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Volumn 65, Issue , 2011, Pages 219-271

Toward automated glycan analysis

Author keywords

Automated glycan analysis; Biomarkers; Glycoblotting; Glycomics; Mass spectrometry; Reverse glycoblotting

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 2 MACROGLOBULIN; BETA2 GLYCOPROTEIN 1; CARBOXYLESTERASE; CERULOPLASMIN; CLUSTERIN; COMPLEMENT COMPONENT C4B; COMPLEMENT COMPONENT C4B BINDING PROTEIN; COMPLEMENT FACTOR H; FETUIN A; GLYCAN; GLYCOPROTEIN; HAPTOGLOBIN; IMMUNOGLOBULIN G2B; IMMUNOGLOBULIN J CHAIN; OROSOMUCOID; THROMBOSPONDIN 1; TRANSFERRIN;

EID: 79960311716     PISSN: 00652318     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385520-6.00005-4     Document Type: Chapter
Times cited : (58)

References (116)
  • 1
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation-potential for therapeutics and diagnostics
    • Dube D.H., Bertozzi C.R. Glycans in cancer and inflammation-potential for therapeutics and diagnostics. Nat. Rev. Drug Discov. 2005, 4:477-488.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 2
    • 4544280219 scopus 로고    scopus 로고
    • A synthetic antithrombin III binding pentasaccharide is now a drug! What comes next?
    • Petitou M., van Boeckel C.A. A synthetic antithrombin III binding pentasaccharide is now a drug! What comes next?. Angew. Chem. Int. Ed. 2004, 43:3118-3133.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 3118-3133
    • Petitou, M.1    van Boeckel, C.A.2
  • 3
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek R.A. Glycobiology: Toward understanding the function of sugars. Chem. Rev. 1996, 96:683-720.
    • (1996) Chem. Rev. , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 4
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R., Mann M. Mass spectrometry-based proteomics. Nature 2003, 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 5
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia
    • Saiki R.K., Scharf S., Faloona F., Mullis K.B., Horn G.T., Erlich H.A., Arnheim N. Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science 1985, 230:1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.K.1    Scharf, S.2    Faloona, F.3    Mullis, K.B.4    Horn, G.T.5    Erlich, H.A.6    Arnheim, N.7
  • 9
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N-α-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • Pratt M.R., Hang H.C., Ten Hagen H.K.G., Rarick J., Gerken T.A., Tabak L.A., Bertozzi C.R. Deconvoluting the functions of polypeptide N-α-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem. Biol. 2004, 11:1009-1016.
    • (2004) Chem. Biol. , vol.11 , pp. 1009-1016
    • Pratt, M.R.1    Hang, H.C.2    Ten Hagen, H.K.G.3    Rarick, J.4    Gerken, T.A.5    Tabak, L.A.6    Bertozzi, C.R.7
  • 10
    • 70350441377 scopus 로고    scopus 로고
    • Oppotunities and challenges in synthetic oligosaccharide and glycoconjugate research
    • Boltje T.J., Buskas T., Boons G.-J. Oppotunities and challenges in synthetic oligosaccharide and glycoconjugate research. Nat. Chem. 2009, 1:611-622.
    • (2009) Nat. Chem. , vol.1 , pp. 611-622
    • Boltje, T.J.1    Buskas, T.2    Boons, G.-J.3
  • 11
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson N.L., Anderson N.G. The human plasma proteome: History, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1:845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 13
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu I., Kerek F. A simple and rapid method for the permethylation of carbohydrates. Carbohydr. Res. 1984, 131:209-217.
    • (1984) Carbohydr. Res. , vol.131 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 15
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M., Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 1988, 60:2299-2301.
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 19
    • 33748168091 scopus 로고
    • Electrospray ion source. Another varlation on the free-jet theme
    • Yamashita M., Fenn J.B. Electrospray ion source. Another varlation on the free-jet theme. J. Phys. Chem. 1984, 88:4451-4459.
    • (1984) J. Phys. Chem. , vol.88 , pp. 4451-4459
    • Yamashita, M.1    Fenn, J.B.2
  • 20
    • 33845471401 scopus 로고
    • Negative ion production with the electrospray ion source
    • Yamashita M., Fenn J.B. Negative ion production with the electrospray ion source. J. Phys. Chem. 1984, 88:4671-4675.
