444375706 scopus 로고    scopus 로고
    • Complementary structural information from a tryptic N-linked glycopeptide via electron transfer ion/ion reactions and collision-induced dissociation
    • Hogan, J. M.; Pitteri, S. J.; Chrisman, P. A.; McLuckey, S. A. Complementary structural information from a tryptic N-linked glycopeptide via electron transfer ion/ion reactions and collision-induced dissociation J. Proteome Res. 2005, 4 (2) 628-32
    • (2005) J. Proteome Res. , vol.4 , Issue.2 , pp. 628-632
    • Hogan, J.M.1    Pitteri, S.J.2    Chrisman, P.A.3    McLuckey, S.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.