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Volumn 896, Issue , 2015, Pages 85-92

The role of proton mobility in determining the energy-resolved vibrational activation/dissociation channels of N-glycopeptide ions

Author keywords

Collision induced dissociation; Glycopeptides; Glycoproteins; Glycoproteomics; Proton mobility; Tandem mass spectrometry

Indexed keywords

ACTIVATION ENERGY; AMIDES; DISSOCIATION; GLYCOPROTEINS; IONS; MASS SPECTROMETRY; POLYSACCHARIDES; PROTONATION;

EID: 84944442157     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2015.09.013     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 33750097998 scopus 로고    scopus 로고
    • The use of mass spectrometry for the proteomic analysis of glycosylation
    • Morelle W., Canis K., Chirat F., Faid V., Michalski J.C. The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics 2006, 6:3993-4015.
    • (2006) Proteomics , vol.6 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.C.5
  • 2
    • 44249099705 scopus 로고    scopus 로고
    • Glycopeptide analysis by mass spectrometry
    • Dalpathado D.S., Desaire H. Glycopeptide analysis by mass spectrometry. Analyst 2008, 133:731-738.
    • (2008) Analyst , vol.133 , pp. 731-738
    • Dalpathado, D.S.1    Desaire, H.2
  • 6
    • 84859861608 scopus 로고    scopus 로고
    • N-glycoproteomics: mass spectrometry-based glycosylation site annotation
    • Pasing Y., Sickmann A., Lewandrowski U. N-glycoproteomics: mass spectrometry-based glycosylation site annotation. Biol. Chem. 2012, 393:249-258.
    • (2012) Biol. Chem. , vol.393 , pp. 249-258
    • Pasing, Y.1    Sickmann, A.2    Lewandrowski, U.3
  • 7
    • 84865578480 scopus 로고    scopus 로고
    • Glycoprotein analysis using mass spectrometry: unraveling the layers of complexity
    • Schiel J.E. Glycoprotein analysis using mass spectrometry: unraveling the layers of complexity. Anal. Bioanal. Chem. 2012, 404:1141-1149.
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 1141-1149
    • Schiel, J.E.1
  • 8
    • 84920713443 scopus 로고    scopus 로고
    • Engaging challenges in glycoproteomics: recent advances in MS-based glycopeptide analysis
    • Kolli V., Schumacher K.N., Dodds E.D. Engaging challenges in glycoproteomics: recent advances in MS-based glycopeptide analysis. Bioanalysis 2015, 7:113-131.
    • (2015) Bioanalysis , vol.7 , pp. 113-131
    • Kolli, V.1    Schumacher, K.N.2    Dodds, E.D.3
  • 9
    • 84876125044 scopus 로고    scopus 로고
    • High-sensitivity analytical approaches for the structural characterization of glycoproteins
    • Alley W.R., Mann B.F., Novotny M.V. High-sensitivity analytical approaches for the structural characterization of glycoproteins. Chem. Rev. 2013, 113:2668-2732.
    • (2013) Chem. Rev. , vol.113 , pp. 2668-2732
    • Alley, W.R.1    Mann, B.F.2    Novotny, M.V.3
  • 10
    • 84875987561 scopus 로고    scopus 로고
    • Glycopeptide analysis, recent developments and applications
    • Desaire H. Glycopeptide analysis, recent developments and applications. Mol. Cell. Proteom. 2013, 12:893-901.
    • (2013) Mol. Cell. Proteom. , vol.12 , pp. 893-901
    • Desaire, H.1
  • 11
    • 84920716663 scopus 로고    scopus 로고
    • Carbohydrate and glycoconjugate analysis by ion mobility mass spectrometry: opportunities and challenges
    • Huang Y., Gelb A.S., Dodds E.D. Carbohydrate and glycoconjugate analysis by ion mobility mass spectrometry: opportunities and challenges. Curr. Metabolomics 2013, 1:291-305.
    • (2013) Curr. Metabolomics , vol.1 , pp. 291-305
    • Huang, Y.1    Gelb, A.S.2    Dodds, E.D.3
  • 12
    • 84902215375 scopus 로고    scopus 로고
    • Advances in LC-MS/MS-based glycoproteomics: getting closer to system-wide site-specific mapping of the N- and O-glycoproteome
    • Thaysen-Andersen M., Packer N.H. Advances in LC-MS/MS-based glycoproteomics: getting closer to system-wide site-specific mapping of the N- and O-glycoproteome. Biochim. Biophys. Acta 2014, 1844:1437-1452.
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1437-1452
    • Thaysen-Andersen, M.1    Packer, N.H.2
  • 13
    • 34047164035 scopus 로고    scopus 로고
    • Glycoproteomics based on tandem mass spectrometry of glycopeptides
