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Volumn 2, Issue 1, 2005, Pages 87-101

Proteomic analysis of glycosylation: Structural determination of N- and O-linked glycans by mass spectrometry

Author keywords

Carbohydrates; Electrospray; Fragmentation; MALDI; Mass spectrometry; N linked glycans; Negative ions; O linked glycans

Indexed keywords

5 METHOXYSALICYLIC ACID; GLYCAN DERIVATIVE; GLYCOPROTEIN; ISOQUINOLINE; MONOSACCHARIDE; SPERMINE;

EID: 14344257501     PISSN: 14789450     EISSN: None     Source Type: Journal    
DOI: 10.1586/14789450.2.1.87     Document Type: Review
Times cited : (142)

References (142)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130 (1993).
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 2
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Towards understanding the function of sugars
    • Dwek RA. Glycobiology: towards understanding the function of sugars. Chem. Rev. 96, 683-720 (1996).
    • (1996) Chem. Rev. , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 3
    • 4944266697 scopus 로고    scopus 로고
    • N-glycosylation at Asn in the Asn-Xaa-Cys motif of human transferrin
    • Satomi Y, Shimonishi Y, Takao T. N-glycosylation at Asn in the Asn-Xaa-Cys motif of human transferrin. FEBS Letts. 576, 51-56 (2004).
    • (2004) FEBS Letts. , vol.576 , pp. 51-56
    • Satomi, Y.1    Shimonishi, Y.2    Takao, T.3
  • 4
    • 0025677742 scopus 로고
    • Linkage analysis using Lindberg method
    • Hellerqvist CG. Linkage analysis using Lindberg method. Methods Enzymol. 193, 554-573 (1990).
    • (1990) Methods Enzymol. , vol.193 , pp. 554-573
    • Hellerqvist, C.G.1
  • 6
    • 0030839756 scopus 로고    scopus 로고
    • Rapid, sensitive sequencing of oligosaccharides from glycoproteins
    • Rudd PM, Dwek RA. Rapid, sensitive sequencing of oligosaccharides from glycoproteins. Curr. Opin. Biotechnol. 8, 488-497 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 488-497
    • Rudd, P.M.1    Dwek, R.A.2
  • 7
    • 0030876711 scopus 로고    scopus 로고
    • Oligosaccharide sequencing technology
    • Rudd PM, Guile GR, Küster B, Harvey DJ, Opdenakker G, Dwek RA. Oligosaccharide sequencing technology. Nature 388, 205-207 (1997). Describes N-glycan sequencing by high-performance liquid chromatography and exoglycosidase digestions.
    • (1997) Nature , vol.388 , pp. 205-207
    • Rudd, P.M.1    Guile, G.R.2    Küster, B.3    Harvey, D.J.4    Opdenakker, G.5    Dwek, R.A.6
  • 8
    • 0035260309 scopus 로고    scopus 로고
    • A high-performance liquid chromatography based strategy for rapid, sensitive sequencing of N-linked oligosaccharide modifications to proteins in sodium dodecyl sulfate polyacrylamide electrophoresis gel bands
    • Rudd PM, Colominas C, Royle L et al. A high-performance liquid chromatography based strategy for rapid, sensitive sequencing of N-linked oligosaccharide modifications to proteins in sodium dodecyl sulfate polyacrylamide electrophoresis gel bands. Proteomics 1, 285-294 (2001).
    • (2001) Proteomics , vol.1 , pp. 285-294
    • Rudd, P.M.1    Colominas, C.2    Royle, L.3
  • 9
    • 0028349781 scopus 로고
    • Site-specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorption mass spectrometry
    • Sutton CW, O'Neill JA, Cottrell JS. Site-specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorption mass spectrometry. Anal. Biochem. 218, 34-46 (1994).
    • (1994) Anal. Biochem. , vol.218 , pp. 34-46
    • Sutton, C.W.1    O'Neill, J.A.2    Cottrell, J.S.3
  • 10
    • 84989028063 scopus 로고
    • Examination of complex oligosaccharides by matrix-assisted laser desorption/ionization mass spectrometry on time-of-flight and magnetic sector instruments
    • Harvey DJ, Rudd PM, Bateman RH et al. Examination of complex oligosaccharides by matrix-assisted laser desorption/ionization mass spectrometry on time-of-flight and magnetic sector instruments. Org. Mass Spectrom. 29, 753-765 (1994).
    • (1994) Org. Mass Spectrom. , vol.29 , pp. 753-765
    • Harvey, D.J.1    Rudd, P.M.2    Bateman, R.H.3
  • 11
    • 0036571275 scopus 로고    scopus 로고
    • An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins
    • Royle L, Mattu TS, Hart E et al. An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins. Anal. Biochem. 304, 70-90 (2002). Describes the analysis of O-linked glycans and containing an extensive database of O-glycan structures.
    • (2002) Anal. Biochem. , vol.304 , pp. 70-90
    • Royle, L.1    Mattu, T.S.2    Hart, E.3
  • 12
    • 0038574979 scopus 로고    scopus 로고
    • Ion suppression in mass spectrometry
    • Annesley TM. Ion suppression in mass spectrometry. Clin. Chem. 49, 1041-1044 (2003).
    • (2003) Clin. Chem. , vol.49 , pp. 1041-1044
    • Annesley, T.M.1
  • 13
    • 0027462384 scopus 로고
    • Selective identification and differentiation of N- And O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry
    • Carr SA, Huddleston MJ, Bean ME Selective identification and differentiation of N- and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry. Protein Sci. 2, 183-196 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 183-196
    • Carr, S.A.1    Huddleston, M.J.2    Bean, M.E.3
  • 14
    • 0000108345 scopus 로고    scopus 로고
    • The utility of nonspecific proteases in the characterization of glycoproteins by high-resolution time-of-flight mass spectrometry
    • Juhasz P, Martin SA. The utility of nonspecific proteases in the characterization of glycoproteins by high-resolution time-of-flight mass spectrometry. Int. J. Mass Spectrom. Ion Processes 169/170, 217-230 (1997).
    • (1997) Int. J. Mass Spectrom. Ion Processes , vol.169-170 , pp. 217-230
    • Juhasz, P.1    Martin, S.A.2
  • 16
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An HJ, Peavy TR, Hedrick JL, Lebrilla CB. Determination of N-glycosylation sites and site heterogeneity in glycoproteins. Anal. Chem. 75, 5628-5637 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 17
    • 0033541695 scopus 로고    scopus 로고
    • Partial vapor-phase hydrolysis of peptide bonds: A method for mass spectrometric determination of O-glycosylated sites in glycopeptides
    • Mirgorodskaya E, Hassan H, Wandall HH, Clausen H, Roepstorff P. Partial vapor-phase hydrolysis of peptide bonds: a method for mass spectrometric determination of O-glycosylated sites in glycopeptides. Anal. Biochem. 269, 54-65 (1999).
    • (1999) Anal. Biochem. , vol.269 , pp. 54-65
    • Mirgorodskaya, E.1    Hassan, H.2    Wandall, H.H.3    Clausen, H.4    Roepstorff, P.5
  • 18
    • 0031637003 scopus 로고    scopus 로고
    • HPLC and HPAEC of oligosaccharides and glycopeptides
    • Davies MJ, Hounsell EE. HPLC and HPAEC of oligosaccharides and glycopeptides. Methods Mol. Biol. 76, 79-100 (1998).
    • (1998) Methods Mol. Biol. , vol.76 , pp. 79-100
    • Davies, M.J.1    Hounsell, E.E.2
  • 19
    • 0020020233 scopus 로고
    • Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides
    • Takasaki S, Misuochi T, Kobata A. Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides. Methods Enzymol. 83, 263-268 (1982).
    • (1982) Methods Enzymol. , vol.83 , pp. 263-268
    • Takasaki, S.1    Misuochi, T.2    Kobata, A.3
  • 20
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- And O-linked oligosaccharides from glycoproteins
    • Patel T, Bruce J, Merry A et al. Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry 32, 679-693 (1993). Glycan release by hydrazinolysis.
