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Volumn 34, Issue 2, 2015, Pages 148-165

Quantitative mass spectrometric analysis of glycoproteins combined with enrichment methods

Author keywords

Affinity enrichment; Hydrazide; Lectin; Multiple reaction monitoring; Protein glycosylation; Quantitative mass spectrometry; Stable isotope labeling

Indexed keywords

CARBON; CHROMATOGRAPHY; EXTRACTION; GLYCOSYLATION; HYDROPHILICITY; ISOTOPES; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PHASE SEPARATION; PROTEINS; SPECTROMETRY;

EID: 84923081608     PISSN: 02777037     EISSN: 10982787     Source Type: Journal    
DOI: 10.1002/mas.21428     Document Type: Article
Times cited : (72)

References (146)
  • 2
    • 76649133774 scopus 로고    scopus 로고
    • Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis
    • Abbott KL, Lim JM, Wells L, Benigno BB, McDonald JF, Pierce M. 2010. Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis. Proteomics 10:470-481.
    • (2010) Proteomics , vol.10 , pp. 470-481
    • Abbott, K.L.1    Lim, J.M.2    Wells, L.3    Benigno, B.B.4    McDonald, J.F.5    Pierce, M.6
  • 3
    • 0032435872 scopus 로고    scopus 로고
    • Malononitrile as a new derivatizing reagent for high-sensitivity analysis of oligosaccharides by electrospray ionization mass spectrometry
    • Ahn YH, Yoo JS. 1998. Malononitrile as a new derivatizing reagent for high-sensitivity analysis of oligosaccharides by electrospray ionization mass spectrometry. Rapid Commun Mass Spectrom 12:2011-2015.
    • (1998) Rapid Commun Mass Spectrom , vol.12 , pp. 2011-2015
    • Ahn, Y.H.1    Yoo, J.S.2
  • 4
    • 70349932824 scopus 로고    scopus 로고
    • Quantitative analysis of an aberrant glycoform of TIMP1 from colon cancer serum by L-PHA-enrichment and SISCAPA with MRM mass spectrometry
    • Ahn YH, Lee JY, Lee JY, Kim YS, Ko JH, Yoo JS. 2009. Quantitative analysis of an aberrant glycoform of TIMP1 from colon cancer serum by L-PHA-enrichment and SISCAPA with MRM mass spectrometry. J Proteome Res 8:4216-4224.
    • (2009) J Proteome Res , vol.8 , pp. 4216-4224
    • Ahn, Y.H.1    Lee, J.Y.2    Lee, J.Y.3    Kim, Y.S.4    Ko, J.H.5    Yoo, J.S.6
  • 5
    • 77953007006 scopus 로고    scopus 로고
    • Comparative quantitation of aberrant glycoforms by lectin-based glycoprotein enrichment coupled with multiple-reaction monitoring mass spectrometry
    • Ahn YH, Kim YS, Ji ES, Lee JY, Jung JA, Ko JH, Yoo JS. 2010. Comparative quantitation of aberrant glycoforms by lectin-based glycoprotein enrichment coupled with multiple-reaction monitoring mass spectrometry. Anal Chem 82:4441-4447.
    • (2010) Anal Chem , vol.82 , pp. 4441-4447
    • Ahn, Y.H.1    Kim, Y.S.2    Ji, E.S.3    Lee, J.Y.4    Jung, J.A.5    Ko, J.H.6    Yoo, J.S.7
  • 6
    • 84862930256 scopus 로고    scopus 로고
    • A multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry
    • Ahn YH, Ji ES, Shin PM, Kim KH, Kim YS, Ko JH, Yoo JS. 2012a. A multiplex lectin-channel monitoring method for human serum glycoproteins by quantitative mass spectrometry. Analyst 137:691-703.
    • (2012) Analyst , vol.137 , pp. 691-703
    • Ahn, Y.H.1    Ji, E.S.2    Shin, P.M.3    Kim, K.H.4    Kim, Y.S.5    Ko, J.H.6    Yoo, J.S.7
  • 7
    • 84863055814 scopus 로고    scopus 로고
    • Identification of low-abundance cancer biomarker candidate TIMP1 from serum with lectin fractionation and peptide affinity enrichment by ultrahigh-resolution mass spectrometry
    • Ahn YH, Kim KH, Shin PM, Ji ES, Kim H, Yoo JS. 2012b. Identification of low-abundance cancer biomarker candidate TIMP1 from serum with lectin fractionation and peptide affinity enrichment by ultrahigh-resolution mass spectrometry. Anal Chem 84:1425-1431.
    • (2012) Anal Chem , vol.84 , pp. 1425-1431
    • Ahn, Y.H.1    Kim, K.H.2    Shin, P.M.3    Ji, E.S.4    Kim, H.5    Yoo, J.S.6
  • 8
    • 84862808990 scopus 로고    scopus 로고
    • A lectin-coupled, multiple reaction monitoring-based quantitative analysis of human plasma glycoproteins by mass spectrometry
    • Ahn YH, Shin PM, Ji ES, Kim H, Yoo JS. 2012c. A lectin-coupled, multiple reaction monitoring-based quantitative analysis of human plasma glycoproteins by mass spectrometry. Anal Bioanal Chem 402:2101-2112.
    • (2012) Anal Bioanal Chem , vol.402 , pp. 2101-2112
    • Ahn, Y.H.1    Shin, P.M.2    Ji, E.S.3    Kim, H.4    Yoo, J.S.5
  • 9
    • 84865540669 scopus 로고    scopus 로고
    • A lectin-coupled, targeted proteomic mass spectrometry (MRM MS) platform for identification of multiple liver cancer biomarkers in human plasma
    • Ahn YH, Shin PM, Oh NR, Park GW, Kim H, Yoo JS. 2012d. A lectin-coupled, targeted proteomic mass spectrometry (MRM MS) platform for identification of multiple liver cancer biomarkers in human plasma. J Proteomics 75:5507-5515.
    • (2012) J Proteomics , vol.75 , pp. 5507-5515
    • Ahn, Y.H.1    Shin, P.M.2    Oh, N.R.3    Park, G.W.4    Kim, H.5    Yoo, J.S.6
  • 10
    • 60549101068 scopus 로고    scopus 로고
    • Use of activated graphitized carbon chips for liquid chromatography/mass spectrometric and tandem mass spectrometric analysis of tryptic glycopeptides
    • Alley WR Jr, Mechref Y, Novotny MV. 2009. Use of activated graphitized carbon chips for liquid chromatography/mass spectrometric and tandem mass spectrometric analysis of tryptic glycopeptides. Rapid Commun Mass Spectrom 23:495-505.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 495-505
    • Alley, W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 11
    • 0025173758 scopus 로고
    • Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds
    • Alpert AJ. 1990. Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds. J Chromatogr 499:177-196.
    • (1990) J Chromatogr , vol.499 , pp. 177-196
    • Alpert, A.J.1
  • 12
    • 41149110237 scopus 로고    scopus 로고
    • Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides
    • Alpert AJ. 2008. Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides. Anal Chem 80:62-76.
    • (2008) Anal Chem , vol.80 , pp. 62-76
    • Alpert, A.J.1
  • 13
    • 0142135856 scopus 로고    scopus 로고
    • Determination of Nglycosylation sites and site heterogeneity in glycoproteins
    • An HJ, Peavy TR, Hedrick JL, Lebrilla CB. 2003. Determination of Nglycosylation sites and site heterogeneity in glycoproteins. Anal Chem 75:5628-5637.
