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Volumn 9, Issue 1, 2010, Pages 104-112

Identification of N-glycan serum markers associated with hepatocellular carcinoma from mass spectrometry data

Author keywords

Biomarker discovery; Glycan biomarker; Hepatocellular carcinoma; Mass spectrometry; Recursive feature selection; Support vector machine

Indexed keywords

GLYCAN;

EID: 73649106224     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900397n     Document Type: Article
Times cited : (60)

References (46)
  • 1
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh, G.; Jefferis, R. Post-translational modifications in the context of therapeutic proteins. Nat. Biotechnol. 2006, 24 (10), 1241-52.
    • (2006) Nat. Biotechnol , vol.24 , Issue.10 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 2
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • Fuster, M. M.; Esko, J. D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 2005, 5 (7), 526-42.
    • (2005) Nat. Rev. Cancer , vol.5 , Issue.7 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 3
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation-- potential for therapeutics and diagnostics
    • Dube, D. H.; Bertozzi, C. R. Glycans in cancer and inflammation-- potential for therapeutics and diagnostics. Nat. Rev. Drug Discovery 2005, 4 (6), 477-88.
    • (2005) Nat. Rev. Drug Discovery , vol.4 , Issue.6 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 4
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • Kobata, A.; Amano, J. Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours. Immunol. Cell Biol. 2005, 83 (4), 429-39.
    • (2005) Immunol. Cell Biol , vol.83 , Issue.4 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 5
    • 0032845735 scopus 로고    scopus 로고
    • Carcinoembryonic antigen screening: Pros and cons
    • Macdonald, J. S. Carcinoembryonic antigen screening: pros and cons. Semin. Oncol. 1999, 26 (5), 556-60.
    • (1999) Semin. Oncol , vol.26 , Issue.5 , pp. 556-560
    • Macdonald, J.S.1
  • 7
    • 0037756682 scopus 로고    scopus 로고
    • Lectin and serum-PSA interaction as a screening test for prostate cancer
    • Basu, P. S.; Majhi, R.; Batabyal, S. K. Lectin and serum-PSA interaction as a screening test for prostate cancer. Clin. Biochem. 2003, 36 (5), 373-6.
    • (2003) Clin. Biochem , vol.36 , Issue.5 , pp. 373-376
    • Basu, P.S.1    Majhi, R.2    Batabyal, S.K.3
  • 8
    • 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, D. J.; Dwek, R. A.; Rudd, P. M.; de Llorens, R. Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins. Glycobiology 2003, 13 (6), 457-70.
    • (2003) Glycobiology , vol.13 , Issue.6 , 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
  • 9
    • 61849174789 scopus 로고    scopus 로고
    • Glycoproteomics for Prostate Cancer Detection: Changes in Serum PSA Glycosylation Patterns
    • Meany, D. L.; Zhang, Z.; Sokoll, L. J.; Zhang, H.; Chan, D. W. Glycoproteomics for Prostate Cancer Detection: Changes in Serum PSA Glycosylation Patterns. J. Proteome Res. 2009, 8 (2), 613-9.
    • (2009) J. Proteome Res , vol.8 , Issue.2 , pp. 613-619
    • Meany, D.L.1    Zhang, Z.2    Sokoll, L.J.3    Zhang, H.4    Chan, D.W.5
  • 11
    • 22244464888 scopus 로고    scopus 로고
    • Glypican-3 and alphafetoprotein as diagnostic tests for hepatocellular carcinoma
    • Filmus, J.; Capurro, M. Glypican-3 and alphafetoprotein as diagnostic tests for hepatocellular carcinoma. Mol. Diagn. 2004, 8 (4), 207-12.
    • (2004) Mol. Diagn , vol.8 , Issue.4 , pp. 207-212
    • Filmus, J.1    Capurro, M.2
  • 12
    • 29144508692 scopus 로고    scopus 로고