    • (1984) J. Phys. Chem. , vol.88 , pp. 4671-4675
    • Yamashita, M.1    Fenn, J.B.2
  • 21
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn J.B., Mann M., Meng C.K., Wong S.F., Whitehouse C.M. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 23
    • 16344380985 scopus 로고    scopus 로고
    • Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra
    • Goldberg D., Sutton-Smith M., Paulson J.C., Dell A. Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra. Proteomics 2005, 5:865-875.
    • (2005) Proteomics , vol.5 , pp. 865-875
    • Goldberg, D.1    Sutton-Smith, M.2    Paulson, J.C.3    Dell, A.4
  • 24
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod: A software tool for determining glycosylation compositions from mass spectrometric data
    • Cooper C.A., Gasteiger E., Packer N.H. GlycoMod: A software tool for determining glycosylation compositions from mass spectrometric data. Proteomics 2001, 1:340-349.
    • (2001) Proteomics , vol.1 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.H.3
  • 25
    • 0037250530 scopus 로고    scopus 로고
    • GlycoSuiteDB: A curated relational database of glycoprotein glycan structures and their biological sources. 2003 update
    • Cooper C.A., Joshi H.J., Harrison M.J., Wilkins M.R., Packer N.H. GlycoSuiteDB: A curated relational database of glycoprotein glycan structures and their biological sources. 2003 update. Nucleic Acids Res. 2003, 31:511-513.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 511-513
    • Cooper, C.A.1    Joshi, H.J.2    Harrison, M.J.3    Wilkins, M.R.4    Packer, N.H.5
  • 26
  • 27
    • 2942568109 scopus 로고    scopus 로고
    • Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data
    • Joshi H.J., Harrison M.J., Schulz B.L., Cooper C.A., Packer N.H., Karlsson N.G. Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data. Proteomics 2004, 4:1650-1664.
    • (2004) Proteomics , vol.4 , pp. 1650-1664
    • Joshi, H.J.1    Harrison, M.J.2    Schulz, B.L.3    Cooper, C.A.4    Packer, N.H.5    Karlsson, N.G.6
  • 28
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. USA 1993, 90:5011-5015.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 29
    • 0027608882 scopus 로고
    • Use of mass spectrometric molecular weight information to identify proteins in sequence databases
    • Mann M., Højrup P., Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol. Mass Spectrom. 1993, 6:338-345.
    • (1993) Biol. Mass Spectrom. , vol.6 , pp. 338-345
    • Mann, M.1    Højrup, P.2    Roepstorff, P.3
  • 30
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., Mccormack A.L., Yates J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    Mccormack, A.L.2    Yates, J.R.3
  • 31
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans
    • Ceroni A., Maass K., Geyer H., Geyer R., Dell A., Haslam S.M. GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans. J. Proteome Res. 2008, 7:1650-1659.
    • (2008) J. Proteome Res. , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 32
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon B., Costello C.E. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 1988, 5:397.
    • (1988) Glycoconj. J. , vol.5 , pp. 397
    • Domon, B.1    Costello, C.E.2
  • 33
    • 68249131729 scopus 로고    scopus 로고
    • Automated measurement of permethylated serum N-glycans by MALDI-linear ion trap mass spectrometry
    • Guillard M., Gloerich J., Wessels H.J.C.T., Morava E., Wevers R.A., Lefeber D.J. Automated measurement of permethylated serum N-glycans by MALDI-linear ion trap mass spectrometry. Carbohydr. Res. 2009, 344:1550-1557.
    • (2009) Carbohydr. Res. , vol.344 , pp. 1550-1557
    • Guillard, M.1    Gloerich, J.2    Wessels, H.J.C.T.3    Morava, E.4    Wevers, R.A.5    Lefeber, D.J.6
  • 34
    • 0043208919 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks
    • Walsh G. Biopharmaceutical benchmarks. Nat. Biotechnol. 2003, 21:865-870.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 865-870
    • Walsh, G.1
  • 36
    • 0037526514 scopus 로고    scopus 로고
    • Darbepoetin alpha: A new approach to the treatment of chemotherapy-induced anaemia
    • Vansteenkiste J., Rossi G., Foote M. Darbepoetin alpha: A new approach to the treatment of chemotherapy-induced anaemia. Expert Opin. Biol. Ther. 2003, 3:501-508.
