메뉴 건너뛰기




Volumn 13, Issue 3, 2014, Pages 1485-1493

N-glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry

Author keywords

glycopeptide; glycoproteomics; hydrophilic interaction liquid chromatography; mass spectrometry; Saccharomyces cerevisiae; yeast

Indexed keywords

GLYCOPEPTIDE; GLYCOSIDASE; GLYCOSIDASE ENDO HF; GLYCOSIDASE PNGASE P; SACCHAROMYCES CEREVISIAE PROTEIN; UNCLASSIFIED DRUG;

EID: 84896792357     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr401049e     Document Type: Article
Times cited : (29)

References (53)
  • 1
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: A model organism helps elucidate congenital human diseases
    • Lehle, L.; Strahl, S.; Tanner, W. Protein glycosylation, conserved from yeast to man: A model organism helps elucidate congenital human diseases Angew. Chem., Int. Ed. 2006, 45 (41) 6802-6818
    • (2006) Angew. Chem., Int. Ed. , vol.45 , Issue.41 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 2
    • 0032960606 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from yeast
    • Knauer, R.; Lehle, L. The oligosaccharyltransferase complex from yeast Biochim. Biophys. Acta 1999, 1426 (2) 259-273
    • (1999) Biochim. Biophys. Acta , vol.1426 , Issue.2 , pp. 259-273
    • Knauer, R.1    Lehle, L.2
  • 3
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: The advent of fully humanized yeast
    • Hamilton, S. R.; Gerngross, T. U. Glycosylation engineering in yeast: the advent of fully humanized yeast Curr. Opin. Biotechnol. 2007, 18 (5) 387-392
    • (2007) Curr. Opin. Biotechnol. , vol.18 , Issue.5 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 4
    • 0035279221 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Genetic model systems lead the way
    • Aebi, M.; Hennet, T. Congenital disorders of glycosylation: genetic model systems lead the way Trends Cell Biol. 2001, 11 (3) 136-141
    • (2001) Trends Cell Biol. , vol.11 , Issue.3 , pp. 136-141
    • Aebi, M.1    Hennet, T.2
  • 5
    • 38349080026 scopus 로고    scopus 로고
    • N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry
    • Hulsmeier, A. J.; Paesold-Burda, P.; Hennet, T. N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry Mol. Cell. Proteomics 2007, 6 (12) 2132-2138
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.12 , pp. 2132-2138
    • Hulsmeier, A.J.1    Paesold-Burda, P.2    Hennet, T.3
  • 6
    • 84862905517 scopus 로고    scopus 로고
    • Diseases of glycosylation beyond classical congenital disorders of glycosylation
    • Hennet, T. Diseases of glycosylation beyond classical congenital disorders of glycosylation Biochim. Biophys. Acta 2012, 1820 (9) 1306-1317
    • (2012) Biochim. Biophys. Acta , vol.1820 , Issue.9 , pp. 1306-1317
    • Hennet, T.1
  • 7
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • Geyer, H.; Geyer, R. Strategies for analysis of glycoprotein glycosylation Biochim. Biophys. Acta Proteins Proteomics 2006, 1764 (12) 1853-1869
    • (2006) Biochim. Biophys. Acta Proteins Proteomics , vol.1764 , Issue.12 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 8
    • 78651105000 scopus 로고    scopus 로고
    • Mass Spectrometry Based Glycoproteomics-From a Proteomics Perspective
    • (R110.003251
    • Pan, S.; Chen, R.; Aebersold, R.; Brentnall, T. A. Mass Spectrometry Based Glycoproteomics-From a Proteomics Perspective Mol. Cell. Proteomics 2011, 10 (1 R110.003251
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.1
    • Pan, S.1    Chen, R.2    Aebersold, R.3    Brentnall, T.A.4
  • 9