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3
  • 21
    • 0036570965 scopus 로고    scopus 로고
    • Recovery of intact 2-aminobenzamide-labeled O-glycans released from glycoproteins by hydrazinolysis
    • Merry AH, Neville DCA, Royle L et al. Recovery of intact 2-aminobenzamide-labeled O-glycans released from glycoproteins by hydrazinolysis. Anal. Biochem. 304, 91-99 (2002).
    • (2002) Anal. Biochem. , vol.304 , pp. 91-99
    • Merry, A.H.1    Neville, D.C.A.2    Royle, L.3
  • 22
    • 0022426933 scopus 로고
    • Hydrazinolysis-N-teacetylation of glycopeptides and glycoproteins. Model studies using 2-acetamido-1-N-(L-aspart-4-oyl)-2-deoxy-α-D- glucopyranosylamine
    • Bendiac B, Cumming DA. Hydrazinolysis-N-teacetylation of glycopeptides and glycoproteins. Model studies using 2-acetamido-1-N-(L-aspart-4-oyl)-2-deoxy- α-D-glucopyranosylamine. Carbohydrate Res. 144, 1-12 (1985).
    • (1985) Carbohydrate Res. , vol.144 , pp. 1-12
    • Bendiac, B.1    Cumming, D.A.2
  • 23
    • 0026556916 scopus 로고
    • A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins
    • Gerken TA, Gupta R, Jentoft N. A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins. Biochemistry 31, 639-648 (1992).
    • (1992) Biochemistry , vol.31 , pp. 639-648
    • Gerken, T.A.1    Gupta, R.2    Jentoft, N.3
  • 24
    • 0030894597 scopus 로고    scopus 로고
    • Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:GalNAc transferase peptide binding site
    • Gerken TA, Owens CL, Pasumarthy M. Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:GalNAc transferase peptide binding site. J. Biol. Chem. 272, 9709-9719 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 9709-9719
    • Gerken, T.A.1    Owens, C.L.2    Pasumarthy, M.3
  • 25
    • 0035894307 scopus 로고    scopus 로고
    • Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis
    • Huang Y, Mechref Y, Novotny MV. Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis. Anal. Chem. 73, 6063-6069 (2001).
    • (2001) Anal. Chem. , vol.73 , pp. 6063-6069
    • Huang, Y.1    Mechref, Y.2    Novotny, M.V.3
  • 26
    • 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. Matrix-assisted laser desorption/ionization mass spectrometry compatible β-elimination of O-linked oligosaccharides. Rapid Commun. Mass Spectrom. 16, 1199-1204 (2002).
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1199-1204
    • Huang, Y.1    Konse, T.2    Mechref, Y.3    Novotny, M.V.4
  • 27
    • 0035282989 scopus 로고    scopus 로고
    • Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments
    • Hanisch FG, Jovanovic M, Peter-Katalinic J. Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments. Anal. Biochem. 290, 47-59 (2001).
    • (2001) Anal. Biochem. , vol.290 , pp. 47-59
    • Hanisch, F.G.1    Jovanovic, M.2    Peter-Katalinic, J.3
  • 28
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F
    • Tarentino AL, Gómez CM, Plummer TH Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24, 4665-5671 (1985).
    • (1985) Biochemistry , vol.24 , pp. 4665-5671
    • Tarentino, A.L.1    Gómez, C.M.2    Plummer Jr., T.H.3
  • 30
    • 0031091162 scopus 로고    scopus 로고
    • Ammonium-containing buffers should be avoided during enzymatic release of glycans from glycoproteins when followed by reducing terminal derivatization
    • Küster B, Harvey DJ. Ammonium-containing buffers should be avoided during enzymatic release of glycans from glycoproteins when followed by reducing terminal derivatization. Glycobiology 7, vii-ix. (1997).
    • (1997) Glycobiology , vol.7
    • Küster, B.1    Harvey, D.J.2
  • 31
    • 0025923253 scopus 로고
    • Peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1-3 to the asparagine-linked N-acetylglucosamine residue
    • Tretter V, Altmann F, März L. Peptide-N4-(N-acetyl-β- glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1-3 to the asparagine-linked N-acetylglucosamine residue. Eur. J. Biochem. 199, 647-652 (1991).
    • (1991) Eur. J. Biochem. , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    März, L.3
  • 32
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ ionization mass spectrometry and normal-phase high performance liquid chromatography
    • Küster B, Wheeler SF, Hunter AP, Dwek RA, Harvey DJ. Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ ionization mass spectrometry and normal-phase high performance liquid chromatography. Anal. Biochem. 250, 82-101 (1997). Describes the release of N-linked glycans from sodium dodecyl sulfate polyaaylamide electrophoresis gels.
    • (1997) Anal. Biochem. , vol.250 , pp. 82-101
    • Küster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 33
    • 0029741839 scopus 로고    scopus 로고
    • Stabilization of sialic acids in N-linked oligosaccharides and gangliosides for analysis by positive ion matrix-assisted laser desorption-ionization mass spectrometry
    • Powell AK, Harvey DJ. Stabilization of sialic acids in N-linked oligosaccharides and gangliosides for analysis by positive ion matrix-assisted laser desorption-ionization mass spectrometry. Rapid Commun. Mass Spectrom. 10, 1027-1032 (1996).
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1027-1032
    • Powell, A.K.1    Harvey, D.J.2
  • 34
    • 0035450194 scopus 로고    scopus 로고
    • Extension of the in-gel release method for structural analysis of neutral and sialylated N-linked glycans to the analysis of sulfated glycans
    • Wheeler SF, Harvey DJ. Extension of the in-gel release method for structural analysis of neutral and sialylated N-linked glycans to the analysis of sulfated glycans. Anal. Biochem. 296, 92-100 (2001).
    • (2001) Anal. Biochem. , vol.296 , pp. 92-100
    • Wheeler, S.F.1    Harvey, D.J.2
  • 35
    • 0035260323 scopus 로고    scopus 로고
    • Immobilization of antibodies in gels allows the improved release and identification of glycans
    • Charlwood J, Skehel JM, Camilleri E Immobilization of antibodies in gels allows the improved release and identification of glycans. Proteomics 1, 275-284 (2001).
    • (2001) Proteomics , vol.1 , pp. 275-284
    • Charlwood, J.1    Skehel, J.M.2    Camilleri, E.3
  • 37
    • 0034663549 scopus 로고    scopus 로고
    • Analysis of N-linked oligosaccharides released from glycoproteins separated by two-dimensional gel electrophoresis
    • Charlwood J, Skehel JM, Camilleri R Analysis of N-linked oligosaccharides released from glycoproteins separated by two-dimensional gel electrophoresis. Anal. Biochem. 284, 49-59 (2000).
    • (2000) Anal. Biochem. , vol.284 , pp. 49-59
    • Charlwood, J.1    Skehel, J.M.2    Camilleri, R.3
  • 38
    • 0034786349 scopus 로고    scopus 로고
    • Analysis of N-linked oligosaccharides: Progress towards the characterization of glycoprotein-linked carbohydrates
    • Charlwood J, Bryant D, Skehel JM, Camilleri R Analysis of N-linked oligosaccharides: progress towards the characterization of glycoprotein-linked carbohydrates. Biomol. Eng. 18, 229-240 (2001).
    • (2001) Biomol. Eng. , vol.18 , pp. 229-240
    • Charlwood, J.1    Bryant, D.2    Skehel, J.M.3    Camilleri, R.4
  • 39
    • 0034127012 scopus 로고    scopus 로고
    • A probe for the versatile analysis and characterization of N-linked oligosaccharides
    • Charrwood J, Birrell H, Gribble A, Burdes V, Tolson D, Camilleri P. A probe for the versatile analysis and characterization of N-linked oligosaccharides. Anal. Chem. 72, 1453-1461 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 1453-1461
    • Charrwood, J.1    Birrell, H.2    Gribble, A.3    Burdes, V.4    Tolson, D.5    Camilleri, P.6
  • 40
    • 0034948464 scopus 로고    scopus 로고
    • Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment
    • Callewaert N, Geysens S, Molemans F, Contreras R. Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment. Glycobiology 11, 275-281 (2001).