    • Bayesian neural network approaches to ovarian cancer identification from high-resolution mass spectrometry data
    • Suppl 1, i487-94
    • Yu, J.; Chen, X. W. Bayesian neural network approaches to ovarian cancer identification from high-resolution mass spectrometry data. Bioinformatics 2005, 21 (Suppl 1), i487-94.
    • (2005) Bioinformatics , vol.21
    • Yu, J.1    Chen, X.W.2
  • 15
    • 0141738784 scopus 로고    scopus 로고
    • Comparison of statistical methods for classification of ovarian cancer using mass spectrometry data
    • Wu, B.; Abbott, T.; Fishman, D.; McMurray, W.; Mor, G.; Stone, K.; Ward, D.; Williams, K.; Zhao, H. Comparison of statistical methods for classification of ovarian cancer using mass spectrometry data. Bioinformatics 2003, 19 (13), 1636-43.
    • (2003) Bioinformatics , vol.19 , Issue.13 , pp. 1636-1643
    • Wu, B.1    Abbott, T.2    Fishman, D.3    McMurray, W.4    Mor, G.5    Stone, K.6    Ward, D.7    Williams, K.8    Zhao, H.9
  • 16
    • 35448932757 scopus 로고    scopus 로고
    • Derivation of stable microarray cancerdifferentiating signatures using consensus scoring of multiple random sampling and gene-ranking consistency evaluation
    • Tang, Z. Q.; Han, L. Y.; Lin, H. H.; Cui, J.; Jia, J.; Low, B. C.; Li, B. W.; Chen, Y. Z. Derivation of stable microarray cancerdifferentiating signatures using consensus scoring of multiple random sampling and gene-ranking consistency evaluation. Cancer Res. 2007, 67 (20), 9996-10003.
    • (2007) Cancer Res , vol.67 , Issue.20 , pp. 9996-10003
    • Tang, Z.Q.1    Han, L.Y.2    Lin, H.H.3    Cui, J.4    Jia, J.5    Low, B.C.6    Li, B.W.7    Chen, Y.Z.8
  • 17
    • 54749109964 scopus 로고    scopus 로고
    • Analysis of metabolomic data using support vector machines
    • Mahadevan, S.; Shah, S. L.; Marrie, T. J.; Slupsky, C. M. Analysis of metabolomic data using support vector machines. Anal. Chem. 2008, 80 (19), 7562-70.
    • (2008) Anal. Chem , vol.80 , Issue.19 , pp. 7562-7570
    • Mahadevan, S.1    Shah, S.L.2    Marrie, T.J.3    Slupsky, C.M.4
  • 22
    • 27744591857 scopus 로고    scopus 로고
    • New hyphenated methodologies in high-sensitivity glycoprotein analysis
    • Novotny, M. V.; Mechref, Y. New hyphenated methodologies in high-sensitivity glycoprotein analysis. J. Sep. Sci. 2005, 28 (15), 1956-68.
    • (2005) J. Sep. Sci , vol.28 , Issue.15 , pp. 1956-1968
    • Novotny, M.V.1    Mechref, Y.2
  • 24
    • 18744411077 scopus 로고    scopus 로고
    • Improved peak detection and quantification of mass spectrometry data acquired from surface-enhanced laser desorption and ionization by denoising spectra with the undecimated discrete wavelet transform
    • Coombes, K. R.; Tsavachidis, S.; Morris, J. S.; Baggerly, K. A.; Hung, M. C.; Kuerer, H. M. Improved peak detection and quantification of mass spectrometry data acquired from surface-enhanced laser desorption and ionization by denoising spectra with the undecimated discrete wavelet transform. Proteomics 2005, 5 (16), 4107-17.
    • (2005) Proteomics , vol.5 , Issue.16 , pp. 4107-4117
    • Coombes, K.R.1    Tsavachidis, S.2    Morris, J.S.3    Baggerly, K.A.4    Hung, M.C.5    Kuerer, H.M.6
  • 25
    • 25144448206 scopus 로고    scopus 로고
    • Algorithms for alignment of mass spectrometry proteomic data
    • Jeffries, N. Algorithms for alignment of mass spectrometry proteomic data. Bioinformatics 2005, 21 (14), 3066-73.
    • (2005) Bioinformatics , vol.21 , Issue.14 , pp. 3066-3073
    • Jeffries, N.1
  • 29
    • 53749104774 scopus 로고    scopus 로고
    • Computational prediction of human proteins that can be secreted into the bloodstream
