메뉴 건너뛰기




Volumn 10, Issue 1, 2011, Pages

Mass spectrometry based glycoproteomics - From a proteomics perspective

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; BIOLOGICAL MARKER; PROTEOME;

EID: 78651105000     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.R110.003251     Document Type: Review
Times cited : (215)

References (216)
  • 1
    • 0035170507 scopus 로고    scopus 로고
    • GlycoSuiteDB: A new curated relational database of glycoprotein glycan structures and their biological sources
    • Cooper, C. A., Harrison, M. J., Wilkins, M. R., and Packer, N. H. (2001) GlycoSuiteDB: a new curated relational database of glycoprotein glycan structures and their biological sources. Nucleic Acids Res. 29, 332-335
    • (2001) Nucleic Acids Res. , vol.29 , pp. 332-335
    • Cooper, C.A.1    Harrison, M.J.2    Wilkins, M.R.3    Packer, N.H.4
  • 2
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd, P. M., and Dwek, R. A. (1997) Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32, 1-100
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 5
    • 0024695270 scopus 로고
    • Altered glycosylation of surface glycoproteins in tumor cells and its clinical application
    • Kobata, A. (1989) Altered glycosylation of surface glycoproteins in tumor cells and its clinical application. Pigment Cell Res. 2, 304-308
    • (1989) Pigment Cell Res. , vol.2 , pp. 304-308
    • Kobata, A.1
  • 6
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • Kobata, A., and Amano, J. (2005) Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours. Immunol. Cell Biol. 83, 429-439
    • (2005) Immunol. Cell Biol. , vol.83 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 7
    • 62549156308 scopus 로고    scopus 로고
    • The potentials of glycomics in biomarker discovery
    • Kam, R. K. T., and Poon, T. C. W. (2008) The potentials of glycomics in biomarker discovery. Clin. Proteom. 4, 67-79
    • (2008) Clin. Proteom. , vol.4 , pp. 67-79
    • Kam, R.K.T.1    Poon, T.C.W.2
  • 8
    • 6444222045 scopus 로고    scopus 로고
    • Glycomics: A pathway to a class of new and improved therapeutics
    • DOI 10.1038/nrd1521
    • Shriver, Z., Raguram, S., and Sasisekharan, R. (2004) Glycomics: a pathway to a class of new and improved therapeutics. Nat. Rev. Drug Discov. 3, 863-873 (Pubitemid 39405947)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.10 , pp. 863-873
    • Shriver, Z.1    Raguram, S.2    Sasisekharan, R.3
  • 9
    • 33750966067 scopus 로고    scopus 로고
    • Glyconutrients: The state of the science and the impact of glycomics
    • NY
    • Sierpina, V. S., and Murray, R. K. (2006) Glyconutrients: the state of the science and the impact of glycomics. Explore (NY) 2, 488-494
    • (2006) Explore , vol.2 , pp. 488-494
    • Sierpina, V.S.1    Murray, R.K.2
  • 10
    • 50449096184 scopus 로고    scopus 로고
    • Toward cancer biomarker discovery using the glycomics approach
    • Taniguchi, N. (2008) Toward cancer biomarker discovery using the glycomics approach. Proteomics 8, 3205-3208
    • (2008) Proteomics , vol.8 , pp. 3205-3208
    • Taniguchi, N.1
  • 12
    • 1642309129 scopus 로고    scopus 로고
    • Glycosylation defining cancer cell motility and invasiveness
    • Ono, M., and Hakomori, S. (2004) Glycosylation defining cancer cell motility and invasiveness. Glycoconj. J. 20, 71-78
    • (2004) Glycoconj. J. , vol.20 , pp. 71-78
    • Ono, M.1    Hakomori, S.2
  • 13
    • 10044265684 scopus 로고    scopus 로고
    • Glycoprotein tumor antigens for immunotherapy of breast cancer
    • Vlad, A. M., and Finn, O. J. (2004) Glycoprotein tumor antigens for immunotherapy of breast cancer. Breast Dis. 20, 73-79
    • (2004) Breast Dis. , vol.20 , pp. 73-79
    • Vlad, A.M.1    Finn, O.J.2
  • 14
    • 28544446695 scopus 로고    scopus 로고
    • Biomarkers in cancer staging, prognosis and treatment selection
    • Ludwig, J. A., and Weinstein, J. N. (2005) Biomarkers in cancer staging, prognosis and treatment selection. Nat. Rev. Cancer 5, 845-856
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 845-856
    • Ludwig, J.A.1    Weinstein, J.N.2
  • 15
    • 85128759053 scopus 로고    scopus 로고
    • A list of candidate cancer biomarkers for targeted proteomics
    • Polanski, M., and Anderson, N. L. (2007) A list of candidate cancer biomarkers for targeted proteomics. Biomark. Insights. 1, 1-48
    • (2007) Biomark. Insights. , vol.1 , pp. 1-48
    • Polanski, M.1    Anderson, N.L.2
  • 18
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: The long and uncertain path to clinical utility
    • Rifai, N., Gillette, M. A., and Carr, S. A. (2006) Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat. Biotechnol. 24, 971-983
    • (2006) Nat. Biotechnol. , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 19
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause, E. (1983) Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem. J. 209, 331-336
    • (1983) Biochem. J. , vol.209 , pp. 331-336
    • Bause, E.1
  • 20
    • 65549120632 scopus 로고    scopus 로고
    • Comparative glycoproteomics: Approaches and applications
    • Wei, X., and 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
  • 21
    • 70349684668 scopus 로고    scopus 로고
    • Thiyl glycosylation of olefinic proteins: S-linked glycoconjugate synthesis
    • Floyd, N., Vijayakrishnan, B., Koeppe, J. R., and Davis, B. G. (2009) Thiyl glycosylation of olefinic proteins: S-linked glycoconjugate synthesis. Angew. Chem. Int. Ed Engl. 48, 7798-7802
    • (2009) Angew. Chem. Int. Ed Engl. , vol.48 , pp. 7798-7802
    • Floyd, N.1    Vijayakrishnan, B.2    Koeppe, J.R.3    Davis, B.G.4
  • 22
    • 0015087975 scopus 로고
    • Identification in urine of a low-molecular-weight highly polar glycopeptide containing cysteinyl-galactose
    • Lote, C. J., and Weiss, J. B. (1971) Identification in urine of a low-molecular-weight highly polar glycopeptide containing cysteinyl-galactose. Biochem. J. 123, 25P
    • (1971) Biochem. J. , vol.123
    • Lote, C.J.1    Weiss, J.B.2
  • 23
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 24
    • 44949258057 scopus 로고    scopus 로고
    • An introduction to bioinformatics for glycomics research
    • Aoki-Kinoshita, K. F. (2008) An introduction to bioinformatics for glycomics research. PLoS. Comput. Biol. 4, e1000075
    • (2008) PLoS. Comput. Biol. , vol.4
    • Aoki-Kinoshita, K.F.1
  • 25
    • 33646108830 scopus 로고    scopus 로고
    • The role of informatics in glycobiology research with special emphasis on automatic interpretation of MS spectra
    • von der Lieth, C. W., Lütteke, T., and Frank, M. (2006) The role of informatics in glycobiology research with special emphasis on automatic interpretation of MS spectra. Biochim. Biophys. Acta 1760, 568-577
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 568-577
    • Von Der Lieth, C.W.1    Lütteke, T.2    Frank, M.3
  • 26
    • 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. (2009) Mass spectrometry in the analysis of N-linked and O-linked glycans. Curr. Opin. Struct. Biol. 19, 498-506
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 498-506
    • North, S.J.1    Hitchen, P.G.2    Haslam, S.M.3    Dell, A.4
  • 27
    • 43049127826 scopus 로고    scopus 로고
    • PeptideAtlas: A resource for target selection for emerging targeted proteomics workflows
    • Deutsch, E. W., Lam, H., and Aebersold, R. (2008) PeptideAtlas: a resource for target selection for emerging targeted proteomics workflows. EMBO Rep. 9, 429-434
    • (2008) EMBO Rep. , vol.9 , pp. 429-434
    • Deutsch, E.W.1    Lam, H.2    Aebersold, R.3
  • 28
    • 28444460388 scopus 로고    scopus 로고
    • Differential analysis of site-specific glycans on plasma and cellular fibronectins: Application of a hydrophilic affinity method for glycopeptide enrichment
    • Tajiri, M., Yoshida, S., and Wada, Y. (2005) Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment. Glycobiology 15, 1332-1340
    • (2005) Glycobiology , vol.15 , pp. 1332-1340
    • Tajiri, M.1    Yoshida, S.2    Wada, Y.3
  • 30
    • 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. (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
  • 31
    • 33646873090 scopus 로고    scopus 로고
    • Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electrospray linear ion trap - Fourier transform mass spectrometry
    • DOI 10.1093/glycob/cwj091
    • Wang, Y., Wu, S. L., and Hancock, W. S. (2006) Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electrospray linear ion trap-Fourier transform mass spectrometry. Glycobiology 16, 514-523 (Pubitemid 43779047)
    • (2006) Glycobiology , vol.16 , Issue.6 , pp. 514-523
    • Wang, Y.1    Wu, S.-L.2    Hancock, W.S.3
  • 32
    • 0035836061 scopus 로고    scopus 로고
    • Proteomics of glycoproteins based on affinity selection of glycopeptides from tryptic digests
    • Geng, M., Zhang, X., Bina, M., and 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
  • 34
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multilectin affinity column