    • 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 (14) 3993-4015
    • (2006) Proteomics , vol.6 , Issue.14 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.C.5
  • 10
    • 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 (1-2) 115-128
    • (2007) J. Chromatogr., B , vol.849 , Issue.12 , pp. 115-128
    • Wuhrer, M.1    Catalina, M.I.2    Deelder, A.M.3    Hokke, C.H.4
  • 11
    • 44249099705 scopus 로고    scopus 로고
    • Glycopeptide analysis by mass spectrometry
    • Dalpathado, D. S.; Desaire, H. Glycopeptide analysis by mass spectrometry Analyst 2008, 133 (6) 731-738
    • (2008) Analyst , vol.133 , Issue.6 , pp. 731-738
    • Dalpathado, D.S.1    Desaire, H.2
  • 12
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada, Y.; Tajiri, M.; Yoshida, S. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics Anal. Chem. 2004, 76 (22) 6560-6565
    • (2004) Anal. Chem. , vol.76 , Issue.22 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 13
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano, C. D.; Zambonin, C. G.; Jensen, O. N. Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry J. Proteomics 2008, 71 (3) 304-317
    • (2008) J. Proteomics , vol.71 , Issue.3 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 14
    • 53549093906 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry
    • Picariello, G.; Ferranti, P.; Mamone, G.; Roepstorff, P.; Addeo, F. Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry Proteomics 2008, 8 (18) 3833-3847
    • (2008) Proteomics , vol.8 , Issue.18 , pp. 3833-3847
    • Picariello, G.1    Ferranti, P.2    Mamone, G.3    Roepstorff, P.4    Addeo, F.5
  • 15
    • 42949172966 scopus 로고    scopus 로고
    • Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites
    • Zhang, Y.; Go, E. P.; Desaire, H. Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites Anal. Chem. 2008, 80 (9) 3144-3158
    • (2008) Anal. Chem. , vol.80 , Issue.9 , pp. 3144-3158
    • Zhang, Y.1    Go, E.P.2    Desaire, H.3
  • 16
    • 66149118626 scopus 로고    scopus 로고
    • Site-Specific Glycoprofiling of N-Linked Glycopeptides Using MALDI-TOF MS: Strong Correlation between Signal Strength and Glycoform Quantities
    • Thaysen-Andersen, M.; Mysling, S.; Hojrup, P. Site-Specific Glycoprofiling of N-Linked Glycopeptides Using MALDI-TOF MS: Strong Correlation between Signal Strength and Glycoform Quantities Anal. Chem. 2009, 81 (10) 3933-3943
    • (2009) Anal. Chem. , vol.81 , Issue.10 , pp. 3933-3943
    • Thaysen-Andersen, M.1    Mysling, S.2    Hojrup, P.3
  • 17
    • 77954203412 scopus 로고    scopus 로고
    • Utilizing Ion-Pairing Hydrophilic Interaction Chromatography Solid Phase Extraction for Efficient Glycopeptide Enrichment in Glycoproteomics
    • Mysling, S.; Palmisano, G.; Hojrup, P.; Thaysen-Andersen, M. Utilizing Ion-Pairing Hydrophilic Interaction Chromatography Solid Phase Extraction for Efficient Glycopeptide Enrichment in Glycoproteomics Anal. Chem. 2010, 82 (13) 5598-5609
    • (2010) Anal. Chem. , vol.82 , Issue.13 , pp. 5598-5609
    • Mysling, S.1    Palmisano, G.2    Hojrup, P.3    Thaysen-Andersen, M.4
  • 18
    • 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 (4) 249-258
    • (2012) Biol. Chem. , vol.393 , Issue.4 , pp. 249-258
    • Pasing, Y.1    Sickmann, A.2    Lewandrowski, U.3
  • 19
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H.; Li, X. J.; Martin, D. B.; Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 2003, 21 (6) 660-666
    • (2003) Nat. Biotechnol. , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 20