    • (2003) Anal Chem , vol.75 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 14
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • Anderson NL, Anderson NG, Haines LR, Hardie DB, Olafson RW, Pearson TW. 2004. Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA). J Proteome Res 3:235-244.
    • (2004) J Proteome Res , vol.3 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 16
    • 79960119959 scopus 로고    scopus 로고
    • Extensive mannose phosphorylation on leukemia inhibitory factor (LIF) controls its extracellular levels by multiple mechanisms
    • Barnes J, Lim JM, Godard A, Blanchard F, Wells L, Steet R. 2011. Extensive mannose phosphorylation on leukemia inhibitory factor (LIF) controls its extracellular levels by multiple mechanisms. J Biol Chem 286:24855-24864.
    • (2011) J Biol Chem , vol.286 , pp. 24855-24864
    • Barnes, J.1    Lim, J.M.2    Godard, A.3    Blanchard, F.4    Wells, L.5    Steet, R.6
  • 17
    • 77950662044 scopus 로고    scopus 로고
    • Optimizing performance of glycopeptide capture for plasma proteomics
    • Berven FS, Ahmad R, Clauser KR, Carr SA. 2010. Optimizing performance of glycopeptide capture for plasma proteomics. J Proteome Res 9:1706-1715.
    • (2010) J Proteome Res , vol.9 , pp. 1706-1715
    • Berven, F.S.1    Ahmad, R.2    Clauser, K.R.3    Carr, S.A.4
  • 18
    • 77950421797 scopus 로고    scopus 로고
    • Comparative glycomics using a tetraplex stableisotope coded tag
    • Bowman MJ, Zaia J. 2010. Comparative glycomics using a tetraplex stableisotope coded tag. Anal Chem 82:3023-3031.
    • (2010) Anal Chem , vol.82 , pp. 3023-3031
    • Bowman, M.J.1    Zaia, J.2
  • 19
    • 61849115201 scopus 로고    scopus 로고
    • Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach
    • Cao J, Shen C,Wang H, Shen H, Chen Y, Nie A, Yan G, Lu H, Liu Y, Yang P. 2009. Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach. J Proteome Res 8:662-672.
    • (2009) J Proteome Res , vol.8 , pp. 662-672
    • Cao, J.1    Shen, C.2    Wang, H.3    Shen, H.4    Chen, Y.5    Nie, A.6    Yan, G.7    Lu, H.8    Liu, Y.9    Yang, P.10
  • 20
    • 70349330348 scopus 로고    scopus 로고
    • Boronate affinity monolith for highly selective enrichment of glycopeptides and glycoproteins
    • Chen M, Lu Y, Ma Q, Guo L, Feng YQ. 2009. Boronate affinity monolith for highly selective enrichment of glycopeptides and glycoproteins. Analyst 134:2158-2164.
    • (2009) Analyst , vol.134 , pp. 2158-2164
    • Chen, M.1    Lu, Y.2    Ma, Q.3    Guo, L.4    Feng, Y.Q.5
  • 21
    • 84855188603 scopus 로고    scopus 로고
    • Development of glycoprotein capture-based label-free method for the high-throughput screening of differential glycoproteins in hepatocellular carcinoma
    • 006445
    • Chen R, Tan Y, Wang M, Wang F, Yao Z, Dong L, Ye M, Wang H, Zou H. 2011. Development of glycoprotein capture-based label-free method for the high-throughput screening of differential glycoproteins in hepatocellular carcinoma. Mol Cell Proteomics 10:M110.006445.
    • (2011) Mol Cell Proteomics , vol.10 , pp. M110
    • Chen, R.1    Tan, Y.2    Wang, M.3    Wang, F.4    Yao, Z.5    Dong, L.6    Ye, M.7    Wang, H.8    Zou, H.9
  • 22
    • 84862786913 scopus 로고    scopus 로고
    • Development of a combined chemical and enzymatic approach for the mass spectrometric identification and quantification of aberrant N-glycosylation
    • Chen R, Wang F, Tan Y, Sun Z, Song C, Ye M, Wang H, Zou H. 2012. Development of a combined chemical and enzymatic approach for the mass spectrometric identification and quantification of aberrant N-glycosylation. J Proteomics 75:1666-1674.
    • (2012) J Proteomics , vol.75 , pp. 1666-1674
    • Chen, R.1    Wang, F.2    Tan, Y.3    Sun, Z.4    Song, C.5    Ye, M.6    Wang, H.7    Zou, H.8
  • 23
    • 83755205413 scopus 로고    scopus 로고
    • High-throughput lectin magnetic bead array-coupled tandem mass spectrometry for glycoprotein biomarker discovery
    • Choi E, Loo D, Dennis JW, O'Leary CA, Hill MM. 2011. High-throughput lectin magnetic bead array-coupled tandem mass spectrometry for glycoprotein biomarker discovery. Electrophoresis 32:3564-3575.
    • (2011) Electrophoresis , vol.32 , pp. 3564-3575
    • Choi, E.1    Loo, D.2    Dennis, J.W.3    O'Leary, C.A.4    Hill, M.M.5
  • 24
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu I, Kerek F. 1984. A simple and rapid method for the permethylation of carbohydrates. Carbohydr Res 131:209-217.
    • (1984) Carbohydr Res , vol.131 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 27
    • 77957887133 scopus 로고    scopus 로고
    • Linkage specific fucosylation of alpha-1-antitrypsin in liver cirrhosis and cancer patients: Implications for a biomarker of hepatocellular carcinoma
    • Comunale MA, Rodemich-Betesh L, Hafner J, Wang M, Norton P, Di Bisceglie AM, Block T, Mehta A. 2010. Linkage specific fucosylation of alpha-1-antitrypsin in liver cirrhosis and cancer patients: Implications for a biomarker of hepatocellular carcinoma. PLoS ONE 5:e12419.
    • (2010) PLoS ONE , vol.5
    • Comunale, M.A.1    Rodemich-Betesh, L.2    Hafner, J.3    Wang, M.4    Norton, P.5    Di Bisceglie, A.M.6    Block, T.7    Mehta, A.8
  • 28
    • 34548681626 scopus 로고    scopus 로고
    • A glycomics platform for the analysis of permethylated oligosaccharide alditols
    • Costello CE, Contado-Miller JM, Cipollo JF. 2007. A glycomics platform for the analysis of permethylated oligosaccharide alditols. J Am Soc Mass Spectrom 18:1799-1812.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 1799-1812
    • Costello, C.E.1    Contado-Miller, J.M.2    Cipollo, J.F.3
  • 29
    • 70449970103 scopus 로고    scopus 로고
    • Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein markers
    • Dai Z, Zhou J, Qiu SJ, Liu YK, Fan J. 2009. Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein markers. Electrophoresis 30:2957-2966.
    • (2009) Electrophoresis , vol.30 , pp. 2957-2966
    • Dai, Z.1    Zhou, J.2    Qiu, S.J.3    Liu, Y.K.4    Fan, J.5
  • 30
    • 80053951339 scopus 로고    scopus 로고
    • Differential profiling studies of N-linked glycoproteins in glioblastoma cancer stem cells upon treatment with γ-secretase inhibitor
    • Dai L, Liu Y, He J, Flack CG, Talsma CE, Crowley JG, Muraszko KM, Fan X, Lubman DM. 2011. Differential profiling studies of N-linked glycoproteins in glioblastoma cancer stem cells upon treatment with γ-secretase inhibitor. Proteomics 11:4021-4028.