    • Cui, J.; Liu, Q.; Puett, D.; Xu, Y. Computational prediction of human proteins that can be secreted into the bloodstream. Bioinformatics 2008, 24 (20), 2370-5.
    • (2008) Bioinformatics , vol.24 , Issue.20 , pp. 2370-2375
    • Cui, J.1    Liu, Q.2    Puett, D.3    Xu, Y.4
  • 31
    • 0037822222 scopus 로고    scopus 로고
    • Asymptotic behaviors of support vector machines with Gaussian kernel
    • Keerthi, S. S.; Lin, C. J. Asymptotic behaviors of support vector machines with Gaussian kernel. Neural Comput. 2003, 15 (7), 1667-89.
    • (2003) Neural Comput , vol.15 , Issue.7 , pp. 1667-1689
    • Keerthi, S.S.1    Lin, C.J.2
  • 33
    • 0031991256 scopus 로고    scopus 로고
    • Mass spectrometric mapping and sequencing of N-linked oligosaccharides derived from submicrogram amounts of glycoproteins
    • Mechref, Y.; Novotny, M. V. Mass spectrometric mapping and sequencing of N-linked oligosaccharides derived from submicrogram amounts of glycoproteins. Anal. Chem. 1998, 70 (3), 455-63.
    • (1998) Anal. Chem , vol.70 , Issue.3 , pp. 455-463
    • Mechref, Y.1    Novotny, M.V.2
  • 34
    • 0036084258 scopus 로고    scopus 로고
    • Therapeutic Target Database
    • Chen, X.; Ji, Z. L.; Chen, Y. Z. TTD: Therapeutic Target Database. Nucleic Acids Res. 2002, 30 (1), 412-5.
    • (2002) Nucleic Acids Res , vol.30 , Issue.1 , pp. 412-415
    • Chen, X.1    Ji, Z.L.2    Chen, Y.Z.T.3
  • 35
    • 0020491102 scopus 로고
    • Structural studies of the endoglycosidase H-resistant oligosaccharides present on human beta-glucuronidase
    • Howard, D. R.; Natowicz, M.; Baenziger, J. U. Structural studies of the endoglycosidase H-resistant oligosaccharides present on human beta-glucuronidase. J. Biol. Chem. 1982, 257 (18), 10861-8.
    • (1982) J. Biol. Chem , vol.257 , Issue.18 , pp. 10861-10868
    • Howard, D.R.1    Natowicz, M.2    Baenziger, J.U.3
  • 36
    • 0027526896 scopus 로고
    • An N-terminal glycosylation signal on cytochrome P450 is restricted to the endoplasmic reticulum in a luminal orientation
    • Szczesna-Skorupa, E.; Kemper, B. An N-terminal glycosylation signal on cytochrome P450 is restricted to the endoplasmic reticulum in a luminal orientation. J. Biol. Chem. 1993, 268 (3), 1757-62.
    • (1993) J. Biol. Chem , vol.268 , Issue.3 , pp. 1757-1762
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 37
    • 0025992391 scopus 로고
    • Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy
    • Weisshaar, G.; Hiyama, J.; Renwick, A. G. Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy. Glycobiology 1991, 1 (4), 393-404.
    • (1991) Glycobiology , vol.1 , Issue.4 , pp. 393-404
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.3
  • 38
    • 0023243297 scopus 로고
    • Systematic fractionation of oligosaccharides of human immunoglobulin G by serial affinity chromatography on immobilized lectin columns
    • Harada, H.; Kamei, M.; Tokumoto, Y.; Yui, S.; Koyama, F.; Kochibe, N.; Endo, T.; Kobata, A. Systematic fractionation of oligosaccharides of human immunoglobulin G by serial affinity chromatography on immobilized lectin columns. Anal. Biochem. 1987, 164 (2), 374-81.
    • (1987) Anal. Biochem , vol.164 , Issue.2 , pp. 374-381
    • Harada, H.1    Kamei, M.2    Tokumoto, Y.3    Yui, S.4    Koyama, F.5    Kochibe, N.6    Endo, T.7    Kobata, A.8
  • 39
    • 0024617469 scopus 로고
    • Structural analysis of carbohydrate chains of normal and myeloma immunoglobulins G using HPLC]
    • Arbatskii, N. P.; Martynova, M. D.; Aleshkin, V. A.; Derevitskaia, V. A. [Structural analysis of carbohydrate chains of normal and myeloma immunoglobulins G using HPLC]. Bioorg. Khim 1989, 15 (2), 175-80.