    • 77956014533 scopus 로고    scopus 로고
    • The Lectin Riddle: Glycoproteins Fractionated from Complex Mixtures Have Similar Glycomic Profiles
    • Lee, A.; Nakano, M.; Hincapie, M.; Kolarich, D.; Baker, M. S.; Hancock, W. S.; Packer, N. H. The Lectin Riddle: Glycoproteins Fractionated from Complex Mixtures Have Similar Glycomic Profiles Omics 2010, 14 (4) 487-499
    • (2010) Omics , vol.14 , Issue.4 , pp. 487-499
    • Lee, A.1    Nakano, M.2    Hincapie, M.3    Kolarich, D.4    Baker, M.S.5    Hancock, W.S.6    Packer, N.H.7
  • 21
    • 61849115201 scopus 로고    scopus 로고
    • Identification of N-Glycosylation Sites on Secreted Proteins of Human Hepatocellular Carcinoma Cells with a Complementary Proteomics Approach
    • Cao, J.; Shen, C. P.; Wang, H.; Shen, H. L.; Chen, Y. C.; Nie, A. Y.; Yan, G. Q.; Lu, H. J.; Liu, Y. K.; Yang, P. Y. Identification of N-Glycosylation Sites on Secreted Proteins of Human Hepatocellular Carcinoma Cells with a Complementary Proteomics Approach J. Proteome Res. 2009, 8 (2) 662-672
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 662-672
    • Cao, J.1    Shen, C.P.2    Wang, H.3    Shen, H.L.4    Chen, Y.C.5    Nie, A.Y.6    Yan, G.Q.7    Lu, H.J.8    Liu, Y.K.9    Yang, P.Y.10
  • 22
    • 77950632171 scopus 로고    scopus 로고
    • Simultaneous Characterization of Glyco- and Phosphoproteomes of Mouse Brain Membrane Proteome with Electrostatic Repulsion Hydrophilic Interaction Chromatography
    • Zhang, H. M.; Guo, T. N.; Li, X.; Datta, A.; Park, J. E.; Yang, J.; Lim, S. K.; Tam, J. P.; Sze, S. K. Simultaneous Characterization of Glyco- and Phosphoproteomes of Mouse Brain Membrane Proteome with Electrostatic Repulsion Hydrophilic Interaction Chromatography Mol. Cell. Proteomics 2010, 9 (4) 635-647
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.4 , pp. 635-647
    • Zhang, H.M.1    Guo, T.N.2    Li, X.3    Datta, A.4    Park, J.E.5    Yang, J.6    Lim, S.K.7    Tam, J.P.8    Sze, S.K.9
  • 23
    • 71549118236 scopus 로고    scopus 로고
    • Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage
    • Yu, L.; Li, X. L.; Guo, Z. M.; Zhang, X. L.; Liang, X. M. Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage Chem.-Eur. J. 2009, 15 (46) 12618-12626
    • (2009) Chem. - Eur. J. , vol.15 , Issue.46 , pp. 12618-12626
    • Yu, L.1    Li, X.L.2    Guo, Z.M.3    Zhang, X.L.4    Liang, X.M.5
  • 24
    • 78650402921 scopus 로고    scopus 로고
    • Selective enrichment of N-linked glycopeptides by using a highly hydrophilic matrix synthesized via click chemistry
    • Yu, L.; Li, X. L.; Dong, J.; Zhang, X. L.; Guo, Z. M.; Liang, X. M. Selective enrichment of N-linked glycopeptides by using a highly hydrophilic matrix synthesized via click chemistry Anal. Methods 2010, 2 (11) 1667-1670
    • (2010) Anal. Methods , vol.2 , Issue.11 , pp. 1667-1670
    • Yu, L.1    Li, X.L.2    Dong, J.3    Zhang, X.L.4    Guo, Z.M.5    Liang, X.M.6
  • 25
    • 84879462715 scopus 로고    scopus 로고
    • Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides
    • Cao, L. W.; Yu, L.; Guo, Z. M.; Li, X. L.; Xue, X. Y.; Liang, X. M. Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides J. Chromatogr., A 2013, 1299, 18-24
    • (2013) J. Chromatogr., A , vol.1299 , pp. 18-24
    • Cao, L.W.1    Yu, L.2    Guo, Z.M.3    Li, X.L.4    Xue, X.Y.5    Liang, X.M.6
  • 26
    • 78650302522 scopus 로고    scopus 로고
    • Recent advances in the MS analysis of glycoproteins: Theoretical considerations
