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Volumn 6, Issue , 2013, Pages 237-265

Structural glycomic analyses at high sensitivity: A decade of progress

Author keywords

biomolecular mass spectrometry; capillary electrophoresis; carbohydrates; permethylation; porous graphitic carbon; sialic acids

Indexed keywords

CARBOHYDRATES; CARBON; MASS SPECTROMETRY; POROUS MATERIALS;

EID: 84879625177     PISSN: 19361327     EISSN: 19361335     Source Type: Book Series    
DOI: 10.1146/annurev-anchem-062012-092609     Document Type: Article
Times cited : (52)

References (147)
  • 1
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • Hart GW, Copeland RJ. 2010. Glycomics hits the big time. Cell 143:672-76
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 2
    • 15944393490 scopus 로고    scopus 로고
    • The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation
    • Nita-Lazar M, Wacker M, Schegg B, Amber S, Aebi M. 2005. The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology 15:361-67
    • (2005) Glycobiology , vol.15 , pp. 361-367
    • Nita-Lazar, M.1    Wacker, M.2    Schegg, B.3    Amber, S.4    Aebi, M.5
  • 3
    • 78650373542 scopus 로고    scopus 로고
    • Improved mass spectrometric characterization of protein glycosylation reveals unusual glycosylation of maize-derived bovine trypsin
    • ZhangH,Huang RY, Jalili PR, Irungu JW, Nicol GR, et al. 2010. Improved mass spectrometric characterization of protein glycosylation reveals unusual glycosylation of maize-derived bovine trypsin. Anal. Chem. 82:10095-101
    • (2010) Anal. Chem. , vol.82 , pp. 10095-10101
    • Zhang, H.1    Huang, R.Y.2    Jalili, P.R.3    Irungu, J.W.4    Nicol, G.R.5
  • 4
    • 77952378813 scopus 로고    scopus 로고
    • Glutamine-linked and non-consensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs
    • Valliere-Douglass JF, Eakin CM, Wallace A, Ketchem RR, Wang W, et al. 2010. Glutamine-linked and non-consensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs. J. Biol. Chem. 285:16012-22
    • (2010) J. Biol. Chem. , vol.285 , pp. 16012-16022
    • Valliere-Douglass, J.F.1    Eakin, C.M.2    Wallace, A.3    Ketchem, R.R.4    Wang, W.5
  • 5
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: Diversity, synthesis and function
    • Moremen KW, Tiemeyer M, Nairn AV. 2012. Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13:448-62
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 6
    • 0028033725 scopus 로고
    • New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us
    • Hofsteenge J,Müller DR, de Beer T, Löffler A, Richter WJ, Vliegenthart JF. 1994. New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us. Biochemistry 33:13524-30
    • (1994) Biochemistry , vol.33 , pp. 13524-13530
    • Hofsteenge, J.1    Müller, D.R.2    De Beer, T.3    Löffler, A.4    Richter, W.J.5    Vliegenthart, J.F.6
  • 9
    • 77955440095 scopus 로고    scopus 로고
    • Characterization of site-specific. O-glycan structures within the mucin-like domain of α-dystroglycan from human skeletal muscle
    • Nilsson J, Larson G, Grahn A. 2010. Characterization of site-specific O-glycan structures within the mucin-like domain of α-dystroglycan from human skeletal muscle. Glycobiology 20:1160-69
    • (2010) Glycobiology , vol.20 , pp. 1160-1169
    • Nilsson, J.1    Larson, G.2    Grahn, A.3
  • 10
    • 77955286333 scopus 로고    scopus 로고
    • Site mapping and characterization of O-glycan structures on α-dystroglycan isolated from rabbit skeletal muscle
    • Stalnaker SH,Hashmi S,Lim JM,AokiK, PorterfieldM, et al. 2010. Site mapping and characterization of O-glycan structures on α-dystroglycan isolated from rabbit skeletal muscle. J. Biol. Chem. 285:24882-91
    • (2010) J. Biol. Chem. , vol.285 , pp. 24882-24891
    • Stalnaker, S.H.1    Hashmi, S.2    Lim, J.M.3    Aoki, K.4    Porterfield, M.5
  • 12
    • 84865300414 scopus 로고    scopus 로고
    • Phosphofructokinase 1 glycosylation regulates cell growth and metabolism
    • Yi W, Clark PM, Mason DE, Keenan MC, Hill C, et al. 2012. Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337:975-80
    • (2012) Science , vol.337 , pp. 975-980
    • Yi, W.1    Clark, P.M.2    Mason, D.E.3    Keenan, M.C.4    Hill, C.5
  • 13
    • 68549091059 scopus 로고    scopus 로고
    • Proposal for a standard system for drawing structural diagrams of N-andO-linked carbohydrates and related compounds
    • Harvey DJ, Merry AH, Royle L, Campbell MP, Dwek RA, Rudd PM. 2009. Proposal for a standard system for drawing structural diagrams ofN-andO-linked carbohydrates and related compounds. Proteomics 9:3796-801
    • (2009) Proteomics , vol.9 , pp. 3796-3801
    • Harvey, D.J.1    Merry, A.H.2    Royle, L.3    Campbell, M.P.4    Dwek, R.A.5    Rudd, P.M.6
  • 14
    • 0035894307 scopus 로고    scopus 로고
    • Microscale nonreductive release of O-linked glycans for subsequent analysis throughMALDImass spectrometry and capillary electrophoresis
    • Huang Y,Mechref Y, Novotny MV. 2001. Microscale nonreductive release ofO-linked glycans for subsequent analysis throughMALDImass spectrometry and capillary electrophoresis. Anal. Chem. 73:6063-69
    • (2001) Anal. Chem. , vol.73 , pp. 6063-6069
    • Huang, Y.1    Mechref, Y.2    Novotny, M.V.3
  • 15
    • 0035983383 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry compatible β-elimination of O-linked oligosaccharides
    • Huang Y, Konse T, Mechref Y, Novotny MV. 2002. Matrix-assisted laser desorption/ionization mass spectrometry compatible β-elimination of O-linked oligosaccharides. Rapid Commun. Mass Spectrom. 16:1199-204
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1199-1204
    • Huang, Y.1    Konse, T.2    Mechref, Y.3    Novotny, M.V.4
  • 16
    • 78650370233 scopus 로고    scopus 로고
    • Glycoblotting-assisted Oglycomics: Ammonium carbamate allows for highly efficient O-glycan release from glycoproteins
    • Miura Y, Kato K, Takegawa Y, Kurogochi M, Furukawa J, et al. 2010. Glycoblotting-assisted Oglycomics: Ammonium carbamate allows for highly efficient O-glycan release from glycoproteins. Anal. Chem. 82:10021-29
    • (2010) Anal. Chem. , vol.82 , pp. 10021-10029
    • Miura, Y.1    Kato, K.2    Takegawa, Y.3    Kurogochi, M.4    Furukawa, J.5
  • 17
    • 0021189137 scopus 로고
    • Demonstration of peptide: N-glycosidase F activity in endo-β-N-acetylglucosaminidase F preparations
    • Plummer TH Jr, Elder JH, Alexander S, Phelan AW, Tarentino AL. 1984. Demonstration of peptide: N-glycosidase F activity in endo-β-N- acetylglucosaminidase F preparations. J. Biol. Chem. 259:10700-4
    • (1984) J. Biol. Chem. , vol.259 , pp. 10700-10704
    • Plummer Jr., T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 18
    • 0025923253 scopus 로고
    • Peptide-N 4-(N-acetyl-β-glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α(1→3) to the asparagine-linked N-acetylglucosamine residue
    • Tretter V, Altmann F, Marz L. 1991. Peptide-N4-(N-acetyl-β- glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α(1→3) to the asparagine-linked N-acetylglucosamine residue. Eur. J. Biochem. 199:647-52
    • (1991) Eur. J. Biochem. , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    Marz, L.3
  • 19
    • 0033106490 scopus 로고    scopus 로고
    • 18O-labeling of N-glycosylation sites to improve the identification of gelseparated glycoproteins using peptide mass mapping and database searching
    • Kuster B, Mann M. 1999. 18O-labeling of N-glycosylation sites to improve the identification of gelseparated glycoproteins using peptide mass mapping and database searching. Anal. Chem. 71:1431-40