    • (2011) Proteomics , vol.11 , pp. 4021-4028
    • Dai, L.1    Liu, Y.2    He, J.3    Flack, C.G.4    Talsma, C.E.5    Crowley, J.G.6    Muraszko, K.M.7    Fan, X.8    Lubman, D.M.9
  • 31
    • 0026794731 scopus 로고
    • High-performance liquid chromatography of oligosaccharide alditols and glycopeptides on a graphitized carbon column
    • Davies M, Smith KD, Harbin AM, Hounsell EF. 1992. High-performance liquid chromatography of oligosaccharide alditols and glycopeptides on a graphitized carbon column. J Chromatogr 609:125-131.
    • (1992) J Chromatogr , vol.609 , pp. 125-131
    • Davies, M.1    Smith, K.D.2    Harbin, A.M.3    Hounsell, E.F.4
  • 32
    • 0023255440 scopus 로고
    • Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • Dennis JW, Laferte S, Waghorne C, Breitman ML, Kerbel RS. 1987. Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science 236:582-585.
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.W.1    Laferte, S.2    Waghorne, C.3    Breitman, M.L.4    Kerbel, R.S.5
  • 33
    • 33750620940 scopus 로고    scopus 로고
    • Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers
    • Drake RR, Schwegler EE, Malik G, Diaz J, Block T, Mehta A, Semmes OJ. 2006. Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers. Mol Cell Proteomics 5:1957-1967.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1957-1967
    • Drake, R.R.1    Schwegler, E.E.2    Malik, G.3    Diaz, J.4    Block, T.5    Mehta, A.6    Semmes, O.J.7
  • 36
    • 79960379703 scopus 로고    scopus 로고
    • Nano-LC-MS/MS of glycopeptides produced by nonspecific proteolysis enables rapid and extensive site-specific glycosylation determination
    • Froehlich JW, Barboza M, Chu C, Lerno LA Jr, Clowers BH, Zivkovic AM, German JB, Lebrilla CB. 2011. Nano-LC-MS/MS of glycopeptides produced by nonspecific proteolysis enables rapid and extensive site-specific glycosylation determination. Anal Chem 83:5541-5547.
    • (2011) Anal Chem , vol.83 , pp. 5541-5547
    • Froehlich, J.W.1    Barboza, M.2    Chu, C.3    Lerno, L.A.4    Clowers, B.H.5    Zivkovic, A.M.6    German, J.B.7    Lebrilla, C.B.8
  • 37
    • 0035836061 scopus 로고    scopus 로고
    • Proteomics of glycoproteins based on affinity selection of glycopeptides from tryptic digests
    • Geng M, Zhang X, Bina M, Regnier F. 2001. Proteomics of glycoproteins based on affinity selection of glycopeptides from tryptic digests. J Chromatogr B Biomed Sci Appl 752:293-306.
    • (2001) J Chromatogr B Biomed Sci Appl , vol.752 , pp. 293-306
    • Geng, M.1    Zhang, X.2    Bina, M.3    Regnier, F.4
  • 38
    • 45049083308 scopus 로고    scopus 로고
    • A relative and absolute quantification of neutral N-linked oligosaccharides using modification with carboxymethyl trimethylammonium hydrazide and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Gil GC, Kim YG, Kim BG. 2008. A relative and absolute quantification of neutral N-linked oligosaccharides using modification with carboxymethyl trimethylammonium hydrazide and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Biochem 379:45-59.
    • (2008) Anal Biochem , vol.379 , pp. 45-59
    • Gil, G.C.1    Kim, Y.G.2    Kim, B.G.3
  • 39
    • 80655145639 scopus 로고    scopus 로고
    • Characterization of glycoprotein digests with hydrophilic interaction chromatography and mass spectrometry
    • Gilar M, Yu YQ, Ahn J, Xie H, Han H, Ying W, Qian X. 2011. Characterization of glycoprotein digests with hydrophilic interaction chromatography and mass spectrometry. Anal Biochem 417:80-88.
    • (2011) Anal Biochem , vol.417 , pp. 80-88
    • Gilar, M.1    Yu, Y.Q.2    Ahn, J.3    Xie, H.4    Han, H.5    Ying, W.6    Qian, X.7
  • 41
    • 79958102986 scopus 로고    scopus 로고
    • Analysis of recombinant human follicle-stimulating hormone (FSH) by mass spectrometric approaches
    • Grass J, Pabst M, Chang M, Wozny M, Altmann F. 2011. Analysis of recombinant human follicle-stimulating hormone (FSH) by mass spectrometric approaches. Anal Bioanal Chem 400:2427-2438.
    • (2011) Anal Bioanal Chem , vol.400 , pp. 2427-2438
    • Grass, J.1    Pabst, M.2    Chang, M.3    Wozny, M.4    Altmann, F.5
  • 42
    • 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 ON, Roepstorff P. 2004. 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 3:556-566.
    • (2004) J Proteome Res , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 43
    • 34548186744 scopus 로고    scopus 로고
    • An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins
    • Hagglund P, Matthiesen R, Elortza F, Hojrup P, Roepstorff P, Jensen ON, Bunkenborg J. 2007. An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins. J Proteome Res 6:3021-3031.
    • (2007) J Proteome Res , vol.6 , pp. 3021-3031
    • Hagglund, P.1    Matthiesen, R.2    Elortza, F.3    Hojrup, P.4    Roepstorff, P.5    Jensen, O.N.6    Bunkenborg, J.7
  • 45
    • 37049026705 scopus 로고    scopus 로고
    • Identification of putative serum glycoprotein biomarkers for human lung adenocarcinoma by multilectin affinity chromatography and LC-MS/MS
    • Heo SH, Lee SJ, Ryoo HM, Park JY, Cho JY. 2007. Identification of putative serum glycoprotein biomarkers for human lung adenocarcinoma by multilectin affinity chromatography and LC-MS/MS. Proteomics 7:4292-4302.
    • (2007) Proteomics , vol.7 , pp. 4292-4302
    • Heo, S.H.1    Lee, S.J.2    Ryoo, H.M.3    Park, J.Y.4    Cho, J.Y.5
  • 46
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth MA, Swanson BJ. 2004. Mucins in cancer: Protection and control of the cell surface. Nat Rev Cancer 4:45-60.
    • (2004) Nat Rev Cancer , vol.4 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 49
    • 80052024809 scopus 로고    scopus 로고
    • Development of quantitative plasma N-glycoproteomics using label-free 2-D LC-MALDI MS and its applicability for biomarker discovery in hepatocellular carcinoma
    • Ishihara T, Fukuda I, Morita A, Takinami Y, Okamoto H, Nishimura S, Numata Y. 2011. Development of quantitative plasma N-glycoproteomics using label-free 2-D LC-MALDI MS and its applicability for biomarker discovery in hepatocellular carcinoma. J Proteomics 74:2159-2168.
    • (2011) J Proteomics , vol.74 , pp. 2159-2168
    • Ishihara, T.1    Fukuda, I.2    Morita, A.3    Takinami, Y.4    Okamoto, H.5    Nishimura, S.6    Numata, Y.7
  • 52
    • 2942568109 scopus 로고    scopus 로고
    • Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data
    • Joshi HJ, Harrison MJ, Schulz BL, Cooper CA, Packer NH, Karlsson NG. 2004. Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data. Proteomics 4:1650-1664.