    • Yang, Z., and Hancock, W. S. (2004) Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multilectin affinity column. J. Chromatogr. A 1053, 79-88
    • (2004) J. Chromatogr. A , vol.1053 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 35
    • 33749537286 scopus 로고    scopus 로고
    • Targeted glycoproteomics: Serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome
    • Durham, M., and Regnier, F. E. (2006) Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome. J. Chromatogr. A 1132, 165-173
    • (2006) J. Chromatogr. A , vol.1132 , pp. 165-173
    • Durham, M.1    Regnier, F.E.2
  • 36
    • 18144419694 scopus 로고    scopus 로고
    • Use of multidimensional lectin affinity chromatography in differential glycoproteomics
    • Qiu, R., and Regnier, F. E. (2005) Use of multidimensional lectin affinity chromatography in differential glycoproteomics. Anal. Chem. 77, 2802-2809
    • (2005) Anal. Chem. , vol.77 , pp. 2802-2809
    • Qiu, R.1    Regnier, F.E.2
  • 37
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H., Li, X. J., Martin, D. B., and 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
  • 38
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu, T., Qian, W. J., Gritsenko, M. A., Camp, D. G., Monroe, M. E., Moore, R. J., and Smith, R. D. (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
  • 40
    • 33746542437 scopus 로고    scopus 로고
    • Isolation of glycoproteins and identification of their N-linked glycosylation sites
    • Zhang, H., and Aebersold, R. (2006) Isolation of glycoproteins and identification of their N-linked glycosylation sites. Methods Mol. Biol. 328, 177-185
    • (2006) Methods Mol. Biol. , vol.328 , pp. 177-185
    • Zhang, H.1    Aebersold, R.2
  • 41
    • 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. (2007) Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics. Mol. Cell Proteomics 6, 141-149
    • (2007) Mol. Cell Proteomics , vol.6 , 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
  • 42
    • 34547800600 scopus 로고    scopus 로고
    • Isolation of N-linked glycopeptides from plasma
    • Zhou, Y., Aebersold, R., and Zhang, H. (2007) Isolation of N-linked glycopeptides from plasma. Anal. Chem. 79, 5826-5837
    • (2007) Anal. Chem. , vol.79 , pp. 5826-5837
    • Zhou, Y.1    Aebersold, R.2    Zhang, H.3
  • 43
    • 23944469911 scopus 로고    scopus 로고
    • A study of glycoproteins in human serum and plasma reference standards (HUPO) using multilectin affinity chromatography coupled with RPLC-MS/MS
    • DOI 10.1002/pmic.200401190
    • Yang, Z., Hancock, W. S., Chew, T. R., and Bonilla, L. (2005) A study of glycoproteins in human serum and plasma reference standards (HUPO) using multilectin affinity chromatography coupled with RPLC-MS/MS. Proteomics. 5, 3353-3366 (Pubitemid 41192041)
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3353-3366
    • Yang, Z.1    Hancock, W.S.2    Chew, T.R.3    Bonilla, L.4
  • 44
    • 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., and 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
  • 45
    • 33746318976 scopus 로고    scopus 로고
    • Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles
    • Sparbier, K., Wenzel, T., and Kostrzewa, M. (2006) Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 840, 29-36
    • (2006) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.840 , pp. 29-36
    • Sparbier, K.1    Wenzel, T.2    Kostrzewa, M.3
  • 46
    • 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., 3rd, Guo, Y., Warren, N.L., Orlando, R., and Pierce, M. (2006) Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites. J. Proteome Res. 5, 701-708
    • (2006) J. Proteome Res. , vol.5 , pp. 701-708
    • Alvarez-Manilla, G.1    Atwood III, J.2    Guo, Y.3    Warren, N.L.4    Orlando, R.5    Pierce, M.6
  • 47
    • 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
    • Hägglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., and 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
    • Hägglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 48
    • 14944367556 scopus 로고    scopus 로고
    • Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry
    • Larsen, M. R., Højrup, P., and Roepstorff, P. (2005) Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry. Mol. Cell Proteomics 4, 107-119
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 107-119
    • Larsen, M.R.1    Højrup, P.2    Roepstorff, P.3
  • 49
    • 0030069007 scopus 로고    scopus 로고
    • Fractionation of glycoprotein-derived oligosaccharides by affinity chromatography using immobilized lectin columns
    • Endo, T. (1996) Fractionation of glycoprotein-derived oligosaccharides by affinity chromatography using immobilized lectin columns. J. Chromatogr. A 720, 251-261
    • (1996) J. Chromatogr. A , vol.720 , pp. 251-261
    • Endo, T.1
  • 50
    • 0026138224 scopus 로고
    • Concanavalin a: A useful ligand for glycoenzyme immobilization-a review
    • Saleemuddin, M., and Husain, Q. (1991) Concanavalin A: a useful ligand for glycoenzyme immobilization-a review. Enzyme Microb. Technol. 13, 290-295
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 290-295
    • Saleemuddin, M.1    Husain, Q.2
  • 51
    • 0016662480 scopus 로고
    • The covalent and three-dimensional structure of concanavalin A. Structure of the monomer and its interactions with metals and saccharides
    • Becker, J. W., Reeke, G. N., Jr., and Wang, J. L., Cunningham, B. A., Edelman, G. M. (1975) The covalent and three-dimensional structure of concanavalin A. Structure of the monomer and its interactions with metals and saccharides. J. Biol. Chem. 250, 1513-1524
    • (1975) J. Biol. Chem. , vol.250 , pp. 1513-1524
    • Becker, J.W.1    Reeke Jr., G.N.2    Wang, J.L.3    Cunningham, B.A.4    Edelman, G.M.5
  • 52
    • 0025943451 scopus 로고
    • Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin
    • Bakry, N., Kamata, Y., and Simpson, L. L. (1991) Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin. J. Pharmacol. Exp. Ther. 258, 830-836
    • (1991) J. Pharmacol. Exp. Ther. , vol.258 , pp. 830-836
    • Bakry, N.1    Kamata, Y.2    Simpson, L.L.3
  • 53
    • 0030666267 scopus 로고    scopus 로고
    • Alterations in the O-linked glycosylation of IgA1 in children with Henoch-Schonlein purpura
    • Saulsbury, F. T. (1997) Alterations in the O-linked glycosylation of IgA1 in children with Henoch-Schonlein purpura. J. Rheumatol. 24, 2246-2249
    • (1997) J. Rheumatol. , vol.24 , pp. 2246-2249
    • Saulsbury, F.T.1
  • 54
    • 0020368287 scopus 로고
    • Fractionation of asparagine-linked oligosaccharides by serial lectin-Agarose affinity chromatography. A rapid, sensitive, and specific technique
    • Cummings, R. D., and Kornfeld, S. (1982) Fractionation of asparagine-linked oligosaccharides by serial lectin-Agarose affinity chromatography. A rapid, sensitive, and specific technique. J. Biol. Chem. 257, 11235-11240
    • (1982) J. Biol. Chem. , vol.257 , pp. 11235-11240
    • Cummings, R.D.1    Kornfeld, S.2
  • 55
    • 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. (2005) Comparative glycoproteomics of N-linked complex-type glycoforms containing sialic acid in human serum. Anal. Chem. 77, 7225-7231
    • (2005) Anal. Chem. , vol.77 , pp. 7225-7231
    • Qiu, R.1    Regnier, F.E.2
  • 57
    • 33745039982 scopus 로고    scopus 로고
    • Monitoring of glycoprotein products in cell culture lysates using lectin affinity chromatography and capillary HPLC coupled to electrospray linear ion trap-Fourier transform mass spectrometry (LTQ/FTMS)
    • Wang, Y., Wu, S. L., and Hancock, W. S. (2006) Monitoring of glycoprotein products in cell culture lysates using lectin affinity chromatography and capillary HPLC coupled to electrospray linear ion trap-Fourier transform mass spectrometry (LTQ/FTMS). Biotechnol. Prog. 22, 873-880
    • (2006) Biotechnol. Prog. , vol.22 , pp. 873-880
    • Wang, Y.1    Wu, S.L.2    Hancock, W.S.3
  • 58
    • 33749145859 scopus 로고    scopus 로고
    • Multilectin affinity chromatography for characterization of multiple glycoprotein biomarker candidates in serum from breast cancer patients
    • Yang, Z., Harris, L. E., Palmer-Toy, D. E., and Hancock, W. S. (2006) Multilectin affinity chromatography for characterization of multiple glycoprotein biomarker candidates in serum from breast cancer patients. Clin. Chem. 52, 1897-1905
    • (2006) Clin. Chem. , vol.52 , pp. 1897-1905
    • Yang, Z.1    Harris, L.E.2    Palmer-Toy, D.E.3    Hancock, W.S.4
  • 59
    • 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, W. S., and 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
  • 60
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg, J., Pilch, B. J., Podtelejnikov, A. V., and Wiśniewski, J. R. (2004) Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 4, 454-465
    • (2004) Proteomics , vol.4 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wiśniewski, J.R.4
  • 61
    • 37049026705 scopus 로고    scopus 로고
