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Volumn 8, Issue 4, 2011, Pages 269-277

Recent Mass Spectrometric Based Methods in Quantitative N-linked Glycoproteomics

Author keywords

Glycopeptide capture; Glycopeptides; Glycoprotein enrichment; Glycoproteomics; Lectin affinity chromatography; Mass spectrometry; N linked glycosylation; Quantitation

Indexed keywords

GLYCOPEPTIDE; GLYCOPROTEIN;

EID: 82155171404     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016411798220844     Document Type: Review
Times cited : (4)

References (63)
  • 2
    • 49149129527 scopus 로고    scopus 로고
    • Mass spectrometric analysis of carbohydrate heterogeneity for the characterization of glycoprotein-based products
    • Nana, K.; Satsuki, I.; Noritaka, H.; Akira, H.; Daisuke, T. and Teruhida, Y. Mass spectrometric analysis of carbohydrate heterogeneity for the characterization of glycoprotein-based products. Trends Glycosci. Glycotechnol., 2008, 20(112), 97-116.
    • (2008) Trends Glycosci. Glycotechnol , vol.20 , Issue.112 , pp. 97-116
    • Nana, K.1    Satsuki, I.2    Noritaka, H.3    Akira, H.4    Daisuke, T.5    Teruhida, Y.6
  • 3
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia, J. Mass spectrometry and the emerging field of glycomics. Chem. Biol., 2008, 15(9), 881-892.
    • (2008) Chem. Biol , vol.15 , Issue.9 , pp. 881-892
    • Zaia, J.1
  • 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. The impact of glycosylation on the biological function and structure of human immunoglobulins. Ann. Rev. Immunol., 2007, 25, 21-50.
    • (2007) Ann. 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
  • 5
    • 70349275888 scopus 로고    scopus 로고
    • Mass spectrometry in the analysis of N-linked and O-linked glycans
    • North, S.J.; Hitchen, P.G.; Haslam, S.M. and Dell, A. Mass spectrometry in the analysis of N-linked and O-linked glycans. Curr. Opin. Struct. Biol., 2009, 19(5), 498-506.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , Issue.5 , pp. 498-506
    • North, S.J.1    Hitchen, P.G.2    Haslam, S.M.3    Dell, A.4
  • 7
    • 33845449090 scopus 로고    scopus 로고
    • Global methods for protein glycosylation analysis by mass spectrometry
    • Budnik, B.A.; Lee, R.S. and Steen, J.A.J. Global methods for protein glycosylation analysis by mass spectrometry. Biochim. Biophys. Acta, 2006, 1764(12), 1870-1880.
    • (2006) Biochim. Biophys. Acta , vol.1764 , Issue.12 , pp. 1870-1880
    • Budnik, B.A.1    Lee, R.S.2    Steen, J.A.J.3
  • 8
    • 0035937542 scopus 로고    scopus 로고
    • Glycoprotein structure determination mass spectrometry
    • Dell, A. and Morris, H.R. Glycoprotein structure determination mass spectrometry. Science, 2001, 291(5512), 2351-2356.
    • (2001) Science , vol.291 , Issue.5512 , pp. 2351-2356
    • Dell, A.1    Morris, H.R.2
  • 9
    • 0033135747 scopus 로고    scopus 로고
    • Protein glycosylation in development and disease
    • Dennis, J.W.; Granovsky, M. and Warren, C.E. Protein glycosylation in development and disease. Bio Essays, 1999, 21(5), 412-421.
    • (1999) Bio Essays , vol.21 , Issue.5 , pp. 412-421
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 10
    • 0030866216 scopus 로고    scopus 로고
    • Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and Atypical (Asn-X-Cys) glycosylation motifs
    • Vance, B.A.; Wu, W.; Ribaudo, R.K.; Segal, D.M.; Kearse, K.P. Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and Atypical (Asn-X-Cys) glycosylation motifs. J. Biol. Chem., 1997, 272(37), 23117-23122.
    • (1997) J. Biol. Chem , vol.272 , Issue.37 , pp. 23117-23122
    • Vance, B.A.1    Wu, W.2    Ribaudo, R.K.3    Segal, D.M.4    Kearse, K.P.5
  • 11
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R.G. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology, 2002, 12(4), 43R-56R.