    • (1999) Anal. Chem. , vol.71 , pp. 1431-1440
    • Kuster, B.1    Mann, M.2
  • 20
    • 77953240454 scopus 로고    scopus 로고
    • Precisionmapping of an in vivoN-glycoproteome reveals rigid topological and sequence constraints
    • ZielinskaDF, Gnad F, Wisniewski JR,MannM. 2010. Precisionmapping of an in vivoN-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    Wisniewski, J.R.3    Mann, M.4
  • 21
    • 84857873715 scopus 로고    scopus 로고
    • Chemical deamidation: A common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses
    • Palmisano G, Melo-Braga MN, Engholm-Keller K, Parker BL, Larsen MR. 2012. Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses. J. Proteome Res. 11:1949-57
    • (2012) J. Proteome Res. , vol.11 , pp. 1949-1957
    • Palmisano, G.1    Melo-Braga, M.N.2    Engholm-Keller, K.3    Parker, B.L.4    Larsen, M.R.5
  • 23
    • 33750632035 scopus 로고    scopus 로고
    • Rapid removal of N-linked oligosaccharides using microwave assisted enzyme catalyzed deglycosylation
    • Sandoval WN, Arellano F, Arnott D, Raab H, Vandlen R, Lill JR. 2007. Rapid removal of N-linked oligosaccharides using microwave assisted enzyme catalyzed deglycosylation. Int. J. Mass Spectrom. 259:117-23
    • (2007) Int. J. Mass Spectrom. , vol.259 , pp. 117-123
    • Sandoval, W.N.1    Arellano, F.2    Arnott, D.3    Raab, H.4    Vandlen, R.5    Lill, J.R.6
  • 24
    • 51549116674 scopus 로고    scopus 로고
    • Facile MALDI-MS analysis of neutral glycans inNaOH-doped matrixes: Microwave-assisted deglycosylation and one-step purification with diamond nanoparticles
    • Tzeng YK, Chang CC, Huang CN, Wu CC, Han CC, Chang HC. 2008. Facile MALDI-MS analysis of neutral glycans inNaOH-doped matrixes: microwave-assisted deglycosylation and one-step purification with diamond nanoparticles. Anal. Chem. 80:6809-14
    • (2008) Anal. Chem. , vol.80 , pp. 6809-6814
    • Tzeng, Y.K.1    Chang, C.C.2    Huang, C.N.3    Wu, C.C.4    Han, C.C.5    Chang, H.C.6
  • 25
    • 33748505442 scopus 로고    scopus 로고
    • Mass spectrometry-based glycomics strategy for explorin N-linked glycosylation in eukaryotes and bacteria
    • Liu X, McNally DJ, Nothaft H, Szymanski CM, Brisson JR, Li J. 2006. Mass spectrometry-based glycomics strategy for exploringN-linked glycosylation in eukaryotes and bacteria. Anal. Chem. 78:6081-87
    • (2006) Anal. Chem. , vol.78 , pp. 6081-6087
    • Liu, X.1    McNally, D.J.2    Nothaft, H.3    Szymanski, C.M.4    Brisson, J.R.5    Li, J.6
  • 26
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An HJ, Peavy TR, Hedrick JL, Lebrilla CB. 2003. Determination of N-glycosylation sites and site heterogeneity in glycoproteins. Anal. Chem. 75:5628-37
    • (2003) Anal. Chem. , vol.75 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 27
    • 33846200859 scopus 로고    scopus 로고
    • Pronase-immobilized enzyme reactor: An approach for automation in glycoprotein analysis by LC/LC-ESI/MS
    • TemporiniC, Perani E,Calleri E, Dolcini L, Lubda D, et al. 2007. Pronase-immobilized enzyme reactor: an approach for automation in glycoprotein analysis by LC/LC-ESI/MS. Anal. Chem. 79:355-63
    • (2007) Anal. Chem. , vol.79 , pp. 355-363
    • Temporinic1    Perani, E.2    Calleri, E.3    Dolcini, L.4    Lubda, D.5
  • 28
    • 0027346353 scopus 로고
    • Release of O-linked glycoprotein glycans by endo-α-N- acetylgalactosaminidase
    • Iwase H,Hotta K. 1993. Release ofO-linked glycoprotein glycans by endo-α-N-acetylgalactosaminidase. Methods Mol. Biol. 14:151-59
    • (1993) Methods Mol. Biol. , vol.14 , pp. 151-159
    • Iwase, H.1    Hotta, K.2
  • 29
    • 0014408452 scopus 로고
    • Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins
    • Carlson DM. 1968. Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins. J. Biol. Chem. 243:616-26
    • (1968) J. Biol. Chem. , vol.243 , pp. 616-626
    • Carlson, D.M.1
  • 30
    • 84989069128 scopus 로고
    • Determination of glycosylation sites in O-linked glycopeptides: A sensitive mass spectrometric protocol
    • Rademaker JG, Haverkamp J, Thomas-Oates J. 1993. Determination of glycosylation sites in O-linked glycopeptides: a sensitive mass spectrometric protocol. Org. Mass Spectrom. 28:1536-41
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1536-1541
    • Rademaker, J.G.1    Haverkamp, J.2    Thomas-Oates, J.3
  • 31
    • 77949858337 scopus 로고    scopus 로고
    • Rapid de-O-glycosylation concomitant with peptide labeling using microwave radiation and an alkyl amine base
    • Maniatis S, Zhou H, Reinhold V. 2010. Rapid de-O-glycosylation concomitant with peptide labeling using microwave radiation and an alkyl amine base. Anal. Chem. 82:2421-25
    • (2010) Anal. Chem. , vol.82 , pp. 2421-2425
    • Maniatis, S.1    Zhou, H.2    Reinhold, V.3
  • 32
    • 73249128479 scopus 로고    scopus 로고
    • Enzymatic/chemical release of O-glycans allowing MS analysis at high sensitivity
    • Goetz JA, Novotny MV, Mechref Y. 2009. Enzymatic/chemical release of O-glycans allowing MS analysis at high sensitivity. Anal. Chem. 81:9546-52
    • (2009) Anal. Chem. , vol.81 , pp. 9546-9552
    • Goetz, J.A.1    Novotny, M.V.2    Mechref, Y.3
  • 33
    • 79955616736 scopus 로고    scopus 로고
    • Derivatization of carbohydrates for analysis by chromatography, electrophoresis and mass spectrometry
    • Harvey DJ. 2011. Derivatization of carbohydrates for analysis by chromatography, electrophoresis and mass spectrometry. J. Chromatogr. B 879:1196-225
    • (2011) J. Chromatogr. B , vol.879 , pp. 1196-1225
    • Harvey, D.J.1
  • 34
    • 77955764774 scopus 로고
    • A rapid permethylation of glycolipid and polysaccharide catalyzed by methylsulfinyl carbanion in dimethyl sulfoxide
    • Hakomori S. 1964. A rapid permethylation of glycolipid and polysaccharide catalyzed by methylsulfinyl carbanion in dimethyl sulfoxide. J. Biochem. 55:205-8
    • (1964) J. Biochem. , vol.55 , pp. 205-208
    • Hakomori, S.1
  • 35
    • 34447326804 scopus 로고
    • A simple and rapidmethod for the permethylation of carbohydrates
    • Ciucanu I,Kerek F. 1984. A simple and rapidmethod for the permethylation of carbohydrates. Carbohydr. Res. 131:209-17
    • (1984) Carbohydr. Res. , vol.131 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 36
    • 0347064294 scopus 로고    scopus 로고
    • Elimination of oxidative degradation during the per O-methylation of carbohydrates
    • Ciucanu I, Costello CE. 2003. Elimination of oxidative degradation during the per-O-methylation of carbohydrates. J. Am. Chem. Soc. 125:16213-19
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16213-16219
    • Ciucanu, I.1    Costello, C.E.2
  • 38
    • 40649108313 scopus 로고    scopus 로고
    • High-throughput solid-phase permethylation of glycans prior to mass spectrometry
    • Kang P, Mechref Y, Novotny MV. 2008. High-throughput solid-phase permethylation of glycans prior to mass spectrometry. Rapid Commun. Mass Spectrom. 22:721-34
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 721-734
    • Kang, P.1    Mechref, Y.2    Novotny, M.V.3
  • 39
    • 83755224361 scopus 로고    scopus 로고
    • Enhanced sensitivity of LC-MS analysis of permethylated N-glycans through online purification
    • Desantos-Garcia JL, Khalil SI, Hussein A, Hu Y, Mechref Y. 2011. Enhanced sensitivity of LC-MS analysis of permethylated N-glycans through online purification. Electrophoresis 32:3516-25
    • (2011) Electrophoresis , vol.32 , pp. 3516-3525