    • Identification of putative serum glycoprotein biomarkers for human lung adenocarcinoma by multilectin affinity chromatography and LC-MS/MS
    • Heo, S. H., Lee, S. J., Ryoo, H. M., Park, J. Y., and Cho, J. Y. (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
  • 62
    • 15744387329 scopus 로고    scopus 로고
    • Monitoring glycosylation pattern changes of glycoproteins using multi-lectin affinity chromatography
    • Yang, Z., and Hancock, W. S. (2005) Monitoring glycosylation pattern changes of glycoproteins using multi-lectin affinity chromatography. J. Chromatogr. A 1070, 57-64
    • (2005) J. Chromatogr. A , vol.1070 , pp. 57-64
    • Yang, Z.1    Hancock, W.S.2
  • 63
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wiśniewski, J. R., and Mann, M. (2010) Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 65
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano, C. D., Zambonin, C. G., and Jensen, O. N. (2008) Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry. J. Proteomics 71, 304-317
    • (2008) J. Proteomics , vol.71 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 66
    • 61849130124 scopus 로고    scopus 로고
    • Rat liver membrane glycoproteome: Enrichment by phase partitioning and glycoprotein capture
    • Lee, A., Kolarich, D., Haynes, P. A., Jensen, P. H., Baker, M. S., and Packer, N. H. (2009) Rat liver membrane glycoproteome: enrichment by phase partitioning and glycoprotein capture. J. Proteome Res. 8, 770-781
    • (2009) J. Proteome Res. , vol.8 , pp. 770-781
    • Lee, A.1    Kolarich, D.2    Haynes, P.A.3    Jensen, P.H.4    Baker, M.S.5    Packer, N.H.6
  • 67
    • 61649103556 scopus 로고    scopus 로고
    • Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome
    • McDonald, C. A., Yang, J. Y., Marathe, V., Yen, T. Y., and Macher, B. A. (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
  • 68
    • 0023127085 scopus 로고
    • Use of fluorescein hydrazide and fluorescein thiosemicarbazide reagents for the fluorometric determination of protein carbonyl groups and for the detection of oxidized protein on polyacrylamide gels
    • Ahn, B., Rhee, S. G., and Stadtman, E. R. (1987) Use of fluorescein hydrazide and fluorescein thiosemicarbazide reagents for the fluorometric determination of protein carbonyl groups and for the detection of oxidized protein on polyacrylamide gels. Anal. Biochem. 161, 245-257
    • (1987) Anal. Biochem. , vol.161 , pp. 245-257
    • Ahn, B.1    Rhee, S.G.2    Stadtman, E.R.3
  • 69
    • 34247464726 scopus 로고    scopus 로고
    • Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry
    • Meany, D. L., Xie, H., Thompson, L. V., Arriaga, E. A., and Griffin, T. J. (2007) Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry. Proteomics 7, 1150-1163
    • (2007) Proteomics , vol.7 , pp. 1150-1163
    • Meany, D.L.1    Xie, H.2    Thompson, L.V.3    Arriaga, E.A.4    Griffin, T.J.5
  • 70
    • 33846025822 scopus 로고    scopus 로고
    • Identification of yeast oxidized proteins: Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast
    • Mirzaei, H., and Regnier, F. (2007) Identification of yeast oxidized proteins: chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast. J. Chromatogr. A 1141, 22-31
    • (2007) J. Chromatogr. A , vol.1141 , pp. 22-31
    • Mirzaei, H.1    Regnier, F.2
  • 71
    • 0016219421 scopus 로고
    • The binding of boronic acids to chymotrypsin
    • Rawn, J. D., and Lienhard, G. E. (1974) The binding of boronic acids to chymotrypsin. Biochemistry 13, 3124-3130
    • (1974) Biochemistry , vol.13 , pp. 3124-3130
    • Rawn, J.D.1    Lienhard, G.E.2
  • 72
    • 0030046793 scopus 로고    scopus 로고
    • Characterization of protein glycosylation by mass spectrometry
    • Burlingame, A. L. (1996) Characterization of protein glycosylation by mass spectrometry. Curr. Opin. Biotechnol. 7, 4-10
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 4-10
    • Burlingame, A.L.1
  • 73
    • 14344257501 scopus 로고    scopus 로고
    • Proteomic analysis of glycosylation: Structural determination of N- and O-linked glycans by mass spectrometry
    • DOI 10.1586/14789450.2.1.87
    • Harvey, D. J. (2005) Proteomic analysis of glycosylation: structural determination of N- and O-linked glycans by mass spectrometry. Expert. Rev. Proteomics. 2, 87-101 (Pubitemid 40292582)
    • (2005) Expert Review of Proteomics , vol.2 , Issue.1 , pp. 87-101
    • Harvey, D.J.1
  • 74
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher, N. L. (2004) Top-down proteomics. Anal. Chem. 76, 197A-203A
    • (2004) Anal. Chem. , vol.76
    • Kelleher, N.L.1
  • 75
    • 0027462384 scopus 로고
    • Selective identification and differentiation of N- and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry
    • Carr, S. A., Huddleston, M. J., and Bean, M. F. (1993) Selective identification and differentiation of N- and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry. Protein Sci. 2, 183-196
    • (1993) Protein Sci. , vol.2 , pp. 183-196
    • Carr, S.A.1    Huddleston, M.J.2    Bean, M.F.3
  • 76
    • 0027586797 scopus 로고
    • Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: Methods for selective detection of glycopeptides in protein digests
    • Huddleston, M. J., Bean, M. F., and Carr, S. A. (1993) Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: methods for selective detection of glycopeptides in protein digests. Anal. Chem. 65, 877-884
    • (1993) Anal. Chem. , vol.65 , pp. 877-884
    • Huddleston, M.J.1    Bean, M.F.2    Carr, S.A.3
  • 77
    • 0028816610 scopus 로고
    • Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation
    • Kieliszewski, M. J., O'Neill, M., Leykam, J., and Orlando, R. (1995) Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation. J. Biol. Chem. 270, 2541-2549
    • (1995) J. Biol. Chem. , vol.270 , pp. 2541-2549
    • Kieliszewski, M.J.1    O'Neill, M.2    Leykam, J.3    Orlando, R.4
  • 79
    • 0024996989 scopus 로고
    • Characterization of O-glycosylation sites in recombinant B-chain of platelet-derived growth factor expressed in yeast using liquid secondary ion mass spectrometry, tandem mass spectrometry and Edman sequence analysis
    • Settineri, C. A., Medzihradszky, K. F., Masiarz, F. R., Burlingame, A. L., Chu, C., and George-Nascimento, C. (1990) Characterization of O-glycosylation sites in recombinant B-chain of platelet-derived growth factor expressed in yeast using liquid secondary ion mass spectrometry, tandem mass spectrometry and Edman sequence analysis. Biomed. Environ. Mass Spectrom. 19, 665-676
    • (1990) Biomed. Environ. Mass Spectrom. , vol.19 , pp. 665-676
    • Settineri, C.A.1    Medzihradszky, K.F.2    Masiarz, F.R.3    Burlingame, A.L.4    Chu, C.5    George-Nascimento, C.6
  • 80
    • 77249145900 scopus 로고    scopus 로고
    • Evaluation of the specific structures of IgA1 hinge glycopeptide in 30 IgA nephropathy patients by mass spectrometry
    • Odani, H., Yamamoto, K., Iwayama, S., Iwase, H., Takasaki, A., Takahashi, K., Fujita, Y., Sugiyama, S., and Hiki, Y. (2010) Evaluation of the specific structures of IgA1 hinge glycopeptide in 30 IgA nephropathy patients by mass spectrometry. J. Nephrol. 23, 70-76
    • (2010) J. Nephrol. , vol.23 , pp. 70-76
    • Odani, H.1    Yamamoto, K.2    Iwayama, S.3    Iwase, H.4    Takasaki, A.5    Takahashi, K.6    Fujita, Y.7    Sugiyama, S.8    Hiki, Y.9
  • 81
    • 66349099854 scopus 로고    scopus 로고
    • Hexose rearrangements upon fragmentation of N-glycopeptides and reductively aminated N-glycans
    • Wuhrer, M., Koeleman, C. A., and Deelder, A. M. (2009) Hexose rearrangements upon fragmentation of N-glycopeptides and reductively aminated N-glycans. Anal. Chem. 81, 4422-4432
    • (2009) Anal. Chem. , vol.81 , pp. 4422-4432
    • Wuhrer, M.1    Koeleman, C.A.2    Deelder, A.M.3
  • 82
    • 61849147415 scopus 로고    scopus 로고
    • Extracting both peptide sequence and glycan structural information by 157 nm photodissociation of N-linked glycopeptides
    • Zhang, L., and Reilly, J. P. (2009) Extracting both peptide sequence and glycan structural information by 157 nm photodissociation of N-linked glycopeptides. J. Proteome Res. 8, 734-742
    • (2009) J. Proteome Res. , vol.8 , pp. 734-742
    • Zhang, L.1    Reilly, J.P.2
  • 83
    • 33846200859 scopus 로고    scopus 로고
    • Pronase-immobilized enzyme reactor: An approach for automation in glycoprotein analysis by LC/LC-ESI/MSn
    • Temporini, C., Perani, E., Calleri, E., Dolcini, L., Lubda, D., Caccialanza, G., and Massolini, G. (2007) Pronase-immobilized enzyme reactor: an approach for automation in glycoprotein analysis by LC/LC-ESI/MSn. Anal. Chem. 79, 355-363
    • (2007) Anal. Chem. , vol.79 , pp. 355-363
    • Temporini, C.1    Perani, E.2    Calleri, E.3    Dolcini, L.4    Lubda, D.5    Caccialanza, G.6    Massolini, G.7
  • 84
    • 2642563583 scopus 로고    scopus 로고
    • Selective detection of glycopeptides on ion trap mass spectrometers
    • Sullivan, B., Addona, T. A., and Carr, S. A. (2004) Selective detection of glycopeptides on ion trap mass spectrometers. Anal. Chem. 76, 3112-3118