    • (2001) Glycobiology , vol.11 , pp. 275-281
    • Callewaert, N.1    Geysens, S.2    Molemans, F.3    Contreras, R.4
  • 41
    • 0040074701 scopus 로고    scopus 로고
    • The structure of the oligosaccharides of α3β1 integrin from human ureter epithelium (HCV29) cell line
    • Litynska A, Pochec E, Hoja-Lukowicz D et al. The structure of the oligosaccharides of α3β1 integrin from human ureter epithelium (HCV29) cell line. Acta Biochemica Polonica 49, 491-500 (2002).
    • (2002) Acta Biochemica Polonica , vol.49 , pp. 491-500
    • Litynska, A.1    Pochec, E.2    Hoja-Lukowicz, D.3
  • 42
    • 0036535507 scopus 로고    scopus 로고
    • Use of a meltable polyacrylamide matrix for sodium dodecyl sulfate-polyacrylamide gel electrophoresis in a procedure for N-glycan analysis on picomole amounts of glycoproteins
    • Callewaert N, Vervecken W, van Hecke A, Contreras R. Use of a meltable polyacrylamide matrix for sodium dodecyl sulfate-polyacrylamide gel electrophoresis in a procedure for N-glycan analysis on picomole amounts of glycoproteins. Anal. Biochem. 303, 93-95 (2002).
    • (2002) Anal. Biochem. , vol.303 , pp. 93-95
    • Callewaert, N.1    Vervecken, W.2    Van Hecke, A.3    Contreras, R.4
  • 43
    • 0034307511 scopus 로고    scopus 로고
    • N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: Application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1
    • Kolarich D, Altmann F. N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal. Biochem. 285, 64-75 (2000).
    • (2000) Anal. Biochem. , vol.285 , pp. 64-75
    • Kolarich, D.1    Altmann, F.2
  • 45
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile GR, Rudd PM, Wing DR, Prime SB, Dwek RA. A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem. 240, 210-226 (1996).
    • (1996) Anal. Biochem. , vol.240 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5
  • 46
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-aminobenzamide and anthranilic acid
    • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB. Nonselective and efficient fluorescent labeling of glycans using 2-aminobenzamide and anthranilic acid. Anal. Biochem. 230, 229-238 (1995). 2-aminobenzamide labeling of carbohydrates.
    • (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
  • 47
    • 0027346832 scopus 로고
    • Analysis of sugar chains by pyridylamination
    • Hase S. Analysis of sugar chains by pyridylamination. Methods Mol. Biol. 14, 69-80 (1993).
    • (1993) Methods Mol. Biol. , vol.14 , pp. 69-80
    • Hase, S.1
  • 48
    • 0030051116 scopus 로고    scopus 로고
    • Analysis of pyridylaminated O-linked sugar chains by two-dimensional sugar mapping
    • Kuraya N, Hase S. Analysis of pyridylaminated O-linked sugar chains by two-dimensional sugar mapping. Anal. Biochem. 233, 205-211 (1996).
    • (1996) Anal. Biochem. , vol.233 , pp. 205-211
    • Kuraya, N.1    Hase, S.2
  • 49
    • 0035048665 scopus 로고    scopus 로고
    • Isolation and characterization of an N-linked oligosaccharide that is significantly increased in sera from patients with non-small cell lung cancer
    • Otake Y, Fujimoto I, Tanaka F et al. Isolation and characterization of an N-linked oligosaccharide that is significantly increased in sera from patients with non-small cell lung cancer. J. Biochem. (Tokyo) 129, 537-542 (2001).
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 537-542
    • Otake, Y.1    Fujimoto, I.2    Tanaka, F.3
  • 50
    • 0035886994 scopus 로고    scopus 로고
    • Qualitative and quantitative analysis of the glycosylation pattern of recombinant proteins
    • Viseux N, Hironowski X, Delaney J, Domon B. Qualitative and quantitative analysis of the glycosylation pattern of recombinant proteins. Anal. Chem. 73, 4755-4762 (2001).
    • (2001) Anal. Chem. , vol.73 , pp. 4755-4762
    • Viseux, N.1    Hironowski, X.2    Delaney, J.3    Domon, B.4
  • 51
    • 0035017333 scopus 로고    scopus 로고
    • Mass spectrometric strategies: Providing structural clues for helminth glycoproteins
    • Haslam SM, Morris HR, Dell A. Mass spectrometric strategies: providing structural clues for helminth glycoproteins. Trends Parasitol. 17, 231-235 (2001).
    • (2001) Trends Parasitol. , vol.17 , pp. 231-235
    • Haslam, S.M.1    Morris, H.R.2    Dell, A.3
  • 53
    • 0023474057 scopus 로고
    • FAB Mass spectrometry of carbohydrates
    • Dell A. FAB Mass spectrometry of carbohydrates. Adv. Carbohydrate Chem. Biochem. 45, 19-72 (1987).
    • (1987) Adv. Carbohydrate Chem. Biochem. , vol.45 , pp. 19-72
    • Dell, A.1
  • 54
    • 0024098842 scopus 로고
    • Fast atom bombardment mass spectrometric strategies for characterizing carbohydrate-containing biopolymers
    • Dell A, Carman NH, Tiller PR, Thomas-Oates JE. Fast atom bombardment mass spectrometric strategies for characterizing carbohydrate-containing biopolymers. Biomed. Environ. Mass Spectrom. 16, 19-24 (1987).
    • (1987) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 19-24
    • Dell, A.1    Carman, N.H.2    Tiller, P.R.3    Thomas-Oates, J.E.4
  • 55
    • 0002918083 scopus 로고
    • Fast atom bombardment-mass spectrometry (FAB-MS): Sample preparation and analytical strategies
    • Biermann CJ, McGinnis GD (Eds), CRC Press: Boca Raton, FL, USA
    • Dell A, Thomas-Oates JE. Fast atom bombardment-mass spectrometry (FAB-MS): sample preparation and analytical strategies, In: Analysis of Carbohydrates by GLC and MS. Biermann CJ, McGinnis GD (Eds), CRC Press: Boca Raton, FL, USA, 217-235 (1989).
    • (1989) Analysis of Carbohydrates by GLC and MS , pp. 217-235
    • Dell, A.1    Thomas-Oates, J.E.2
  • 56
    • 0035937542 scopus 로고    scopus 로고
    • Glycoprotein structure determination by mass spectrometry
    • Dell A, Morris HR. Glycoprotein structure determination by mass spectrometry. Science 291, 2351-2356 (2001).
    • (2001) Science , vol.291 , pp. 2351-2356
    • Dell, A.1    Morris, H.R.2
  • 58
    • 0025923543 scopus 로고
    • The analysis of underivatized oligosaccharides by matrix-assisted laser desorption mass spectrometry
    • Mock KK, Davy M, Cottrell JS. The analysis of underivatized oligosaccharides by matrix-assisted laser desorption mass spectrometry. Biochem. Biophys. Res. Commun. 177, 644-651 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 644-651
    • Mock, K.K.1    Davy, M.2    Cottrell, J.S.3
  • 59
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey DJ. Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrom. Rev. 18, 349-451 (1999). Comprehensive review of the application of matrix-assisted laser desorption/ionization mass spectrometry to carbohydrates.
    • (1999) Mass Spectrom. Rev. , vol.18 , pp. 349-451
    • Harvey, D.J.1
  • 60
    • 0002867501 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of N-linked carbohydrates and related compounds
    • Burlingame AL, Carr SA, Baldwin MA (Eds), Humana Press, NJ, USA
    • Harvey DJ, Küster B, Wheeler SF, Hunter AP, Bateman RH, Dwek RA. Matrix-assisted laser desorption/ionization mass spectrometry of N-linked carbohydrates and related compounds, In: Mass Spectrometry in Biology and Medicine. Burlingame AL, Carr SA, Baldwin MA (Eds), Humana Press, NJ, USA, 407-437 (2000).
    • (2000) Mass Spectrometry in Biology and Medicine , pp. 407-437
    • Harvey, D.J.1    Küster, B.2    Wheeler, S.F.3    Hunter, A.P.4    Bateman, R.H.5    Dwek, R.A.6
  • 61
    • 0037445404 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates and glycoconjugates
    • Harvey DJ. Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates and glycoconjugates. Int. J. Mass Spectrum. 226, 1-35 (2003).