    • Desantos-Garcia, J.L.1    Khalil, S.I.2    Hussein, A.3    Hu, Y.4    Mechref, Y.5
  • 40
    • 29144484770 scopus 로고    scopus 로고
    • Characterisation and proposed origin of mass spectrometric ions observed 30 Th above the ionised molecules of per O-methylated carbohydrates
    • Robinson S, Routledge A, Thomas-Oates J. 2005. Characterisation and proposed origin of mass spectrometric ions observed 30 Th above the ionised molecules of per-O-methylated carbohydrates. Rapid Commun. Mass Spectrom. 19:3681-88
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 3681-3688
    • Robinson, S.1    Routledge, A.2    Thomas-Oates, J.3
  • 41
    • 77953555196 scopus 로고    scopus 로고
    • Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: A potential methodology for cancer-biomarker discovery
    • Alley WR Jr, Madera M, Mechref Y, Novotny MV. 2010. Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: a potential methodology for cancer-biomarker discovery. Anal. Chem. 82:5095-106
    • (2010) Anal. Chem. , vol.82 , pp. 5095-5106
    • Alley Jr., W.R.1    Madera, M.2    Mechref, Y.3    Novotny, M.V.4
  • 43
    • 70249134568 scopus 로고    scopus 로고
    • Enabling techniques and strategic workflow for sulfoglycomics based on mass spectrometry mapping and sequencing of permethylated sulfated glycans
    • Yu SY, Wu SW, Hsiao HH, Khoo KH. 2009. Enabling techniques and strategic workflow for sulfoglycomics based on mass spectrometry mapping and sequencing of permethylated sulfated glycans. Glycobiology 19:1136-49
    • (2009) Glycobiology , vol.19 , pp. 1136-1149
    • Yu, S.Y.1    Wu, S.W.2    Hsiao, H.H.3    Khoo, K.H.4
  • 44
    • 69549088131 scopus 로고    scopus 로고
    • Structural analysis of sulfated glycans by sequential double permethylation using methyl iodide and deuteromethyl iodide
    • Lei M, Mechref Y, Novotny MV. 2009. Structural analysis of sulfated glycans by sequential double permethylation using methyl iodide and deuteromethyl iodide. J. Am. Soc. Mass Spectrom. 20:1660-71
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1660-1671
    • Lei, M.1    Mechref, Y.2    Novotny, M.V.3
  • 45
    • 76749097658 scopus 로고    scopus 로고
    • Sequential enrichment of sulfated glycans by strong anionexchange chromatography prior tomass spectrometric measurements
    • Lei M, Novotny MV, Mechref Y. 2010. Sequential enrichment of sulfated glycans by strong anionexchange chromatography prior tomass spectrometric measurements. J. Am. Soc.Mass Spectrom. 21:348-57
    • (2010) J. Am. Soc.Mass Spectrom. , vol.21 , pp. 348-357
    • Lei, M.1    Novotny, M.V.2    Mechref, Y.3
  • 46
    • 0029687475 scopus 로고    scopus 로고
    • Aspects of the sequencing of carbohydrates and oligonucleotides by matrixassisted laser desorption/ionization post-source decay
    • Talbo G, Mann M. 1996. Aspects of the sequencing of carbohydrates and oligonucleotides by matrixassisted laser desorption/ionization post-source decay. Rapid Commun. Mass Spectrom. 10:100-3
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 100-103
    • Talbo, G.1    Mann, M.2
  • 47
    • 0029741839 scopus 로고    scopus 로고
    • Stabilization of sialic acids in N-linked oligosaccharides and gangliosides for analysis by positive ion matrix-assisted laser desorption/ionizationmass spectrometry
    • Powell AK, Harvey DJ. 1996. Stabilization of sialic acids in N-linked oligosaccharides and gangliosides for analysis by positive ion matrix-assisted laser desorption/ionizationmass spectrometry. Rapid Commun. Mass Spectrom. 10:1027-32
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1027-1032
    • Powell, A.K.1    Harvey, D.J.2
  • 48
    • 34249022300 scopus 로고    scopus 로고
    • "One-pot" methylation in glycomics application: Esterification of sialic acids and permanent charge construction
    • Liu X, Li X, Chan K, Zou W, Pribil P, et al. 2007. "One-pot" methylation in glycomics application: esterification of sialic acids and permanent charge construction. Anal. Chem. 79:3894-900
    • (2007) Anal. Chem. , vol.79 , pp. 3894-3900
    • Liu, X.1    Li, X.2    Chan, K.3    Zou, W.4    Pribil, P.5
  • 49
    • 23044435003 scopus 로고    scopus 로고
    • Derivatization for stabilizing sialic acids inMALDI-MS
    • Sekiya S, Wada Y, Tanaka K. 2005. Derivatization for stabilizing sialic acids inMALDI-MS. Anal. Chem. 77:4962-68
    • (2005) Anal. Chem. , vol.77 , pp. 4962-4968
    • Sekiya, S.1    Wada, Y.2    Tanaka, K.3
  • 50
    • 60149097254 scopus 로고    scopus 로고
    • Derivatization of sialic acids for stabilization in matrixassisted laser desorption/ionization mass spectrometry and concomitant differentiation of α(2→3) and α(2→6) isomers
    • Wheeler SF, Domann P, Harvey DJ. 2009. Derivatization of sialic acids for stabilization in matrixassisted laser desorption/ionization mass spectrometry and concomitant differentiation of α(2→3) and α(2→6) isomers. Rapid Commun. Mass Spectrom. 23:303-12
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 303-312
    • Wheeler, S.F.1    Domann, P.2    Harvey, D.J.3
  • 51
    • 77954601866 scopus 로고    scopus 로고
    • Glycomic analysis of sialic acid linkages in glycans derived from blood serum glycoproteins
    • Alley WR Jr, Novotny MV. 2010. Glycomic analysis of sialic acid linkages in glycans derived from blood serum glycoproteins. J. Proteome Res. 9:3062-72
    • (2010) J. Proteome Res. , vol.9 , pp. 3062-3072
    • Alley Jr., W.R.1    Novotny, M.V.2
  • 52
    • 84867824272 scopus 로고    scopus 로고
    • Smoking-and lung cancer-induced changes in N-glycosylation of blood serum proteins
    • Vasseur JA, Goetz JA, Alley WR Jr, Novotny MV. 2012. Smoking-and lung cancer-induced changes in N-glycosylation of blood serum proteins. Glycobiology 22:1684-708
    • (2012) Glycobiology , vol.22 , pp. 1684-1708
    • Vasseur, J.A.1    Goetz, J.A.2    Alley Jr., W.R.3    Novotny, M.V.4
  • 53
    • 46849116602 scopus 로고    scopus 로고
    • Quantitative derivatization of sialic acids for the detection of sialoglycans by MALDI MS
    • Toyoda M, Ito H, Matsuno YK, Narimatsu H, Kameyama A. 2008. Quantitative derivatization of sialic acids for the detection of sialoglycans by MALDI MS. Anal. Chem. 80:5211-18
    • (2008) Anal. Chem. , vol.80 , pp. 5211-5218
    • Toyoda, M.1    Ito, H.2    Matsuno, Y.K.3    Narimatsu, H.4    Kameyama, A.5
  • 54
    • 77957318349 scopus 로고    scopus 로고
    • Methylamidation for sialoglycomics by MALDI-MS: A facile derivatization strategy for both α2,3-and α2,6-linked sialic acids
    • Liu X, Qiu H, Lee RK, Chen W, Li J. 2010. Methylamidation for sialoglycomics by MALDI-MS: a facile derivatization strategy for both α2,3-and α2,6-linked sialic acids. Anal. Chem. 82:8300-6
    • (2010) Anal. Chem. , vol.82 , pp. 8300-8306
    • Liu, X.1    Qiu, H.2    Lee, R.K.3    Chen, W.4    Li, J.5
  • 55
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB. 1995. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 230:229-38
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 56
    • 77953853129 scopus 로고    scopus 로고
    • 2-Picoline-borane: A nontoxic reducing agent for oligosaccharide labeling by reductive amination
    • Ruhaak LR, Steenvoorden E, Koeleman CA, Deelder AM, Wuhrer M. 2010. 2-Picoline-borane: a nontoxic reducing agent for oligosaccharide labeling by reductive amination. Proteomics 10:2330-36
    • (2010) Proteomics , vol.10 , pp. 2330-2336
    • Ruhaak, L.R.1    Steenvoorden, E.2    Koeleman, C.A.3    Deelder, A.M.4    Wuhrer, M.5
  • 58
    • 0029401607 scopus 로고