    • (2004) Proteomics , vol.4 , pp. 1650-1664
    • Joshi, H.J.1    Harrison, M.J.2    Schulz, B.L.3    Cooper, C.A.4    Packer, N.H.5    Karlsson, N.G.6
  • 53
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography
    • Jung K, Cho W, Regnier FE. 2009. Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography. J Proteome Res 8:643-650.
    • (2009) J Proteome Res , vol.8 , pp. 643-650
    • Jung, K.1    Cho, W.2    Regnier, F.E.3
  • 55
    • 34548836006 scopus 로고    scopus 로고
    • Mass spectrometric identification of N-linked glycopeptides using lectin-mediated affinity capture and glycosylation site-specific stable isotope tagging
    • Kaji H, Yamauchi Y, Takahashi N, Isobe T. 2006. Mass spectrometric identification of N-linked glycopeptides using lectin-mediated affinity capture and glycosylation site-specific stable isotope tagging. Nat Protoc 1:3019-3027.
    • (2006) Nat Protoc , vol.1 , pp. 3019-3027
    • Kaji, H.1    Yamauchi, Y.2    Takahashi, N.3    Isobe, T.4
  • 59
    • 77952034762 scopus 로고    scopus 로고
    • Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach
    • Klement E, Lipinszki Z, Kupihár Z, Udvardy A, Medzihradszky KF. 2010. Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach. J Proteome Res 9:2200-2206.
    • (2010) J Proteome Res , vol.9 , pp. 2200-2206
    • Klement, E.1    Lipinszki, Z.2    Kupihár, Z.3    Udvardy, A.4    Medzihradszky, K.F.5
  • 60
    • 0032211243 scopus 로고    scopus 로고
    • Analysis of 2-aminobenzamide-labeled oligosaccharides by high-pH anion-exchange chromatography with fluorometric detection
    • Kotani N, Takasaki S. 1998. Analysis of 2-aminobenzamide-labeled oligosaccharides by high-pH anion-exchange chromatography with fluorometric detection. Anal Biochem 264:66-73.
    • (1998) Anal Biochem , vol.264 , pp. 66-73
    • Kotani, N.1    Takasaki, S.2
  • 61
    • 51049087078 scopus 로고    scopus 로고
    • Preparation of a high-performance multi-lectin affinity chromatography (HP-M-LAC) adsorbent for the analysis of human plasma glycoproteins
    • Kullolli M, Hancock WS, Hincapie M. 2008. Preparation of a high-performance multi-lectin affinity chromatography (HP-M-LAC) adsorbent for the analysis of human plasma glycoproteins. J Sep Sci 31:2733-2739.
    • (2008) J Sep Sci , vol.31 , pp. 2733-2739
    • Kullolli, M.1    Hancock, W.S.2    Hincapie, M.3
  • 62
    • 0032951103 scopus 로고    scopus 로고
    • Clinical utility of Lens culinaris agglutinin-reactive alphafetoprotein in small hepatocellular carcinoma: Special reference to imaging diagnosis
    • Kumada T, Nakano S, Takeda I, Kiriyama S, Sone Y, Hayashi K, Katoh H, Endoh T, Sassa T, Satomura S. 1999. Clinical utility of Lens culinaris agglutinin-reactive alphafetoprotein in small hepatocellular carcinoma: Special reference to imaging diagnosis. J Hepatol 30:125-130.
    • (1999) J Hepatol , vol.30 , pp. 125-130
    • Kumada, T.1    Nakano, S.2    Takeda, I.3    Kiriyama, S.4    Sone, Y.5    Hayashi, K.6    Katoh, H.7    Endoh, T.8    Sassa, T.9    Satomura, S.10
  • 63
    • 84858699350 scopus 로고    scopus 로고
    • Rapid glycopeptide enrichment and N-glycosylation site mapping strategies based on amine-functionalized magnetic nanoparticles
    • Kuo CW, Wu IL, Hsiao HH, Khoo KH. 2012. Rapid glycopeptide enrichment and N-glycosylation site mapping strategies based on amine-functionalized magnetic nanoparticles. Anal Bioanal Chem 402:2765-2776.
    • (2012) Anal Bioanal Chem , vol.402 , pp. 2765-2776
    • Kuo, C.W.1    Wu, I.L.2    Hsiao, H.H.3    Khoo, K.H.4
  • 66
    • 77957883394 scopus 로고    scopus 로고
    • Online coupling of reverse-phase and hydrophilic interaction liquid chromatography for protein and glycoprotein characterization
    • Lam MP, Siu SO, Lau E, Mao X, Sun HZ, Chiu PC, Yeung WS, Cox DM, Chu IK. 2010. Online coupling of reverse-phase and hydrophilic interaction liquid chromatography for protein and glycoprotein characterization. Anal Bioanal Chem 398:791-804.
    • (2010) Anal Bioanal Chem , vol.398 , pp. 791-804
    • Lam, M.P.1    Siu, S.O.2    Lau, E.3    Mao, X.4    Sun, H.Z.5    Chiu, P.C.6    Yeung, W.S.7    Cox, D.M.8    Chu, I.K.9
  • 67
    • 80054984666 scopus 로고    scopus 로고
    • Online combination of reversed-phase/reversed-phase and porous graphitic carbon liquid chromatography for multicomponent separation of proteomics and glycoproteomics samples
    • Lam MP, Lau E, Siu SO, Ng DC, Kong RP, Chiu PC, Yeung WS, Lo C, Chu IK. 2011. Online combination of reversed-phase/reversed-phase and porous graphitic carbon liquid chromatography for multicomponent separation of proteomics and glycoproteomics samples. Electrophoresis 32:2930-2940.
    • (2011) Electrophoresis , vol.32 , pp. 2930-2940
    • Lam, M.P.1    Lau, E.2    Siu, S.O.3    Ng, D.C.4    Kong, R.P.5    Chiu, P.C.6    Yeung, W.S.7    Lo, C.8    Chu, I.K.9
  • 69
    • 23844545246 scopus 로고    scopus 로고
    • Immobilization of aminophenylboronic acid on magnetic beads for the direct determination of glycoproteins by matrix assisted laser desorption ionization mass spectrometry
    • Lee JH, Kim Y, Ha MY, Lee EK, Choo J. 2005. Immobilization of aminophenylboronic acid on magnetic beads for the direct determination of glycoproteins by matrix assisted laser desorption ionization mass spectrometry. J Am Soc Mass Spectrom 16:1456-1460.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 1456-1460
    • Lee, J.H.1    Kim, Y.2    Ha, M.Y.3    Lee, E.K.4    Choo, J.5
  • 71
    • 79960957828 scopus 로고    scopus 로고
    • Preparation and evaluation of a phenylboronate affinity monolith for selective capture of glycoproteins by capillary liquid chromatography
    • Lin ZA, Pang JL, Lin Y, Huang H, Cai ZW, Zhang L, Chen GN. 2011. Preparation and evaluation of a phenylboronate affinity monolith for selective capture of glycoproteins by capillary liquid chromatography. Analyst 136:3281-3288.
    • (2011) Analyst , vol.136 , pp. 3281-3288
    • Lin, Z.A.1    Pang, J.L.2    Lin, Y.3    Huang, H.4    Cai, Z.W.5    Zhang, L.6    Chen, G.N.7
  • 72
    • 0030606909 scopus 로고    scopus 로고
    • Separation of acetylated core histones by hydrophilic-interaction liquid chromatography
    • Lindner H, Sarg B, Meraner C, Helliger W. 1996. Separation of acetylated core histones by hydrophilic-interaction liquid chromatography. J Chromatogr A 743:137-144.