    • Wuhrer M., Catalina M.I., Deelder A.M., Hokke C.H. Glycoproteomics based on tandem mass spectrometry of glycopeptides. J. Chromatogr. B 2007, 849:115-128.
    • (2007) J. Chromatogr. B , vol.849 , pp. 115-128
    • Wuhrer, M.1    Catalina, M.I.2    Deelder, A.M.3    Hokke, C.H.4
  • 14
    • 84867576799 scopus 로고    scopus 로고
    • Gas-phase dissociation of glycosylated peptide ions
    • Dodds E.D. Gas-phase dissociation of glycosylated peptide ions. Mass Spectrom. Rev. 2012, 31:666-682.
    • (2012) Mass Spectrom. Rev. , vol.31 , pp. 666-682
    • Dodds, E.D.1
  • 15
    • 70349113034 scopus 로고    scopus 로고
    • Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
    • An H.J., Froehlich J.W., Lebrilla C.B. Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. Curr. Opin. Chem. Biol. 2009, 13:421-426.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 421-426
    • An, H.J.1    Froehlich, J.W.2    Lebrilla, C.B.3
  • 17
    • 61849147415 scopus 로고    scopus 로고
    • Extracting both peptide sequence and glycan structural information by 157 nm photodissociation of N-linked glycopeptides
    • Zhang L., Reilly J.P. Extracting both peptide sequence and glycan structural information by 157 nm photodissociation of N-linked glycopeptides. J. Proteome Res. 2008, 8:734-742.
    • (2008) J. Proteome Res. , vol.8 , pp. 734-742
    • Zhang, L.1    Reilly, J.P.2
  • 18
    • 84885014675 scopus 로고    scopus 로고
    • Concurrent automated sequencing of the glycan and peptide portions of O-linked glycopeptide anions by ultraviolet photodissociation mass spectrometry
    • Madsen J.A., Ko B.J., Xu H., Iwashkiw J.A., Robotham S.A., Shaw J.B., Feldman M.F., Brodbelt J.S. Concurrent automated sequencing of the glycan and peptide portions of O-linked glycopeptide anions by ultraviolet photodissociation mass spectrometry. Anal. Chem. 2013, 85:9253-9261.
    • (2013) Anal. Chem. , vol.85 , pp. 9253-9261
    • Madsen, J.A.1    Ko, B.J.2    Xu, H.3    Iwashkiw, J.A.4    Robotham, S.A.5    Shaw, J.B.6    Feldman, M.F.7    Brodbelt, J.S.8
  • 19
    • 33644839418 scopus 로고    scopus 로고
    • Infrared multiphoton dissociation and electron capture dissociation of high-mannose type glycopeptides
    • Adamson J.T., Hakansson K. Infrared multiphoton dissociation and electron capture dissociation of high-mannose type glycopeptides. J. Proteome Res. 2006, 5:493-501.
    • (2006) J. Proteome Res. , vol.5 , pp. 493-501
    • Adamson, J.T.1    Hakansson, K.2
  • 20
    • 34248203257 scopus 로고    scopus 로고
    • Sequencing of O-glycopeptides derived from an S-layer glycoprotein of geobacillus stearothermophilus NRS 2004/3a containing up to 51 monosaccharide residues at a single glycosylation site by fourier transform ion cyclotron resonance infrared multiphoton dissociation mass spectrometry
    • Bindila L., Steiner K., Schaffer C., Messner P., Mormann M., Peter-Katalinic J. Sequencing of O-glycopeptides derived from an S-layer glycoprotein of geobacillus stearothermophilus NRS 2004/3a containing up to 51 monosaccharide residues at a single glycosylation site by fourier transform ion cyclotron resonance infrared multiphoton dissociation mass spectrometry. Anal. Chem. 2007, 79:3271-3279.
    • (2007) Anal. Chem. , vol.79 , pp. 3271-3279
    • Bindila, L.1    Steiner, K.2    Schaffer, C.3    Messner, P.4    Mormann, M.5    Peter-Katalinic, J.6
  • 22
    • 61849145815 scopus 로고    scopus 로고
    • Exploiting differential dissociation chemistries of O-linked glycopeptide ions for the localization of mucin-type protein glycosylation
    • Seipert R.R., Dodds E.D., Lebrilla C.B. Exploiting differential dissociation chemistries of O-linked glycopeptide ions for the localization of mucin-type protein glycosylation. J. Proteome Res. 2009, 8:493-501.
    • (2009) J. Proteome Res. , vol.8 , pp. 493-501
    • Seipert, R.R.1    Dodds, E.D.2    Lebrilla, C.B.3
  • 23
    • 77951572809 scopus 로고    scopus 로고
    • Characterizing protein glycosylation sites through higher-energy C-trap dissociation
    • Segu Z.M., Mechref Y. Characterizing protein glycosylation sites through higher-energy C-trap dissociation. Rapid Commun. Mass Spectrom. 2010, 24:1217-1225.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 1217-1225