    • Use of the derivatizing agent 4-aminobenzoic acid 2-(diethylamino)ethyl ester for high-sensitivity detection of oligosaccharides by electrospray ionization mass spectrometry
    • Yoshino K, Takao T, Murata H, Shimonishi Y. 1995. Use of the derivatizing agent 4-aminobenzoic acid 2-(diethylamino)ethyl ester for high-sensitivity detection of oligosaccharides by electrospray ionization mass spectrometry. Anal. Chem. 67:4028-31
    • (1995) Anal. Chem. , vol.67 , pp. 4028-4031
    • Yoshino, K.1    Takao, T.2    Murata, H.3    Shimonishi, Y.4
  • 59
    • 18044365208 scopus 로고    scopus 로고
    • Influence of the labeling group on ionization and fragmentation of carbohydrates in mass spectrometry
    • Lattova E, Snovida S, Perreault H, Krokhin O. 2005. Influence of the labeling group on ionization and fragmentation of carbohydrates in mass spectrometry. J. Am. Soc. Mass Spectrom. 16:683-96
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 683-696
    • Lattova, E.1    Snovida, S.2    Perreault, H.3    Krokhin, O.4
  • 60
    • 33845513762 scopus 로고    scopus 로고
    • Differentiation of isomeric N-glycan structures by normal-phase liquid chromatography-MALDI-TOF/TOF tandem mass spectrometry
    • Maslen S, Sadowski P, Adam A, Lilley K, Stephens E. 2006. Differentiation of isomeric N-glycan structures by normal-phase liquid chromatography-MALDI- TOF/TOF tandem mass spectrometry. Anal. Chem. 78:8491-98
    • (2006) Anal. Chem. , vol.78 , pp. 8491-8498
    • Maslen, S.1    Sadowski, P.2    Adam, A.3    Lilley, K.4    Stephens, E.5
  • 61
    • 19544373158 scopus 로고    scopus 로고
    • Collision-induced fragmentation of negative ions from N-linked glycans derivatized with 2-aminobenzoic acid
    • Harvey DJ. 2005. Collision-induced fragmentation of negative ions from N-linked glycans derivatized with 2-aminobenzoic acid. J. Mass Spectrom. 40:642-53
    • (2005) J. Mass Spectrom. , vol.40 , pp. 642-653
    • Harvey, D.J.1
  • 62
    • 77951859489 scopus 로고    scopus 로고
    • 3-Aminoquinoline acting as matrix and derivatizing agent for MALDI MS analysis of oligosaccharides
    • Rohmer M, Meyer B,Mank M, Stahl B, Bahr U, Karas M. 2010. 3-Aminoquinoline acting as matrix and derivatizing agent for MALDI MS analysis of oligosaccharides. Anal. Chem. 82:3719-26
    • (2010) Anal. Chem. , vol.82 , pp. 3719-3726
    • Rohmer, M.1    Meyer, B.2    Mank, M.3    Stahl, B.4    Bahr, U.5    Karas, M.6
  • 63
    • 0038445722 scopus 로고    scopus 로고
    • Labelling saccharides with phenylhydrazine for electrospray and matrixassisted laser desorption/ionization mass spectrometry
    • Lattova E, Perreault H. 2003. Labelling saccharides with phenylhydrazine for electrospray and matrixassisted laser desorption/ionization mass spectrometry. J. Chromatogr. B 793:167-79
    • (2003) J. Chromatogr. B , vol.793 , pp. 167-179
    • Lattova, E.1    Perreault, H.2
  • 64
    • 80052329656 scopus 로고    scopus 로고
    • Hydrophobic derivatization of N-linked glycans for increased ion abundance in electrospray ionization mass spectrometry
    • Walker SH,Lilley LM, Enamorado MF, Comins DL,Muddiman DC. 2011. Hydrophobic derivatization of N-linked glycans for increased ion abundance in electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 22:1309-17
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1309-1317
    • Walker, S.H.1    Lilley, L.M.2    Enamorado, M.F.3    Comins, D.L.4    Muddiman, D.C.5
  • 65
    • 77955144560 scopus 로고    scopus 로고
    • Interplay of permanent charge and hydrophobicity in the electrospray ionization of glycans
    • Walker SH, Papas BN, Comins DL, Muddiman DC. 2010. Interplay of permanent charge and hydrophobicity in the electrospray ionization of glycans. Anal. Chem. 82:6636-42
    • (2010) Anal. Chem. , vol.82 , pp. 6636-6642
    • Walker, S.H.1    Papas, B.N.2    Comins, D.L.3    Muddiman, D.C.4
  • 66
    • 34548012656 scopus 로고    scopus 로고
    • Comparative glycomicmapping through quantitative permethylation and stable-isotope labeling
    • Kang P, Mechref Y,Kyselova Z,Goetz JA, Novotny MV. 2007. Comparative glycomicmapping through quantitative permethylation and stable-isotope labeling. Anal. Chem. 79:6064-73
    • (2007) Anal. Chem. , vol.79 , pp. 6064-6073
    • Kang, P.1    Mechref, Y.2    Kyselova, Z.3    Goetz, J.A.4    Novotny, M.V.5
  • 67
    • 34447312516 scopus 로고    scopus 로고
    • Tools for glycomics: Relative quantitation of glycans by isotopic permethylation using 13CH3I
    • Alvarez-Manilla G, Warren NL, Abney T, Atwood JA 3rd, Azadi P, et al. 2007. Tools for glycomics: relative quantitation of glycans by isotopic permethylation using 13CH3I. Glycobiology 17:677-87
    • (2007) Glycobiology , vol.17 , pp. 677-687
    • Alvarez-Manilla, G.1    Warren, N.L.2    Abney, T.3    Atwood Iii., J.A.4    Azadi, P.5
  • 69
    • 57749107717 scopus 로고    scopus 로고
    • Evolutionary differences in glycosaminoglycan fine structure detected by quantitative glycan reductive isotope labeling
    • Lawrence R, Olson SK, Steele RE, Wang L, Warrior R, et al. 2008. Evolutionary differences in glycosaminoglycan fine structure detected by quantitative glycan reductive isotope labeling. J. Biol. Chem. 283:33674-84
    • (2008) J. Biol. Chem. , vol.283 , pp. 33674-33684
    • Lawrence, R.1    Olson, S.K.2    Steele, R.E.3    Wang, L.4    Warrior, R.5
  • 70
    • 50649105755 scopus 로고    scopus 로고
    • Oligosaccharide relative quantitation using isotope tagging and normal-phase liquid chromatography/mass spectrometry
    • Ridlova G,Mortimer JC, Maslen SL,Dupree P, Stephens E. 2008. Oligosaccharide relative quantitation using isotope tagging and normal-phase liquid chromatography/mass spectrometry. Rapid Commun. Mass Spectrom. 22:2723-30
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 2723-2730
    • Ridlova, G.1    Mortimer, J.C.2    Maslen, S.L.3    Dupree, P.4    Stephens, E.5
  • 72
    • 59449086729 scopus 로고    scopus 로고
    • Alteration of Nglycosylation in the kidney in a mouse model of systemic lupus erythematosus: Relative quantification of N-glycans using an isotope-tagging method
    • Hashii N, Kawasaki N, Itoh S, Nakajima Y, Kawanishi T, Yamaguchi T. 2009. Alteration of Nglycosylation in the kidney in a mouse model of systemic lupus erythematosus: relative quantification of N-glycans using an isotope-tagging method. Immunology 126:336-45
    • (2009) Immunology , vol.126 , pp. 336-345
    • Hashii, N.1    Kawasaki, N.2    Itoh, S.3    Nakajima, Y.4    Kawanishi, T.5    Yamaguchi, T.6
  • 73
    • 76849086981 scopus 로고    scopus 로고
    • Mass spectrometric-based stable isotopic 2-aminobenzoic acid glycan mapping for rapid glycan screening of biotherapeutics
    • Prien JM, Prater BD, Qin Q, Cockrill SL. 2010. Mass spectrometric-based stable isotopic 2-aminobenzoic acid glycan mapping for rapid glycan screening of biotherapeutics. Anal. Chem. 82:1498-508
    • (2010) Anal. Chem. , vol.82 , pp. 1498-1508
    • Prien, J.M.1    Prater, B.D.2    Qin, Q.3    Cockrill, S.L.4
  • 74
    • 80052268765 scopus 로고    scopus 로고
    • Relative quantitation of glycans using stable isotopic labels 1-(d0/d5) phenyl-3-methyl-5-pyrazolone by mass spectrometry
    • Zhang P, Zhang Y, Xue X, Wang C, Wang Z, Huang L. 2011. Relative quantitation of glycans using stable isotopic labels 1-(d0/d5) phenyl-3-methyl-5-pyrazolone by mass spectrometry. Anal. Biochem. 418:1-9
    • (2011) Anal. Biochem. , vol.418 , pp. 1-9
    • Zhang, P.1    Zhang, Y.2    Xue, X.3    Wang, C.4    Wang, Z.5    Huang, L.6