    • (2004) Anal. Chem. , vol.76 , pp. 3112-3118
    • Sullivan, B.1    Addona, T.A.2    Carr, S.A.3
  • 85
    • 33947204534 scopus 로고    scopus 로고
    • Electron transfer dissociation of N-glycopeptides: Loss of the entire N-glycosylated asparagine side chain
    • Catalina, M. I., Koeleman, C. A., Deelder, A. M., and Wuhrer, M. (2007) Electron transfer dissociation of N-glycopeptides: loss of the entire N-glycosylated asparagine side chain. Rapid Commun. Mass Spectrom. 21, 1053-1061
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 1053-1061
    • Catalina, M.I.1    Koeleman, C.A.2    Deelder, A.M.3    Wuhrer, M.4
  • 86
    • 3142669720 scopus 로고    scopus 로고
    • Determination of glycopeptide structures by multistage mass spectrometry with low-energy collision-induced dissociation: Comparison of electrospray ionization quadrupole ion trap and matrix-assisted laser desorption/ionization quadrupole ion trap reflectron time-of-flight approaches
    • Demelbauer, U. M., Zehl, M., Plematl, A., Allmaier, G., and Rizzi, A. (2004) Determination of glycopeptide structures by multistage mass spectrometry with low-energy collision-induced dissociation: comparison of electrospray ionization quadrupole ion trap and matrix-assisted laser desorption/ionization quadrupole ion trap reflectron time-of-flight approaches. Rapid Commun. Mass Spectrom. 18, 1575-1582
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 1575-1582
    • Demelbauer, U.M.1    Zehl, M.2    Plematl, A.3    Allmaier, G.4    Rizzi, A.5
  • 88
    • 67650354379 scopus 로고    scopus 로고
    • Identification of glycoproteins carrying a target glycan-motif by liquid chromatography/multiple-stage mass spectrometry: Identification of Lewis x-conjugated glycoproteins in mouse kidney
    • Hashii, N., Kawasaki, N., Itoh, S., Nakajima, Y., Harazono, A., Kawanishi, T., and Yamaguchi, T. (2009) Identification of glycoproteins carrying a target glycan-motif by liquid chromatography/multiple-stage mass spectrometry: identification of Lewis x-conjugated glycoproteins in mouse kidney. J. Proteome Res. 8, 3415-3429
    • (2009) J. Proteome Res. , vol.8 , pp. 3415-3429
    • Hashii, N.1    Kawasaki, N.2    Itoh, S.3    Nakajima, Y.4    Harazono, A.5    Kawanishi, T.6    Yamaguchi, T.7
  • 89
    • 31844444062 scopus 로고    scopus 로고
    • A novel approach for identification and characterization of glycoproteins using a hybrid linear ion trap/FT-ICR mass spectrometer
    • Peterman, S. M., and Mulholland, J. J. (2006) A novel approach for identification and characterization of glycoproteins using a hybrid linear ion trap/FT-ICR mass spectrometer. J. Am. Soc. Mass Spectrom. 17, 168-179
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 168-179
    • Peterman, S.M.1    Mulholland, J.J.2
  • 90
    • 33847347565 scopus 로고    scopus 로고
    • Structural analysis of O-glycopeptides employing negative- and positive-ion multi-stage mass spectra obtained by collision-induced and electron-capture dissociations in linear ion trap time-of-flight mass spectrometry
    • Deguchi, K., Ito, H., Baba, T., Hirabayashi, A., Nakagawa, H., Fumoto, M., Hinou, H., and Nishimura, S. (2007) Structural analysis of O-glycopeptides employing negative- and positive-ion multi-stage mass spectra obtained by collision-induced and electron-capture dissociations in linear ion trap time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 21, 691-698
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 691-698
    • Deguchi, K.1    Ito, H.2    Baba, T.3    Hirabayashi, A.4    Nakagawa, H.5    Fumoto, M.6    Hinou, H.7    Nishimura, S.8
  • 91
    • 33845314440 scopus 로고    scopus 로고
    • Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSn spectral matching
    • Ito, H., Takegawa, Y., Deguchi, K., Nagai, S., Nakagawa, H., and Shinohara, Y., Nishimura, S. (2006) Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSn spectral matching. Rapid Commun. Mass Spectrom. 20, 3557-3565
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 3557-3565
    • Ito, H.1    Takegawa, Y.2    Deguchi, K.3    Nagai, S.4    Nakagawa, H.5    Shinohara, Y.6    Nishimura, S.7
  • 92
    • 10844221548 scopus 로고    scopus 로고
    • Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry
    • Satomi, Y., Shimonishi, Y., Hase, T., and Takao, T. (2004) Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 18, 2983-2988
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 2983-2988
    • Satomi, Y.1    Shimonishi, Y.2    Hase, T.3    Takao, T.4
  • 93
    • 4944266697 scopus 로고    scopus 로고
    • N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin
    • Satomi, Y., Shimonishi, Y., and Takao, T. (2004) N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin. FEBS Lett. 576, 51-56
    • (2004) FEBS Lett. , vol.576 , pp. 51-56
    • Satomi, Y.1    Shimonishi, Y.2    Takao, T.3
  • 94
    • 27944462543 scopus 로고    scopus 로고
    • Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography-electrospray mass spectrometry
    • Imre, T., Schlosser, G., Pocsfalvi, G., Siciliano, R., Molnár-Szöllosi, E., Kremmer, T., Malorni, A., and Vékey, K. (2005) Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography-electrospray mass spectrometry. J. Mass Spectrom. 40, 1472-1483
    • (2005) J. Mass Spectrom. , vol.40 , pp. 1472-1483
    • Imre, T.1    Schlosser, G.2    Pocsfalvi, G.3    Siciliano, R.4    Molnár- Szöllosi, E.5    Kremmer, T.6    Malorni, A.7    Vékey, K.8
  • 95
    • 29244474577 scopus 로고    scopus 로고
    • Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry
    • Harazono, A., Kawasaki, N., Itoh, S., Hashii, N., Ishii-Watabe, A., Kawanishi, T., and Hayakawa, T. (2006) Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry. Anal. Biochem. 348, 259-268
    • (2006) Anal. Biochem. , vol.348 , pp. 259-268
    • Harazono, A.1    Kawasaki, N.2    Itoh, S.3    Hashii, N.4    Ishii-Watabe, A.5    Kawanishi, T.6    Hayakawa, T.7
  • 98
    • 33144484350 scopus 로고    scopus 로고
    • Determination and characterization of site-specific N-glycosylation using MALDI-Qq-TOF tandem mass spectrometry: Case study with a plant protease
    • Bykova, N. V., Rampitsch, C., Krokhin, O., Standing, K. G., and Ens, W. (2006) Determination and characterization of site-specific N-glycosylation using MALDI-Qq-TOF tandem mass spectrometry: case study with a plant protease. Anal. Chem. 78, 1093-1103
    • (2006) Anal. Chem. , vol.78 , pp. 1093-1103
    • Bykova, N.V.1    Rampitsch, C.2    Krokhin, O.3    Standing, K.G.4    Ens, W.5
  • 99
    • 4544337907 scopus 로고    scopus 로고
    • Site-specific N-glycosylation analysis: Matrix-assisted laser desorption/ionization quadrupole-quadrupole time-of-flight tandem mass spectral signatures for recognition and identification of glycopeptides
    • DOI 10.1002/rcm.1585
    • Krokhin, O., Ens, W., Standing, K. G., Wilkins, J., and Perreault, H. (2004) Site-specific N-glycosylation analysis: matrix-assisted laser desorption/ionization quadrupole-quadrupole time-of-flight tandem mass spectral signatures for recognition and identification of glycopeptides. Rapid Commun. Mass Spectrom. 18, 2020-2030 (Pubitemid 39222440)
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , Issue.18 , pp. 2020-2030
    • Krokhin, O.1    Ens, W.2    Standing, K.G.3    Wilkins, J.4    Perreault, H.5
  • 100
    • 33645740901 scopus 로고    scopus 로고
    • MALDI QqTOF MS combined with off-line HPLC for characterization of protein primary structure and post-translational modifications
    • Krokhin, O. V., Ens, W., and Standing, K. G. (2005) MALDI QqTOF MS combined with off-line HPLC for characterization of protein primary structure and post-translational modifications. J. Biomol. Tech. 16, 429-440
    • (2005) J. Biomol. Tech. , vol.16 , pp. 429-440
    • Krokhin, O.V.1    Ens, W.2    Standing, K.G.3
  • 103
    • 3543136464 scopus 로고    scopus 로고
    • Glycopeptide analysis by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry reveals novel features of horseradish peroxidase glycosylation
    • Wuhrer, M., Hokke, C. H., and Deelder, A. M. (2004) Glycopeptide analysis by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry reveals novel features of horseradish peroxidase glycosylation. Rapid Commun. Mass Spectrom. 18, 1741-1748
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 1741-1748
    • Wuhrer, M.1    Hokke, C.H.2    Deelder, A.M.3
  • 104
    • 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. (2008) 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. 19, 1209-1220
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , 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
  • 105
    • 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., and 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
  • 106
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon, B., and Costello, C. E. (1988) A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconjugate J. 5, 397-409
    • (1988) Glycoconjugate J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 107