    • Segu, Z.M.1    Mechref, Y.2
  • 24
    • 84904304611 scopus 로고    scopus 로고
    • Strategy integrating stepped fragmentation and glycan diagnostic ion-based spectrum refinement for the identification of core fucosylated glycoproteome using mass spectrometry
    • Cao Q., Zhao X., Zhao Q., Lv X., Ma C., Li X., Zhao Y., Peng B., Ying W., Qian X. Strategy integrating stepped fragmentation and glycan diagnostic ion-based spectrum refinement for the identification of core fucosylated glycoproteome using mass spectrometry. Anal. Chem. 2014, 86:6804-6811.
    • (2014) Anal. Chem. , vol.86 , pp. 6804-6811
    • Cao, Q.1    Zhao, X.2    Zhao, Q.3    Lv, X.4    Ma, C.5    Li, X.6    Zhao, Y.7    Peng, B.8    Ying, W.9    Qian, X.10
  • 25
    • 84898714929 scopus 로고    scopus 로고
    • Energy-resolved collision-induced dissociation pathways of model N-linked glycopeptides: implications for capturing glycan connectivity and peptide sequence in a single experiment
    • Kolli V., Dodds E.D. Energy-resolved collision-induced dissociation pathways of model N-linked glycopeptides: implications for capturing glycan connectivity and peptide sequence in a single experiment. Analyst 2014, 139:2144-2153.
    • (2014) Analyst , vol.139 , pp. 2144-2153
    • Kolli, V.1    Dodds, E.D.2
  • 26
    • 84924907812 scopus 로고    scopus 로고
    • A comparison of energy-resolved vibrational activation/dissociation characteristics of protonated and sodiated high mannose N-glycopeptides
    • Aboufazeli F., Kolli V., Dodds E.D. A comparison of energy-resolved vibrational activation/dissociation characteristics of protonated and sodiated high mannose N-glycopeptides. J. Am. Soc. Mass Spectrom. 2015, 26:587-595.
    • (2015) J. Am. Soc. Mass Spectrom. , vol.26 , pp. 587-595
    • Aboufazeli, F.1    Kolli, V.2    Dodds, E.D.3
  • 27
    • 61849083637 scopus 로고    scopus 로고
    • Dissociation profile of protonated fucosyl glycopeptides and quantitation of fucosylation levels of glycoproteins by mass spectrometry
    • Tajiri M., Kadoya M., Wada Y. Dissociation profile of protonated fucosyl glycopeptides and quantitation of fucosylation levels of glycoproteins by mass spectrometry. J. Proteome Res. 2009, 8:688-693.
    • (2009) J. Proteome Res. , vol.8 , pp. 688-693
    • Tajiri, M.1    Kadoya, M.2    Wada, Y.3
  • 29
    • 0029810698 scopus 로고    scopus 로고
    • Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: evidence for the mobile proton model
    • Dongré A.R., Jones J.L., Somogyi Á., Wysocki V.H. Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: evidence for the mobile proton model. J. Am. Chem. Soc. 1996, 118:8365-8374.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8365-8374
    • Dongré, A.R.1    Jones, J.L.2    Somogyi, A.3    Wysocki, V.H.4
  • 30
    • 0034501099 scopus 로고    scopus 로고
    • Mobile and localized protons: a framework for understanding peptide dissociation
    • Wysocki V.H., Tsaprailis G., Smith L.L., Breci L.A. Mobile and localized protons: a framework for understanding peptide dissociation. J. Mass Spectrom. 2000, 35:1399-1406.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1399-1406
    • Wysocki, V.H.1    Tsaprailis, G.2    Smith, L.L.3    Breci, L.A.4
  • 32
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff P., Fohlman J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 1984, 11:601.
    • (1984) Biomed. Mass Spectrom. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 33
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon B., Costello C.E. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 1988, 5:397-409.
    • (1988) Glycoconj. J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 34
    • 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 S.A. The utility of nonspecific proteases in the characterization of glycoproteins by high-resolution time-of-flight mass spectrometry. Int. J. Mass Spectrom. Ion. Proc. 1997, 169/170:217-230.
    • (1997) Int. J. Mass Spectrom. Ion. Proc. , pp. 217-230
    • Juhasz, P.1    Martin, S.A.2
  • 35
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An H.J., Peavy T.R., Hedrick J.L., Lebrilla C.B. Determination of N-glycosylation sites and site heterogeneity in glycoproteins. Anal. Chem. 2003, 75:5628-5637.
