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Volumn 361, Issue 1, 2007, Pages 149-151

Analysis of variable N-glycosylation site occupancy in glycoproteins by liquid chromatography electrospray ionization mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY;

EID: 33845896286     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.11.005     Document Type: Article
Times cited : (11)

References (12)
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    • Butters T.D., Sparks L.M., Harlos K., Ikemizu S., Stuart D.I., Jones E.Y., and Davis S.J. Effects of N-butyldeoxynojirimycin and the Lec3.2.8.1 mutant phenotype on N-glycan processing in Chinese hamster ovary cells: application to glycoprotein crystallization. Protein Sci. 8 (1999) 1696-1701
    • (1999) Protein Sci. , vol.8 , pp. 1696-1701
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  • 2
    • 0030219388 scopus 로고    scopus 로고
    • Why mammalian cell surface proteins are glycoproteins
    • Gahmberg C.G., and Tolvanen M. Why mammalian cell surface proteins are glycoproteins. Trends Biochem. Sci. 21 (1996) 308-311
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 308-311
    • Gahmberg, C.G.1    Tolvanen, M.2
  • 5
    • 33749071408 scopus 로고    scopus 로고
    • Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding
    • Petrescu A.J., Wormald M.R., and Dwek R.A. Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding. Curr. Opin. Struct. Biol. 16 (2006) 1-8
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 1-8
    • Petrescu, A.J.1    Wormald, M.R.2    Dwek, R.A.3
  • 6
    • 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. 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 (2004) 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
  • 7
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    • Chromatographic interactions between proteins and sulfoalkylbetaine-based zwitterionic copolymers in fully aqueous low-salt buffers
    • Viklund C., Sjögren A., Irgum K., and Ness I. Chromatographic interactions between proteins and sulfoalkylbetaine-based zwitterionic copolymers in fully aqueous low-salt buffers. Anal. Chem. 73 (2001) 444-452
    • (2001) Anal. Chem. , vol.73 , pp. 444-452
    • Viklund, C.1    Sjögren, A.2    Irgum, K.3    Ness, I.4
  • 8
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R., and Brunak S. Prediction of glycosylation across the human proteome and the correlation to protein function. Pac. Symp. Biocomput. 7 (2002) 310-322
    • (2002) Pac. Symp. Biocomput. , vol.7 , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 10
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    • The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins
    • Krause E., Wenschuh H., and Jungblut P.R. The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins. Anal. Chem. 71 (1999) 4160-4165
    • (1999) Anal. Chem. , vol.71 , pp. 4160-4165
    • Krause, E.1    Wenschuh, H.2    Jungblut, P.R.3
  • 11
    • 0033783397 scopus 로고    scopus 로고
    • Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides
    • Brancia F.L., Oliver S.G., and Gaskell S.J. Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides. Rapid Commun. Mass Spectrum. 14 (2000) 2070-2073
    • (2000) Rapid Commun. Mass Spectrum. , vol.14 , pp. 2070-2073
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    • Increased sensitivity of tryptic peptide detection by MALDI-TOF mass spectrometry is achieved by conversion of lysine to homoarginine
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.