    • (2003) Expert Opin. Biol. Ther. , vol.3 , pp. 501-508
    • Vansteenkiste, J.1    Rossi, G.2    Foote, M.3
  • 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., Aerbersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 2003, 21:660-666.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aerbersold, R.4
  • 39
    • 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., Smith R.D. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 2005, 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
    • 34547800600 scopus 로고    scopus 로고
    • Isolation of N-linked glycopeptides from plasma
    • Zhou Y., Aebersold R., Zhang H. Isolation of N-linked glycopeptides from plasma. Anal. Chem. 2007, 79:5826-5837.
    • (2007) Anal. Chem. , vol.79 , pp. 5826-5837
    • Zhou, Y.1    Aebersold, R.2    Zhang, H.3
  • 41
    • 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., Zou H. Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J. Proteome Res. 2009, 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
  • 44
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada Y., Tajiri M., Yoshida S. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal. Chem. 2004, 76:6560-6565.
    • (2004) Anal. Chem. , vol.76 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 45
    • 77950810853 scopus 로고    scopus 로고
    • Enhanced glyco-profiling by specific glycopeptide enrichment and complementary monolithic nano-LC (ZIC-HILIC/RP18e)/ESI-MS analysis
    • Wohlgemuth J., Karas M., Jiang W., Hendriks R., Andrecht S. Enhanced glyco-profiling by specific glycopeptide enrichment and complementary monolithic nano-LC (ZIC-HILIC/RP18e)/ESI-MS analysis. J. Sep. Sci. 2010, 33:880-890.
    • (2010) J. Sep. Sci. , vol.33 , pp. 880-890
    • Wohlgemuth, J.1    Karas, M.2    Jiang, W.3    Hendriks, R.4    Andrecht, S.5
  • 46
    • 45949094992 scopus 로고    scopus 로고
    • Profiling of N- and O-glycopeptides of erythropoietin by capillary zwitterionic type of hydrophilic interaction chromatography
    • Takegawa Y., Ito H., Keira T., Deguchi K., Nakagawa H., Nishimura S.-I. Profiling of N- and O-glycopeptides of erythropoietin by capillary zwitterionic type of hydrophilic interaction chromatography. J. Sep. Sci. 2008, 31:1585-1593.
    • (2008) J. Sep. Sci. , vol.31 , pp. 1585-1593
    • Takegawa, Y.1    Ito, H.2    Keira, T.3    Deguchi, K.4    Nakagawa, H.5    Nishimura, S.-I.6
  • 47
    • 45949110688 scopus 로고    scopus 로고
    • Chromatographic deuterium isotope effects of derivatized N-glycans and N-glycopeptides in a zwitterionic type of hydrophilic interaction chromatography
    • Takegawa Y., Hato M., Deguchi K., Nakagawa H., Nishimura S.-I. Chromatographic deuterium isotope effects of derivatized N-glycans and N-glycopeptides in a zwitterionic type of hydrophilic interaction chromatography. J. Sep. Sci. 2008, 31:1594-1597.
    • (2008) J. Sep. Sci. , vol.31 , pp. 1594-1597
    • Takegawa, Y.1    Hato, M.2    Deguchi, K.3    Nakagawa, H.4    Nishimura, S.-I.5
  • 48
    • 60549101068 scopus 로고    scopus 로고
    • Use of activated graphitized carbon chips for liquid chromatography/mass spectrometric and tandem mass spectrometric analysis of tryptic peptides
    • Alley W.R., Mechref Y., Novotny M.V. Use of activated graphitized carbon chips for liquid chromatography/mass spectrometric and tandem mass spectrometric analysis of tryptic peptides. Rapid Commun. Mass Spectrom. 2009, 23:495-505.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 495-505
    • Alley, W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 53
    • 70449970103 scopus 로고    scopus 로고
    • Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein biomarkers
    • Dai Z., Zhou J., Qiu S.-J., Liu Y.-K., Fan J. Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein biomarkers. Electrophoresis 2009, 30:2957-2966.
    • (2009) Electrophoresis , vol.30 , pp. 2957-2966
    • Dai, Z.1    Zhou, J.2    Qiu, S.-J.3    Liu, Y.-K.4    Fan, J.5
  • 54
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • Darula Z., Medzihradszky K.F. Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum. Mol. Cell. Proteomics 2009, 8:2515-2526.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 55
    • 75749150176 scopus 로고    scopus 로고
    • Automated platform for fractionation of human plasma glycoproteome in clinical proteomics
    • Kullolli M., Hancock W.S., Hincapie M. Automated platform for fractionation of human plasma glycoproteome in clinical proteomics. Anal. Chem. 2010, 82:115-120.
