메뉴 건너뛰기




Volumn 30, Issue 2, 2013, Pages 85-87

Glycomic profiling of glycoproteins

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; EPITOPE; GLYCAN; GLYCOPROTEIN; HYALURONIC ACID; IMMUNOGLOBULIN FC FRAGMENT; MONOCLONAL ANTIBODY; PROTEOME;

EID: 84878857730     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-012-9467-1     Document Type: Review
Times cited : (2)

References (16)
  • 1
    • 77953555196 scopus 로고    scopus 로고
    • Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: A potential methodology for cancer-biomarker discovery
    • 20491449 10.1021/ac100131e 1:CAS:528:DC%2BC3cXmsVCrsbw%3D
    • Alley Jr.; W.R.; Madera, M.; Mechref, Y.; Novotny, M.V.: Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: a potential methodology for cancer-biomarker discovery. Anal. Chem. 82, 5095-5106 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 5095-5106
    • Alley, Jr.W.R.1    Madera, M.2    Mechref, Y.3    Novotny, M.V.4
  • 3
    • 53249151506 scopus 로고    scopus 로고
    • Microbial recognition of human cell surface glycoconjugates
    • 18809496 10.1016/j.sbi.2008.08.001 1:CAS:528:DC%2BD1cXht1egu7rM
    • Imberty, A.; Varrot, A.: Microbial recognition of human cell surface glycoconjugates. Curr. Opin. Struct. Biol. 18, 567-576 (2008)
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 567-576
    • Imberty, A.1    Varrot, A.2
  • 4
    • 79956257405 scopus 로고    scopus 로고
    • Secretor genotype (FUT2 gene) is strongly associated with the composition of Bifidobacteria in the human intestine
    • 21625510 10.1371/journal.pone.0020113 1:CAS:528:DC%2BC3MXms1KhurY%3D
    • Wacklin, P.; Makivuokko, H.; Alakulppi, N.; Nikkila, J.; Tenkanen, H.; Rabina, J.; Partanen, J.; Aranko, K.; Matto, J.: Secretor genotype (FUT2 gene) is strongly associated with the composition of Bifidobacteria in the human intestine. PLoS One 6, e20113 (2011)
    • (2011) PLoS One , vol.6 , pp. 20113
    • Wacklin, P.1    Makivuokko, H.2    Alakulppi, N.3    Nikkila, J.4    Tenkanen, H.5    Rabina, J.6    Partanen, J.7    Aranko, K.8    Matto, J.9
  • 5
    • 77956690413 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2010
    • 20829826 10.1038/nbt0910-917 1:CAS:528:DC%2BC3cXhtFegsbnO
    • Walsh, G.: Biopharmaceutical benchmarks 2010. Nat. Biotechnol. 28, 917-924 (2010)
    • (2010) Nat. Biotechnol. , vol.28 , pp. 917-924
    • Walsh, G.1
  • 6
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • 17029568 10.1146/annurev.immunol.25.022106.141702 1:CAS:528: DC%2BD2sXltlagurc%3D
    • Arnold, J.N.; Wormald, M.R.; Sim, R.B.; Rudd, P.M.; Dwek, R.A.: The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21-50 (2007)
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 7
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • 18606225 10.1016/j.coi.2008.06.007 1:CAS:528:DC%2BD1cXpslSltL0%3D
    • Raju, T.S.: Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr. Opin. Immunol. 20, 471-478 (2008)
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 8
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • 16888140 10.1126/science.1129594 1:CAS:528:DC%2BD28Xnsl2hsbY%3D
    • Kaneko, Y.; Nimmerjahn, F.; Ravetch, J.V.: Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313, 670-673 (2006)
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 9
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • 19247305 10.1038/nrd2804 1:CAS:528:DC%2BD1MXisVShtb0%3D
    • Jefferis, R.: Glycosylation as a strategy to improve antibody-based therapeutics. Nat. Rev. Drug Discov. 8, 226-234 (2009)
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 11
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
    • 20657583 10.1038/nbt.1651 1:CAS:528:DC%2BC3cXpt1art7c%3D
    • Ghaderi, D.; Taylor, R.E.; Padler-Karavani, V.; Diaz, S.; Varki, A.: Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat. Biotechnol. 28, 863-867 (2010)
    • (2010) Nat. Biotechnol. , vol.28 , pp. 863-867
    • Ghaderi, D.1    Taylor, R.E.2    Padler-Karavani, V.3    Diaz, S.4    Varki, A.5
  • 12
    • 84868553080 scopus 로고    scopus 로고
    • High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples
    • 23026777 10.1016/j.ab.2012.09.032 1:CAS:528:DC%2BC38XhslSmtbnE
    • Reusch, D.; Haberger, M.; Selman, M.H.; Bulau, P.; Deelder, A.M.; Wuhrer, M.; Engler, N.: High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples. Anal. Biochem. 432, 82-89 (2013)
    • (2013) Anal. Biochem. , vol.432 , pp. 82-89
    • Reusch, D.1    Haberger, M.2    Selman, M.H.3    Bulau, P.4    Deelder, A.M.5    Wuhrer, M.6    Engler, N.7
  • 14
    • 61849098877 scopus 로고    scopus 로고
    • Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens
    • 18942870 10.1021/pr800651j 1:CAS:528:DC%2BD1cXht1OlsbzM
    • Wuhrer, M.; Porcelijn, L.; Kapur, R.; Koeleman, C.A.; Deelder, A.; de Haas, M.; Vidarsson, G.: Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens. J. Proteome Res. 8, 450-456 (2009)
    • (2009) J. Proteome Res. , vol.8 , pp. 450-456
    • Wuhrer, M.1    Porcelijn, L.2    Kapur, R.3    Koeleman, C.A.4    Deelder, A.5    De Haas, M.6    Vidarsson, G.7
  • 15
    • 77956297334 scopus 로고    scopus 로고
    • Large-scale glycomics for discovering cancer-associated N-glycans by integrating glycoblotting and mass spectrometry
    • 20816476 10.1016/S0076-6879(10)78004-6 1:CAS:528:DC%2BC3cXhsVOju73F
    • Amano, M.; Nishimura, S.: Large-scale glycomics for discovering cancer-associated N-glycans by integrating glycoblotting and mass spectrometry. Methods Enzymol. 478, 109-125 (2010)
    • (2010) Methods Enzymol. , vol.478 , pp. 109-125
    • Amano, M.1    Nishimura, S.2
  • 16
    • 78650370233 scopus 로고    scopus 로고
    • Glycoblotting-assisted O-glycomics: Ammonium carbamate allows for highly efficient o-glycan release from glycoproteins
    • 21077635 10.1021/ac101599p 1:CAS:528:DC%2BC3cXhsVaju7zF
    • Miura, Y.; Kato, K.; Takegawa, Y.; Kurogochi, M.; Furukawa, J.; Shinohara, Y.; Nagahori, N.; Amano, M.; Hinou, H.; Nishimura, S.: Glycoblotting-assisted O-glycomics: ammonium carbamate allows for highly efficient o-glycan release from glycoproteins. Anal. Chem. 82, 10021-10029 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 10021-10029
    • Miura, Y.1    Kato, K.2    Takegawa, Y.3    Kurogochi, M.4    Furukawa, J.5    Shinohara, Y.6    Nagahori, N.7    Amano, M.8    Hinou, H.9    Nishimura, S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.