    • (1996) J Chromatogr A , vol.743 , pp. 137-144
    • Lindner, H.1    Sarg, B.2    Meraner, C.3    Helliger, W.4
  • 73
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu T, Qian WJ, Gritsenko MA, Camp DG II, Monroe ME, Moore RJ, Smith RD. 2005. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res 4:2070-2080.
    • (2005) J Proteome Res , vol.4 , pp. 2070-2080
    • Liu, T.1    Qian, W.J.2    Gritsenko, M.A.3    Camp, D.G.4    Monroe, M.E.5    Moore, R.J.6    Smith, R.D.7
  • 75
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley F, Trimble RB, Tarentino AL, Plummer TH Jr. 1989. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal Biochem 180:195-204.
    • (1989) Anal Biochem , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer, T.H.4
  • 76
    • 84863794084 scopus 로고    scopus 로고
    • Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins
    • 015792
    • Mann BF, Goetz JA, House MG, Schmidt CM, Novotny MV. 2012. Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins. Mol Cell Proteomics 11:M111.015792.
    • (2012) Mol Cell Proteomics , vol.11 , pp. M111
    • Mann, B.F.1    Goetz, J.A.2    House, M.G.3    Schmidt, C.M.4    Novotny, M.V.5
  • 77
    • 77956886210 scopus 로고    scopus 로고
    • A high-throughput method for quantification of glycoprotein sialylation
    • Markely LR, Ong BT, Hoi KM, Teo G, Lu MY, Wang DI. 2010. A high-throughput method for quantification of glycoprotein sialylation. Anal Biochem 407:128-133.
    • (2010) Anal Biochem , vol.407 , pp. 128-133
    • Markely, L.R.1    Ong, B.T.2    Hoi, K.M.3    Teo, G.4    Lu, M.Y.5    Wang, D.I.6
  • 78
    • 61649103556 scopus 로고    scopus 로고
    • Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome
    • McDonald CA, Yang JY, Marathe V, Yen TY, Macher BA. 2009. Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome. Mol Cell Proteomics 8:287-301.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 287-301
    • McDonald, C.A.1    Yang, J.Y.2    Marathe, V.3    Yen, T.Y.4    Macher, B.A.5
  • 80
    • 37549061023 scopus 로고    scopus 로고
    • Lens culinaris agglutinin-reactive alpha-fetoprotein and protein induced by vitamin K absence II are potential indicators of a poor prognosis: A histopathological study of surgically resected hepatocellular carcinoma
    • Miyaaki H, Nakashima O, Kurogi M, Eguchi K, Kojiro M. 2007. Lens culinaris agglutinin-reactive alpha-fetoprotein and protein induced by vitamin K absence II are potential indicators of a poor prognosis: A histopathological study of surgically resected hepatocellular carcinoma. J Gastroenterol 42:962-968.
    • (2007) J Gastroenterol , vol.42 , pp. 962-968
    • Miyaaki, H.1    Nakashima, O.2    Kurogi, M.3    Eguchi, K.4    Kojiro, M.5
  • 81
    • 0021054473 scopus 로고
    • Structures of the asparagine-linked sugar chains of human chorionic gonadotropin produced in choriocarcinoma: Appearance of triantennary sugar chains and unique biantennary sugar chains
    • Mizuochi T, Nishimura R, Derappe C, Taniguchi T, Hamamoto T, Mochizuki M, Kobata A. 1983. Structures of the asparagine-linked sugar chains of human chorionic gonadotropin produced in choriocarcinoma: Appearance of triantennary sugar chains and unique biantennary sugar chains. J Biol Chem 258:14126-14129.
    • (1983) J Biol Chem , vol.258 , pp. 14126-14129
    • Mizuochi, T.1    Nishimura, R.2    Derappe, C.3    Taniguchi, T.4    Hamamoto, T.5    Mochizuki, M.6    Kobata, A.7
  • 82
    • 33750097998 scopus 로고    scopus 로고
    • The use of mass spectrometry for the proteomic analysis of glycosylation
    • Morelle W, Canis K, Chirat F, Faid V, Michalski JC. 2006. The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics 6:3993-4015.
    • (2006) Proteomics , vol.6 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.C.5
  • 83
    • 0142258161 scopus 로고    scopus 로고
    • Bioanalytical liquid chromatography tandem mass spectrometry methods on underivatized silica columns with aqueous/organic mobile phases
    • Naidong W. 2003. Bioanalytical liquid chromatography tandem mass spectrometry methods on underivatized silica columns with aqueous/organic mobile phases. J Chromatogr B Analyt Technol Biomed Life Sci 796:209-224.
    • (2003) J Chromatogr B Analyt Technol Biomed Life Sci , vol.796 , pp. 209-224
    • Naidong, W.1
  • 84
    • 58149347362 scopus 로고    scopus 로고
    • Capillary electrophoresis-electrospray ionization mass spectrometry for rapid and sensitive N-glycan analysis of glycoproteins as 9-fluorenylmethyl derivatives
    • Nakano M, Higo D, Arai E, Nakagawa T, Kakehi K, Taniguchi N, Kondo A. 2009. Capillary electrophoresis-electrospray ionization mass spectrometry for rapid and sensitive N-glycan analysis of glycoproteins as 9-fluorenylmethyl derivatives. Glycobiology 19:135-143.
    • (2009) Glycobiology , vol.19 , pp. 135-143
    • Nakano, M.1    Higo, D.2    Arai, E.3    Nakagawa, T.4    Kakehi, K.5    Taniguchi, N.6    Kondo, A.7
  • 85
    • 79955840214 scopus 로고    scopus 로고
    • Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides
    • Neue K, Mormann M, Peter-Katalinić J, Pohlentz G. 2011. Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides. J Proteome Res 10:2248-2260.
    • (2011) J Proteome Res , vol.10 , pp. 2248-2260
    • Neue, K.1    Mormann, M.2    Peter-Katalinić, J.3    Pohlentz, G.4
  • 88
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K, Marth JD. 2006. Glycosylation in cellular mechanisms of health and disease. Cell 126:855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 89
    • 4444231395 scopus 로고    scopus 로고
    • Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy
    • Ohyama C, Hosono M, Nitta K, Oh-eda M, Yoshikawa K, Habuchi T, Arai Y, Fukuda M. 2004. Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy. Glycobiology 14:671-679.
    • (2004) Glycobiology , vol.14 , pp. 671-679
    • Ohyama, C.1    Hosono, M.2    Nitta, K.3    Oh-eda, M.4    Yoshikawa, K.5    Habuchi, T.6    Arai, Y.7    Fukuda, M.8
  • 90
    • 0033048787 scopus 로고    scopus 로고
    • Clinical aspects of altered glycosylation of glycoproteins in cancer
    • Orntoft TF, Vestergaard EM. 1999. Clinical aspects of altered glycosylation of glycoproteins in cancer. Electrophoresis 20:362-371.
    • (1999) Electrophoresis , vol.20 , pp. 362-371
    • Orntoft, T.F.1    Vestergaard, E.M.2
  • 92
    • 78649961364 scopus 로고    scopus 로고
    • Selective enrichment of sialic acid-containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry
    • Palmisano G, Lendal SE, Engholm-Keller K, Leth-Larsen R, Parker BL, Larsen MR. 2010. Selective enrichment of sialic acid-containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry. Nat Protoc 5:1974-1982.
