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Volumn 11, Issue 6, 2012, Pages

Mapping yeast N-glycosites with isotopically recoded glycans

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN DERIVATIVE; GLYCOPROTEIN; PROTEOME; N ACETYLGLUCOSAMINE; PEPTIDE FRAGMENT; POLYSACCHARIDE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84862320557     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.015339     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J. D., and Aebersold, R. (2001) A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19, 375-378
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 2
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 3
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., and Zhao, Y. (2009) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol. Cell. Proteomics 8, 215-225
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 215-225
    • Zhang, J.1    Sprung, R.2    Pei, J.3    Tan, X.4    Kim, S.5    Zhu, H.6    Liu, C.F.7    Grishin, N.V.8    Zhao, Y.9
  • 4
    • 79551500427 scopus 로고    scopus 로고
    • Targeted large-scale analysis of protein acetylation
    • Mischerikow, N., and Heck, A. J. (2011) Targeted large-scale analysis of protein acetylation. Proteomics 11, 571-589
    • (2011) Proteomics , vol.11 , pp. 571-589
    • Mischerikow, N.1    Heck, A.J.2
  • 5
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G., Paige, J. S., and Jaffrey, S. R. (2010) Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 28, 868-873
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 8
    • 76649126396 scopus 로고    scopus 로고
    • Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry
    • Wang, Z., Udeshi, N. D., O'Malley, M., Shabanowitz, J., Hunt, D. F., and Hart, G. W. (2010) Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry. Mol. Cell. Proteomics 9, 153-160
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 153-160
    • Wang, Z.1    Udeshi, N.D.2    O'Malley, M.3    Shabanowitz, J.4    Hunt, D.F.5    Hart, G.W.6
  • 9
    • 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., and Aebersold, R. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21, 660-666
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 10
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wiśniewski, J. R., and Mann, M. (2010) Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 11
    • 31844444062 scopus 로고    scopus 로고
    • A novel approach for identification and characterization of glycoproteins using a hybrid linear ion trap/FT-ICR mass spectrometer
    • Peterman, S. M., and Mulholland, J. J. (2006) A novel approach for identification and characterization of glycoproteins using a hybrid linear ion trap/FT-ICR mass spectrometer. J. Am. Soc. Mass Spectrom. 17, 168-179
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 168-179
    • Peterman, S.M.1    Mulholland, J.J.2
  • 12
    • 2942585313 scopus 로고    scopus 로고
    • Glycoform composition profiling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of flight-mass spectrometry
    • Pouria, S., Corran, P. H., Smith, A. C., Smith, H. W., Hendry, B. M., Challacombe, S. J., and Tarelli, E. (2004) Glycoform composition profiling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of flight-mass spectrometry. Anal. Biochem. 330, 257-263
    • (2004) Anal. Biochem. , vol.330 , pp. 257-263
    • Pouria, S.1    Corran, P.H.2    Smith, A.C.3    Smith, H.W.4    Hendry, B.M.5    Challacombe, S.J.6    Tarelli, E.7
  • 13
    • 62549123339 scopus 로고    scopus 로고
    • Glycomic approaches to study GlcNAcylation: Protein identification, site-mapping, and site-specific O-GlcNAc quantitation
    • Wang, Z., and Hart, G. W. (2008) Glycomic approaches to study GlcNAcylation: Protein identification, site-mapping, and site-specific O-GlcNAc quantitation. Clin. Proteomics 4, 5-13
    • (2008) Clin. Proteomics , vol.4 , pp. 5-13
    • Wang, Z.1    Hart, G.W.2
  • 14
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B., and Aebersold, R. (2006) Mass spectrometry and protein analysis. Science 312, 212-217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 15
    • 0032938979 scopus 로고    scopus 로고
    • Asparagine-linked glycosylation in the yeast Golgi