    • Lazar, I. M.; Lazar, A. C.; Cortes, D. F.; Kabulski, J. L. Recent advances in the MS analysis of glycoproteins: Theoretical considerations Electrophoresis 2011, 32 (1) 3-13
    • (2011) Electrophoresis , vol.32 , Issue.1 , pp. 3-13
    • Lazar, I.M.1    Lazar, A.C.2    Cortes, D.F.3    Kabulski, J.L.4
  • 27
    • 26444476996 scopus 로고    scopus 로고
    • Protein glycosylation analysis by liquid chromatography-mass spectrometry
    • Wuhrer, M.; Deelder, A. M.; Hokke, C. H. Protein glycosylation analysis by liquid chromatography-mass spectrometry J. Chromatogr., B 2005, 825 (2) 124-133
    • (2005) J. Chromatogr., B , vol.825 , Issue.2 , pp. 124-133
    • Wuhrer, M.1    Deelder, A.M.2    Hokke, C.H.3
  • 28
    • 79551475593 scopus 로고    scopus 로고
    • The good, the bad, the ugly: Validating the mass spectrometric analysis of modified peptides
    • Beck, F.; Lewandrowski, U.; Wiltfang, M.; Feldmann, I.; Geiger, J.; Sickmann, A.; Zahedi, R. P. The good, the bad, the ugly: Validating the mass spectrometric analysis of modified peptides Proteomics 2011, 11 (6) 1099-1109
    • (2011) Proteomics , vol.11 , Issue.6 , pp. 1099-1109
    • Beck, F.1    Lewandrowski, U.2    Wiltfang, M.3    Feldmann, I.4    Geiger, J.5    Sickmann, A.6    Zahedi, R.P.7
  • 29
    • 84871984532 scopus 로고    scopus 로고
    • Glycoproteomics on the rise: Established methods, advanced techniques, sophisticated biological applications
    • Lazar, I. M.; Lee, W.; Lazar, A. C. Glycoproteomics on the rise: Established methods, advanced techniques, sophisticated biological applications Electrophoresis 2013, 34 (1) 113-125
    • (2013) Electrophoresis , vol.34 , Issue.1 , pp. 113-125
    • Lazar, I.M.1    Lee, W.2    Lazar, A.C.3
  • 30
    • 80054030914 scopus 로고    scopus 로고
    • Detection, Evaluation and Minimization of Nonenzymatic Deamidation in Proteomic Sample Preparation
    • (O111.009381
    • Hao, P. L.; Ren, Y.; Alpert, A. J.; Sze, S. K. Detection, Evaluation and Minimization of Nonenzymatic Deamidation in Proteomic Sample Preparation Mol. Cell. Proteomics 2011, 10 (10 O111.009381
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.10
    • Hao, P.L.1    Ren, Y.2    Alpert, A.J.3    Sze, S.K.4
  • 32
    • 84857873715 scopus 로고    scopus 로고
    • Chemical Deamidation: A Common Pitfall in Large-Scale N-Linked Glycoproteomic Mass Spectrometry-Based Analyses
    • Palmisano, G.; Melo-Braga, M. N.; Engholm-Keller, K.; Parker, B. L.; Larsen, M. R. Chemical Deamidation: A Common Pitfall in Large-Scale N-Linked Glycoproteomic Mass Spectrometry-Based Analyses J. Proteome Res. 2012, 11 (3) 1949-1957
    • (2012) J. Proteome Res. , vol.11 , Issue.3 , pp. 1949-1957
    • Palmisano, G.1    Melo-Braga, M.N.2    Engholm-Keller, K.3    Parker, B.L.4    Larsen, M.R.5
  • 34
    • 21444449702 scopus 로고    scopus 로고
    • PFind: A novel database-searching software system for automated peptide and protein identification via tandem mass spectrometry
    • Li, D. Q.; Fu, Y.; Sun, R. X.; Ling, C. X.; Wei, Y. G.; Zhou, H.; Zeng, R.; Yang, Q.; He, S. M.; Gao, W. pFind: a novel database-searching software system for automated peptide and protein identification via tandem mass spectrometry Bioinformatics 2005, 21 (13) 3049-3050
    • (2005) Bioinformatics , vol.21 , Issue.13 , pp. 3049-3050
    • Li, D.Q.1    Fu, Y.2    Sun, R.X.3    Ling, C.X.4    Wei, Y.G.5    Zhou, H.6    Zeng, R.7    Yang, Q.8    He, S.M.9    Gao, W.10
  • 35
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J. C.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999, 20 (18) 3551-3567
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 36