    • (2002) Glycobiology , vol.12 , Issue.4
    • Spiro, R.G.1
  • 12
    • 44249099705 scopus 로고    scopus 로고
    • Glycopeptide analysis by mass spectrometry
    • Dalpathado, D.S. and Desaire, H. Glycopeptide analysis by mass spectrometry. Analyst, 2008, 133(6), 731-738.
    • (2008) Analyst , vol.133 , Issue.6 , pp. 731-738
    • Dalpathado, D.S.1    Desaire, H.2
  • 13
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides - all of the theories are correct
    • Varki, A. Biological roles of oligosaccharides - all of the theories are correct. Glycobiology, 1993, 3(2), 97-130.
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 14
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • Haltiwanger, R.S. and Lowe, J.B. Role of glycosylation in development. Annu. Rev. Biochem., 2004, 73, 491-537.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 15
    • 27744591857 scopus 로고    scopus 로고
    • New hyphenated methodologies in high-sensitivity glycoprotein analysis
    • Novotny, M.V. and Mechref, Y. New hyphenated methodologies in high-sensitivity glycoprotein analysis. J. Sep. Sci., 2005, 28(15), 1956-1968.
    • (2005) J. Sep. Sci , vol.28 , Issue.15 , pp. 1956-1968
    • Novotny, M.V.1    Mechref, Y.2
  • 16
    • 62549163033 scopus 로고    scopus 로고
    • Comparison of N-linked glycoproteins in human whole saliva, parotid, submandibular, and sublingual glandular secretions identified using hydrazide chemistry and mass spectrometry
    • Ramachandran, P.; Boontheung, P.; Pang, E.; Yan, W.; Wong, D.T. and Loo, J.A. Comparison of N-linked glycoproteins in human whole saliva, parotid, submandibular, and sublingual glandular secretions identified using hydrazide chemistry and mass spectrometry. Clin. Proteomics, 2008, 4, 80-104.
    • (2008) Clin. Proteomics , vol.4 , pp. 80-104
    • Ramachandran, P.1    Boontheung, P.2    Pang, E.3    Yan, W.4    Wong, D.T.5    Loo, J.A.6
  • 17
    • 33846488076 scopus 로고    scopus 로고
    • Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics
    • Sun, B.; Ranish, J.A.; Utleg, A.G.; White, J.T.; Yan, X.; Lin, B. and Hood, L. Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics. Mol. Cell. Proteomics, 2007, 6(1), 141-149.
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.1 , pp. 141-149
    • Sun, B.1    Ranish, J.A.2    Utleg, A.G.3    White, J.T.4    Yan, X.5    Lin, B.6    Hood, L.7
  • 18
    • 77949266037 scopus 로고    scopus 로고
    • Carbohydrate analysis throughout the development of a protein therapeutic
    • Higgins, E. Carbohydrate analysis throughout the development of a protein therapeutic. Glycoconjugate J., 2010, 27(2), 211-225.
    • (2010) Glycoconjugate J , vol.27 , Issue.2 , pp. 211-225
    • Higgins, E.1
  • 19
    • 33745932059 scopus 로고    scopus 로고
    • Glycoform characterization of erythropoietin combining glycan and intact protein analysis by capillary electrophoresis electrospray time-of-flight mass spectrometry
    • Balaguer, E.; Demelbauer, U.; Pelzing, M.; Sanz-Nebot, V.; Barbosa, J. and Neusü, C. Glycoform characterization of erythropoietin combining glycan and intact protein analysis by capillary electrophoresis electrospray time-of-flight mass spectrometry. Electrophoresis, 2006. 27(13), 2638-2650.