    • (1989) Bioorg. Khim , vol.15 , Issue.2 , pp. 175-180
    • Arbatskii, N.P.1    Martynova, M.D.2    Aleshkin, V.A.3    Derevitskaia, V.A.4
  • 40
    • 0021774503 scopus 로고
    • Possible role for peptide-oligosaccharide interactions in differential oligosaccharide processing at asparagine-107 of the light chain and asparagine-297 of the heavy chain in a monoclonal IgG1 kappa
    • Savvidou, G.; Klein, M.; Grey, A. A.; Dorrington, K. J.; Carver, J. P. Possible role for peptide-oligosaccharide interactions in differential oligosaccharide processing at asparagine-107 of the light chain and asparagine-297 of the heavy chain in a monoclonal IgG1 kappa. Biochemistry 1984, 23 (16), 3736-40.
    • (1984) Biochemistry , vol.23 , Issue.16 , pp. 3736-3740
    • Savvidou, G.1    Klein, M.2    Grey, A.A.3    Dorrington, K.J.4    Carver, J.P.5
  • 41
    • 0021916168 scopus 로고
    • Structures of the carbohydrate moieties of two monoclonal human lambda-type immunoglobulin light chains
    • Ohkura, T.; Isobe, T.; Yamashita, K.; Kobata, A. Structures of the carbohydrate moieties of two monoclonal human lambda-type immunoglobulin light chains. Biochemistry 1985, 24 (2), 503-8.
    • (1985) Biochemistry , vol.24 , Issue.2 , pp. 503-508
    • Ohkura, T.1    Isobe, T.2    Yamashita, K.3    Kobata, A.4
  • 42
    • 0024409951 scopus 로고
    • The structures of the asparagine-linked sugar chains of human apolipoprotein B-100
    • Taniguchi, T.; Ishikawa, Y.; Tsunemitsu, M.; Fukuzaki, H. The structures of the asparagine-linked sugar chains of human apolipoprotein B-100. Arch. Biochem. Biophys. 1989, 273 (1), 197-205.
    • (1989) Arch. Biochem. Biophys , vol.273 , Issue.1 , pp. 197-205
    • Taniguchi, T.1    Ishikawa, Y.2    Tsunemitsu, M.3    Fukuzaki, H.4
  • 43
    • 0020586243 scopus 로고
    • Comparative study of the carbohydrate moieties of normal and pathological human immunoglobulins M
    • Cahour, A.; Debeire, P.; Hartmann, L.; Montreuil, J. Comparative study of the carbohydrate moieties of normal and pathological human immunoglobulins M. Biochem. J. 1983, 211 (1), 55-63.
    • (1983) Biochem. J , vol.211 , Issue.1 , pp. 55-63
    • Cahour, A.1    Debeire, P.2    Hartmann, L.3    Montreuil, J.4
  • 44
    • 0026557394 scopus 로고
    • Glycosylation of interleukin-6 purified from normal human blood mononuclear cells
    • Parekh, R. B.; Dwek, R. A.; Rademacher, T. W.; Opdenakker, G.; Van Damme, J. Glycosylation of interleukin-6 purified from normal human blood mononuclear cells. Eur. J. Biochem. 1992, 203 (1-2), 135-41.
    • (1992) Eur. J. Biochem , vol.203 , Issue.1-2 , pp. 135-141
    • Parekh, R.B.1    Dwek, R.A.2    Rademacher, T.W.3    Opdenakker, G.4    Van Damme, J.5
  • 45
    • 0026641016 scopus 로고
    • Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody
    • Patel, T. P.; Parekh, R. B.; Moellering, B. J.; Prior, C. P. Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody. Biochem. J. 1992, 285 (Pt 3), 839-45.
    • (1992) Biochem. J , vol.285 , Issue.PART 3 , pp. 839-845
    • Patel, T.P.1    Parekh, R.B.2    Moellering, B.J.3    Prior, C.P.4
  • 46
    • 0027136155 scopus 로고
    • Structural study of the sugar chains of human leukocyte common antigen CD45
    • Sato, T.; Furukawa, K.; Autero, M.; Gahmberg, C. G.; Kobata, A. Structural study of the sugar chains of human leukocyte common antigen CD45. Biochemistry 1993, 32 (47), 12694-704.
    • (1993) Biochemistry , vol.32 , Issue.47 , pp. 12694-12704
    • Sato, T.1    Furukawa, K.2    Autero, M.3    Gahmberg, C.G.4    Kobata, A.5


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