    • (2010) Nat Protoc , vol.5 , pp. 1974-1982
    • Palmisano, G.1    Lendal, S.E.2    Engholm-Keller, K.3    Leth-Larsen, R.4    Parker, B.L.5    Larsen, M.R.6
  • 95
    • 66249119691 scopus 로고    scopus 로고
    • De novo glycan structure search with the CID MS/MS spectra of native N-glycopeptides
    • Peltoniemi H, Joenväärä S, Renkonen R. 2009. De novo glycan structure search with the CID MS/MS spectra of native N-glycopeptides. Glycobiology 19:707-714.
    • (2009) Glycobiology , vol.19 , pp. 707-714
    • Peltoniemi, H.1    Joenväärä, S.2    Renkonen, R.3
  • 96
    • 0038618896 scopus 로고    scopus 로고
    • Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins
    • Peracaula R, Tabares G, Royle L, Harvey DJ, Dwek RA, Rudd PM, de Llorens R. 2003. Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins. Glycobiology 13:457-470.
    • (2003) Glycobiology , vol.13 , pp. 457-470
    • Peracaula, R.1    Tabares, G.2    Royle, L.3    Harvey, D.J.4    Dwek, R.A.5    Rudd, P.M.6    De Llorens, R.7
  • 97
    • 0022993375 scopus 로고
    • Rous sarcoma virus-transformed baby hamster kidney cells express higher levels of asparagine-linked tri- and tetraantennary glycopeptides containing [GlcNAc-beta (1,6)Man-alpha (1,6)Man] and poly-N-acetyllactosamine sequences than baby hamster kidney cells
    • Pierce M, Arango J. 1986. Rous sarcoma virus-transformed baby hamster kidney cells express higher levels of asparagine-linked tri- and tetraantennary glycopeptides containing [GlcNAc-beta (1,6)Man-alpha (1,6)Man] and poly-N-acetyllactosamine sequences than baby hamster kidney cells. J Biol Chem 261:10772-10777.
    • (1986) J Biol Chem , vol.261 , pp. 10772-10777
    • Pierce, M.1    Arango, J.2
  • 98
    • 84875976604 scopus 로고    scopus 로고
    • Site-specific glycoforms of haptoglobin in liver cirrhosis and hepatocellular carcinoma
    • Pompach P, Brnakova Z, Sanda M, Wu J, Edwards N, Goldman R. 2013. Site-specific glycoforms of haptoglobin in liver cirrhosis and hepatocellular carcinoma. Mol Cell Proteomics 12:1281-1293.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1281-1293
    • Pompach, P.1    Brnakova, Z.2    Sanda, M.3    Wu, J.4    Edwards, N.5    Goldman, R.6
  • 99
    • 76849086981 scopus 로고    scopus 로고
    • Mass spectrometric-based stable isotopic 2-aminobenzoic acid glycan mapping for rapid glycan screening of biotherapeutics
    • Prien JM, Prater BD, Qin Q, Cockrill SL. 2010. Mass spectrometric-based stable isotopic 2-aminobenzoic acid glycan mapping for rapid glycan screening of biotherapeutics. Anal Chem 82:1498-1508.
    • (2010) Anal Chem , vol.82 , pp. 1498-1508
    • Prien, J.M.1    Prater, B.D.2    Qin, Q.3    Cockrill, S.L.4
  • 100
    • 84862833624 scopus 로고    scopus 로고
    • Integrated sample pretreatment system for N-linked glycosylation site profiling with combination of hydrophilic interaction chromatography and PNGase F immobilized enzymatic reactor via a strong cation exchange precolumn
    • Qu Y, Xia S, Yuan H, Wu Q, Li M, Zou L, Zhang L, Liang Z, Zhang Y. 2011. Integrated sample pretreatment system for N-linked glycosylation site profiling with combination of hydrophilic interaction chromatography and PNGase F immobilized enzymatic reactor via a strong cation exchange precolumn. Anal Chem 83:7457-7463.
    • (2011) Anal Chem , vol.83 , pp. 7457-7463
    • Qu, Y.1    Xia, S.2    Yuan, H.3    Wu, Q.4    Li, M.5    Zou, L.6    Zhang, L.7    Liang, Z.8    Zhang, Y.9
  • 101
    • 79959503211 scopus 로고    scopus 로고
    • New technologies for glycomic analysis: Toward a systematic understanding of the glycome
    • Rakus JF, Mahal LK. 2011. New technologies for glycomic analysis: Toward a systematic understanding of the glycome. Annu Rev Anal Chem (Palo Alto Calif) 4:367-392.
    • (2011) Annu Rev Anal Chem (Palo Alto Calif) , vol.4 , pp. 367-392
    • Rakus, J.F.1    Mahal, L.K.2
  • 103
    • 84877619420 scopus 로고    scopus 로고
    • Quantitative liquid chromatography-mass spectrometry-multiple reaction monitoring (LC-MS-MRM) analysis of site-specific glycoforms of haptoglobin in liver disease
    • Sanda M, Pompach P, Brnakova Z, Wu J, Makambi K, Goldman R. 2013. Quantitative liquid chromatography-mass spectrometry-multiple reaction monitoring (LC-MS-MRM) analysis of site-specific glycoforms of haptoglobin in liver disease. Mol Cell Proteomics 12:1294-1305.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1294-1305
    • Sanda, M.1    Pompach, P.2    Brnakova, Z.3    Wu, J.4    Makambi, K.5    Goldman, R.6
  • 105
    • 77956566726 scopus 로고    scopus 로고
    • 3-labeling of solid-phase enriched glycopeptides
    • 3-labeling of solid-phase enriched glycopeptides. Anal Chem 82:7722-7728.
    • (2010) Anal Chem , vol.82 , pp. 7722-7728
    • Shakey, Q.1    Bates, B.2    Wu, J.3
  • 106
    • 0028166921 scopus 로고
    • Assay of myo-inositol in cerebrospinal fluid and plasma by chemical ionization mass spectrometry of the hexaacetate derivative
    • Shetty HU, Holloway HW. 1994. Assay of myo-inositol in cerebrospinal fluid and plasma by chemical ionization mass spectrometry of the hexaacetate derivative. Biol Mass Spectrom 23:440-444.
    • (1994) Biol Mass Spectrom , vol.23 , pp. 440-444
    • Shetty, H.U.1    Holloway, H.W.2
  • 107
    • 78449283443 scopus 로고    scopus 로고
    • Investigation of sialylation aberration in N-linked glycopeptides by lectin and tandem labeling (LTL) quantitative proteomics
    • Shetty V, Nickens Z, Shah P, Sinnathamby G, Semmes OJ, Philip R. 2010. Investigation of sialylation aberration in N-linked glycopeptides by lectin and tandem labeling (LTL) quantitative proteomics. Anal Chem 82:9201-9210.
    • (2010) Anal Chem , vol.82 , pp. 9201-9210
    • Shetty, V.1    Nickens, Z.2    Shah, P.3    Sinnathamby, G.4    Semmes, O.J.5    Philip, R.6
  • 108
    • 33645748520 scopus 로고    scopus 로고
    • Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles
    • Sparbier K, Koch S, Kessler I, Wenzel T, Kostrzewa M. 2005. Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles. J Biomol Tech 16:407-413.