    • (2006) Electrophoresis , vol.27 , Issue.13 , pp. 2638-2650
    • Balaguer, E.1    Demelbauer, U.2    Pelzing, M.3    Sanz-Nebot, V.4    Barbosa, J.5    Neusü, C.6
  • 22
    • 34948905277 scopus 로고    scopus 로고
    • Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2- nitrobenzensulfenyl (NBS) stable isotope labeling: A new approach for the novel biomarker discovery for cancer
    • Ueda, K.; Katagiri, T.; Shimada, T.; Irie, S.; Sato, T.-A.; Nakamura, Y. and Daigo, Y. Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2- nitrobenzensulfenyl (NBS) stable isotope labeling: a new approach for the novel biomarker discovery for cancer. J. Proteome Res., 2007, 6(9), 3475-3483.
    • (2007) J. Proteome Res , vol.6 , Issue.9 , pp. 3475-3483
    • Ueda, K.1    Katagiri, T.2    Shimada, T.3    Irie, S.4    Sato, T.-A.5    Nakamura, Y.6    Daigo, Y.7
  • 24
    • 38349080026 scopus 로고    scopus 로고
    • N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry
    • Hulsmeier, A.J.; Paesold-Burda, P. and Hennet, T. N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry. Mol. Cell. Proteomics, 2007, 6(12), 2132-2138.
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.12 , pp. 2132-2138
    • Hulsmeier, A.J.1    Paesold-Burda, P.2    Hennet, T.3
  • 25
    • 73649148401 scopus 로고    scopus 로고
    • Tandem 18O stable isotope labeling for quantification of N- glycoproteome
    • Liu, Z.; Cao, J.; He, Y.; Qiao, L.; Xu, C.; Lu, H. and Yang, P. Tandem 18O stable isotope labeling for quantification of N- glycoproteome. J. Proteome Res., 2010, 9(1), 227-236.
    • (2010) J. Proteome Res , vol.9 , Issue.1 , pp. 227-236
    • Liu, Z.1    Cao, J.2    He, Y.3    Qiao, L.4    Xu, C.5    Lu, H.6    Yang, P.7
  • 26
    • 33748294165 scopus 로고    scopus 로고
    • Semiautomated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry
    • Madera, M.; Mechref, Y.; Klouckova, I. and Novotny, M.V. Semiautomated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry. J. Proteome Res., 2006, 5(9), 2348-2363.
    • (2006) J. Proteome Res , vol.5 , Issue.9 , pp. 2348-2363
    • Madera, M.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 27
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography
    • Jung, K.; Cho, W. and Regnier, F.E. Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography. J. Proteome Res., 2009, 8(2), 643-650.
    • (2009) J. Proteome Res , vol.8 , Issue.2 , pp. 643-650
    • Jung, K.1    Cho, W.2    Regnier, F.E.3
  • 28
    • 62549154105 scopus 로고    scopus 로고
    • Liquid chromatography/mass spectrometry (LC/MS)-based glycoproteomics technologies for cancer biomarker discovery
    • Kaji, H. and Isobe, T. Liquid chromatography/mass spectrometry (LC/MS)-based glycoproteomics technologies for cancer biomarker discovery. Clin. Proteomics, 2008, 4, 14-24.
    • (2008) Clin. Proteomics , vol.4 , pp. 14-24
    • Kaji, H.1    Isobe, T.2
  • 29
    • 53049096773 scopus 로고    scopus 로고
    • Lectin microarrays identify cell-specific and functionally significant cell surface glycan markers
    • Tao, S.-C.; Li, Y.; Zhou, J.; Qian, J.; Schnaar, R.L.; Zhang, Y.; Goldstein, I.J.; Zhu, H. and Schneck, J.P. Lectin microarrays identify cell-specific and functionally significant cell surface glycan markers. Glycobiology, 2008, 18(10), 761-769.
    • (2008) Glycobiology , vol.18 , Issue.10 , pp. 761-769
    • Tao, S.-C.1    Li, Y.2    Zhou, J.3    Qian, J.4    Schnaar, R.L.5    Zhang, Y.6    Goldstein, I.J.7    Zhu, H.8    Schneck, J.P.9
  • 30
    • 62149124853 scopus 로고    scopus 로고
    • Glycoproteomic analysis of two mouse mammary cell lines during transforming growth factor (TGF)-beta induced epithelial to mesenchymal transition
    • Hill, J.J.; Tremblay, T.-L.; Cantin, C.; O'Connor-McCourt, M.; Kelly, J.F. and Lenferink, A.E.G. Glycoproteomic analysis of two mouse mammary cell lines during transforming growth factor (TGF)-beta induced epithelial to mesenchymal transition. Proteome Sci., 2009, 7(2), 1-17.