    • Dean, N. (1999) Asparagine-linked glycosylation in the yeast Golgi. Biochim. Biophys. Acta 1426, 309-322
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 309-322
    • Dean, N.1
  • 16
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerapana, E., and Imperiali, B. (2006) Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems. Glycobiology 16, 91R-101R
    • (2006) Glycobiology , vol.16
    • Weerapana, E.1    Imperiali, B.2
  • 17
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • Imperiali, B., and Rickert, K. W. (1995) Conformational implications of asparagine-linked glycosylation. Proc. Natl. Acad. Sci. U.S.A. 92, 97-101
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 97-101
    • Imperiali, B.1    Rickert, K.W.2
  • 18
    • 0032321747 scopus 로고    scopus 로고
    • Protein N-glycosylation: Molecular genetics and functional significance
    • Kukuruzinska, M. A., and Lennon, K. (1998) Protein N-glycosylation: Molecular genetics and functional significance. Crit. Rev. Oral Biol. Med. 9, 415-448
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 415-448
    • Kukuruzinska, M.A.1    Lennon, K.2
  • 19
    • 0021296628 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharides
    • Elbein, A. D. (1984) Inhibitors of the biosynthesis and processing of N-linked oligosaccharides. CRC Crit. Rev. Biochem. 16, 21-49
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 21-49
    • Elbein, A.D.1
  • 20
    • 0035089105 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Glycosylation defects in man and biological models for their study
    • Marquardt, T., and Freeze, H. (2001) Congenital disorders of glycosylation: Glycosylation defects in man and biological models for their study. Biol. Chem. 382, 161-177
    • (2001) Biol. Chem. , vol.382 , pp. 161-177
    • Marquardt, T.1    Freeze, H.2
  • 23
    • 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
    • Hägglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., and Roepstorff, P. (2004) 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. 3, 556-566
    • (2004) J. Proteome Res. , vol.3 , pp. 556-566
    • Hägglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 24
    • 79958132038 scopus 로고    scopus 로고
    • Large-scale assignment of N-glycosylation sites using complementary enzymatic deglycosylation
    • Zhang, W., Wang, H., Zhang, L., Yao, J., and Yang, P. (2011) Large-scale assignment of N-glycosylation sites using complementary enzymatic deglycosylation. Talanta 85, 499-505
    • (2011) Talanta , vol.85 , pp. 499-505
    • Zhang, W.1    Wang, H.2    Zhang, L.3    Yao, J.4    Yang, P.5
  • 25
    • 80051967494 scopus 로고    scopus 로고
    • Isotopic signature transfer and mass pattern prediction (IsoStamp): An enabling technique for chemically-directed proteomics
    • Palaniappan, K. K., Pitcher, A. A., Smart, B. P., Spiciarich, D. R., Iavarone, A. T., and Bertozzi, C. R. (2011) Isotopic signature transfer and mass pattern prediction (IsoStamp): An enabling technique for chemically-directed proteomics. ACS Chem Biol. 6, 829-336
    • (2011) ACS Chem Biol. , vol.6 , pp. 829-1336
    • Palaniappan, K.K.1    Pitcher, A.A.2    Smart, B.P.3    Spiciarich, D.R.4    Iavarone, A.T.5    Bertozzi, C.R.6
  • 26
    • 0034653646 scopus 로고    scopus 로고
    • Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching
    • Goodlett, D. R., Bruce, J. E., Anderson, G. A., Rist, B., Pasa-Tolic, L., Fiehn, O., Smith, R. D., and Aebersold, R. (2000) Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching. Anal. Chem. 72, 1112-1118
    • (2000) Anal. Chem. , vol.72 , pp. 1112-1118
    • Goodlett, D.R.1    Bruce, J.E.2    Anderson, G.A.3    Rist, B.4    Pasa-Tolic, L.5    Fiehn, O.6    Smith, R.D.7    Aebersold, R.8
  • 28
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wiśniewski, J. R., Zougman, A., Nagaraj, N., and Mann, M. (2009) Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wiśniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 29
    • 33748659203 scopus 로고    scopus 로고
    • Improved peak detection in mass spectrum by incorporating continuous wavelet transform-based pattern matching
    • Du, P., Kibbe, W. A., and Lin, S. M. (2006) Improved peak detection in mass spectrum by incorporating continuous wavelet transform-based pattern matching. Bioinformatics 22, 2059-2065