    • (2003) Int. J. Mass Spectrum. , vol.226 , pp. 1-35
    • Harvey, D.J.1
  • 62
    • 44949273956 scopus 로고
    • 2,5-Dihydroxybenzoic acid: A new matrix for laser desorption-ionization mass spectrometry
    • Strupat K, Karas M, Hillenkamp F. 2,5-Dihydroxybenzoic acid: a new matrix for laser desorption-ionization mass spectrometry. Int. J. Mass Spectrom. Ion Processes 111, 89-102 (1991).
    • (1991) Int. J. Mass Spectrom. Ion Processes , vol.111 , pp. 89-102
    • Strupat, K.1    Karas, M.2    Hillenkamp, F.3
  • 63
    • 0027630825 scopus 로고
    • Quantitative aspects of the matrix-assisted laser desorption mass spectrometry of complex oligosaccharides
    • Harvey DJ. Quantitative aspects of the matrix-assisted laser desorption mass spectrometry of complex oligosaccharides. Rapid Commun. Mass Spectrom. 7, 614-619 (1993).
    • (1993) Rapid Commun. Mass Spectrom. , vol.7 , pp. 614-619
    • Harvey, D.J.1
  • 64
    • 84989023337 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry with additives to 2,5-dihydroxybenzoic acid
    • Karas M, Ehring H, Nordhoff E et al. Matrix-assisted laser desorption/ionization mass spectrometry with additives to 2,5-dihydroxybenzoic acid. Org. Mass Spectrom. 28, 1476-1481 (1993).
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1476-1481
    • Karas, M.1    Ehring, H.2    Nordhoff, E.3
  • 65
    • 0029175060 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry: Improved matrix for oligosaccharides
    • Mohr MD, Börnsen KO, Widmer HM. Matrix-assisted laser desorption/ionization mass spectrometry: improved matrix for oligosaccharides. Rapid Commun. Mass Spectrom. 9, 809-814 (1995).
    • (1995) Rapid Commun. Mass Spectrom. , vol.9 , pp. 809-814
    • Mohr, M.D.1    Börnsen, K.O.2    Widmer, H.M.3
  • 66
    • 11944271340 scopus 로고
    • Improvement of signal reproducibility and matrix/comatrix effects in MALDI analysis
    • Gusev AI, Wilkinson WR, Proctor A, Hercules DM. Improvement of signal reproducibility and matrix/comatrix effects in MALDI analysis. Anal. Chem. 67, 1034-1041 (1995).
    • (1995) Anal. Chem. , vol.67 , pp. 1034-1041
    • Gusev, A.I.1    Wilkinson, W.R.2    Proctor, A.3    Hercules, D.M.4
  • 67
    • 0032216567 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of acidic glycoconjugates facilitated by the use of spermine as a co-matrix
    • Mechref Y, Novotny MV. Matrix-assisted laser desorption/ionization mass spectrometry of acidic glycoconjugates facilitated by the use of spermine as a co-matrix. J. Am. Soc. Mass Spectrom. 9, 1292-1302 (1998).
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 1292-1302
    • Mechref, Y.1    Novotny, M.V.2
  • 68
    • 0030587060 scopus 로고    scopus 로고
    • Analysis of acidic oligosaccharides and glycopeptides by matrix assisted laser desorption/ ionization time-of-flight mass spectrometry
    • Papac DI, Wong A, Jones AJS. Analysis of acidic oligosaccharides and glycopeptides by matrix assisted laser desorption/ ionization time-of-flight mass spectrometry. Anal. Chem. 68, 3215-3223 (1996).
    • (1996) Anal. Chem. , vol.68 , pp. 3215-3223
    • Papac, D.I.1    Wong, A.2    Jones, A.J.S.3
  • 69
    • 0001061864 scopus 로고
    • Analysis of neutral oligosaccharides by matrix-assisted laser desorption/ionization mass spectrometry
    • Stahl B, Steup M, Karas M, Hillenkamp F. Analysis of neutral oligosaccharides by matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 63, 1463-1466 (1991).
    • (1991) Anal. Chem. , vol.63 , pp. 1463-1466
    • Stahl, B.1    Steup, M.2    Karas, M.3    Hillenkamp, F.4
  • 70
    • 0031887937 scopus 로고    scopus 로고
    • β-carboline alkaloids as matrices for UV-matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in positive and negative ion modes. Analysis of proteins of high molecular mass, and of cyclic and acyclic oligosaccharides
    • Nonami H, Tanaka K, Fukuyama Y, Erra-Balsells R. β-carboline alkaloids as matrices for UV-matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in positive and negative ion modes. Analysis of proteins of high molecular mass, and of cyclic and acyclic oligosaccharides. Rapid Commun. Mass Spectrom. 12, 285-296 (1998).
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 285-296
    • Nonami, H.1    Tanaka, K.2    Fukuyama, Y.3    Erra-Balsells, R.4
  • 71
    • 0842263432 scopus 로고    scopus 로고
    • The relationship between in-source and post-source fragment ions in the MALDI mass spectra of carbohydrates recorded with reflectron-TOF mass spectrometers
    • Harvey DJ, Hunter AP, Bateman RH, Brown J, Critchley G. The relationship between in-source and post-source fragment ions in the MALDI mass spectra of carbohydrates recorded with reflectron-TOF mass spectrometers. Int. J. Mass Spectrom. Ion Processes 188, 131-146 (1999).
    • (1999) Int. J. Mass Spectrom. Ion Processes , vol.188 , pp. 131-146
    • Harvey, D.J.1    Hunter, A.P.2    Bateman, R.H.3    Brown, J.4    Critchley, G.5
  • 72
    • 0029842929 scopus 로고    scopus 로고
    • Effect of structure on the signal strength of oligosaccharides in matrix-assisted laser desorption/ionization mass spectrometry on time-of-flight and magnetic sector instruments
    • Naven TJP, Harvey DJ. Effect of structure on the signal strength of oligosaccharides in matrix-assisted laser desorption/ionization mass spectrometry on time-of-flight and magnetic sector instruments. Rapid Commun. Mass Spectrom. 10, 1361-1366 (1996).
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1361-1366
    • Naven, T.J.P.1    Harvey, D.J.2
  • 73
    • 0031734879 scopus 로고    scopus 로고
    • A general approach to desalting oligosaccharides released from glycoproteins
    • Packer NH, Lawson MA, Jardine DR, Redmond JW. A general approach to desalting oligosaccharides released from glycoproteins. Glycoconjugate J. 15, 737-747 (1998).
    • (1998) Glycoconjugate J. , vol.15 , pp. 737-747
    • Packer, N.H.1    Lawson, M.A.2    Jardine, D.R.3    Redmond, J.W.4
  • 74
    • 0029902699 scopus 로고    scopus 로고
    • On-the-probe sample cleanup strategies for grycoprotein-released carbohydrates prior to matrix-assisted laser desorption-ionization time-of-flight mass spectrometry
    • Rouse JC, Vath JE. On-the-probe sample cleanup strategies for grycoprotein-released carbohydrates prior to matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. Anal. Biochem. 238, 82-92 (1996).
    • (1996) Anal. Biochem. , vol.238 , pp. 82-92
    • Rouse, J.C.1    Vath, J.E.2
  • 75
    • 8544264747 scopus 로고
    • Ion exchange and purification of carbohydrates on a Nafion® membrane as a new sample pretreatment for matrix-assisted laser desorption-ionization mass spectrometry
    • Bornsen KO, Mohr MD, Widmer HM. Ion exchange and purification of carbohydrates on a Nafion® membrane as a new sample pretreatment for matrix-assisted laser desorption-ionization mass spectrometry. Rapid Commun. Mass Spectrom. 9, 1031-1034 (1995). Use of Nafion® (Perms Pure LLC) membrane for clean-up of carbohydrates for mass spectrometric analysis.