    • (2009) Proteome Sci , vol.7 , Issue.2 , pp. 1-17
    • Hill, J.J.1    Tremblay, T.-L.2    Cantin, C.3    O'Connor-McCourt, M.4    Kelly, J.F.5    Lenferink, A.E.G.6
  • 31
    • 27944475591 scopus 로고    scopus 로고
    • Comparative glycoproteomics of N-linked complex-type glycoforms containing sialic acid in human serum
    • Qiu, R. and Regnier, F.E. Comparative glycoproteomics of N-linked complex-type glycoforms containing sialic acid in human serum. Anal. Chem., 2005, 77(22), 7225-7231.
    • (2005) Anal. Chem , vol.77 , Issue.22 , pp. 7225-7231
    • Qiu, R.1    Regnier, F.E.2
  • 32
    • 73649124980 scopus 로고    scopus 로고
    • Simple method for quantitative analysis of N-linked glycoproteins in hepatocellular carcinoma specimens
    • Lee, H.-J.; Na, K.; Choi, E.-Y.; Kim, K.S.; Kim, H. and Paik, Y.-K. Simple method for quantitative analysis of N-linked glycoproteins in hepatocellular carcinoma specimens. J. Proteome Res., 2010, 9(1), 308-318.
    • (2010) J. Proteome Res , vol.9 , Issue.1 , pp. 308-318
    • Lee, H.-J.1    Na, K.2    Choi, E.-Y.3    Kim, K.S.4    Kim, H.5    Paik, Y.-K.6
  • 33
    • 60549116901 scopus 로고    scopus 로고
    • Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification
    • Hill, J.J.; Moreno, M.J.; Lam, J.C.Y.; Haqqani, A.S. and Kelly, J.F. Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification. Proteomics, 2009, 9(3), 535-549.
    • (2009) Proteomics , vol.9 , Issue.3 , pp. 535-549
    • Hill, J.J.1    Moreno, M.J.2    Lam, J.C.Y.3    Haqqani, A.S.4    Kelly, J.F.5
  • 34
    • 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.; Martin, D.B. and Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol., 2003, 21(6), 660-666.
    • (2003) Nat. Biotechnol , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.2    Martin, D.B.3    Aebersold, R.4
  • 37
    • 76149085857 scopus 로고    scopus 로고
    • Immunoglobulin G glycopeptide profiling by matrix-assisted laser desorption ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Selman, M.H.J.; McDonnell, L.A.; Palmblad, M.; Ruhaak, R.; Deelder, A.M. and Wuhrer, M. Immunoglobulin G glycopeptide profiling by matrix-assisted laser desorption ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem., 2010, 82(3), 1073-1081.
    • (2010) Anal. Chem , vol.82 , Issue.3 , pp. 1073-1081
    • Selman, M.H.J.1    McDonnell, L.A.2    Palmblad, M.3    Ruhaak, R.4    Deelder, A.M.5    Wuhrer, M.6
  • 38
  • 39
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada, Y.; Tajiri, M. and Yoshida, S. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal. Chem., 2004, 76(22), 6560-6565.
    • (2004) Anal. Chem , vol.76 , Issue.22 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 40
    • 42949172966 scopus 로고    scopus 로고
    • Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites
    • Zhang, Y.; Go, E.P. and Desaire, H. Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites. Anal. Chem., 2008, 80(9), 3144-3158.
    • (2008) Anal. Chem , vol.80 , Issue.9 , pp. 3144-3158
    • Zhang, Y.1    Go, E.P.2    Desaire, H.3
  • 41
    • 71049170514 scopus 로고    scopus 로고
    • Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry
    • Ding, W.; Nothaft, H.; Szymanski, C.M. and Kelly, J. Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry. Mol. Cell. Proteomics, 2009, 8(9), 2170-2185.