    • (2005) J Biomol Tech , vol.16 , pp. 407-413
    • Sparbier, K.1    Koch, S.2    Kessler, I.3    Wenzel, T.4    Kostrzewa, M.5
  • 109
    • 36048977494 scopus 로고    scopus 로고
    • Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection
    • Sparbier K, Asperger A, Resemann A, Kessler I, Koch S, Wenzel T, Stein G, Vorwerg L, Suckau D, Kostrzewa M. 2007. Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection. J Biomol Tech 18:252-258.
    • (2007) J Biomol Tech , vol.18 , pp. 252-258
    • Sparbier, K.1    Asperger, A.2    Resemann, A.3    Kessler, I.4    Koch, S.5    Wenzel, T.6    Stein, G.7    Vorwerg, L.8    Suckau, D.9    Kostrzewa, M.10
  • 111
    • 84860544131 scopus 로고    scopus 로고
    • Automated interpretation of MS/MS spectra of oligosaccharides
    • Tang H, Mechref Y, Novotny MV. 2005. Automated interpretation of MS/MS spectra of oligosaccharides. Bioinformatics 21:i431-439.
    • (2005) Bioinformatics , vol.21 , pp. i431-i439
    • Tang, H.1    Mechref, Y.2    Novotny, M.V.3
  • 112
    • 70949105966 scopus 로고    scopus 로고
    • On-plate-selective enrichment of glycopeptides using boronic acid-modified gold nanoparticles for direct MALDI-QIT-TOF MS analysis
    • Tang J, Liu Y, Qi D, Yao G, Deng C, Zhang X. 2009. On-plate-selective enrichment of glycopeptides using boronic acid-modified gold nanoparticles for direct MALDI-QIT-TOF MS analysis. Proteomics 9:5046-5055.
    • (2009) Proteomics , vol.9 , pp. 5046-5055
    • Tang, J.1    Liu, Y.2    Qi, D.3    Yao, G.4    Deng, C.5    Zhang, X.6
  • 114
    • 84862322594 scopus 로고    scopus 로고
    • Altered expression of sialylated glycoproteins in breast cancer using hydrazide chemistry and mass spectrometry
    • 011403
    • Tian Y, Esteva FJ, Song J, Zhang H. 2012. Altered expression of sialylated glycoproteins in breast cancer using hydrazide chemistry and mass spectrometry. Mol Cell Proteomics 11:M111.011403.
    • (2012) Mol Cell Proteomics , vol.11 , pp. M111
    • Tian, Y.1    Esteva, F.J.2    Song, J.3    Zhang, H.4
  • 115
    • 84869475312 scopus 로고    scopus 로고
    • Quantitative structural characterization of local N-glycan microheterogeneity in therapeutic antibodies by energy-resolved oxonium ion monitoring
    • Toyama A, Nakagawa H, Matsuda K, Sato TA, Nakamura Y, Ueda K. 2012. Quantitative structural characterization of local N-glycan microheterogeneity in therapeutic antibodies by energy-resolved oxonium ion monitoring. Anal Chem 84:9655-9662.
    • (2012) Anal Chem , vol.84 , pp. 9655-9662
    • Toyama, A.1    Nakagawa, H.2    Matsuda, K.3    Sato, T.A.4    Nakamura, Y.5    Ueda, K.6
  • 116
    • 84862926505 scopus 로고    scopus 로고
    • Ultrasmall gold nanoparticles for highly specific isolation/enrichment of N-linked glycosylated peptides
    • Tran TH, Park S, Lee H, Park S, Kim B, Kim OH, Oh BC, Lee D, Lee H. 2012. Ultrasmall gold nanoparticles for highly specific isolation/enrichment of N-linked glycosylated peptides. Analyst 137:991-998.
    • (2012) Analyst , vol.137 , pp. 991-998
    • Tran, T.H.1    Park, S.2    Lee, H.3    Park, S.4    Kim, B.5    Kim, O.H.6    Oh, B.C.7    Lee, D.8    Lee, H.9
  • 117
    • 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 TA, Nakamura Y, Daigo Y. 2007. 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 6:3475-3483.
    • (2007) J Proteome Res , vol.6 , 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
  • 119
    • 84991541846 scopus 로고    scopus 로고
    • Label-free analysis of O-glycosylation site-occupancy based on the signal intensity of glycopeptide/peptide ions
    • Wada Y. 2012. Label-free analysis of O-glycosylation site-occupancy based on the signal intensity of glycopeptide/peptide ions. Mass Spectrom 1:A0008.
    • (2012) Mass Spectrom , vol.1
    • Wada, Y.1
  • 120
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada Y, Tajiri M, Yoshida S. 2004. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal Chem 76:6560-6565.
    • (2004) Anal Chem , vol.76 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 123
    • 77949862643 scopus 로고    scopus 로고
    • Quantitation of saccharide compositions of O-glycans by mass spectrometry of glycopeptides and its application to rheumatoid arthritis
    • Wada Y, Tajiri M, Ohshima S. 2010b. Quantitation of saccharide compositions of O-glycans by mass spectrometry of glycopeptides and its application to rheumatoid arthritis. J Proteome Res 9:1367-1373.
    • (2010) J Proteome Res , vol.9 , pp. 1367-1373
    • Wada, Y.1    Tajiri, M.2    Ohshima, S.3
  • 124
    • 80052327326 scopus 로고    scopus 로고
    • Stable-isotope labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry
    • Walker SH, Budhathoki-Uprety J, Novak BM, Muddiman DC. 2011. Stable-isotope labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry. Anal Chem 83:6738-6745.
    • (2011) Anal Chem , vol.83 , pp. 6738-6745
    • Walker, S.H.1    Budhathoki-Uprety, J.2    Novak, B.M.3    Muddiman, D.C.4
  • 125
    • 80054050510 scopus 로고    scopus 로고
    • Zirconia layer coated mesoporous silica microspheres as HILIC SPE materials for selective glycopeptide enrichment
    • Wan H, Yan J, Yu L, Sheng Q, Zhang X, Xue X, Li X, Liang X. 2011. Zirconia layer coated mesoporous silica microspheres as HILIC SPE materials for selective glycopeptide enrichment. Analyst 136:4422-4430.
    • (2011) Analyst , vol.136 , pp. 4422-4430
    • Wan, H.1    Yan, J.2    Yu, L.3    Sheng, Q.4    Zhang, X.5    Xue, X.6    Li, X.7    Liang, X.8
  • 126
    • 77955158545 scopus 로고    scopus 로고
    • Liquid chromatography electrospray ionization Fourier transform ion cyclotron resonance mass spectrometric characterization of N-linked glycans and glycopeptides
    • Wang X, Emmett MR, Marshall AG. 2010. Liquid chromatography electrospray ionization Fourier transform ion cyclotron resonance mass spectrometric characterization of N-linked glycans and glycopeptides. Anal Chem 82:6542-6548.
    • (2010) Anal Chem , vol.82 , pp. 6542-6548
    • Wang, X.1    Emmett, M.R.2    Marshall, A.G.3
  • 128
    • 65549120632 scopus 로고    scopus 로고
    • Comparative glycoproteomics: Approaches and applications
    • Wei X, Li L. 2009. Comparative glycoproteomics: Approaches and applications. Brief Funct Genomic Proteomic 8:104-113.
    • (2009) Brief Funct Genomic Proteomic , vol.8 , pp. 104-113
    • Wei, X.1    Li, L.2
  • 129
    • 77955164751 scopus 로고    scopus 로고
    • Characterization of murine brain membrane glycoproteins by detergent assisted lectin affinity chromatography
    • Wei X, Dulberger C, Li L. 2010. Characterization of murine brain membrane glycoproteins by detergent assisted lectin affinity chromatography. Anal Chem 82:6329-6333.