    • (1995) Rapid Commun. Mass Spectrom. , vol.9 , pp. 1031-1034
    • Bornsen, K.O.1    Mohr, M.D.2    Widmer, H.M.3
  • 76
    • 0029804882 scopus 로고    scopus 로고
    • Rapid approach for sequencing neutral oligosaccharides by exoglycosidase digestion and matrix-assisted laser desorption/ionization rime-of-flight mass spectrometry
    • Küster B, Naven TJP, Harvey DJ. Rapid approach for sequencing neutral oligosaccharides by exoglycosidase digestion and matrix-assisted laser desorption/ionization rime-of-flight mass spectrometry. J. Mass Spectrom. 31, 1131-1140 (1996),
    • (1996) J. Mass Spectrom. , vol.31 , pp. 1131-1140
    • Küster, B.1    Naven, T.J.P.2    Harvey, D.J.3
  • 77
    • 0033118805 scopus 로고    scopus 로고
    • On-target exoglycosidase digestions, MALDI-MS for determining the primary structures of carbohydrate chains
    • Colangelo J, Orlando R. On-target exoglycosidase digestions, MALDI-MS for determining the primary structures of carbohydrate chains. Anal. Chem. 71, 1479-1482 (1999),
    • (1999) Anal. Chem. , vol.71 , pp. 1479-1482
    • Colangelo, J.1    Orlando, R.2
  • 78
    • 0031991256 scopus 로고    scopus 로고
    • Mass spectrometric mapping and sequencing of N-linked oligosaccharides derived from submicrogram amounts of glycoproteins
    • Mechref Y, Novotny MV. Mass spectrometric mapping and sequencing of N-linked oligosaccharides derived from submicrogram amounts of glycoproteins. Anal. Chem. 70, 455-463 (1998). On-target sequencing of N-linked glycans.
    • (1998) Anal. Chem. , vol.70 , pp. 455-463
    • Mechref, Y.1    Novotny, M.V.2
  • 79
    • 0033597124 scopus 로고    scopus 로고
    • Analysis of the pre-S2 N- And O-linked glycans of the M surface protein from human hepatitis B virus
    • Schmitt S, Glebe D, Alving K et al. Analysis of the pre-S2 N- and O-linked glycans of the M surface protein from human hepatitis B virus. J. Biol. Chem. 274, 11945-11957 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 11945-11957
    • Schmitt, S.1    Glebe, D.2    Alving, K.3
  • 80
    • 0033555321 scopus 로고    scopus 로고
    • Structural analysis of glycoconjugates by on-target enzymatic digestion and MALDI-TOF-MS
    • Geyer H, Schmitt S, Wuhrer M, Geyer R. Structural analysis of glycoconjugates by on-target enzymatic digestion and MALDI-TOF-MS. Anal Chem. 71, 476-482 (1999).
    • (1999) Anal Chem. , vol.71 , pp. 476-482
    • Geyer, H.1    Schmitt, S.2    Wuhrer, M.3    Geyer, R.4
  • 81
    • 0033763508 scopus 로고    scopus 로고
    • Collision-induced fragmentation of underivatised N-linked carbohydrates ionized by electrospray
    • Harvey DJ. Collision-induced fragmentation of underivatised N-linked carbohydrates ionized by electrospray. J. Mass Spectrom. 35, 1178-1190 (2000). Positive ion fragmentation of N-linked glycans.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1178-1190
    • Harvey, D.J.1
  • 82
    • 0029009068 scopus 로고
    • Carbohydrate molecular weight profiling, sequence, linkage and branching data: ES-MS and CID
    • Reinhold VN, Reinhold BB, Costello CE. Carbohydrate molecular weight profiling, sequence, linkage and branching data: ES-MS and CID. Anal Chem. 67, 1772-1784 (1995). Review of carbohydrate fragmentation.
    • (1995) Anal Chem. , vol.67 , pp. 1772-1784
    • Reinhold, V.N.1    Reinhold, B.B.2    Costello, C.E.3
  • 83
    • 0031037943 scopus 로고    scopus 로고
    • High-energy collision-induced fragmentation of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry
    • Harvey DJ, Bateman RH, Green MR. High-energy collision-induced fragmentation of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 32, 167-187 (1997).
    • (1997) J. Mass Spectrom. , vol.32 , pp. 167-187
    • Harvey, D.J.1    Bateman, R.H.2    Green, M.R.3
  • 84
    • 0033730299 scopus 로고    scopus 로고
    • Ionization and fragmentation of complex glycans with a Q-TOF mass spectrometer fitted with a MALDI ion source
    • Harvey DJ, Bateman RH, Bordoli RS, Tyldesley R. Ionization and fragmentation of complex glycans with a Q-TOF mass spectrometer fitted with a MALDI ion source. Rapid Commun. Mass Spectrom. 14, 2135-2142 (2000).
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 2135-2142
    • Harvey, D.J.1    Bateman, R.H.2    Bordoli, R.S.3    Tyldesley, R.4
  • 85
    • 0034114976 scopus 로고    scopus 로고
    • N-[2-diethylaminoethyl-4-aminobenzamide derivatives for high sensitivity mass spectrometric detection and structure determination of N-linked carbohydrates
    • Harvey DJ. N-[2-diethylamino)ethyl-4-aminobenzamide derivatives for high sensitivity mass spectrometric detection and structure determination of N-linked carbohydrates. Rapid Commun. Mass Spectrom. 14, 862-871 (2000).
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 862-871
    • Harvey, D.J.1
  • 86
    • 0033994103 scopus 로고    scopus 로고
    • Electrospray mass spectrometry and collision-induced fragmentation of 2-aminobenzamide-labelled neutral N-linked glycans
    • Harvey DJ. Electrospray mass spectrometry and collision-induced fragmentation of 2-aminobenzamide-labelled neutral N-linked glycans. The Analyst 125, 609-617 (2000).
    • (2000) The Analyst , vol.125 , pp. 609-617
    • Harvey, D.J.1
  • 87
    • 0034475474 scopus 로고    scopus 로고
    • Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatised at the reducing terminus
    • Harvey DJ. Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatised at the reducing terminus. J. Am. Soc. Mass Spectrom. 11, 900-915 (2000).
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 900-915
    • Harvey, D.J.1
  • 88
    • 0032908264 scopus 로고    scopus 로고
    • Anion dopant for oligosaccharides in matrix-assisted laser desorption/ionization mass spectrometry
    • Wong AW, Cancilla MT, Voss LR, Lebrilla CB. Anion dopant for oligosaccharides in matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 71, 205-211 (1999).
    • (1999) Anal. Chem. , vol.71 , pp. 205-211
    • Wong, A.W.1    Cancilla, M.T.2    Voss, L.R.3    Lebrilla, C.B.4
  • 89
    • 0032956938 scopus 로고    scopus 로고
    • Chloride ion attachment in negative ion electrospray ionization mass spectrometry
    • Cole RB, Zhu J. Chloride ion attachment in negative ion electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 13, 607-611 (1999).
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 607-611
    • Cole, R.B.1    Zhu, J.2
  • 90
    • 0034111157 scopus 로고    scopus 로고
    • Selection of anionic dopant for quantifying desialylation reactions with MALDI-FTMS
    • Wong AW Wang H, Lebrilla CB. Selection of anionic dopant for quantifying desialylation reactions with MALDI-FTMS. Anal. Chem. 72, 1419-1425 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 1419-1425
    • Wong, A.W.1    Wang, H.2    Lebrilla, C.B.3
  • 91
    • 0034488256 scopus 로고    scopus 로고
    • -, in negative ion electrospray ionization mass spectrometry
    • -, in negative ion electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 11, 932-941 (2000).
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 932-941
    • Zhu, J.1    Cole, R.B.2
  • 92
    • 0013228897 scopus 로고    scopus 로고
    • Evaluation of the role of multiple hydrogen bonding in offering stability to negative ion adduces in electrospray mass spectrometry
    • Cai Y, Concha MC, Murray JS, Cole RB. Evaluation of the role of multiple hydrogen bonding in offering stability to negative ion adduces in electrospray mass spectrometry. J. Am. Soc. Mass Spectrom. 13, 1360-1369 (2002).
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 1360-1369
    • Cai, Y.1    Concha, M.C.2    Murray, J.S.3    Cole, R.B.4
  • 93
    • 0037398303 scopus 로고    scopus 로고
    • Anionic adducts of oligosaccharides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Cai Y, Jiang Y, Cole RB. Anionic adducts of oligosaccharides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Chem. 75, 1638-1644 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 1638-1644
    • Cai, Y.1    Jiang, Y.2    Cole, R.B.3
  • 94
    • 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
    • In Press
    • Harvey DJ. 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. (2005) (In Press).