    • 79955009170 scopus 로고    scopus 로고
    • A novel zwitterionic HILIC stationary phase based on "thiol- ene" click chemistry between cysteine and vinyl silica
    • Shen, A. J.; Guo, Z. M.; Yu, L.; Cao, L. W.; Liang, X. M. A novel zwitterionic HILIC stationary phase based on "thiol-ene" click chemistry between cysteine and vinyl silica Chem. Commun. 2011, 47 (15) 4550-4552
    • (2011) Chem. Commun. , vol.47 , Issue.15 , pp. 4550-4552
    • Shen, A.J.1    Guo, Z.M.2    Yu, L.3    Cao, L.W.4    Liang, X.M.5
  • 37
    • 3543136464 scopus 로고    scopus 로고
    • Glycopeptide analysis by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry reveals novel features of horseradish peroxidase glycosylation
    • Wuhrer, M.; Hokke, C. H.; Deelder, A. M. Glycopeptide analysis by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry reveals novel features of horseradish peroxidase glycosylation Rapid Commun. Mass Spectrom. 2004, 18 (15) 1741-1748
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , Issue.15 , pp. 1741-1748
    • Wuhrer, M.1    Hokke, C.H.2    Deelder, A.M.3
  • 38
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner, J.; Premsler, T.; Sickmann, A. Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications Proteomics 2008, 8 (21) 4466-4483
    • (2008) Proteomics , vol.8 , Issue.21 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 40
    • 70349333832 scopus 로고    scopus 로고
    • Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes
    • doi: 10.1038/Msb.2009.64.
    • Kung, L. A.; Tao, S. C.; Qian, J.; Smith, M. G.; Snyder, M.; Zhu, H. Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes. Mol. Syst. Biol. 2009, 5, doi: 10.1038/Msb.2009.64.
    • (2009) Mol. Syst. Biol. , vol.5
    • Kung, L.A.1    Tao, S.C.2    Qian, J.3    Smith, M.G.4    Snyder, M.5    Zhu, H.6
  • 41
    • 33748471966 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography
    • Hemstrom, P.; Irgum, K. Hydrophilic interaction chromatography J. Sep. Sci. 2006, 29 (12) 1784-1821
    • (2006) J. Sep. Sci. , vol.29 , Issue.12 , pp. 1784-1821
    • Hemstrom, P.1    Irgum, K.2
  • 42
    • 65249134633 scopus 로고    scopus 로고
    • Structural Glycomics Using Hydrophilic Interaction Chromatography (Hilic) with Mass Spectrometry
    • Wuhrer, M.; de Boer, A. R.; Deelder, A. M. Structural Glycomics Using Hydrophilic Interaction Chromatography (Hilic) with Mass Spectrometry Mass Spectrom. Rev. 2009, 28 (2) 192-206
    • (2009) Mass Spectrom. Rev. , vol.28 , Issue.2 , pp. 192-206
    • Wuhrer, M.1    De Boer, A.R.2    Deelder, A.M.3
  • 43
    • 42449147408 scopus 로고    scopus 로고
    • Hydrophilic interaction liquid chromatography (HILIC) in proteomics
    • Boersema, P. J.; Mohammed, S.; Heck, A. J. R. Hydrophilic interaction liquid chromatography (HILIC) in proteomics Anal. Bioanal. Chem. 2008, 391 (1) 151-159
    • (2008) Anal. Bioanal. Chem. , vol.391 , Issue.1 , pp. 151-159
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.R.3
  • 44
    • 70349784960 scopus 로고    scopus 로고
    • Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies
    • Wohlgemuth, J.; Karas, M.; Eichhorn, T.; Hendriks, R.; Andrecht, S. Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies Anal. Biochem. 2009, 395 (2) 178-188
    • (2009) Anal. Biochem. , vol.395 , Issue.2 , pp. 178-188
    • Wohlgemuth, J.1    Karas, M.2    Eichhorn, T.3    Hendriks, R.4    Andrecht, S.5
  • 45
    • 1842525883 scopus 로고    scopus 로고
    • Amide molecular clocks in drosophila proteins: Potential regulators of aging and other processes