    • 6044274617 scopus 로고    scopus 로고
    • Structural characterization of N-glycopeptides by matrix-dependent selective fragmentation of MALDI-TOF/TOF tandem mass spectrometry
    • Kurogochi, M., and Nishimura, S. (2004) Structural characterization of N-glycopeptides by matrix-dependent selective fragmentation of MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 76, 6097-6101
    • (2004) Anal. Chem. , vol.76 , pp. 6097-6101
    • Kurogochi, M.1    Nishimura, S.2
  • 108
    • 4544320924 scopus 로고    scopus 로고
    • Post-translational modifications on proteins: Facile and efficient procedure for the identification of O-glycosylation sites by MALDI-LIFT-TOF/TOF mass spectrometry
    • Kurogochi, M., Matsushita, T., and Nishimura, S. (2004) Post-translational modifications on proteins: facile and efficient procedure for the identification of O-glycosylation sites by MALDI-LIFT-TOF/TOF mass spectrometry. Angew. Chem. Int. Ed Engl. 43, 4071-4075
    • (2004) Angew. Chem. Int. Ed Engl. , vol.43 , pp. 4071-4075
    • Kurogochi, M.1    Matsushita, T.2    Nishimura, S.3
  • 110
    • 33645821470 scopus 로고    scopus 로고
    • Highly sensitive multistage mass spectrometry enables small-scale analysis of protein glycosylation from two-dimensional polyacrylamide gels
    • Takemori, N., Komori, N., and Matsumoto, H. (2006) Highly sensitive multistage mass spectrometry enables small-scale analysis of protein glycosylation from two-dimensional polyacrylamide gels. Electrophoresis 27, 1394-1406
    • (2006) Electrophoresis , vol.27 , pp. 1394-1406
    • Takemori, N.1    Komori, N.2    Matsumoto, H.3
  • 111
    • 19744375004 scopus 로고    scopus 로고
    • New features of site-specific horseradish peroxidase (HRP) glycosylation uncovered by nano-LC-MS with repeated ion-isolation/fragmentation cycles
    • Wuhrer, M., Balog, C. I., Koeleman, C. A., Deelder, A. M., and Hokke, C. H. (2005) New features of site-specific horseradish peroxidase (HRP) glycosylation uncovered by nano-LC-MS with repeated ion-isolation/fragmentation cycles. Biochim. Biophys. Acta 1723, 229-239
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 229-239
    • Wuhrer, M.1    Balog, C.I.2    Koeleman, C.A.3    Deelder, A.M.4    Hokke, C.H.5
  • 112
    • 33644839418 scopus 로고    scopus 로고
    • Infrared multiphoton dissociation and electron capture dissociation of high-mannose type glycopeptides
    • Adamson, J. T., and Håkansson, K. (2006) Infrared multiphoton dissociation and electron capture dissociation of high-mannose type glycopeptides. J. Proteome Res. 5, 493-501
    • (2006) J. Proteome Res. , vol.5 , pp. 493-501
    • Adamson, J.T.1    Håkansson, K.2
  • 113
    • 0035884155 scopus 로고    scopus 로고
    • Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information
    • Håkansson, K., Cooper, H. J., Emmett, M. R., Costello, C. E., Marshall, A. G., and Nilsson, C. L. (2001) Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information. Anal. Chem. 73, 4530-4536
    • (2001) Anal. Chem. , vol.73 , pp. 4530-4536
    • Håkansson, K.1    Cooper, H.J.2    Emmett, M.R.3    Costello, C.E.4    Marshall, A.G.5    Nilsson, C.L.6
  • 114
    • 0038676364 scopus 로고    scopus 로고
    • Combined electron capture and infrared multiphoton dissociation for multistage MS/MS in a Fourier transform ion cyclotron resonance mass spectrometer
    • Håkansson, K., Chalmers, M. J., Quinn, J. P., McFarland, M. A., Hendrickson, C. L., and Marshall, A. G. (2003) Combined electron capture and infrared multiphoton dissociation for multistage MS/MS in a Fourier transform ion cyclotron resonance mass spectrometer. Anal. Chem. 75, 3256-3262
    • (2003) Anal. Chem. , vol.75 , pp. 3256-3262
    • Håkansson, K.1    Chalmers, M.J.2    Quinn, J.P.3    McFarland, M.A.4    Hendrickson, C.L.5    Marshall, A.G.6
  • 117
    • 0012252007 scopus 로고    scopus 로고
    • Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage
    • Kjeldsen, F., Haselmann, K. F., Budnik, B. A., Sørensen, E. S., and Zubarev, R. A. (2003) Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage. Anal. Chem. 75, 2355-2361
    • (2003) Anal. Chem. , vol.75 , pp. 2355-2361
    • Kjeldsen, F.1    Haselmann, K.F.2    Budnik, B.A.3    Sørensen, E.S.4    Zubarev, R.A.5
  • 118
    • 0032731855 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer
    • Mirgorodskaya, E., Roepstorff, P., and Zubarev, R. A. (1999) Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer. Anal. Chem. 71, 4431-4436
    • (1999) Anal. Chem. , vol.71 , pp. 4431-4436
    • Mirgorodskaya, E.1    Roepstorff, P.2    Zubarev, R.A.3
  • 119
    • 29144433431 scopus 로고    scopus 로고
    • Electron capture dissociation of O-glycosylated peptides: Radical site-induced fragmentation of glycosidic bonds
    • Mormann, M., Paulsen, H., and Peter-Katalinic, J. (2005) Electron capture dissociation of O-glycosylated peptides: radical site-induced fragmentation of glycosidic bonds. Eur. J. Mass Spectrom. (Chichester, Eng) 11, 497-511
    • (2005) Eur. J. Mass Spectrom. (Chichester, Eng) , vol.11 , pp. 497-511
    • Mormann, M.1    Paulsen, H.2    Peter-Katalinic, J.3
  • 120
    • 21444448470 scopus 로고    scopus 로고
    • Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation fourier transform-ion cyclotron resonance mass spectrometry
    • Renfrow, M. B., Cooper, H. J., Tomana, M., Kulhavy, R., Hiki, Y., Toma, K., Emmett, M. R., Mestecky, J., Marshall, A. G., and Novak, J. (2005) Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation fourier transform-ion cyclotron resonance mass spectrometry. J. Biol. Chem. 280, 19136-19145
    • (2005) J. Biol. Chem. , vol.280 , pp. 19136-19145
    • Renfrow, M.B.1    Cooper, H.J.2    Tomana, M.3    Kulhavy, R.4    Hiki, Y.5    Toma, K.6    Emmett, M.R.7    Mestecky, J.8    Marshall, A.G.9    Novak, J.10
  • 121
    • 77949569318 scopus 로고    scopus 로고
    • A simple cellulose column procedure for selective enrichment of glycopeptides and characterization by nano LC coupled with electron-transfer and high-energy collisional-dissociation tandem mass spectrometry
    • Snovida, S. I., Bodnar, E. D., Viner, R., Saba, J., and Perreault, H. (2010) A simple cellulose column procedure for selective enrichment of glycopeptides and characterization by nano LC coupled with electron-transfer and high-energy collisional-dissociation tandem mass spectrometry. Carbohydr. Res. 345, 792-801
    • (2010) Carbohydr. Res. , vol.345 , pp. 792-801
    • Snovida, S.I.1    Bodnar, E.D.2    Viner, R.3    Saba, J.4    Perreault, H.5
  • 122
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • Darula, Z., and Medzihradszky, K. F. (2009) Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum. Mol. Cell Proteomics 8, 2515-2526
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 123
    • 60149111900 scopus 로고    scopus 로고
    • Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data
    • Alley, W. R., Jr., Mechref, Y., and Novotny, M. V. (2009) Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data. Rapid Commun. Mass Spectrom. 23, 161-170
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 161-170
    • Alley Jr., W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 124
    • 44249099705 scopus 로고    scopus 로고
    • Glycopeptide analysis by mass spectrometry
    • Dalpathado, D. S., and Desaire, H. (2008) Glycopeptide analysis by mass spectrometry. Analyst 133, 731-738
    • (2008) Analyst , vol.133 , pp. 731-738
    • Dalpathado, D.S.1    Desaire, H.2
  • 126
    • 0035894178 scopus 로고    scopus 로고
    • Capillary electrophoresis-electrospray mass spectrometry for the characterization of high-mannose-type N-glycosylation and differential oxidation in glycoproteins by charge reversal and protease/glycosidase digestion
    • Liu, T., Li, J. D., Zeng, R., Shao, X. X., Wang, K. Y., and Xia, Q. C. (2001) Capillary electrophoresis-electrospray mass spectrometry for the characterization of high-mannose-type N-glycosylation and differential oxidation in glycoproteins by charge reversal and protease/glycosidase digestion. Anal. Chem. 73, 5875-5885
    • (2001) Anal. Chem. , vol.73 , pp. 5875-5885
    • Liu, T.1    Li, J.D.2    Zeng, R.3    Shao, X.X.4    Wang, K.Y.5    Xia, Q.C.6
  • 127
    • 12244254420 scopus 로고    scopus 로고
    • Site-specific characterization of the N-linked oligosaccharides of a murine immunoglobulin M by high-performance liquid chromatography/electrospray mass spectrometry
    • DOI 10.1016/S0003-2697(02)00693-0
    • Wang, F., Nakouzi, A., Angeletti, R. H., and Casadevall, A. (2003) Site-specific characterization of the N-linked oligosaccharides of a murine immunoglobulin M by high-performance liquid chromatography/electrospray mass spectrometry. Anal. Biochem. 314, 266-280 (Pubitemid 36315909)
    • (2003) Analytical Biochemistry , vol.314 , Issue.2 , pp. 266-280
    • Wang, F.1    Nakouzi, A.2    Angeletti, R.H.3    Casadevall, A.4
  • 128
    • 33746034592 scopus 로고    scopus 로고