    • (2005) J. Am. Soc. Mass Spectrom.
    • Harvey, D.J.1
  • 95
    • 0031573166 scopus 로고    scopus 로고
    • High sensitivity analysis of neutral underivatized oligosaccharides by nanoelectrospray mass spectrometry
    • Bahr U, Pfenninger A, Karas M, Stahl B. High sensitivity analysis of neutral underivatized oligosaccharides by nanoelectrospray mass spectrometry. Anal. Chem. 69, 4530-4535 (1997).
    • (1997) Anal. Chem. , vol.69 , pp. 4530-4535
    • Bahr, U.1    Pfenninger, A.2    Karas, M.3    Stahl, B.4
  • 96
    • 0842283940 scopus 로고    scopus 로고
    • Normal-phase nanoscale liquid chromatography-mass spectrometry of underivatized oligosaccharides at low-femtomole sensitivity
    • Wuhrer M, Koeleman CAM, Deelder AM, Hokke CH. Normal-phase nanoscale liquid chromatography-mass spectrometry of underivatized oligosaccharides at low-femtomole sensitivity. Anal. Chem. 76, 833-838 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 833-838
    • Wuhrer, M.1    Koeleman, C.A.M.2    Deelder, A.M.3    Hokke, C.H.4
  • 97
    • 1442274866 scopus 로고    scopus 로고
    • Nano-scale liquid chromatography-mass spectrometry of 2-aminobenzamide-labeled oligosaccharides at low femtomole sensitivity
    • Wuhrer M, Koeleman CAM, Hokke CH, Decider AM. Nano-scale liquid chromatography-mass spectrometry of 2-aminobenzamide-labeled oligosaccharides at low femtomole sensitivity. Int. J. Mass Spectrom. 232, 51-57 (2004).
    • (2004) Int. J. Mass Spectrom. , vol.232 , pp. 51-57
    • Wuhrer, M.1    Koeleman, C.A.M.2    Ch, H.3    Decider, A.M.4
  • 98
    • 0036143264 scopus 로고    scopus 로고
    • Enzymatic degradation of carboxymethyl cellulose hydrolyzed by the endoglucanases Cel5A, Cel7B, and Cel45A from Humicola insolens and Cel7B, Cel12A and Cel45Acore from Trichoderma reesei
    • Karlsson J, Momcilovic D, Wittgren B, Schülein M, Tjerneld F, Brinkmalm G. Enzymatic degradation of carboxymethyl cellulose hydrolyzed by the endoglucanases Cel5A, Cel7B, and Cel45A from Humicola insolens and Cel7B, Cel12A and Cel45Acore from Trichoderma reesei. Biopolymers 63, 32-40 (2002).
    • (2002) Biopolymers , vol.63 , pp. 32-40
    • Karlsson, J.1    Momcilovic, D.2    Wittgren, B.3    Schülein, M.4    Tjerneld, F.5    Brinkmalm, G.6
  • 99
    • 0037266318 scopus 로고    scopus 로고
    • Structural elucidation of zwitterionic carbohydrates derived from glycosphingolipids of the porcine parasitic nematode Ascaris suum
    • Friedl CH, Lochnit G, Zähringer U, Bahr U, Geyer R. Structural elucidation of zwitterionic carbohydrates derived from glycosphingolipids of the porcine parasitic nematode Ascaris suum. Biochem. J. 369, 89-102 (2003).
    • (2003) Biochem. J. , vol.369 , pp. 89-102
    • Friedl, C.H.1    Lochnit, G.2    Zähringer, U.3    Bahr, U.4    Geyer, R.5
  • 100
    • 0037397064 scopus 로고    scopus 로고
    • Coupling capillary electrochromatography with electrospray Fourier transform mass spectrometry for characterizing complex oligosaccharide pools
    • Que AH, Mechref Y, Huang Y, Taraszka JA, Clemmer DE, Novotny MV. Coupling capillary electrochromatography with electrospray Fourier transform mass spectrometry for characterizing complex oligosaccharide pools. Anal. Chem. 75, 1684-1690 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 1684-1690
    • Que, A.H.1    Mechref, Y.2    Huang, Y.3    Taraszka, J.A.4    Clemmer, D.E.5    Novotny, M.V.6
  • 101
    • 0342844280 scopus 로고    scopus 로고
    • Capillary electrophoresis and off-line capillary electrophoresis- electrospray ionization quadrupole time-of-flight tandem mass spectrometry of carbohydrates
    • Zamfir A, Konig S, Althoff J, Peter-Katalinc J. Capillary electrophoresis and off-line capillary electrophoresis-electrospray ionization quadrupole time-of-flight tandem mass spectrometry of carbohydrates. J. Chromatogr. A 895, 291-299 (2000).
    • (2000) J. Chromatogr. A , vol.895 , pp. 291-299
    • Zamfir, A.1    Konig, S.2    Althoff, J.3    Peter-Katalinc, J.4
  • 102
    • 4344616485 scopus 로고    scopus 로고
    • Characterization of glyco isoforms in plasma derived human antithrombin by on-line capillary zone electrophoresis-electrospray ionization-quadrupole ion trap-mass spectrometry of the intact glycoproteins
    • Demelbauer UM, Plematl A, Kremser L, Allmaier G, Josic D, Rizzi A. Characterization of glyco isoforms in plasma derived human antithrombin by on-line capillary zone electrophoresis-electrospray ionization-quadrupole ion trap-mass spectrometry of the intact glycoproteins. Electrophoresis 25, 2026-2032 (2004).
    • (2004) Electrophoresis , vol.25 , pp. 2026-2032
    • Demelbauer, U.M.1    Plematl, A.2    Kremser, L.3    Allmaier, G.4    Josic, D.5    Rizzi, A.6
  • 103
    • 4344648993 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry for glycoscreening in biomedical research
    • Zamfir A, Peter-Katalinic J. Capillary electrophoresis-mass spectrometry for glycoscreening in biomedical research. Electrophoresis 25, 1949-1963 (2004).
    • (2004) Electrophoresis , vol.25 , pp. 1949-1963
    • Zamfir, A.1    Peter-Katalinic, J.2
  • 104
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of grycoconjugates
    • Domon B, Costello CE. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of grycoconjugates. Glycoconjugate J. 5, 397-409 (1988). Describes the fragmentation nomenclature for carbohydrates.
    • (1988) Glycoconjugate J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 105
    • 10844287190 scopus 로고    scopus 로고
    • Fragmentation of N-linked glycans with a MALDI-ion trap time-of-flight mass spectrometer
    • Harvey DJ, Martin RL, Jackson KA, Sutton CW. Fragmentation of N-linked glycans with a MALDI-ion trap time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom. 18, 2997-3007 (2004).
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 2997-3007
    • Harvey, D.J.1    Martin, R.L.2    Jackson, K.A.3    Sutton, C.W.4
  • 106
    • 84989031026 scopus 로고
    • Structure analysis of branched oligosaccharides using post-source decay in matrix-assisted laser desorption/ionization mass spectrometry
    • Spengler B, Kirsch D, Kaufmann R, Lemoine J. Structure analysis of branched oligosaccharides using post-source decay in matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 30, 782-787 (1995).
    • (1995) J. Mass Spectrom. , vol.30 , pp. 782-787
    • Spengler, B.1    Kirsch, D.2    Kaufmann, R.3    Lemoine, J.4
  • 107
    • 0034194446 scopus 로고    scopus 로고
    • MALDI Quadrupole time-of-flight mass spectrometry: A powerful tool for proteomic research
    • Shevchenko A, Loboda A, Shevchenko A, Ens W, Standing KG. MALDI Quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research. Anal. Chem. 72, 2132-2141 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 2132-2141
    • Shevchenko, A.1    Loboda, A.2    Shevchenko, A.3    Ens, W.4    Standing, K.G.5
  • 108
    • 0035238444 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ ionization quadrupole time-of-flight mass spectrometry: An elegant tool for peptidomics
    • Verhaert P, Uttenweiler-Joseph S, de Vries M, Loboda A, Ens W, Standing KG. Matrix-assisted laser desorption/ ionization quadrupole time-of-flight mass spectrometry: an elegant tool for peptidomics. Proteomics 1, 118-131 (2001).