    • (2010) Anal Chem , vol.82 , pp. 6329-6333
    • Wei, X.1    Dulberger, C.2    Li, L.3
  • 130
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L, Vosseller K, Cole RN, Cronshaw JM, Matunis MJ, Hart GW. 2002. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol Cell Proteomics 1:791-804.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 131
  • 133
    • 84862954486 scopus 로고    scopus 로고
    • Equal ratio of graphite carbon to activated charcoal for enrichment of N-glycopeptides prior to matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification
    • Xin L, Zhang H, Liu H, Li Z. 2012. Equal ratio of graphite carbon to activated charcoal for enrichment of N-glycopeptides prior to matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification. Rapid Commun Mass Spectrom 26:269-274.
    • (2012) Rapid Commun Mass Spectrom , vol.26 , pp. 269-274
    • Xin, L.1    Zhang, H.2    Liu, H.3    Li, Z.4
  • 134
    • 77649160820 scopus 로고    scopus 로고
    • On-plate enrichment of glycopeptides by using boronic acid functionalized gold-coated Si wafer
    • Xu Y, Zhang L, Lu H, Yang P. 2010. On-plate enrichment of glycopeptides by using boronic acid functionalized gold-coated Si wafer. Proteomics 10:1079-1086.
    • (2010) Proteomics , vol.10 , pp. 1079-1086
    • Xu, Y.1    Zhang, L.2    Lu, H.3    Yang, P.4
  • 135
    • 82555168257 scopus 로고    scopus 로고
    • Synthesis and application of a macroporous boronate affinity monolithic column using a metal-organic gel as a porogenic template for the specific capture of glycoproteins
    • Yang F, Lin Z, He X, Chen L, Zhang Y. 2011. Synthesis and application of a macroporous boronate affinity monolithic column using a metal-organic gel as a porogenic template for the specific capture of glycoproteins. J Chromatogr A 1218:9194-9201.
    • (2011) J Chromatogr A , vol.1218 , pp. 9194-9201
    • Yang, F.1    Lin, Z.2    He, X.3    Chen, L.4    Zhang, Y.5
  • 136
    • 84876474385 scopus 로고    scopus 로고
    • Selective isolation and analysis of glycoprotein fractions and their glycomes from hepatocellular carcinoma sera
    • Yang G, Cui T, Wang Y, Sun S, Ma T, Wang T, Chen Q, Li Z. 2013. Selective isolation and analysis of glycoprotein fractions and their glycomes from hepatocellular carcinoma sera. Proteomics 13:1481-1498.
    • (2013) Proteomics , vol.13 , pp. 1481-1498
    • Yang, G.1    Cui, T.2    Wang, Y.3    Sun, S.4    Ma, T.5    Wang, T.6    Chen, Q.7    Li, Z.8
  • 137
    • 79957491752 scopus 로고    scopus 로고
    • Affinity entrapment of oligosaccharides and glycopeptides using free lectin solution
    • Yodoshi M, Oyama T, Masaki K, Kakehi K, Hayakawa T, Suzuki S. 2011. Affinity entrapment of oligosaccharides and glycopeptides using free lectin solution. Anal Sci 27:395-400.
    • (2011) Anal Sci , vol.27 , pp. 395-400
    • Yodoshi, M.1    Oyama, T.2    Masaki, K.3    Kakehi, K.4    Hayakawa, T.5    Suzuki, S.6
  • 140
    • 79959270103 scopus 로고    scopus 로고
    • A proteomics platform combining depletion, multi-lectin affinity chromatography (M-LAC), and isoelectric focusing to study the breast cancer proteome
    • Zeng Z, Hincapie M, Pitteri SJ, Hanash S, Schalkwijk J, Hogan JM, Wang H, Hancock WS. 2011. A proteomics platform combining depletion, multi-lectin affinity chromatography (M-LAC), and isoelectric focusing to study the breast cancer proteome. Anal Chem 83:4845-4854.
    • (2011) Anal Chem , vol.83 , pp. 4845-4854
    • Zeng, Z.1    Hincapie, M.2    Pitteri, S.J.3    Hanash, S.4    Schalkwijk, J.5    Hogan, J.M.6    Wang, H.7    Hancock, W.S.8
  • 141
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H, Li XJ, Martin DB, Aebersold R. 2003. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 21:660-666.
    • (2003) Nat Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 142
    • 79959229101 scopus 로고    scopus 로고
    • 18O into glycans for relative glycan quantitation
    • 18O into glycans for relative glycan quantitation. Anal Chem 83:4975-4981.
    • (2011) Anal Chem , vol.83 , pp. 4975-4981
    • Zhang, W.1    Wang, H.2    Tang, H.3    Yang, P.4
  • 143
    • 33947581026 scopus 로고    scopus 로고
    • N-linked glycosylation profiling of pancreatic cancer serum using capillary liquid phase separation coupled with mass spectrometric analysis
    • Zhao J, Qiu W, Simeone DM, Lubman DM. 2007. N-linked glycosylation profiling of pancreatic cancer serum using capillary liquid phase separation coupled with mass spectrometric analysis. J Proteome Res 6:1126-1138.
    • (2007) J Proteome Res , vol.6 , pp. 1126-1138
    • Zhao, J.1    Qiu, W.2    Simeone, D.M.3    Lubman, D.M.4
  • 144
    • 81255144234 scopus 로고    scopus 로고
    • Fragmentation and site-specific quantification of core fucosylated glycoprotein by multiple reaction monitoring-mass spectrometry
    • Zhao Y, Jia W, Wang J, Ying W, Zhang Y, Qian X. 2011a. Fragmentation and site-specific quantification of core fucosylated glycoprotein by multiple reaction monitoring-mass spectrometry. Anal Chem 83:8802-8809.
    • (2011) Anal Chem , vol.83 , pp. 8802-8809
    • Zhao, Y.1    Jia, W.2    Wang, J.3    Ying, W.4    Zhang, Y.5    Qian, X.6
  • 145
    • 79954430857 scopus 로고    scopus 로고
    • Reversed-phase depletion coupled with hydrophilic affinity enrichment for the selective isolation of N-linked glycopeptides by using Click OEG-CD matrix
    • Zhao Y, Yu L, Guo Z, Li X, Liang X. 2011b. Reversed-phase depletion coupled with hydrophilic affinity enrichment for the selective isolation of N-linked glycopeptides by using Click OEG-CD matrix. Anal Bioanal Chem 399:3359-3365.
    • (2011) Anal Bioanal Chem , vol.399 , pp. 3359-3365
    • Zhao, Y.1    Yu, L.2    Guo, Z.3    Li, X.4    Liang, X.5
  • 146
    • 39449132134 scopus 로고    scopus 로고
    • Synthesis and evaluation of superparamagnetic silica particles for extraction of glycopeptides in the microtiter plate format
    • Zou Z, Ibisate M, Zhou Y, Aebersold R, Xia Y, Zhang H. 2008. Synthesis and evaluation of superparamagnetic silica particles for extraction of glycopeptides in the microtiter plate format. Anal Chem 80:1228-1234.
    • (2008) Anal Chem , vol.80 , pp. 1228-1234
    • Zou, Z.1    Ibisate, M.2    Zhou, Y.3    Aebersold, R.4    Xia, Y.5    Zhang, H.6


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