  • 75
    • 80052327326 scopus 로고    scopus 로고
    • Stable-isotope labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry
    • Walker SH, Budhathoki-Uprety J, Novak BM,Muddiman DC. 2011. Stable-isotope labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry. Anal. Chem. 83:6738-45
    • (2011) Anal. Chem. , vol.83 , pp. 6738-6745
    • Walker, S.H.1    Budhathoki-Uprety, J.2    Novak, B.M.3    Muddiman, D.C.4
  • 76
    • 34547767471 scopus 로고    scopus 로고
    • Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry
    • Bowman MJ, Zaia J. 2007. Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry. Anal. Chem. 79:5777-84
    • (2007) Anal. Chem. , vol.79 , pp. 5777-5784
    • Bowman, M.J.1    Zaia, J.2
  • 77
    • 77950421797 scopus 로고    scopus 로고
    • Comparative glycomics using a tetraplex stable-isotope coded tag
    • Bowman MJ, Zaia J. 2010. Comparative glycomics using a tetraplex stable-isotope coded tag. Anal. Chem. 82:3023-31
    • (2010) Anal. Chem. , vol.82 , pp. 3023-3031
    • Bowman, M.J.1    Zaia, J.2
  • 78
    • 68549133585 scopus 로고    scopus 로고
    • IDAWG: Metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells
    • Orlando R, Lim JM, Atwood JA 3rd, Angel PM, Fang M, et al. 2009. IDAWG: metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells. J. Proteome Res. 8:3816-23
    • (2009) J. Proteome Res. , vol.8 , pp. 3816-3823
    • Orlando, R.1    Lim, J.M.2    Atwood Iii., J.A.3    Angel, P.M.4    Fang, M.5
  • 79
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon B, Costello CE. 1988. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 5:397-409
    • (1988) Glycoconj. J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 80
    • 0032774471 scopus 로고    scopus 로고
    • Fragmentation reactions in themass spectrometry analysis of neutral oligosaccharides
    • Cancilla MT,Wong AW,Voss LR,Lebrilla CB. 1999. Fragmentation reactions in themass spectrometry analysis of neutral oligosaccharides. Anal. Chem. 71:3206-18
    • (1999) Anal. Chem. , vol.71 , pp. 3206-3218
    • Cancilla, M.T.1    Wong, A.W.2    Voss, L.R.3    Lebrilla, C.B.4
  • 81
    • 0033763508 scopus 로고    scopus 로고
    • Collision-induced fragmentation of underivatized N-linked carbohydrates ionized by electrospray
    • Harvey DJ. 2000. Collision-induced fragmentation of underivatized N-linked carbohydrates ionized by electrospray. J. Mass Spectrom. 35:1178-90
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1178-1190
    • Harvey, D.J.1
  • 82
    • 0141482211 scopus 로고    scopus 로고
    • Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry
    • Mechref Y, Novotny MV, Krishnan C. 2003. Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 75:4895-903
    • (2003) Anal. Chem. , vol.75 , pp. 4895-4903
    • Mechref, Y.1    Novotny, M.V.2    Krishnan, C.3
  • 83
    • 1942454436 scopus 로고    scopus 로고
    • Fragmentation characteristics of neutral Nlinked glycans using a MALDI-TOF/TOF tandem mass spectrometer
    • Stephens E, Maslen SL, Green LG, Williams DH. 2004. Fragmentation characteristics of neutral Nlinked glycans using a MALDI-TOF/TOF tandem mass spectrometer. Anal. Chem. 76:2343-54
    • (2004) Anal. Chem. , vol.76 , pp. 2343-2354
    • Stephens, E.1    Maslen, S.L.2    Green, L.G.3    Williams, D.H.4
  • 84
    • 33645848490 scopus 로고    scopus 로고
    • Differentiating structural isomers of sialylated glycans bymatrixassisted laser desorption/ionization time-of-flight/time-of-flight tandem mass spectrometry
    • MechrefY,KangP,Novotny MV.2006. Differentiating structural isomers of sialylated glycans bymatrixassisted laser desorption/ionization time-of-flight/time-of-flight tandem mass spectrometry. Rapid Commun. Mass Spectrom. 20:1381-89
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 1381-1389
    • Mechref, Y.1    Kang, P.2    Novotny, M.V.3
  • 85
    • 0032527169 scopus 로고    scopus 로고
    • Structural characterization of carbohydrate sequence, linkage, and branching in a quadrupole ion trap mass spectrometer: Neutral oligosaccharides and N-linked glycans
    • Sheeley DM, Reinhold VN. 1998. Structural characterization of carbohydrate sequence, linkage, and branching in a quadrupole ion trap mass spectrometer: neutral oligosaccharides and N-linked glycans. Anal. Chem. 70:3053-59
    • (1998) Anal. Chem. , vol.70 , pp. 3053-3059
    • Sheeley, D.M.1    Reinhold, V.N.2
  • 86
    • 34249087407 scopus 로고    scopus 로고
    • Carbohydrate structural isomers analyzed by sequential mass spectrometry
    • Ashline DJ, Lapadula AJ, Liu YH, LinM,Grace M, et al. 2007. Carbohydrate structural isomers analyzed by sequential mass spectrometry. Anal. Chem. 79:3830-42
    • (2007) Anal. Chem. , vol.79 , pp. 3830-3842
    • Ashline, D.J.1    Lapadula, A.J.2    Liu, Y.H.3    Lin, M.4    Grace, M.5
  • 87
    • 42449103892 scopus 로고    scopus 로고
    • Differentiating N-linked glycan structural isomers in metastatic and nonmetastatic tumor cells using sequential mass spectrometry
    • Prien JM, Huysentruyt LC, Ashline DJ, Lapadula AJ, Seyfried TN, Reinhold VN. 2008. Differentiating N-linked glycan structural isomers in metastatic and nonmetastatic tumor cells using sequential mass spectrometry. Glycobiology 18:353-66
    • (2008) Glycobiology , vol.18 , pp. 353-366
    • Prien, J.M.1    Huysentruyt, L.C.2    Ashline, D.J.3    Lapadula, A.J.4    Seyfried, T.N.5    Reinhold, V.N.6
  • 89
    • 77952820391 scopus 로고    scopus 로고
    • A multi-method approach toward de novo glycan characterization: A Man-5 case study
    • Prien JM, Prater BD, Cockrill SL. 2010. A multi-method approach toward de novo glycan characterization: a Man-5 case study. Glycobiology 20:629-47
    • (2010) Glycobiology , vol.20 , pp. 629-647
    • Prien, J.M.1    Prater, B.D.2    Cockrill, S.L.3
  • 90
    • 41549130879 scopus 로고    scopus 로고
    • Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (β1-4-GlcNAc) residue in N-glycans from IgG
    • Harvey DJ, Crispin M, Scanlan C, Singer BB, Lucka L, et al. 2008. Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (β1-4-GlcNAc) residue in N-glycans from IgG. Rapid Commun. Mass Spectrom. 22:1047-52
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 1047-1052
    • Harvey, D.J.1    Crispin, M.2    Scanlan, C.3    Singer, B.B.4    Lucka, L.5
  • 91
    • 14344259450 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates. Part 1. Use of nitrate and other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates
    • Harvey DJ. 2005. Fragmentation of negative ions from carbohydrates. Part 1. Use of nitrate and other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates. J. Am. Soc. Mass Spectrom. 16:622-30
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 622-630
    • Harvey, D.J.1
  • 92
    • 18044364597 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates. Part 2. Fragmentation of highmannose N-linked glycans
    • Harvey DJ. 2005. Fragmentation of negative ions from carbohydrates. Part 2. Fragmentation of highmannose N-linked glycans. J. Am. Soc. Mass Spectrom. 16:631-46
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 631-646
    • Harvey, D.J.1
  • 93
    • 14344254313 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates. Part 3. Fragmentation of hybrid and complex N-linked glycans
    • Harvey DJ. 2005. Fragmentation of negative ions from carbohydrates. Part 3. Fragmentation of hybrid and complex N-linked glycans. J. Am. Soc. Mass Spectrom. 16:647-59
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 647-659
    • Harvey, D.J.1