    • (2001) Proteomics , vol.1 , pp. 118-131
    • Verhaert, P.1    Uttenweiler-Joseph, S.2    De Vries, M.3    Loboda, A.4    Ens, W.5    Standing, K.G.6
  • 109
    • 0034124238 scopus 로고    scopus 로고
    • A quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: Design and performance
    • Loboda AV, Krutchinsky AN, Bromirski M, Ens W, Standing KG. A quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance. Rapid Commun. Mass Spectrom. 14, 1047-1057 (2000).
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1047-1057
    • Loboda, A.V.1    Krutchinsky, A.N.2    Bromirski, M.3    Ens, W.4    Standing, K.G.5
  • 110
    • 2342521287 scopus 로고    scopus 로고
    • Mass spectrometry of oligosaccharides
    • Zaia J. Mass spectrometry of oligosaccharides. Mass Spectrom. Rev. 23, 161-227 (2004). General review of carbohydrate mass spectrometry.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 161-227
    • Zaia, J.1
  • 111
    • 0029011527 scopus 로고
    • Oligosaccharide characterization using collision-induced dissociation fast atom bombardment mass spectrometry: Evidence for internal monosaccharide residue loss
    • Kovácik V, Hirsch J, Kovac P, Heerma W, Thomas-Oates J, Haverkamp J. Oligosaccharide characterization using collision-induced dissociation fast atom bombardment mass spectrometry: evidence for internal monosaccharide residue loss. J. Mass Spectrom. 30, 949-958 (1995).
    • (1995) J. Mass Spectrom. , vol.30 , pp. 949-958
    • Kovácik, V.1    Hirsch, J.2    Kovac, P.3    Heerma, W.4    Thomas-Oates, J.5    Haverkamp, J.6
  • 113
    • 0032232231 scopus 로고    scopus 로고
    • Observation of internal monosaccharide losses in the collisionally activated dissociation mass spectra of anthracycline aminodisaccharides
    • Warrack BM, Hail ME, Triolo A, Animati F, Seraglia R, Traldi P. Observation of internal monosaccharide losses in the collisionally activated dissociation mass spectra of anthracycline aminodisaccharides. J. Am. Soc. Mass Spectrom. 9, 710-715 (1998).
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 710-715
    • Warrack, B.M.1    Hail, M.E.2    Triolo, A.3    Animati, F.4    Seraglia, R.5    Traldi, P.6
  • 114
    • 0034719127 scopus 로고    scopus 로고
    • O-glycan analysis of natural human neutrophil gelatinase B using a combination of normal phase- HPLC and online tandem mass spectrometry: Implications for the domain organization of the enzyme
    • Mattu TS, Royle L, Langridge J et al. O-glycan analysis of natural human neutrophil gelatinase B using a combination of normal phase- HPLC and online tandem mass spectrometry: Implications for the domain organization of the enzyme. Biochemistry 39, 15695-15704 (2000).
    • (2000) Biochemistry , vol.39 , pp. 15695-15704
    • Mattu, T.S.1    Royle, L.2    Langridge, J.3
  • 115
    • 0037084078 scopus 로고    scopus 로고
    • 'Internal residue loss': Rearrangements occurring during the fragmentation of carbohydrates derivatized at the reducing terminus
    • Harvey DJ, Mattu TS, Wormald MR, Royle L, Dwek RA, Rudd PM. 'Internal residue loss': rearrangements occurring during the fragmentation of carbohydrates derivatized at the reducing terminus. Anal. Chem. 74, 734-740 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 734-740
    • Harvey, D.J.1    Mattu, T.S.2    Wormald, M.R.3    Royle, L.4    Dwek, R.A.5    Rudd, P.M.6
  • 116
    • 0036208688 scopus 로고    scopus 로고
    • Evidence for long-range glycosyl transfer reactions in the gas phase
    • Franz AH, Lebrilla CB. Evidence for long-range glycosyl transfer reactions in the gas phase. J. Am. Soc. Mass Spectrom. 13, 325-337 (2002).
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 325-337
    • Franz, A.H.1    Lebrilla, C.B.2
  • 117
    • 0031763449 scopus 로고    scopus 로고
    • Sodium-cationized oligosaccharides do not appear to undeigo 'internal residue loss' rearrangement processes on tandem mass spectrometry
    • Brüll LP, Kovácik V, Thomas-Oates JE, Heerma W, Haverkamp J. Sodium-cationized oligosaccharides do not appear to undeigo 'internal residue loss' rearrangement processes on tandem mass spectrometry. Rapid Commun. Mass Spectrom. 12, 1520-1532 (1998).
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1520-1532
    • Brüll, L.P.1    Kovácik, V.2    Thomas-Oates, J.E.3    Heerma, W.4    Haverkamp, J.5
  • 118
    • 0025245627 scopus 로고
    • Structural analysis of oligosaccharides by tandem mass spectrometry: Collisional activation of sodium adduct ions
    • Orlando R, Bush CA, Fenselau C. Structural analysis of oligosaccharides by tandem mass spectrometry: collisional activation of sodium adduct ions. Biomed. Environ. Mass Spectrom. 19, 747-754 (1990).
    • (1990) Biomed. Environ. Mass Spectrom. , vol.19 , pp. 747-754
    • Orlando, R.1    Bush, C.A.2    Fenselau, C.3
  • 119
    • 0028389851 scopus 로고
    • Effects of cations and charge types on the metastable decay rates of oligosaccharides
    • Ngoka LC, Gal J-F, Lebrilla CB. Effects of cations and charge types on the metastable decay rates of oligosaccharides. Anal. Chem. 66, 692-698 (1994).
    • (1994) Anal. Chem. , vol.66 , pp. 692-698
    • Ngoka, L.C.1    Gal, J.-F.2    Lebrilla, C.B.3
  • 120
    • 0029929197 scopus 로고    scopus 로고
    • Co-ordination of alkali metals to oligosaccharides dictates fragmentation behavior in matrix assisted laser desorption ionization/Fourier transform mass spectrometry
    • Concilia MT, Penn SG, Carroll JA, Lebrilk CB. Co-ordination of alkali metals to oligosaccharides dictates fragmentation behavior in matrix assisted laser desorption ionization/Fourier transform mass spectrometry. J. Am. Chem. Soc. 118, 6736-6745 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6736-6745
    • Cancilia, M.T.1    Penn, S.G.2    Carroll, J.A.3    Lebrilla, C.B.4
  • 121
    • 0141482211 scopus 로고    scopus 로고
    • Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry
    • Mechref Y, Novotny MV, Krishnan C. Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 75, 4895-4903 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 4895-4903
    • Mechref, Y.1    Novotny, M.V.2    Krishnan, C.3
  • 122
    • 1942454436 scopus 로고    scopus 로고
    • Fragmentation characteristics of neutral N-linked glycans using a MALDI-TOF/TOF tandem mass spectrometer
    • Stephens E, Maslen SL, Green LG, Williams DH. Fragmentation characteristics of neutral N-linked glycans using a MALDI-TOF/TOF tandem mass spectrometer. Anal. Chem. 76, 2343-2354 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 2343-2354
    • Stephens, E.1    Maslen, S.L.2    Green, L.G.3    Williams, D.H.4
  • 123
    • 0035253343 scopus 로고    scopus 로고
    • Negative-ion electrospray mass spectrometry of neutral underivatized oligosaccharides
    • Chai W, Piskarev V, Lawson AM. Negative-ion electrospray mass spectrometry of neutral underivatized oligosaccharides. Anal. Chem. 73, 651-657 (2001).
    • (2001) Anal. Chem. , vol.73 , pp. 651-657
    • Chai, W.1    Piskarev, V.2    Lawson, A.M.3
  • 126
    • 0036618254 scopus 로고    scopus 로고
    • Branching pattern and sequence analysis of underivatized oligosaccharides by combined MS/MS of singly and doubly charged molecular ions in negative-ion electrospray mass spectrometry
    • Chai W, Piskarev V, Lawson AM. Branching pattern and sequence analysis of underivatized oligosaccharides by combined MS/MS of singly and doubly charged molecular ions in negative-ion electrospray mass spectrometry. J. Am. Soc. Mass Spectrom. 13, 670-679 (2002).