    • Comparative glycomics of the glycoprotein follicle stimulating hormone: Glycopeptide analysis of isolates from two mammalian species
    • Dalpathado, D. S., Irungu, J., Go, E. P., Butnev, V. Y., Norton, K., Bousfield, G. R., and Desaire, H. (2006) Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species. Biochemistry 45, 8665-8673
    • (2006) Biochemistry , vol.45 , pp. 8665-8673
    • Dalpathado, D.S.1    Irungu, J.2    Go, E.P.3    Butnev, V.Y.4    Norton, K.5    Bousfield, G.R.6    Desaire, H.7
  • 129
    • 33144474635 scopus 로고    scopus 로고
    • Method for characterizing sulfated glycoproteins in a glycosylation site-specific fashion, using ion pairing and tandem mass spectrometry
    • Irungu, J., Dalpathado, D. S., Go, E. P., Jiang, H., Ha, H. V., Bousfield, G. R., and Desaire, H. (2006) Method for characterizing sulfated glycoproteins in a glycosylation site-specific fashion, using ion pairing and tandem mass spectrometry. Anal. Chem. 78, 1181-1190
    • (2006) Anal. Chem. , vol.78 , pp. 1181-1190
    • Irungu, J.1    Dalpathado, D.S.2    Go, E.P.3    Jiang, H.4    Ha, H.V.5    Bousfield, G.R.6    Desaire, H.7
  • 130
    • 0012252007 scopus 로고    scopus 로고
    • Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage
    • Kjeldsen, F., Haselmann, K. F., Budnik, B. A., Sørensen, E. S., and Zubarev, R. A. (2003) Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage. Anal. Chem. 75, 2355-2361
    • (2003) Anal. Chem. , vol.75 , pp. 2355-2361
    • Kjeldsen, F.1    Haselmann, K.F.2    Budnik, B.A.3    Sørensen, E.S.4    Zubarev, R.A.5
  • 132
    • 0035567107 scopus 로고    scopus 로고
    • Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry
    • Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 12, 1106-1113
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 1106-1113
    • Chalkley, R.J.1    Burlingame, A.L.2
  • 133
    • 0031899415 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry
    • Hanisch, F. G., Green, B. N., Bateman, R., and Peter-Katalinic, J. (1998) Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry. J. Mass Spectrom. 33, 358-362
    • (1998) J. Mass Spectrom. , vol.33 , pp. 358-362
    • Hanisch, F.G.1    Green, B.N.2    Bateman, R.3    Peter-Katalinic, J.4
  • 134
    • 0141653189 scopus 로고    scopus 로고
    • Direct determination of glycosylation sites in O-fucosylated glycopeptides using nanoelectrospray quadrupole time-of-flight mass spectrometry
    • Macek, B., Hofsteenge, J., and Peter-Katalinić, J. (2001) Direct determination of glycosylation sites in O-fucosylated glycopeptides using nanoelectrospray quadrupole time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 15, 771-777
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 771-777
    • Macek, B.1    Hofsteenge, J.2    Peter-Katalinić, J.3
  • 135
    • 0030830164 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo
    • Müller, S., Goletz, S., Packer, N., Gooley, A., Lawson, A. M., and Hanisch, F. G. (1997) Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo. J. Biol. Chem. 272, 24780-24793
    • (1997) J. Biol. Chem. , vol.272 , pp. 24780-24793
    • Müller, S.1    Goletz, S.2    Packer, N.3    Gooley, A.4    Lawson, A.M.5    Hanisch, F.G.6
  • 136
    • 0033603316 scopus 로고    scopus 로고
    • High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells
    • Müller, S., Alving, K., Peter-Katalinic, J., Zachara, N., Gooley, A. A., and Hanisch, F. G. (1999) High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells. J. Biol. Chem. 274, 18165-18172
    • (1999) J. Biol. Chem. , vol.274 , pp. 18165-18172
    • Müller, S.1    Alving, K.2    Peter-Katalinic, J.3    Zachara, N.4    Gooley, A.A.5    Hanisch, F.G.6
  • 138
    • 35648982031 scopus 로고    scopus 로고
    • Site determination of protein glycosylation based on digestion with immobilized nonspecific proteases and Fourier transform ion cyclotron resonance mass spectrometry
    • Clowers, B. H., Dodds, E. D., Seipert, R. R., and Lebrilla, C. B. (2007) Site determination of protein glycosylation based on digestion with immobilized nonspecific proteases and Fourier transform ion cyclotron resonance mass spectrometry. J. Proteome Res. 6, 4032-4040
    • (2007) J. Proteome Res. , vol.6 , pp. 4032-4040
    • Clowers, B.H.1    Dodds, E.D.2    Seipert, R.R.3    Lebrilla, C.B.4
  • 139
    • 35648929345 scopus 로고    scopus 로고
    • Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: Implications for IgA nephropathy
    • Renfrow, M. B., Mackay, C. L., Chalmers, M. J., Julian, B. A., Mestecky, J., Kilian, M., Poulsen, K., Emmett, M. R., Marshall, A. G., and Novak, J. (2007) Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: implications for IgA nephropathy. Anal. Bioanal. Chem. 389, 1397-1407
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 1397-1407
    • Renfrow, M.B.1    Mackay, C.L.2    Chalmers, M.J.3    Julian, B.A.4    Mestecky, J.5    Kilian, M.6    Poulsen, K.7    Emmett, M.R.8    Marshall, A.G.9    Novak, J.10
  • 140
    • 62349122640 scopus 로고    scopus 로고
    • Localization of O-glycans in MUC1 glycoproteins using electron-capture dissociation fragmentation mass spectrometry
    • Sihlbom, C., van, Dijk Härd, I, Lidell, M. E., Noll, T., Hansson, G. C., and Bäckström, M. (2009) Localization of O-glycans in MUC1 glycoproteins using electron-capture dissociation fragmentation mass spectrometry. Glycobiology 19, 375-381
    • (2009) Glycobiology , vol.19 , pp. 375-381
    • Sihlbom, C.1    Van Dijk Härd, I.2    Lidell, M.E.3    Noll, T.4    Hansson, G.C.5    Bäckström, M.6
  • 142
    • 0037176224 scopus 로고    scopus 로고
    • Use of a lectin affinity selector in the search for unusual glycosylation in proteomics
    • Xiong, L., and Regnier, F. E. (2002) Use of a lectin affinity selector in the search for unusual glycosylation in proteomics. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 782, 405-418
    • (2002) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.782 , pp. 405-418
    • Xiong, L.1    Regnier, F.E.2
  • 143
  • 144
    • 0346256786 scopus 로고    scopus 로고
    • Deglycosylation of glycoproteins with trifluoromethanesulphonic acid: Elucidation of molecular structure and function
    • Edge, A. S. (2003) Deglycosylation of glycoproteins with trifluoromethanesulphonic acid: elucidation of molecular structure and function. Biochem. J. 376 (Pt 2), 339-350
    • (2003) Biochem. J. , vol.376 , Issue.PART 2 , pp. 339-350
    • Edge, A.S.1
  • 145
    • 0026556916 scopus 로고
    • A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins
    • Gerken, T. A., Gupta, R., and Jentoft, N. (1992) A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins. Biochemistry 31, 639-648
    • (1992) Biochemistry , vol.31 , pp. 639-648
    • Gerken, T.A.1    Gupta, R.2    Jentoft, N.3
  • 146
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry
    • Greis, K. D., Hayes, B. K., Comer, F. I., Kirk, M., Barnes, S., Lowary, T. L., and Hart, G. W. (1996) Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry. Anal. Biochem. 234, 38-49
    • (1996) Anal. Biochem. , vol.234 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4    Barnes, S.5    Lowary, T.L.6    Hart, G.W.7
  • 147
    • 0034441802 scopus 로고    scopus 로고
    • Alkali-catalyzed beta-elimination of periodate-oxidized glycans: A novel method of chemical deglycosylation of mucin gene products in paraffin embedded sections
    • Hong, J. C., and Kim, Y. S. (2000) Alkali-catalyzed beta-elimination of periodate-oxidized glycans: a novel method of chemical deglycosylation of mucin gene products in paraffin embedded sections. Glycoconj. J. 17, 691-703
    • (2000) Glycoconj. J. , vol.17 , pp. 691-703
    • Hong, J.C.1    Kim, Y.S.2
  • 148
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J., McCormack, A. L., and Yates, J. R., 3rd (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.L.2    Yates III, J.R.3
  • 149
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 150
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • Craig, R., and Beavis, R. C. (2004) TANDEM: matching proteins with tandem mass spectra. Bioinformatics. 20, 1466-1467
    • (2004) Bioinformatics. , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 151
    • 33644898528 scopus 로고    scopus 로고
    • Automated protein identification by tandem mass spectrometry: Issues and strategies
    • Hernandez, P., Müller, M., and Appel, R. D. (2006) Automated protein identification by tandem mass spectrometry: issues and strategies. Mass Spectrom. Rev. 25, 235-254
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 235-254
    • Hernandez, P.1    Müller, M.2    Appel, R.D.3
  • 152
    • 1042266254 scopus 로고    scopus 로고
    • Analysis, statistical validation and dissemination of large-scale proteomics datasets generated by tandem MS
    • Nesvizhskii, A. I., and Aebersold, R. (2004) Analysis, statistical validation and dissemination of large-scale proteomics datasets generated by tandem MS. Drug Discov. Today 9, 173-181
    • (2004) Drug Discov. Today , vol.9 , pp. 173-181
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 153