  • 94
    • 33747730865 scopus 로고    scopus 로고
    • The influence of sialylation on glycan negative ion dissociation and energetics
    • Seymour JL, Costello CE, Zaia J. 2006. The influence of sialylation on glycan negative ion dissociation and energetics. J. Am. Soc. Mass Spectrom. 17:844-54
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 844-854
    • Seymour, J.L.1    Costello, C.E.2    Zaia, J.3
  • 95
    • 80051552400 scopus 로고    scopus 로고
    • Fragmentation of negative ions from N-linked carbohydrates. Part 5. Anionic N-linked glycans
    • Harvey DJ, Rudd PM. 2011. Fragmentation of negative ions from N-linked carbohydrates. Part 5. Anionic N-linked glycans. Int. J. Mass Spectrom. 305:120-30
    • (2011) Int. J. Mass Spectrom. , vol.305 , pp. 120-130
    • Harvey, D.J.1    Rudd, P.M.2
  • 96
    • 27544446037 scopus 로고    scopus 로고
    • Negative-mode MALDI-TOF/TOF-MS of oligosaccharides labeled with 2-aminobenzamide
    • Wuhrer M, Deelder AM. 2005. Negative-mode MALDI-TOF/TOF-MS of oligosaccharides labeled with 2-aminobenzamide. Anal. Chem. 77:6954-59
    • (2005) Anal. Chem. , vol.77 , pp. 6954-6959
    • Wuhrer, M.1    Deelder, A.M.2
  • 97
    • 33846811132 scopus 로고    scopus 로고
    • An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/TOF instrument
    • Pringle SD, Giles K,Wildgoose JL, Williams JP, Slade SE, et al. 2007. An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/TOF instrument. Int. J. Mass Spectrom. 261:1-12
    • (2007) Int. J. Mass Spectrom. , vol.261 , pp. 1-12
    • Pringle, S.D.1    Giles, K.2    Wildgoose, J.L.3    Williams, J.P.4    Slade, S.E.5
  • 99
    • 78349304013 scopus 로고    scopus 로고
    • Characterization of simple isomeric oligosaccharides and the rapid separation of glycan mixtures by ion mobility mass spectrometry
    • Williams JP, Grabenauer M, Carpenter CJ, Holland RJ, Wormald MR, et al. 2010. Characterization of simple isomeric oligosaccharides and the rapid separation of glycan mixtures by ion mobility mass spectrometry. Int. J. Mass Spectrom. 298:119-27
    • (2010) Int. J. Mass Spectrom. , vol.298 , pp. 119-127
    • Williams, J.P.1    Grabenauer, M.2    Carpenter, C.J.3    Holland, R.J.4    Wormald, M.R.5
  • 100
    • 15144345257 scopus 로고    scopus 로고
    • Characterizing oligosaccharides using injected ion mobility/mass spectrometry
    • Liu Y, Clemmer DE. 1997. Characterizing oligosaccharides using injected ion mobility/mass spectrometry. Anal. Chem. 69:2504-9
    • (1997) Anal. Chem. , vol.69 , pp. 2504-2509
    • Liu, Y.1    Clemmer, D.E.2
  • 104
    • 70349970185 scopus 로고    scopus 로고
    • Simultaneous glycoproteomics on the basis of structure using ion mobility-mass spectrometry
    • Fenn LS,McLean JA. 2009. Simultaneous glycoproteomics on the basis of structure using ion mobility-mass spectrometry. Mol. Biosyst. 5:1298-302
    • (2009) Mol. Biosyst. , vol.5 , pp. 1298-1302
    • Fenn, L.S.1    McLean, J.A.2
  • 105
    • 79955753022 scopus 로고    scopus 로고
    • Ionmobilitymass spectrometry for extracting spectra ofN-glycans directly from incubation mixtures following glycan release: Application to glycans from engineered glycoforms of intact, folded HIV gp120
    • Harvey DJ, Sobott F,Crispin M, Wrobel A, Bonomelli C, et al. 2011. Ionmobilitymass spectrometry for extracting spectra ofN-glycans directly from incubation mixtures following glycan release: application to glycans from engineered glycoforms of intact, folded HIV gp120. J. Am. Soc. Mass Spectrom. 22:568-81
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 568-581
    • Harvey, D.J.1    Sobott, F.2    Crispin, M.3    Wrobel, A.4    Bonomelli, C.5
  • 106
    • 0025173758 scopus 로고
    • Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds
    • Alpert AJ. 1990. Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds. J. Chromatogr. 499:177-96
    • (1990) J. Chromatogr. , vol.499 , pp. 177-196
    • Alpert, A.J.1
  • 107
    • 36248972262 scopus 로고    scopus 로고
    • Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG
    • Saldova R, Royle L, Radcliffe CM, Abd Hamid UM, Evans R, et al. 2007. Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG. Glycobiology 17:1344-56
    • (2007) Glycobiology , vol.17 , pp. 1344-1356
    • Saldova, R.1    Royle, L.2    Radcliffe, C.M.3    Abd Hamid, U.M.4    Evans, R.5
  • 108
    • 57049137606 scopus 로고    scopus 로고
    • A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression
    • AbdHamid UM, Royle L, Saldova R, Radcliffe CM,Harvey DJ, et al. 2008. A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression. Glycobiology 18:1105-18
    • (2008) Glycobiology , vol.18 , pp. 1105-1118
    • Abdhamid, U.M.1    Royle, L.2    Saldova, R.3    Radcliffe, C.M.4    Harvey, D.J.5
  • 110
    • 77954518174 scopus 로고    scopus 로고
    • Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans
    • Knezevic A, Gornik O, Polasek O, Pucic M, Redzic I, et al. 2010. Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans. Glycobiology 20:959-69
    • (2010) Glycobiology , vol.20 , pp. 959-969
    • Knezevic, A.1    Gornik, O.2    Polasek, O.3    Pucic, M.4    Redzic, I.5
  • 111
    • 80054016444 scopus 로고    scopus 로고
    • High throughput isolation and glycosylation analysis of IgG variability and heritability of the IgG glycome in three isolated human populations
    • Pucic M, Knezevic A, Vidic J, Adamczyk B, Novokmet M, et al. 2011. High throughput isolation and glycosylation analysis of IgG variability and heritability of the IgG glycome in three isolated human populations. Mol. Cell. Proteomics 10:010090
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 010090
    • Pucic, M.1    Knezevic, A.2    Vidic, J.3    Adamczyk, B.4    Novokmet, M.5
  • 112
    • 34548681626 scopus 로고    scopus 로고
    • A glycomics platform for the analysis of permethylated oligosaccharide alditols
    • Costello CE, Contado-Miller JM, Cipollo JF. 2007. A glycomics platform for the analysis of permethylated oligosaccharide alditols. J. Am. Soc. Mass Spectrom. 18:1799-812
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1799-1812
    • Costello, C.E.1    Contado-Miller, J.M.2    Cipollo, J.F.3
  • 113
    • 34447343820 scopus 로고    scopus 로고
    • Mass + retention time = structure: A strategy for the analysis of N-glycans by carbon LC-ESI-MS and its application to fibrin N-glycans
    • Pabst M, Bondili JS, Stadlmann J, Mach L, Altmann F. 2007. Mass + retention time = structure: a strategy for the analysis of N-glycans by carbon LC-ESI-MS and its application to fibrin N-glycans. Anal. Chem. 79:5051-57
    • (2007) Anal. Chem. , vol.79 , pp. 5051-5057
    • Pabst, M.1    Bondili, J.S.2    Stadlmann, J.3    Mach, L.4    Altmann, F.5
  • 114
    • 84856269227 scopus 로고    scopus 로고
    • Isomeric analysis of oligomannosidic N-glycans and their dolichol-linked precursors
    • PabstM, Grass J, Toegel S, Liebminger E, Strasser R, Altmann F. 2012. Isomeric analysis of oligomannosidic N-glycans and their dolichol-linked precursors. Glycobiology 22:389-99
    • (2012) Glycobiology , vol.22 , pp. 389-399
    • Pabst, M.1    Grass, J.2    Toegel, S.3    Liebminger, E.4    Strasser, R.5    Altmann, F.6
  • 115
    • 54749113731 scopus 로고    scopus 로고
    • Influence of electrosorption, solvent, temperature, and ion polarity on the performance of LC-ESI-MS using graphitic carbon for acidic oligosaccharides
    • Pabst M, Altmann F. 2008. Influence of electrosorption, solvent, temperature, and ion polarity on the performance of LC-ESI-MS using graphitic carbon for acidic oligosaccharides. Anal. Chem. 80:7534-42