    • (2010) Anal. Chem. , vol.82 , pp. 115-120
    • Kullolli, M.1    Hancock, W.S.2    Hincapie, M.3
  • 56
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev R.A., Kelleher N.L., Mclafferty F.W. Electron capture dissociation of multiply charged protein cations. A nonergodic process. J. Am. Chem. Soc. 1998, 120:3265-3266.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    Mclafferty, F.W.3
  • 59
    • 0037156407 scopus 로고    scopus 로고
    • Dissociative capture of hot (3-13 eV) electrons by polypeptide polycations: An efficient process accompanied by secondary fragmentation
    • Kjeldsen F., Haselmann K.F., Budnik B.A., Jensen F., Zubarev R.A. Dissociative capture of hot (3-13 eV) electrons by polypeptide polycations: An efficient process accompanied by secondary fragmentation. Chem. Phys. Lett. 2002, 356:201-206.
    • (2002) Chem. Phys. Lett. , vol.356 , pp. 201-206
    • Kjeldsen, F.1    Haselmann, K.F.2    Budnik, B.A.3    Jensen, F.4    Zubarev, R.A.5
  • 60
    • 0038547949 scopus 로고    scopus 로고
    • Secondary losses via γ-lactam formation in hot electron capture dissociation: A missing link to complete de Novo sequencing of proteins?
    • Kjeldsen F., Zubarev R.A. Secondary losses via γ-lactam formation in hot electron capture dissociation: A missing link to complete de Novo sequencing of proteins?. J. Am. Chem. Soc. 2003, 125:6628-6629.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6628-6629
    • Kjeldsen, F.1    Zubarev, R.A.2
  • 61
    • 0037444520 scopus 로고    scopus 로고
    • Distribution of Iie/Leu amino acid residues in the PP3 protein by (hot) electron capture dissociation in Fourier transform ion cyclotron resonance mass spectrometry
    • Kjeldsen F., Sørensen K.F., Zubarev R.A. Distribution of Iie/Leu amino acid residues in the PP3 protein by (hot) electron capture dissociation in Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 2003, 75:1267-1274.
    • (2003) Anal. Chem. , vol.75 , pp. 1267-1274
    • Kjeldsen, F.1    Sørensen, K.F.2    Zubarev, R.A.3
  • 62
    • 0038610834 scopus 로고    scopus 로고
    • Reactions of polypeptide ions with electrons in the gas phase
    • Zubarev R.A. Reactions of polypeptide ions with electrons in the gas phase. Mass Spectrom. Rev. 2003, 22:57-77.
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 57-77
    • Zubarev, R.A.1
  • 63
    • 1242351309 scopus 로고    scopus 로고
    • Electron-capture dissociation tandem mass spectrometry
    • Zubarev R.A. Electron-capture dissociation tandem mass spectrometry. Curr. Opin. Biotechnol. 2004, 15:12-16.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 12-16
    • Zubarev, R.A.1
  • 65
    • 36448959462 scopus 로고    scopus 로고
    • Fast multiple electron capture dissociation in a linear radio frequency quadrupole ion trap
    • Satake H., Hasegawa H., Hirabayashi A., Hashimoto Y., Baba T., Masuda K. Fast multiple electron capture dissociation in a linear radio frequency quadrupole ion trap. Anal. Chem. 2007, 79:8755-8761.
    • (2007) Anal. Chem. , vol.79 , pp. 8755-8761
    • Satake, H.1    Hasegawa, H.2    Hirabayashi, A.3    Hashimoto, Y.4    Baba, T.5    Masuda, K.6
  • 66
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M., Jensen O.N. Proteomic analysis of post-translational modifications. Nat. Biotechnol. 2003, 21:225-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 225-261
    • Mann, M.1    Jensen, O.N.2
  • 69
    • 0032731855 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer
    • Mirgorodskaya P., Roepstorff P., Zubarev R.A. Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer. Anal. Chem. 1999, 71:4431-4436.
    • (1999) Anal. Chem. , vol.71 , pp. 4431-4436
    • Mirgorodskaya, P.1    Roepstorff, P.2    Zubarev, R.A.3
  • 70
    • 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., Zubarev R.A. 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. 2003, 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
  • 72
    • 17444375706 scopus 로고    scopus 로고
    • Complementary structural information from a tryptic N-linked glycopeptides via electron transfer ion/ion reactions and collision-induced dissociation
    • Hogan J.M., Pitteri S.J., Chrisman P.A., Mcluckey S.A. Complementary structural information from a tryptic N-linked glycopeptides via electron transfer ion/ion reactions and collision-induced dissociation. J. Proteome Res. 2005, 4:628-632.