    • 35848929694 scopus 로고    scopus 로고
    • Analysis and validation of proteomic data generated by tandem mass spectrometry
    • Nesvizhskii, A. I., Vitek, O., and Aebersold, R. (2007) Analysis and validation of proteomic data generated by tandem mass spectrometry. Nat. Methods 4, 787-797
    • (2007) Nat. Methods , vol.4 , pp. 787-797
    • Nesvizhskii, A.I.1    Vitek, O.2    Aebersold, R.3
  • 154
    • 39049175370 scopus 로고    scopus 로고
    • Protein identification by tandem mass spectrometry and sequence database searching
    • Nesvizhskii, A. I. (2007) Protein identification by tandem mass spectrometry and sequence database searching. Methods Mol. Biol. 367, 87-119
    • (2007) Methods Mol. Biol. , vol.367 , pp. 87-119
    • Nesvizhskii, A.I.1
  • 156
    • 33745827045 scopus 로고    scopus 로고
    • Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: Application to pancreatic cancer serum
    • Zhao, J., Simeone, D. M., Heidt, D., Anderson, M. A., and Lubman, D. M. (2006) Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum. J. Proteome Res. 5, 1792-1802
    • (2006) J. Proteome Res. , vol.5 , pp. 1792-1802
    • Zhao, J.1    Simeone, D.M.2    Heidt, D.3    Anderson, M.A.4    Lubman, D.M.5
  • 157
    • 68549098240 scopus 로고    scopus 로고
    • Cell surface and secreted protein profiles of human thyroid cancer cell lines reveal distinct glycoprotein patterns
    • Arcinas, A., Yen, T. Y., Kebebew, E., and Macher, B. A. (2009) Cell surface and secreted protein profiles of human thyroid cancer cell lines reveal distinct glycoprotein patterns. J. Proteome Res. 8, 3958-3968
    • (2009) J. Proteome Res. , vol.8 , pp. 3958-3968
    • Arcinas, A.1    Yen, T.Y.2    Kebebew, E.3    Macher, B.A.4
  • 158
    • 68549135368 scopus 로고    scopus 로고
    • Mass spectrometry (LC-MS/MS) site-mapping of N-glycosylated membrane proteins for breast cancer biomarkers
    • Whelan, S. A., Lu, M., He, J., Yan, W., Saxton, R. E., Faull, K. F., Whitelegge, J. P., and Chang, H. R. (2009) Mass spectrometry (LC-MS/MS) site-mapping of N-glycosylated membrane proteins for breast cancer biomarkers. J. Proteome Res. 8, 4151-4160
    • (2009) J. Proteome Res. , vol.8 , pp. 4151-4160
    • Whelan, S.A.1    Lu, M.2    He, J.3    Yan, W.4    Saxton, R.E.5    Faull, K.F.6    Whitelegge, J.P.7    Chang, H.R.8
  • 160
    • 61649089751 scopus 로고    scopus 로고
    • Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency
    • Schulz, B. L., and Aebi, M. (2009) Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency. Mol. Cell Proteomics 8, 357-364
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 357-364
    • Schulz, B.L.1    Aebi, M.2
  • 162
    • 70349970185 scopus 로고    scopus 로고
    • Simultaneous glycoproteomics on the basis of structure using ion mobility-mass spectrometry
    • Fenn, L. S., and McLean, J. A. (2009) Simultaneous glycoproteomics on the basis of structure using ion mobility-mass spectrometry. Mol. Biosyst. 5, 1298-1302
    • (2009) Mol. Biosyst. , vol.5 , pp. 1298-1302
    • Fenn, L.S.1    McLean, J.A.2
  • 163
    • 0036462601 scopus 로고    scopus 로고
    • Protein N-glycosylation along the secretory pathway: Relationship to organelle topography and function, protein quality control, and cell interactions
    • Roth, J. (2002) Protein N-glycosylation along the secretory pathway: relationship to organelle topography and function, protein quality control, and cell interactions. Chem. Rev. 102, 285-303
    • (2002) Chem. Rev. , vol.102 , pp. 285-303
    • Roth, J.1
  • 165
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography
    • Jung, K., Cho, W., and Regnier, F. E. (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
  • 166
    • 33748294165 scopus 로고    scopus 로고
    • Semi-automated 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. (2006) Semi-automated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry. J. Proteome Res. 5, 2348-2363
    • (2006) J. Proteome Res. , vol.5 , pp. 2348-2363
    • Madera, M.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 168
    • 33750620940 scopus 로고    scopus 로고
    • Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers
    • Drake, R. R., Schwegler, E. E., Malik, G., Diaz, J., Block, T., Mehta, A., and Semmes, O. J. (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
  • 169
    • 61849102357 scopus 로고    scopus 로고
    • Glycoproteomic analysis of plasma from patients with atopic dermatitis: CD5L and ApoE as potential biomarkers
    • Kim, W. K., Hwang, H. R., Kim, do H., Lee, P. Y., In, Y. J., Ryu, H. Y., Park, S. G., Bae, K. H., and Lee, S. C. (2008) Glycoproteomic analysis of plasma from patients with atopic dermatitis: CD5L and ApoE as potential biomarkers. Exp. Mol. Med. 40, 677-685
    • (2008) Exp. Mol. Med. , vol.40 , pp. 677-685
    • Kim, W.K.1    Hwang, H.R.2    Kim Do, H.3    Lee, P.Y.4    In, Y.J.5    Ryu, H.Y.6    Park, S.G.7    Bae, K.H.8    Lee, S.C.9
  • 170
    • 76149089532 scopus 로고    scopus 로고
    • Identification and confirmation of biomarkers using an integrated platform for quantitative analysis of glycoproteins and their glycosylations
    • Liu, Y., He, J., Li, C., Benitez, R., Fu, S., Marrero, J., and Lubman, D. M. (2010) Identification and confirmation of biomarkers using an integrated platform for quantitative analysis of glycoproteins and their glycosylations. J. Proteome Res. 9, 798-805
    • (2010) J. Proteome Res. , vol.9 , pp. 798-805
    • Liu, Y.1    He, J.2    Li, C.3    Benitez, R.4    Fu, S.5    Marrero, J.6    Lubman, D.M.7
  • 173
    • 55249118407 scopus 로고    scopus 로고
    • Glycoproteomic analyses of ovarian cancer cell lines and sera from ovarian cancer patients show distinct glycosylation changes in individual proteins
    • Li, B., An, H. J., Kirmiz, C., Lebrilla, C. B., Lam, K. S., and Miyamoto, S. (2008) Glycoproteomic analyses of ovarian cancer cell lines and sera from ovarian cancer patients show distinct glycosylation changes in individual proteins. J. Proteome Res. 7, 3776-3788
    • (2008) J. Proteome Res. , vol.7 , pp. 3776-3788
    • Li, B.1    An, H.J.2    Kirmiz, C.3    Lebrilla, C.B.4    Lam, K.S.5    Miyamoto, S.6
  • 174
    • 76649133774 scopus 로고    scopus 로고
    • Identification of candidate biomarkers with cancerspecific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis
    • Abbott, K. L., Lim, J. M., Wells, L., Benigno, B. B., McDonald, J. F., and Pierce, M. (2010) Identification of candidate biomarkers with cancerspecific 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
  • 175
    • 53549110284 scopus 로고    scopus 로고
    • Multiplexed glycoproteomic analysis of glycosylation disorders by sequential yolk immunoglobulins immunoseparation and MALDI-TOF MS
    • Sturiale, L., Barone, R., Palmigiano, A., Ndosimao, C. N., Briones, P., Adamowicz, M., Jaeken, J., and Garozzo, D. (2008) Multiplexed glycoproteomic analysis of glycosylation disorders by sequential yolk immunoglobulins immunoseparation and MALDI-TOF MS. Proteomics 8, 3822-3832
    • (2008) Proteomics , vol.8 , pp. 3822-3832
    • Sturiale, L.1    Barone, R.2    Palmigiano, A.3    Ndosimao, C.N.4    Briones, P.5    Adamowicz, M.6    Jaeken, J.7    Garozzo, D.8
  • 176
    • 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, D. M., and Lubman, D. M. (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
  • 177
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • Ramachandran, P., Boontheung, P., Xie, Y., Sondej, M., Wong, D. T., and Loo, J. A. (2006) Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J. Proteome Res. 5, 1493-1503
    • (2006) J. Proteome Res. , vol.5 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4    Wong, D.T.5    Loo, J.A.6
  • 181
    • 34547206144 scopus 로고    scopus 로고
    • Bladder cancer associated glycoprotein signatures revealed by urinary proteomic profiling
    • Kreunin, P., Zhao, J., Rosser, C., Urquidi, V., Lubman, D. M., and Goodison, S. (2007) Bladder cancer associated glycoprotein signatures revealed by urinary proteomic profiling. J. Proteome Res. 6, 2631-2639
    • (2007) J. Proteome Res. , vol.6 , pp. 2631-2639
    • Kreunin, P.1    Zhao, J.2    Rosser, C.3    Urquidi, V.4    Lubman, D.M.5    Goodison, S.6
  • 183
    • 33845974916 scopus 로고    scopus 로고
    • Comparison of pancreas juice proteins from cancer versus pancreatitis using quantitative proteomic analysis
    • Chen, R., Pan, S., Cooke, K., Moyes, K. W., Bronner, M. P., Goodlett, D. R., Aebersold, R., and Brentnall, T. A. (2007) Comparison of pancreas juice proteins from cancer versus pancreatitis using quantitative proteomic analysis. Pancreas 34, 70-79
    • (2007) Pancreas , vol.34 , pp. 70-79
    • Chen, R.1    Pan, S.2    Cooke, K.3    Moyes, K.W.4    Bronner, M.P.5    Goodlett, D.R.6    Aebersold, R.7    Brentnall, T.A.8
  • 185
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Chen, R., Jiang, X., Sun, D., Han, G., Wang, F., Ye, M., Wang, L., and Zou, H. (2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J. Proteome Res. 8, 651-661