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.9 , pp. 2170-2185
    • Ding, W.1    Nothaft, H.2    Szymanski, C.M.3    Kelly, J.4
  • 42
    • 33644841035 scopus 로고    scopus 로고
    • Tools for glycoproteomic analysis: Size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites
    • Alvarez-Manilla, G.; Atwood, J.A., III; Guo, Y.; Warren, N.L.; Orlando, R. and Pierce, M. Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites. J. Proteome Res., 2006, 5(3), 701-708.
    • (2006) J. Proteome Res , vol.5 , Issue.3 , pp. 701-708
    • Alvarez-Manilla, G.1    Atwood III, J.A.2    Guo, Y.3    Warren, N.L.4    Orlando, R.5    Pierce, M.6
  • 44
    • 36349019291 scopus 로고    scopus 로고
    • Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes
    • Lewandrowski, U.; Zahedi, R.P.; Moebius, J.; Walter, U. and Sickmann, A. Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes. Mol. Cell. Proteomics, 2007, 6(11), 1933-1941.
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.11 , pp. 1933-1941
    • Lewandrowski, U.1    Zahedi, R.P.2    Moebius, J.3    Walter, U.4    Sickmann, A.5
  • 47
    • 48349109797 scopus 로고    scopus 로고
    • Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein
    • Irungu, J.; Go, E.P.; Zhang, Y.; Dalpathado, D.S.; Liao, H.-X.; Haynes, B.F. and Desaire, H. Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein. J. Am. Soc. Mass Spectrom., 2008. 19(8), 1209-1220.
    • (2008) J. Am. Soc. Mass Spectrom , vol.19 , Issue.8 , pp. 1209-1220
    • Irungu, J.1    Go, E.P.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.-X.5    Haynes, B.F.6    Desaire, H.7
  • 49
    • 33847174067 scopus 로고    scopus 로고
    • Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • Wiese, S.; Reidegeld, K.A.; Meyer, H.E. and Warscheid, B. Protein labeling by iTRAQ: a new tool for quantitative mass spectrometry in proteome research. Proteomics, 2007, 7(3), 340-350.
    • (2007) Proteomics , vol.7 , Issue.3 , pp. 340-350
    • Wiese, S.1    Reidegeld, K.A.2    Meyer, H.E.3    Warscheid, B.4
  • 50
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ Underestimation In Simple and Complex Mixtures: "the Good, the Bad and The Ugly"
    • Ow, S.Y.; Salim, M.; Noirel, J.; Evans, C.; Rehman, I. and Wright, P.C. iTRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly". J. Proteome Res., 2009, 8(11), 5347-5355.
    • (2009) J. Proteome Res , vol.8 , Issue.11
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 51
    • 51049110528 scopus 로고    scopus 로고
    • Efficacy of glycoprotein enrichment by microscale lectin affinity chromatography
    • Madera, M.; Mann, B.; Mechref, Y. and Novotny, M.V. Efficacy of glycoprotein enrichment by microscale lectin affinity chromatography. J. Sep. Sci., 2008, 31(14), 2722-2732.
    • (2008) J. Sep. Sci , vol.31 , Issue.14 , pp. 2722-2732
    • Madera, M.1    Mann, B.2    Mechref, Y.3    Novotny, M.V.4
  • 52
    • 60149092781 scopus 로고    scopus 로고
    • ProteinQuant Suite: A bundle of automated software tools for label-free quantitative proteomics
    • Mann, B.; Madera, M.; Sheng, Q.; Tang, H.; Mechref, Y. and Novotny, M. ProteinQuant Suite: a bundle of automated software tools for label-free quantitative proteomics. Rapid Commun. Mass Spectrom., 2008, 22(23), 3823-3834.
    • (2008) Rapid Commun. Mass Spectrom , vol.22 , Issue.23 , pp. 3823-3834
    • Mann, B.1    Madera, M.2    Sheng, Q.3    Tang, H.4    Mechref, Y.5    Novotny, M.6
  • 54
    • 66149118626 scopus 로고    scopus 로고
    • Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: Strong correlation between signal strength and glycoform quantities
    • Thaysen-Andersen, M.; Mysling, S. and Hojrup, P. Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities. Anal. Chem., 2009, 81(10), 3933-3943.