    • (2005) J. Proteome Res. , vol.4 , pp. 628-632
    • Hogan, J.M.1    Pitteri, S.J.2    Chrisman, P.A.3    Mcluckey, S.A.4
  • 73
    • 36349016738 scopus 로고    scopus 로고
    • On-line LCMS approach combining collision-induced dissociation (CID), electron transfer dissociation (ETD), and CID of an isolated charge-reduced species for the trace-level characterization of proteins with post-translational modifications
    • Wu S.-I., Huhmer A.F.R., Hao Z., Karger B.L. On-line LCMS approach combining collision-induced dissociation (CID), electron transfer dissociation (ETD), and CID of an isolated charge-reduced species for the trace-level characterization of proteins with post-translational modifications. J. Proteome Res. 2007, 6:4230-4244.
    • (2007) J. Proteome Res. , vol.6 , pp. 4230-4244
    • Wu, S.-I.1    Huhmer, A.F.R.2    Hao, Z.3    Karger, B.L.4
  • 74
    • 62349122640 scopus 로고    scopus 로고
    • Localization of O-glycans in MUC1 glycoproteins using electron-capture dissociation fragmentation mass spectrometry
    • Sihlbom C., Härd I.D., Lidell M.E., Noll T., Hansson G.C., Bäckström M. Localization of O-glycans in MUC1 glycoproteins using electron-capture dissociation fragmentation mass spectrometry. Glycobiology 2009, 19:375-381.
    • (2009) Glycobiology , vol.19 , pp. 375-381
    • Sihlbom, C.1    Härd, I.D.2    Lidell, M.E.3    Noll, T.4    Hansson, G.C.5    Bäckström, M.6
  • 78
    • 0036462598 scopus 로고    scopus 로고
    • Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modeling
    • Wormald M.R., Petrescu A.J., Pao Y.-L., Glithero A., Elliott T., Dwek R.A. Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modeling. Chem. Rev. 2002, 102:371-386.
    • (2002) Chem. Rev. , vol.102 , pp. 371-386
    • Wormald, M.R.1    Petrescu, A.J.2    Pao, Y.-L.3    Glithero, A.4    Elliott, T.5    Dwek, R.A.6
  • 81
    • 4143119749 scopus 로고    scopus 로고
    • Antifreeze glycoproteins: Elucidation of the structural motifs that are essential for antifreeze activity
    • Tachibana Y., Fletcher G.L., Fujitani N., Tsuda S., Monde K., Nishimura S.-I. Antifreeze glycoproteins: Elucidation of the structural motifs that are essential for antifreeze activity. Angew. Chem. Int. Ed. 2004, 43:856-862.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 856-862
    • Tachibana, Y.1    Fletcher, G.L.2    Fujitani, N.3    Tsuda, S.4    Monde, K.5    Nishimura, S.-I.6
  • 82
    • 34247103652 scopus 로고    scopus 로고
    • Electron capture dissociation of oligosaccharides ionized with alkali, alkaline earth, and transition metals
    • Adamson J.T., Håkansson K. Electron capture dissociation of oligosaccharides ionized with alkali, alkaline earth, and transition metals. Anal. Chem. 2007, 79:2901-2910.
    • (2007) Anal. Chem. , vol.79 , pp. 2901-2910
    • Adamson, J.T.1    Håkansson, K.2
  • 83
    • 38349059878 scopus 로고    scopus 로고
    • Collisionally activated dissociation and electron capture dissociation provide complementary structural information for branched permethylated oligosaccharides
    • Zhao C., Xie B., Chan S.-Y., Costello C.E., O'connor P.B. Collisionally activated dissociation and electron capture dissociation provide complementary structural information for branched permethylated oligosaccharides. J. Am. Soc. Mass Spectrom. 2008, 19:138-150.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 138-150
    • Zhao, C.1    Xie, B.2    Chan, S.-Y.3    Costello, C.E.4    O'connor, P.B.5
  • 85
    • 84980111230 scopus 로고
    • Verbindungen des phenylhydrazines mit den zuckerarten
    • Fischer E. Verbindungen des phenylhydrazines mit den zuckerarten. Ber. Dtsch. Chem. Ges. 1884, 17:579-584.