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 670-679
    • Chai, W.1    Piskarev, V.2    Lawson, A.M.3
  • 127
    • 4243584416 scopus 로고    scopus 로고
    • Structural characterisation of both positive- And negative-ion electrospray mass spectrometry of partially methyl-esterified oligogalacturonides purified by semi-preparative high-performance anion-exchange chromatography
    • Quéméner B, Désiré C, Lahaye M, Debrauwer L, Negroni L. Structural characterisation of both positive- and negative-ion electrospray mass spectrometry of partially methyl-esterified oligogalacturonides purified by semi-preparative high-performance anion-exchange chromatography. Eur. J. Mass. Spectrom. 9, 45-60 (2003).
    • (2003) Eur. J. Mass. Spectrom. , vol.9 , pp. 45-60
    • Quéméner, B.1    Désiré, C.2    Lahaye, M.3    Debrauwer, L.4    Negroni, L.5
  • 128
    • 0036726788 scopus 로고    scopus 로고
    • Sequencing of tri- And tetraantennary N-glycans containing sialic acid by negative mode ESI QTOF tandem MS
    • Sagi D, Peter-Katalinic J, Conradt HS, Nimtz M. Sequencing of tri- and tetraantennary N-glycans containing sialic acid by negative mode ESI QTOF tandem MS. J. Am. Soc. Mass Spectrom. 13, 1138-1148 (2002).
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 1138-1148
    • Sagi, D.1    Peter-Katalinic, J.2    Conradt, H.S.3    Nimtz, M.4
  • 129
    • 0034667931 scopus 로고    scopus 로고
    • Negative ion mass spectrometry of sialylated carbohydrates: Discrimination of N-acetylneuraminic acid linkages by matrix-assisted laser desorption/ionizarion-time-of-flight and electrospray-time-of-flight mass spectrometry
    • Wheeler SF, Harvey DJ. Negative ion mass spectrometry of sialylated carbohydrates: Discrimination of N-acetylneuraminic acid linkages by matrix-assisted laser desorption/ionizarion-time-of-flight and electrospray-time-of-flight mass spectrometry. Anal. Chem. 72, 5027-5039 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 5027-5039
    • Wheeler, S.F.1    Harvey, D.J.2
  • 130
    • 18044364597 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates: Part 2; fragmentation of high-mannose N-linked glycans
    • In Press
    • Harvey DJ. Fragmentation of negative ions from carbohydrates: Part 2; fragmentation of high-mannose N-linked glycans. J. Am. Soc. Mass Spectrom. (2005) (In Press). Mechanisms for the negative ion fragmentation of high-mannose N-linked glycans.
    • (2005) J. Am. Soc. Mass Spectrom.
    • Harvey, D.J.1
  • 131
    • 14344254313 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates: Part 3, fragmentation of hybrid and complex N-linked glycans
    • In Press
    • Harvey DJ. Fragmentation of negative ions from carbohydrates: Part 3, fragmentation of hybrid and complex N-linked glycans. J. Am. Soc. Mass Spectrom. (2005) (In Press). Mechanisms for the negative ion fragmentation of hybrid and complex N-linked glycans.
    • (2005) J. Am. Soc. Mass Spectrom.
    • Harvey, D.J.1
  • 133
    • 0032722950 scopus 로고    scopus 로고
    • An automated interpretation of MALDI/TOF postsource decay spectra of oligosaccharides. I. Automated peak assignment
    • Mizuno Y, Sasagawa T, Dohmae N, Takio K. An automated interpretation of MALDI/TOF postsource decay spectra of oligosaccharides. I. Automated peak assignment. Anal. Chem. 71, 4764-4771 (1999).
    • (1999) Anal. Chem. , vol.71 , pp. 4764-4771
    • Mizuno, Y.1    Sasagawa, T.2    Dohmae, N.3    Takio, K.4
  • 134
    • 0034214358 scopus 로고    scopus 로고
    • STAT: A saccharide topology analysis tool used in combination with tandem mass spectrometry
    • Gaucher SP, Morrow J, Leary JA. STAT: a saccharide topology analysis tool used in combination with tandem mass spectrometry. Anal. Chem. 72, 2331-2336 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 2331-2336
    • Gaucher, S.P.1    Morrow, J.2    Leary, J.A.3
  • 136
    • 0347420013 scopus 로고    scopus 로고
    • Application of the StrOligo algorithm for the automated structure assignment of complex N-linked glycans from glycoproteins using tandem mass spectrometry
    • Ethier M, Saba JA, Spearman M et al. Application of the StrOligo algorithm for the automated structure assignment of complex N-linked glycans from glycoproteins using tandem mass spectrometry. Rapid Commun. Mass Spectrom. 17, 2713-2720 (2003).
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2713-2720
    • Ethier, M.1    Saba, J.A.2    Spearman, M.3
  • 137
    • 0142213540 scopus 로고    scopus 로고
    • GLYCO-FRAGMENT: A web tool to support the interpretation of mass spectra of complex carbohydrates
    • Lohmann KK, von der Lieth C-W. GLYCO-FRAGMENT: a web tool to support the interpretation of mass spectra of complex carbohydrates. Proteomics 3, 2028-2035 (2003).
    • (2003) Proteomics , vol.3 , pp. 2028-2035
    • Lohmann, K.K.1    Von Der Lieth, C.-W.2
  • 138
    • 2942568109 scopus 로고    scopus 로고
    • Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data
    • Joshi HJ, Harrison MJ, Schulz BL, Cooper CA, Packer NH, Karlsson NG. Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data. Proteomics 4, 1650-1664 (2004).
    • (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
  • 139
    • 4043113650 scopus 로고    scopus 로고
    • Characterization of protein glycosylation using chip-based Infusion nanoelectrospray linear ion trap
    • Zhang S, Chelius D. Characterization of protein glycosylation using chip-based Infusion nanoelectrospray linear ion trap. J. Biomol. Tech. 15, 120-133 (2004).
    • (2004) J. Biomol. Tech. , vol.15 , pp. 120-133
    • Zhang, S.1    Chelius, D.2
  • 140
    • 10844220663 scopus 로고    scopus 로고
    • Coupling of fully automated chip electrospray to Fourier transform ion cyclotron resonance mass spectrometry for high-performance glycoscreening and sequencing
    • Froesch M, Bindik LM, Baykut G, Allen M, Peter-Katalinic J, Zamfir AD. Coupling of fully automated chip electrospray to Fourier transform ion cyclotron resonance mass spectrometry for high-performance glycoscreening and sequencing. Rapid Commun. Mass Spectrom. 18, 3084-3092 (2004).
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 3084-3092
    • Froesch, M.1    Bindila, L.M.2    Baykut, G.3    Allen, M.4    Peter-Katalinic, J.5    Zamfir, A.D.6
  • 141
    • 0037176207 scopus 로고    scopus 로고
    • Peak capacity of ion mobility mass spectrometry: Separation of peptides in helium buffer gas
    • Ruotolo BT, Gillig KJ, Stone EG, Russell DH. Peak capacity of ion mobility mass spectrometry: separation of peptides in helium buffer gas. J. Chromatogr. B 782, 385-392 (2002).
    • (2002) J. Chromatogr. B , vol.782 , pp. 385-392
    • Ruotolo, B.T.1    Gillig, K.J.2    Stone, E.G.3    Russell, D.H.4
  • 142
    • 0141993586 scopus 로고    scopus 로고
    • Development of high-sensitivity ion trap ion mobility spectrometry time-of-flight techniques: A high-throughput nano-LC-IMS-TOF separation of peptides arising from a Drosophila protein extract
    • Myung S, Lee YJ, Moon MH et al. Development of high-sensitivity ion trap ion mobility spectrometry time-of-flight techniques: a high-throughput nano-LC-IMS-TOF separation of peptides arising from a Drosophila protein extract. Anal. Chem. 75, 5137-5145 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 5137-5145
    • Myung, S.1    Lee, Y.J.2    Moon, M.H.3


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