    • (2006) Bioinformatics , vol.22 , pp. 2059-2065
    • Du, P.1    Kibbe, W.A.2    Lin, S.M.3
  • 30
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng, J. K., Mccormack, A. L., and Yates, J. R. (1994) An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    Mccormack, A.L.2    Yates, J.R.3
  • 32
    • 0021679168 scopus 로고
    • Asparagine-linked glycosylation in Saccharomyces cerevisiae: Genetic analysis of an early step
    • Barnes, G., Hansen, W. J., Holcomb, C. L., and Rine, J. (1984) Asparagine-linked glycosylation in Saccharomyces cerevisiae: Genetic analysis of an early step. Mol. Cell. Biol. 4, 2381-2388
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2381-2388
    • Barnes, G.1    Hansen, W.J.2    Holcomb, C.L.3    Rine, J.4
  • 34
    • 0025670535 scopus 로고
    • Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation
    • Biemann, K. (1990) Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation. Methods Enzymol. 193, 455-479
    • (1990) Methods Enzymol. , vol.193 , pp. 455-479
    • Biemann, K.1
  • 35
    • 0001270151 scopus 로고
    • The determination of glycopeptides by liquid-chromatography mass-spectrometry with collision-induced dissociation
    • Conboy, J. J., and Henion, J. D. (1992) The determination of glycopeptides by liquid-chromatography mass-spectrometry with collision-induced dissociation. J. Am. Soc. Mass Spectrom. 3, 804-814
    • (1992) J. Am. Soc. Mass Spectrom. , vol.3 , pp. 804-814
    • Conboy, J.J.1    Henion, J.D.2
  • 36
    • 79953719716 scopus 로고    scopus 로고
    • More than 100,000 detectable peptide species elute in single shotgun proteomics runs but the majority is inaccessible to data-dependent LC-MS/MS
    • Michalski, A., Cox, J., and Mann, M. (2011) More than 100,000 detectable peptide species elute in single shotgun proteomics runs but the majority is inaccessible to data-dependent LC-MS/MS. J. Proteome Res. 10, 1785-1793
    • (2011) J. Proteome Res. , vol.10 , pp. 1785-1793
    • Michalski, A.1    Cox, J.2    Mann, M.3
  • 37
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • (2010) The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 38, D142-D148
    • (2010) Nucleic Acids Res. , vol.38
  • 39
    • 70349333832 scopus 로고    scopus 로고
    • Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes
    • Kung, L. A., Tao, S. C., Qian, J., Smith, M. G., Snyder, M., and Zhu, H. (2009) Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes. Mol. Syst. Biol. 5, 308
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 308
    • Kung, L.A.1    Tao, S.C.2    Qian, J.3    Smith, M.G.4    Snyder, M.5    Zhu, H.6
  • 40
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 42
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y., and von Heijne, G. (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng. 3, 433-442
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 44
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 45
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • Nesvizhskii, A. I., and Aebersold, R. (2005) Interpretation of shotgun proteomic data: The protein inference problem. Mol. Cell. Proteomics 4, 1419-1440
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 46
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold, R., and Goodlett, D. R. (2001) Mass spectrometry in proteomics. Chem. Rev. 101, 269-295
    • (2001) Chem. Rev. , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 47
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Käll, L., Storey, J. D., MacCoss, M. J., and Noble, W. S. (2008) Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J. Proteome Res. 7, 29-34
    • (2008) J. Proteome Res. , vol.7 , pp. 29-34
    • Käll, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 48
    • 65249097774 scopus 로고    scopus 로고
    • Statistical calibration of the SEQUEST XCorr function
    • Klammer, A. A., Park, C. Y., and Noble, W. S. (2009) Statistical calibration of the SEQUEST XCorr function. J. Proteome Res. 8, 2106-2113
    • (2009) J. Proteome Res. , vol.8 , pp. 2106-2113
    • Klammer, A.A.1    Park, C.Y.2    Noble, W.S.3


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