    • (1884) Ber. Dtsch. Chem. Ges. , vol.17 , pp. 579-584
    • Fischer, E.1
  • 86
    • 33746320524 scopus 로고    scopus 로고
    • Solid-phase oligosaccharide tagging (SPOT): Validation on glycolipid-derived structures
    • Lohse A., Martins R., Jorgensen M.R., Hindsugaul O. Solid-phase oligosaccharide tagging (SPOT): Validation on glycolipid-derived structures. Angew. Chem. Int. Ed. 2006, 45:4167-4172.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4167-4172
    • Lohse, A.1    Martins, R.2    Jorgensen, M.R.3    Hindsugaul, O.4
  • 87
    • 34250313689 scopus 로고    scopus 로고
    • Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry
    • Miura Y., Shinohara Y., Furukawa J.-i., Nagahori N., Nishimura S.-I. Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry. Chem. Eur. J. 2007, 13:4797-4804.
    • (2007) Chem. Eur. J. , vol.13 , pp. 4797-4804
    • Miura, Y.1    Shinohara, Y.2    Furukawa, J.-I.3    Nagahori, N.4    Nishimura, S.-I.5
  • 89
    • 39449136167 scopus 로고    scopus 로고
    • Comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion
    • Furukawa J.-i., Shinohara Y., Kuramoto H., Miura Y., Shimaoka H., Kurogochi M., Nakano M., Nishimura S.-I. Comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion. Anal. Chem. 2008, 80:1094-1101.
    • (2008) Anal. Chem. , vol.80 , pp. 1094-1101
    • Furukawa, J.-I.1    Shinohara, Y.2    Kuramoto, H.3    Miura, Y.4    Shimaoka, H.5    Kurogochi, M.6    Nakano, M.7    Nishimura, S.-I.8
  • 92
    • 0027429703 scopus 로고
    • Structures of N-linked sugar chains expressed mainly in mouse brain
    • Shimizu H., Ochiai K., Ikenaka K., Mikoshiba K., Hase S. Structures of N-linked sugar chains expressed mainly in mouse brain. J. Biochem. 1993, 114:334-338.
    • (1993) J. Biochem. , vol.114 , pp. 334-338
    • Shimizu, H.1    Ochiai, K.2    Ikenaka, K.3    Mikoshiba, K.4    Hase, S.5
  • 93
    • 0032789158 scopus 로고    scopus 로고
    • Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans
    • Zamze S., Harvey D.J., Pesheva P., Mattu T.S., Schachner M., Dwek R.A., Wing D.R. Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans. Glycobiology 1999, 9:823-831.
    • (1999) Glycobiology , vol.9 , pp. 823-831
    • Zamze, S.1    Harvey, D.J.2    Pesheva, P.3    Mattu, T.S.4    Schachner, M.5    Dwek, R.A.6    Wing, D.R.7
  • 97
    • 36749040214 scopus 로고    scopus 로고
    • Reverse glycoblotting allows rapid enrichment glycoproteomics of biopharmaceuticals and disease-related biomarkers
    • Kurogochi M., Amano M., Fumoto M., Takimoto A., Kondo H., Nishimura S.-I. Reverse glycoblotting allows rapid enrichment glycoproteomics of biopharmaceuticals and disease-related biomarkers. Angew. Chem. Int. Ed. 2007, 46:8808-8813.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 8808-8813
    • Kurogochi, M.1    Amano, M.2    Fumoto, M.3    Takimoto, A.4    Kondo, H.5    Nishimura, S.-I.6
  • 98
    • 0015239274 scopus 로고
    • Studies on the chemical and enzymatic modification of glycoproteins
    • Lenten L.V., Ashwell G. Studies on the chemical and enzymatic modification of glycoproteins. J. Biol. Chem. 1971, 246:1889-1894.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1889-1894
    • Lenten, L.V.1    Ashwell, G.2
  • 99
    • 0030070070 scopus 로고    scopus 로고
    • A rapid formaldehyde assay using purpald reagent: Application under periodation conditions
    • Quesenberry M.S., Lee Y.C. A rapid formaldehyde assay using purpald reagent: Application under periodation conditions. Anal. Biochem. 1996, 234:50-55.