    • Robinson, N. E.; Robinson, A. B. Amide molecular clocks in drosophila proteins: potential regulators of aging and other processes Mech. Ageing Dev. 2004, 125 (4) 259-267
    • (2004) Mech. Ageing Dev. , vol.125 , Issue.4 , pp. 259-267
    • Robinson, N.E.1    Robinson, A.B.2
  • 47
    • 77956518417 scopus 로고    scopus 로고
    • Development of Serum Glycoproteomic Profiling Technique; Simultaneous Identification of Glycosylation Sites and Site-Specific Quantification of Glycan Structure Changes
    • Ueda, K.; Takami, S.; Saichi, N.; Daigo, Y.; Ishikawa, N.; Kohno, N.; Katsumata, M.; Yamane, A.; Ota, M.; Sato, T. A.; Nakamura, Y.; Nakagawa, H. Development of Serum Glycoproteomic Profiling Technique; Simultaneous Identification of Glycosylation Sites and Site-Specific Quantification of Glycan Structure Changes Mol. Cell. Proteomics 2010, 9 (9) 1819-1828
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.9 , pp. 1819-1828
    • Ueda, K.1    Takami, S.2    Saichi, N.3    Daigo, Y.4    Ishikawa, N.5    Kohno, N.6    Katsumata, M.7    Yamane, A.8    Ota, M.9    Sato, T.A.10    Nakamura, Y.11    Nakagawa, H.12
  • 48
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund, P.; Bunkenborg, J.; Elortza, F.; Jensen, O. N.; Roepstorff, P. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation J. Proteome Res. 2004, 3 (3) 556-566
    • (2004) J. Proteome Res. , vol.3 , Issue.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 49
    • 33744811996 scopus 로고    scopus 로고
    • Mass spectrometry for congenital disorders of glycosylation, CDG
    • Wada, Y. Mass spectrometry for congenital disorders of glycosylation, CDG J. Chromatogr. B 2006, 838 (1) 3-8
    • (2006) J. Chromatogr. B , vol.838 , Issue.1 , pp. 3-8
    • Wada, Y.1
  • 50
    • 0035827374 scopus 로고    scopus 로고
    • What can yeast tell us about N-linked glycosylation in the Golgi apparatus?
    • Munro, S. What can yeast tell us about N-linked glycosylation in the Golgi apparatus? FEBS Lett. 2001, 498 (2-3) 223-227
    • (2001) FEBS Lett. , vol.498 , Issue.23 , pp. 223-227
    • Munro, S.1
  • 51
    • 35548972537 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: A rapidly expanding disease family
    • Jaeken, J.; Matthijs, G. Congenital disorders of glycosylation: A rapidly expanding disease family Annu. Rev. Genomics Hum. Genet. 2007, 8, 261-278
    • (2007) Annu. Rev. Genomics Hum. Genet. , vol.8 , pp. 261-278
    • Jaeken, J.1    Matthijs, G.2
  • 52
    • 79961168515 scopus 로고    scopus 로고
    • The impact of mass spectrometry in the diagnosis of congenital disorders of glycosylation
    • Sturiale, L.; Barone, R.; Garozzo, D. The impact of mass spectrometry in the diagnosis of congenital disorders of glycosylation J. Inherit. Metab. Dis. 2011, 34 (4) 891-899
    • (2011) J. Inherit. Metab. Dis. , vol.34 , Issue.4 , pp. 891-899
    • Sturiale, L.1    Barone, R.2    Garozzo, D.3
  • 53
    • 0037590885 scopus 로고    scopus 로고
    • A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis
    • Thiel, C.; Schwarz, M.; Peng, J. H.; Grzmil, M.; Hasilik, M.; Braulke, T.; Kohlschutter, A.; von Figura, K.; Lehle, L.; Korner, C. A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis J. Biol. Chem. 2003, 278 (25) 22498-22505
    • (2003) J. Biol. Chem. , vol.278 , Issue.25 , pp. 22498-22505
    • Thiel, C.1    Schwarz, M.2    Peng, J.H.3    Grzmil, M.4    Hasilik, M.5    Braulke, T.6    Kohlschutter, A.7    Von Figura, K.8    Lehle, L.9    Korner, C.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.