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Volumn 951, Issue , 2013, Pages 229-244

Approaches for site mapping and quantification of O-linked glycopeptides

Author keywords

Antibody; HCD ETD; Isolation; Lectin; O GlcNAc; O Mannose; O linked glycosylation; Quantification; Site mapping

Indexed keywords

DITHIOTHREITOL; FORMIC ACID DERIVATIVE; GLYCOPEPTIDE; GLYCOPROTEIN; MANNOSE; N ACETYLGLUCOSAMINE; OXYGEN; PEROXYFORMIC ACID; PHOSPHATASE; THIOL DERIVATIVE; TRYPSIN;

EID: 84878662198     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-146-2_15     Document Type: Article
Times cited : (4)

References (15)
  • 1
    • 0030006293 scopus 로고    scopus 로고
    • O-linked protein glycosylation structure and function
    • Hounsell EF, Davies MJ, Renouf DV (1996) O-linked protein glycosylation structure and function. Glycoconj J 13:19-26
    • (1996) Glycoconj J , vol.13 , pp. 19-26
    • Hounsell, E.F.1    Davies, M.J.2    Renouf, D.V.3
  • 2
    • 0028901083 scopus 로고
    • Alterations in gastric mucin with malignant transformation: Novel pathway for mucin synthesis
    • Yamashita Y, Chung YS, Horie R, Kannagi R, Sowa M (1995) Alterations in gastric mucin with malignant transformation: novel pathway for mucin synthesis. J Natl Cancer Inst 87:441-446
    • (1995) J Natl Cancer Inst , vol.87 , pp. 441-446
    • Yamashita, Y.1    Chung, Y.S.2    Horie, R.3    Kannagi, R.4    Sowa, M.5
  • 3
    • 0027205366 scopus 로고
    • O-linked fucose and other post-translational modifications unique to EGF modules
    • Harris RJ, Spellman MW (1993) O-linked fucose and other post-translational modifications unique to EGF modules. Glycobiology 3:219-224
    • (1993) Glycobiology , vol.3 , pp. 219-224
    • Harris, R.J.1    Spellman, M.W.2
  • 4
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart GW (1997) Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu Rev Biochem 66:315-335
    • (1997) Annu Rev Biochem , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 5
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics A, Orlean P (1993) Glycoprotein biosynthesis in yeast. FASEB J 7:540-550
    • (1993) FASEB J , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 7
    • 34547929295 scopus 로고    scopus 로고
    • Diversity in cell surface sialic acid presentations: Implications for biology and disease
    • Varki NM, Varki A (2007) Diversity in cell surface sialic acid presentations: implications for biology and disease. Lab Invest 87:851-857
    • (2007) Lab Invest , vol.87 , pp. 851-857
    • Varki, N.M.1    Varki, A.2
  • 8
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • Drickamer K, Taylor ME (1998) Evolving views of protein glycosylation. Trends Biochem Sci 23:321-324
    • (1998) Trends Biochem Sci , vol.23 , pp. 321-324
    • Drickamer, K.1    Taylor, M.E.2
  • 9
    • 33748191656 scopus 로고    scopus 로고
    • Nothing in glycobiology makes sense, except in the light of evolution
    • Varki A (2006) Nothing in glycobiology makes sense, except in the light of evolution. Cell 126:841-845
    • (2006) Cell , vol.126 , pp. 841-845
    • Varki, A.1
  • 10
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine posttranslational modifications through stable isotope labeling with dithiothreitol
    • Vosseller K, Hansen KC, Chalkley RJ, Trinidad JC, Wells L, Hart GW, Burlingame AL (2005) Quantitative analysis of both protein expression and serine/threonine posttranslational modifications through stable isotope labeling with dithiothreitol. Proteomics 5:388-398
    • (2005) Proteomics , vol.5 , pp. 388-398
    • Vosseller, K.1    Hansen, K.C.2    Chalkley, R.J.3    Trinidad, J.C.4    Wells, L.5    Hart, G.W.6    Burlingame, A.L.7
  • 11
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L, Vosseller K, Cole RN, Cronshaw JM, Matunis MJ, Hart GW (2002) Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol Cell Proteomics 1:791-804
    • (2002) Mol Cell Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 12
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by betaelimination and tandem electrospray mass spectrometry
    • Greis KD, Hayes BK, Comer FI, Kirk M, Barnes S, Lowary TL, Hart GW (1996) Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by betaelimination and tandem electrospray mass spectrometry. Anal Biochem 234:38-49
    • (1996) Anal Biochem , vol.234 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4    Barnes, S.5    Lowary, T.L.6    Hart, G.W.7
  • 15
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff P, Fohlman J (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom 11:601
    • (1984) Biomed Mass Spectrom , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.