    • (2003) Anal. Chem. , vol.75 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 36
    • 35648982031 scopus 로고    scopus 로고
    • Site determination of protein glycosylation based on digestion with immobilized nonspecific proteases and fourier transform ion cyclotron resonance mass spectrometry
    • Clowers B.H., Dodds E.D., Seipert R.R., Lebrilla C.B. Site determination of protein glycosylation based on digestion with immobilized nonspecific proteases and fourier transform ion cyclotron resonance mass spectrometry. J. Proteome Res. 2007, 6:4032-4040.
    • (2007) J. Proteome Res. , vol.6 , pp. 4032-4040
    • Clowers, B.H.1    Dodds, E.D.2    Seipert, R.R.3    Lebrilla, C.B.4
  • 37
    • 61849103543 scopus 로고    scopus 로고
    • Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics
    • Dodds E.D., Seipert R.R., Clowers B.H., German J.B., Lebrilla C.B. Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics. J. Proteome Res. 2009, 8:502-512.
    • (2009) J. Proteome Res. , vol.8 , pp. 502-512
    • Dodds, E.D.1    Seipert, R.R.2    Clowers, B.H.3    German, J.B.4    Lebrilla, C.B.5
  • 39
    • 84875129178 scopus 로고    scopus 로고
    • Degrees of freedom effect on fragmentation in tandem mass spectrometry of singly charged supramolecular aggregates of sodium sulfonates
    • Indelicato S., Bongiorno D., Indelicato S., Drahos L., Turco Liveri V., Turiák L., Vékey K., Ceraulo L. Degrees of freedom effect on fragmentation in tandem mass spectrometry of singly charged supramolecular aggregates of sodium sulfonates. J. Mass Spectrom. 2013, 48:379-383.
    • (2013) J. Mass Spectrom. , vol.48 , pp. 379-383
    • Indelicato, S.1    Bongiorno, D.2    Indelicato, S.3    Drahos, L.4    Turco Liveri, V.5    Turiák, L.6    Vékey, K.7    Ceraulo, L.8
  • 40
    • 0242653718 scopus 로고    scopus 로고
    • Mining a tandem mass spectrometry database to determine the trends and global factors influencing peptide fragmentation
    • Kapp E.A., Schutz F., Reid G.E., Eddes J.S., Moritz R.L., O'Hair R.A., Speed T.P., Simpson R.J. Mining a tandem mass spectrometry database to determine the trends and global factors influencing peptide fragmentation. Anal. Chem. 2003, 75:6251-6264.
    • (2003) Anal. Chem. , vol.75 , pp. 6251-6264
    • Kapp, E.A.1    Schutz, F.2    Reid, G.E.3    Eddes, J.S.4    Moritz, R.L.5    O'Hair, R.A.6    Speed, T.P.7    Simpson, R.J.8
  • 41
    • 77449152998 scopus 로고    scopus 로고
    • Understanding and exploiting peptide fragment ion intensities using experimental and informatic approaches
    • Gucinski A.C., Dodds E.D., Li W.Z., Wysocki V.H. Understanding and exploiting peptide fragment ion intensities using experimental and informatic approaches. Methods Mol. Biol. 2010, 604:73-94.
    • (2010) Methods Mol. Biol. , vol.604 , pp. 73-94
    • Gucinski, A.C.1    Dodds, E.D.2    Li, W.Z.3    Wysocki, V.H.4
  • 42
    • 21844457685 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • Paizs B., Suhai S. Fragmentation pathways of protonated peptides. Mass Spectrom. Rev. 2005, 24:508-548.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 508-548
    • Paizs, B.1    Suhai, S.2
  • 43
    • 84856152416 scopus 로고    scopus 로고
    • Detection and characterization of low abundance glycopeptides via higher-energy C-trap dissociation and orbitrap mass analysis
    • Hart-Smith G., Raftery M.J. Detection and characterization of low abundance glycopeptides via higher-energy C-trap dissociation and orbitrap mass analysis. J. Am. Soc. Mass Spectrom. 2012, 23:124-140.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 124-140
    • Hart-Smith, G.1    Raftery, M.J.2
  • 44
    • 84875993032 scopus 로고    scopus 로고
    • A classifier based on accurate mass measurements to aid large scale, unbiased glycoproteomics,
    • Froehlich J.W., Dodds E.D., Wilhelm M., Serang O., Steen J.A., Lee R.S. A classifier based on accurate mass measurements to aid large scale, unbiased glycoproteomics,. Mol. Cell. Proteom. 2013, 12:1017-1025.
    • (2013) Mol. Cell. Proteom. , vol.12 , pp. 1017-1025
    • Froehlich, J.W.1    Dodds, E.D.2    Wilhelm, M.3    Serang, O.4    Steen, J.A.5    Lee, R.S.6


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