    • (1996) Anal. Biochem. , vol.234 , pp. 50-55
    • Quesenberry, M.S.1    Lee, Y.C.2
  • 100
    • 0000870645 scopus 로고    scopus 로고
    • Conformational studies of glycopeptides by energy transfer
    • Lee K.B., Lee Y.C. Conformational studies of glycopeptides by energy transfer. J. Biol. Chem. 1996, 271:1462-1469.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1462-1469
    • Lee, K.B.1    Lee, Y.C.2
  • 102
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific proteins that mediate cellular recognition
    • Lis H., Sharon N. Lectins: Carbohydrate-specific proteins that mediate cellular recognition. Chem. Rev. 1998, 98:637-674.
    • (1998) Chem. Rev. , vol.98 , pp. 637-674
    • Lis, H.1    Sharon, N.2
  • 103
    • 70349878950 scopus 로고    scopus 로고
    • Sialic acids as regulators of molecular and cellular interactions
    • Schauer R. Sialic acids as regulators of molecular and cellular interactions. Curr. Opin. Struct. Biol. 2009, 19:507-514.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 507-514
    • Schauer, R.1
  • 104
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki A. Sialic acids in human health and disease. Trends Mol. Med. 2008, 14:351-360.
    • (2008) Trends Mol. Med. , vol.14 , pp. 351-360
    • Varki, A.1
  • 105
    • 62449189961 scopus 로고    scopus 로고
    • Multiple changes in sialic acid biology during human evolution
    • Varki A. Multiple changes in sialic acid biology during human evolution. Glycoconj. J. 2009, 26:231-245.
    • (2009) Glycoconj. J. , vol.26 , pp. 231-245
    • Varki, A.1
  • 106
    • 57049144338 scopus 로고    scopus 로고
    • MRMer, an interactive open source and cross-platform system for data extraction and visualization of multiple reaction monitoring experiments
    • Martin D.B., Holzman T., May D., Peterson A., Eastham A., Eng J., Mcintosh M. MRMer, an interactive open source and cross-platform system for data extraction and visualization of multiple reaction monitoring experiments. Mol. Cell. Proteomics 2008, 7:2270-2278.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2270-2278
    • Martin, D.B.1    Holzman, T.2    May, D.3    Peterson, A.4    Eastham, A.5    Eng, J.6    Mcintosh, M.7
  • 108
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Leigh Anderson L., Hunter C.L. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 2006, 5:573-588.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Leigh Anderson, L.1    Hunter, C.L.2
  • 109
    • 34547872730 scopus 로고    scopus 로고
    • The application of ultra-performance liquid chromatography/tandem mass spectrometry to the detection and quantitation of apolipoproteins in human serum
    • Kay R.G., Gregory B., Grace P.B., Pleasance S. The application of ultra-performance liquid chromatography/tandem mass spectrometry to the detection and quantitation of apolipoproteins in human serum. Rapid Commun. Mass Spectrom. 2007, 21:2585-2593.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 2585-2593
    • Kay, R.G.1    Gregory, B.2    Grace, P.B.3    Pleasance, S.4
  • 111
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian H., Addona T., Burgess M., Kuhn E., Carr S.A. Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell. Proteomics 2007, 6:2212-2229.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5
  • 112
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona T.A., et al. Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat. Biotechnol. 2009, 27:660-666.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 660-666
    • Addona, T.A.1
  • 114
    • 59249099294 scopus 로고    scopus 로고
    • Structural and functional glycosphingolipidomics by glycoblotting with aminooxy-functionalized gold nanoparticle
    • Nagahori N., Abe M., Nishimura S.-I. Structural and functional glycosphingolipidomics by glycoblotting with aminooxy-functionalized gold nanoparticle. Biochemistry 2009, 48:583-594.
    • (2009) Biochemistry , vol.48 , pp. 583-594
    • Nagahori, N.1    Abe, M.2    Nishimura, S.-I.3
  • 116
    • 84942531371 scopus 로고    scopus 로고
    • This project has been supported partly by a grant for "Development of Systems and Technology for Advanced Measurement and Analysis (SENTAN)" from the Japan Science and Technology Agency (JST) from the Ministry of Education, Culture, Science, and Technology, Japan
    • This project has been supported partly by a grant for "Development of Systems and Technology for Advanced Measurement and Analysis (SENTAN)" from the Japan Science and Technology Agency (JST) from the Ministry of Education, Culture, Science, and Technology, Japan (). http://www.jst.go.jp/sentan/en/.


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