    • (2009) Anal. Chem , vol.81 , Issue.10 , pp. 3933-3943
    • Thaysen-Andersen, M.1    Mysling, S.2    Hojrup, P.3
  • 55
    • 61849083637 scopus 로고    scopus 로고
    • Dissociation profile of protonated fucosyl glycopeptides and quantitation of fucosylation levels of glycoproteins by mass spectrometry
    • Tajiri, M.; Kadoya, M. and Wada, Y. Dissociation profile of protonated fucosyl glycopeptides and quantitation of fucosylation levels of glycoproteins by mass spectrometry. J. Proteome Res., 2009, 8(2), 688-693.
    • (2009) J. Proteome Res , vol.8 , Issue.2 , pp. 688-693
    • Tajiri, M.1    Kadoya, M.2    Wada, Y.3
  • 56
    • 70349995796 scopus 로고    scopus 로고
    • Glycopeptide profiling of beta-2- glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome
    • Kondo, A.; Miyamoto, T.; Yonekawa, O.; Giessing, A.M.; østerlund, E.C. and Jensen, O.N. Glycopeptide profiling of beta-2- glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome. J. Proteomics, 2009, 73(1), 123-133.
    • (2009) J. Proteomics , vol.73 , Issue.1 , pp. 123-133
    • Kondo, A.1    Miyamoto, T.2    Yonekawa, O.3    Giessing, A.M.4    østerlund, E.C.5    Jensen, O.N.6
  • 57
    • 77649337746 scopus 로고    scopus 로고
    • LC/MS analysis of complex multiglycosylated human alpha(1)- acid glycoprotein as a model for developing identification and quantitation methods for intact glycopeptide analysis
    • Ivancic, M.M.; Gadgil, H.S.; Halsall, H.B. and Treuheit, M.J. LC/MS analysis of complex multiglycosylated human alpha(1)- acid glycoprotein as a model for developing identification and quantitation methods for intact glycopeptide analysis. Anal. Biochem., 2010, 400(1), 25-32.
    • (2010) Anal. Biochem , vol.400 , Issue.1 , pp. 25-32
    • Ivancic, M.M.1    Gadgil, H.S.2    Halsall, H.B.3    Treuheit, M.J.4
  • 58
    • 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. and Nishimura, S. High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis. Mol. Cell. Proteomics, 2005, 4(12), 1977-1989.
    • (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
  • 59
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
    • Cooper, C.A.; Gasteiger, E. and Packer, N.H. GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data. Proteomics, 2001, 1(2), 340-349.
    • (2001) Proteomics , vol.1 , Issue.2 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.H.3
  • 60
  • 61
    • 34247328263 scopus 로고    scopus 로고
    • Simplification of mass spectral analysis of acidic glycopeptides using GlycoPep ID
    • Irungu, J.; Go, E.P.; Dalpathado, D.S. and Desaire, H. Simplification of mass spectral analysis of acidic glycopeptides using GlycoPep ID. Anal. Chem., 2007, 79(8), 3065-3074.
    • (2007) Anal. Chem , vol.79 , Issue.8 , pp. 3065-3074
    • Irungu, J.1    Go, E.P.2    Dalpathado, D.S.3    Desaire, H.4
  • 63
    • 50049122941 scopus 로고    scopus 로고
    • The way forward, enhanced characterization of therapeutic antibody glycosylation: Comparison of three level mass spectrometry-based strategies
    • Wagner-Rousset, E.; Bednarczyk, A.; Bussat, M.-C.; Colas, O.; Corvaïa, N.; Schaeffer, C.; Dorsselaer, A.V. and Beck, A. The way forward, enhanced characterization of therapeutic antibody glycosylation: comparison of three level mass spectrometry-based strategies. J. Chromatogr. B., 2008, 872, 23-37.
    • (2008) J. Chromatogr. B , vol.872 , pp. 23-37
    • Wagner-Rousset, E.1    Bednarczyk, A.2    Bussat, M.-C.3    Colas, O.4    Corvaïa, N.5    Schaeffer, C.6    Dorsselaer, A.V.7    Beck, A.8


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