    • (2008) Anal. Chem. , vol.80 , pp. 7534-7542
    • Pabst, M.1    Altmann, F.2
  • 116
    • 74049141466 scopus 로고    scopus 로고
    • Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 micron sorbent
    • Ahn J, Bones J, Yu YQ, Rudd PM, Gilar M. 2010. Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 micron sorbent. J. Chromatogr. B 878:403-8
    • (2010) J. Chromatogr. B , vol.878 , pp. 403-408
    • Ahn, J.1    Bones, J.2    Yu, Y.Q.3    Rudd, P.M.4    Gilar, M.5
  • 117
    • 12244255362 scopus 로고    scopus 로고
    • Microfluidic chip for peptide analysis with an integrated HPLC column, sample enrichment column, and nanoelectrospray tip
    • Yin H, Killeen K, Brennen R, Sobek D,Werlich M, van de Goor T. 2005. Microfluidic chip for peptide analysis with an integrated HPLC column, sample enrichment column, and nanoelectrospray tip. Anal. Chem. 77:527-33
    • (2005) Anal. Chem. , vol.77 , pp. 527-533
    • Yin, H.1    Killeen, K.2    Brennen, R.3    Sobek, D.4    Werlich, M.5    Van De Goor, T.6
  • 118
    • 77955462811 scopus 로고    scopus 로고
    • Development of an annotated library of neutral human milk oligosaccharides
    • WuS, TaoN,German JB, Grimm R, Lebrilla CB. 2010. Development of an annotated library of neutral human milk oligosaccharides. J. Proteome Res. 9:4138-51
    • (2010) J. Proteome Res. , vol.9 , pp. 4138-4151
    • Wu, S.1    Tao, N.2    German, J.B.3    Grimm, R.4    Lebrilla, C.B.5
  • 119
    • 79953709953 scopus 로고    scopus 로고
    • Annotation and structural analysis of sialylated human milk oligosaccharides
    • Wu S, Grimm R, German JB, Lebrilla CB. 2011. Annotation and structural analysis of sialylated human milk oligosaccharides. J. Proteome Res. 10:856-68
    • (2011) J. Proteome Res. , vol.10 , pp. 856-868
    • Wu, S.1    Grimm, R.2    German, J.B.3    Lebrilla, C.B.4
  • 120
    • 79955016013 scopus 로고    scopus 로고
    • N-linked glycan profiling of mature human milk by high-performance microfluidic chip liquid chromatography time-of-flight tandem mass spectrometry
    • Dallas DC, Martin WF, Strum JS, Zivkovic AM, Smilowitz JT, et al. 2011. N-linked glycan profiling of mature human milk by high-performance microfluidic chip liquid chromatography time-of-flight tandem mass spectrometry. J. Agric. Food Chem. 59:4255-63
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 4255-4263
    • Dallas, D.C.1    Martin, W.F.2    Strum, J.S.3    Zivkovic, A.M.4    Smilowitz, J.T.5
  • 121
    • 79953727599 scopus 로고    scopus 로고
    • Evolutionary glycomics: Characterization of milk oligosaccharides in primates
    • Tao N, Wu S, Kim J, An HJ, Hinde K, et al. 2011. Evolutionary glycomics: characterization of milk oligosaccharides in primates. J. Proteome Res. 10:1548-57
    • (2011) J. Proteome Res. , vol.10 , pp. 1548-1557
    • Tao, N.1    Wu, S.2    Kim, J.3    An, H.J.4    Hinde, K.5
  • 122
    • 65349151261 scopus 로고    scopus 로고
    • Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on amicrofluidic chip and time-of-flight mass spectrometry
    • Chu CS, Ninonuevo MR, Clowers BH, Perkins PD, An HJ, et al. 2009. Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on amicrofluidic chip and time-of-flight mass spectrometry. Proteomics 9:1939-51
    • (2009) Proteomics , vol.9 , pp. 1939-1951
    • Chu, C.S.1    Ninonuevo, M.R.2    Clowers, B.H.3    Perkins, P.D.4    An, H.J.5
  • 123
    • 80052236392 scopus 로고    scopus 로고
    • Comprehensive native glycan profiling with isomer separation and quantitation for the discovery of cancer biomarkers
    • Hua S, An HJ, Ozcan S, Ro GS, Soares S, et al. 2011. Comprehensive native glycan profiling with isomer separation and quantitation for the discovery of cancer biomarkers. Analyst 136:3663-71
    • (2011) Analyst , vol.136 , pp. 3663-3671
    • Hua, S.1    An, H.J.2    Ozcan, S.3    Ro, G.S.4    Soares, S.5
  • 124
    • 70350633078 scopus 로고    scopus 로고
    • Characterization of IgG N-glycans employing a microfluidic chip that integrates glycan cleavage, sample purification, LC separation, and MS detection
    • Bynum MA, Yin H, Felts K, Lee YM, Monell CR, Killeen K. 2009. Characterization of IgG N-glycans employing a microfluidic chip that integrates glycan cleavage, sample purification, LC separation, and MS detection. Anal. Chem. 81:8818-25
    • (2009) Anal. Chem. , vol.81 , pp. 8818-8825
    • Bynum, M.A.1    Yin, H.2    Felts, K.3    Lee, Y.M.4    Monell, C.R.5    Killeen, K.6
  • 125
    • 0026085573 scopus 로고
    • Ultrasensitive fluorometric detection of carbohydrates as derivatives in mixtures separated by capillary electrophoresis
    • Liu JP, Shirota O, Wiesler D, Novotny M. 1991. Ultrasensitive fluorometric detection of carbohydrates as derivatives in mixtures separated by capillary electrophoresis. Proc. Natl. Acad. Sci. USA 88:2302-6
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2302-2306
    • Liu, J.P.1    Shirota, O.2    Wiesler, D.3    Novotny, M.4
  • 126
    • 0025996623 scopus 로고
    • Separation of fluorescent oligosaccharide derivatives by microcolumn techniques based on electrophoresis and liquid chromatography
    • Liu JP, Shirota O, Novotny M. 1991. Separation of fluorescent oligosaccharide derivatives by microcolumn techniques based on electrophoresis and liquid chromatography. J. Chromatogr. 559:223-35
    • (1991) J. Chromatogr. , vol.559 , pp. 223-235
    • Liu, J.P.1    Shirota, O.2    Novotny, M.3
  • 127
    • 0026887525 scopus 로고
    • Experimental evaluation of the separation efficiency in capillary electrophoresis using open tubular and gel-filled columns
    • Liu J, Dolnik V, Hsieh YZ, Novotny M. 1992. Experimental evaluation of the separation efficiency in capillary electrophoresis using open tubular and gel-filled columns. Anal. Chem. 64:1328-36
    • (1992) Anal. Chem. , vol.64 , pp. 1328-1336
    • Liu, J.1    Dolnik, V.2    Hsieh, Y.Z.3    Novotny, M.4
  • 128
    • 20444419374 scopus 로고    scopus 로고
    • Comprehensive assessment of N-glycans derived from a murine monoclonal antibody: A case for multimethodological approach
    • Mechref Y, Muzikar J, Novotny MV. 2005. Comprehensive assessment of N-glycans derived from a murine monoclonal antibody: a case for multimethodological approach. Electrophoresis 26:2034-46
    • (2005) Electrophoresis , vol.26 , pp. 2034-2046
    • Mechref, Y.1    Muzikar, J.2    Novotny, M.V.3
  • 129
    • 0030852020 scopus 로고    scopus 로고
    • Multistructure sequencing of N-linked fetuin glycans by capillary gel electrophoresis and enzyme matrix digestion
    • Guttman A. 1997. Multistructure sequencing of N-linked fetuin glycans by capillary gel electrophoresis and enzyme matrix digestion. Electrophoresis 18:1136-41
    • (1997) Electrophoresis , vol.18 , pp. 1136-1141
    • Guttman, A.1
  • 130
    • 0029879785 scopus 로고    scopus 로고
    • High-resolution carbohydrate profiling by capillary gel electrophoresis
    • Guttman A. 1996. High-resolution carbohydrate profiling by capillary gel electrophoresis. Nature 380:461-62
    • (1996) Nature , vol.380 , pp. 461-462
    • Guttman, A.1
  • 131
    • 0029983493 scopus 로고    scopus 로고
    • Separation of 1-aminopyrene-3,6,8-trisulfonate-labeled asparagine-linked fetuin glycans by capillary gel electrophoresis
    • Guttman A, Chen FT, Evangelista RA. 1996. Separation of 1-aminopyrene-3,6,8-trisulfonate-labeled asparagine-linked fetuin glycans by capillary gel electrophoresis. Electrophoresis 17:412-17