    • (2009) J. Proteome Res. , vol.8 , pp. 651-661
    • Chen, R.1    Jiang, X.2    Sun, D.3    Han, G.4    Wang, F.5    Ye, M.6    Wang, L.7    Zou, H.8
  • 187
    • 34547183298 scopus 로고    scopus 로고
    • Comparative glycoproteomics based on lectins affinity capture of N-linked glycoproteins from human Chang liver cells and MHCC97-H cells
    • Xu, Z., Zhou, X., Lu, H., Wu, N., Zhao, H., Zhang, L., Zhang, W., Liang, Y. L., Wang, L., Liu, Y., Yang, P., and Zha, X. (2007) Comparative glycoproteomics based on lectins affinity capture of N-linked glycoproteins from human Chang liver cells and MHCC97-H cells. Proteomics 7, 2358-2370
    • (2007) Proteomics , vol.7 , pp. 2358-2370
    • Xu, Z.1    Zhou, X.2    Lu, H.3    Wu, N.4    Zhao, H.5    Zhang, L.6    Zhang, W.7    Liang, Y.L.8    Wang, L.9    Liu, Y.10    Yang, P.11    Zha, X.12
  • 188
    • 77249130649 scopus 로고    scopus 로고
    • Glycoproteomics of paclitaxel resistance in human epithelial ovarian cancer cell lines: Towards the identification of putative biomarkers
    • Di Michele, M., Marcone, S., Cicchillitti, L., Della, Corte A., Ferlini, C., Scambia, G., Donati, M. B., and Rotilio, D. (2010) Glycoproteomics of paclitaxel resistance in human epithelial ovarian cancer cell lines: towards the identification of putative biomarkers. J. Proteomics 73, 879-898
    • (2010) J. Proteomics , vol.73 , pp. 879-898
    • Di Michele, M.1    Marcone, S.2    Cicchillitti, L.3    Della Corte, A.4    Ferlini, C.5    Scambia, G.6    Donati, M.B.7    Rotilio, D.8
  • 189
    • 77952394242 scopus 로고    scopus 로고
    • Concanavalin A-immobilized magnetic nanoparticles for selective enrichment of glycoproteins and application to glycoproteomics in hepatocelluar carcinoma cell line
    • Tang, J., Liu, Y., Yin, P., Yao, G., Yan, G., Deng, C., and Zhang, X. (2010) Concanavalin A-immobilized magnetic nanoparticles for selective enrichment of glycoproteins and application to glycoproteomics in hepatocelluar carcinoma cell line. Proteomics 10, 2000-2014
    • (2010) Proteomics , vol.10 , pp. 2000-2014
    • Tang, J.1    Liu, Y.2    Yin, P.3    Yao, G.4    Yan, G.5    Deng, C.6    Zhang, X.7
  • 190
    • 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., and 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
  • 191
    • 0345598906 scopus 로고    scopus 로고
    • A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
    • Hang, H. C., Yu, C., Kato, D. L., and Bertozzi, C. R. (2003) A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc. Natl Acad. Sci. 100, 14846-14851
    • (2003) Proc. Natl Acad. Sci. , vol.100 , pp. 14846-14851
    • Hang, H.C.1    Yu, C.2    Kato, D.L.3    Bertozzi, C.R.4
  • 192
    • 50449090546 scopus 로고    scopus 로고
    • Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells
    • Vercoutter-Edouart, A. S., Slomianny, M. C., Dekeyzer-Beseme, O., Haeuw, J. F., and Michalski, J. C. (2008) Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells. Proteomics 8, 3236-3256
    • (2008) Proteomics , vol.8 , pp. 3236-3256
    • Vercoutter-Edouart, A.S.1    Slomianny, M.C.2    Dekeyzer-Beseme, O.3    Haeuw, J.F.4    Michalski, J.C.5
  • 193
    • 0037040607 scopus 로고    scopus 로고
    • Global internal standard technology for comparative proteomics
    • Chakraborty, A., and Regnier, F. E. (2002) Global internal standard technology for comparative proteomics. J. Chromatogr. A 949, 173-184
    • (2002) J. Chromatogr. A , vol.949 , pp. 173-184
    • Chakraborty, A.1    Regnier, F.E.2
  • 194
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol. 17, 994-999
    • (1999) Nat Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 196
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1, 376-386
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 197
    • 0033915395 scopus 로고    scopus 로고
    • Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using (18)O-labeled internal standards
    • Mirgorodskaya, O. A., Kozmin, Y. P., Titov, M. I., Körner, R., Sönksen, C. P., and Roepstorff, P. (2000) Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using (18)O-labeled internal standards. Rapid Commun. Mass Spectrom. 14, 1226-1232
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1226-1232
    • Mirgorodskaya, O.A.1    Kozmin, Y.P.2    Titov, M.I.3    Körner, R.4    Sönksen, C.P.5    Roepstorff, P.6
  • 198
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao, X., Freas, A., Ramirez, J., Demirev, P. A., and Fenselau, C. (2001) Proteolytic 18O labeling for comparative proteomics: model studies with two serotypes of adenovirus. Anal. Chem. 73, 2836-2842
    • (2001) Anal. Chem. , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 199
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko, P. V., Chelius, D., and Shaler, T. A. (2002) Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Chem. 74, 4741-4749
    • (2002) Anal. Chem. , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelius, D.2    Shaler, T.A.3
  • 200
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., and Yates, J. R., 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 201
    • 63849182791 scopus 로고    scopus 로고
    • Glycoproteomic profiling of serum peptides in canine lymphoma and transitional cell carcinoma
    • Wilson, C. R., Regnier, F. E., Knapp, D. W., Raskin, R. E., Andrews, D. A., and Hooser, S. B. (2008) Glycoproteomic profiling of serum peptides in canine lymphoma and transitional cell carcinoma. Vet. Comp Oncol. 6, 171-181
    • (2008) Vet. Comp Oncol. , vol.6 , pp. 171-181
    • Wilson, C.R.1    Regnier, F.E.2    Knapp, D.W.3    Raskin, R.E.4    Andrews, D.A.5    Hooser, S.B.6
  • 202
    • 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. (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
  • 203
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways
    • Zeidan, Q., and Hart, G. W. (2010) The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 123 (Pt 1), 13-22
    • (2010) J. Cell Sci. , vol.123 , Issue.PART 1 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 204
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree, C., Park, K., and Hart, G. W. (2010) O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim. Biophys. Acta 1800, 96-106
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 206
    • 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. (2010) Simple method for quantitative analysis of N-linked glycoproteins in hepatocellular carcinoma specimens. J. Proteome Res. 9, 308-318
    • (2010) J. Proteome Res. , vol.9 , 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
  • 207
    • 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. (2010) Tandem 18O stable isotope labeling for quantification of N-glycoproteome. J. Proteome Res. 9, 227-236
    • (2010) J. Proteome Res. , vol.9 , pp. 227-236
    • Liu, Z.1    Cao, J.2    He, Y.3    Qiao, L.4    Xu, C.5    Lu, H.6    Yang, P.7
  • 209
    • 33847339730 scopus 로고    scopus 로고
    • Combination of abundant protein depletion and multi-lectin affinity chromatography (M-LAC) for plasma protein biomarker discovery
    • Plavina, T., Wakshull, E., Hancock, W. S., and Hincapie, M. (2007) Combination of abundant protein depletion and multi-lectin affinity chromatography (M-LAC) for plasma protein biomarker discovery. J. Proteome Res. 6, 662-671
    • (2007) J. Proteome Res. , vol.6 , pp. 662-671
    • Plavina, T.1    Wakshull, E.2    Hancock, W.S.3    Hincapie, M.4
  • 210
    • 0037434994 scopus 로고    scopus 로고
    • Constellations in a cellular universe
    • Aebersold, R. (2003) Constellations in a cellular universe. Nature 422, 115-116
    • (2003) Nature , vol.422 , pp. 115-116
    • Aebersold, R.1
  • 211
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • Anderson, N. L., Anderson, N. G., Haines, L. R., Hardie, D. B., Olafson, R. W., and Pearson, T. W. (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
  • 212
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B., and Aebersold, R. (2006) Mass spectrometry and protein analysis. Science 312, 212-217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 213
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., and Gygi, S. P. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. U.S.A. 100, 6940-6945
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 215
    • 67649445893 scopus 로고    scopus 로고
    • Targeted detection of prostate cancer proteins in serum using heavy peptide standards and MALDI-TOF/TOF
    • Li, Y., Sokoll, L. J., Rush, J., Meany, D., Zou, N., Chan, D. W., and Zhang, H. (2009) Targeted detection of prostate cancer proteins in serum using heavy peptide standards and MALDI-TOF/TOF. Proteomics-Clin. Appl. 3, 597-608
    • (2009) Proteomics-Clin. Appl. , vol.3 , pp. 597-608
    • Li, Y.1    Sokoll, L.J.2    Rush, J.3    Meany, D.4    Zou, N.5    Chan, D.W.6    Zhang, H.7
  • 216
    • 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, Y. H., Lee, J. Y., Lee, J. Y., Kim, Y. S., Ko, J. H., and Yoo, J. S. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.