    • (1996) Electrophoresis , vol.17 , pp. 412-417
    • Guttman, A.1    Chen, F.T.2    Evangelista, R.A.3
  • 132
    • 80052936230 scopus 로고    scopus 로고
    • Rapid and sensitive analyses of glycoprotein-derived oligosaccharides by liquid chromatography and laser-induced fluorometric detection capillary electrophoresis
    • Oyama T, Yodohsi M, Yamane A, Kakehi K, Hayakawa T, Suzuki S. 2011. Rapid and sensitive analyses of glycoprotein-derived oligosaccharides by liquid chromatography and laser-induced fluorometric detection capillary electrophoresis. J. Chromatogr. B 879:2928-34
    • (2011) J. Chromatogr. B , vol.879 , pp. 2928-2934
    • Oyama, T.1    Yodohsi, M.2    Yamane, A.3    Kakehi, K.4    Hayakawa, T.5    Suzuki, S.6
  • 133
    • 83755172774 scopus 로고    scopus 로고
    • Highly sensitive capillary electrophoresis analysis of N-linked oligosaccharides in glycoproteins following fluorescence derivatization with rhodamine 110 and laser-induced fluorescence detection
    • Ijiri S, Todoroki K, Yoshida H, Yoshitake T, Nohta H, Yamaguchi M. 2011. Highly sensitive capillary electrophoresis analysis of N-linked oligosaccharides in glycoproteins following fluorescence derivatization with rhodamine 110 and laser-induced fluorescence detection. Electrophoresis 32:3499-509
    • (2011) Electrophoresis , vol.32 , pp. 3499-3509
    • Ijiri, S.1    Todoroki, K.2    Yoshida, H.3    Yoshitake, T.4    Nohta, H.5    Yamaguchi, M.6
  • 134
    • 56849090276 scopus 로고    scopus 로고
    • N-glycan analysis by CGE-LIF: Profiling influenza A virus hemagglutinin N-glycosylation during vaccine production
    • Schwarzer J, Rapp E, Reichl U. 2008.N-glycan analysis by CGE-LIF: profiling influenza A virus hemagglutinin N-glycosylation during vaccine production. Electrophoresis 29:4203-14
    • (2008) Electrophoresis , vol.29 , pp. 4203-4214
    • Schwarzer, J.1    Rapp, E.2    Reichl, U.3
  • 135
    • 79959926784 scopus 로고    scopus 로고
    • Rapid high-resolution characterization of functionally important monoclonal antibody N-glycans by capillary electrophoresis
    • Szabo Z, Guttman A, Bones J, Karger BL. 2011. Rapid high-resolution characterization of functionally important monoclonal antibody N-glycans by capillary electrophoresis. Anal. Chem. 83:5329-36
    • (2011) Anal. Chem. , vol.83 , pp. 5329-5336
    • Szabo, Z.1    Guttman, A.2    Bones, J.3    Karger, B.L.4
  • 136
    • 67449106681 scopus 로고    scopus 로고
    • GlycoFibroTest is a highly performant liver fibrosis biomarker derived fromDNAsequencer-based serum protein glycomics
    • Vanderschaeghe D, Laroy W, Sablon E, Halfon P, Van Hecke A, et al. 2009. GlycoFibroTest is a highly performant liver fibrosis biomarker derived fromDNAsequencer-based serum protein glycomics. Mol. Cell. Proteomics 8:986-94
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 986-994
    • Vanderschaeghe, D.1    Laroy, W.2    Sablon, E.3    Halfon, P.4    Van Hecke, A.5
  • 137
    • 77956261162 scopus 로고    scopus 로고
    • High-throughput profiling of the serum N-glycome on capillary electrophoresis microfluidics systems: Toward clinical implementation of GlycoHepatoTest
    • Vanderschaeghe D, Szekrenyes A,Wenz C,Gassmann M,Naik N, et al. 2010. High-throughput profiling of the serum N-glycome on capillary electrophoresis microfluidics systems: toward clinical implementation of GlycoHepatoTest. Anal. Chem. 82:7408-15
    • (2010) Anal. Chem. , vol.82 , pp. 7408-7415
    • Vanderschaeghe, D.1    Szekrenyes, A.2    Wenz, C.3    Gassmann, M.4    Naik, N.5
  • 138
    • 16244414647 scopus 로고    scopus 로고
    • Thin chip microsprayer system coupled to quadrupole time-of-flight mass spectrometer for glycoconjugate analysis
    • Zamfir AD, Lion N, Vukelic Z, Bindila L, Rossier J, et al. 2005. Thin chip microsprayer system coupled to quadrupole time-of-flight mass spectrometer for glycoconjugate analysis. Lab. Chip 5:298-307
    • (2005) Lab. Chip , vol.5 , pp. 298-307
    • Zamfir, A.D.1    Lion, N.2    Vukelic, Z.3    Bindila, L.4    Rossier, J.5
  • 140
    • 78449248586 scopus 로고    scopus 로고
    • Chip-based CE for rapid separation of 8-aminopyrene-1,3,6-trisulfonic acid (APTS) derivatized glycans
    • Smejkal P, Szekrenyes A, Ryvolova M, Foret F, Guttman A, et al. 2010. Chip-based CE for rapid separation of 8-aminopyrene-1,3,6-trisulfonic acid (APTS) derivatized glycans. Electrophoresis 31:3783-86
    • (2010) Electrophoresis , vol.31 , pp. 3783-3786
    • Smejkal, P.1    Szekrenyes, A.2    Ryvolova, M.3    Foret, F.4    Guttman, A.5
  • 141
    • 79955591082 scopus 로고    scopus 로고
    • A high-throughput microchip-based glycan screening assay for antibody cell culture samples
    • Primack J, Flynn GC, Pan H. 2011. A high-throughput microchip-based glycan screening assay for antibody cell culture samples. Electrophoresis 32:1129-32
    • (2011) Electrophoresis , vol.32 , pp. 1129-1132
    • Primack, J.1    Flynn, G.C.2    Pan, H.3
  • 142
    • 78650300965 scopus 로고    scopus 로고
    • Recent advances in theMS analysis of glycoproteins: Capillary and microfluidic workflows
    • Cortes DF,Kabulski JL, Lazar AC, Lazar IM. 2011. Recent advances in theMS analysis of glycoproteins: capillary and microfluidic workflows. Electrophoresis 32:14-29
    • (2011) Electrophoresis , vol.32 , pp. 14-29
    • Cortes, D.F.1    Kabulski, J.L.2    Lazar, A.C.3    Lazar, I.M.4
  • 143
    • 78751639679 scopus 로고    scopus 로고
    • Microchip electrophoresis ofN-glycans on serpentine separation channels with asymmetrically tapered turns
    • Zhuang Z, Mitra I,Hussein A, Novotny MV, Mechref Y, Jacobson SC. 2011. Microchip electrophoresis ofN-glycans on serpentine separation channels with asymmetrically tapered turns. Electrophoresis 32:246-53
    • (2011) Electrophoresis , vol.32 , pp. 246-253
    • Zhuang, Z.1    Mitra, I.2    Hussein, A.3    Novotny, M.V.4    Mechref, Y.5    Jacobson, S.C.6
  • 144
    • 46249102843 scopus 로고    scopus 로고
    • Glycosylation analysis of glycoproteins and proteoglycans using capillary electrophoresis-mass spectrometry strategies
    • Amon S, Zamfir AD, Rizzi A. 2008. Glycosylation analysis of glycoproteins and proteoglycans using capillary electrophoresis-mass spectrometry strategies. Electrophoresis 29:2485-507
    • (2008) Electrophoresis , vol.29 , pp. 2485-2507
    • Amon, S.1    Zamfir, A.D.2    Rizzi, A.3
  • 145
    • 65549136329 scopus 로고    scopus 로고
    • Glycomic analysis by capillary electrophoresis-mass spectrometry
    • Mechref Y, Novotny MV. 2009. Glycomic analysis by capillary electrophoresis-mass spectrometry. Mass Spectrom. Rev. 28:207-22
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 207-222
    • Mechref, Y.1    Novotny, M.V.2
  • 146
    • 43949107517 scopus 로고    scopus 로고
    • On-line CE-LIF-MS technology for the direct characterization of N-linked glycans from therapeutic antibodies
    • Gennaro LA, Salas-Solano O. 2008. On-line CE-LIF-MS technology for the direct characterization of N-linked glycans from therapeutic antibodies. Anal. Chem. 80:3838-45
    • (2008) Anal. Chem. , vol.80 , pp. 3838-3845
    • Gennaro, L.A.1    Salas-Solano, O.2
  • 147
    • 0036462597 scopus 로고    scopus 로고
    • Structural investigations of glycoconjugates at high sensitivity
    • Mechref Y, Novotny MV. 2002. Structural investigations of glycoconjugates at high sensitivity. Chem. Rev. 102:321-69
    • (2002) Chem. Rev. , vol.102 , pp. 321-369
    • Mechref, Y.1    Novotny, M.V.2


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