메뉴 건너뛰기




Volumn 13, Issue 5, 2016, Pages 523-534

High-throughput analysis of immunoglobulin G glycosylation

Author keywords

Capillary electrophoresis; glycan biomarker; high throughput; IgG; mass spectrometry; N glycosylation; ultra performance liquid chromatography

Indexed keywords

GLYCAN; GLYCOPEPTIDE; GLYCOPROTEIN; IMMUNOGLOBULIN G; TRYPSIN;

EID: 84964475889     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1080/14789450.2016.1174584     Document Type: Review
Times cited : (33)

References (129)
  • 1
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • K.Ohtsubo, J.D.Marth Glycosylation in cellular mechanisms of health and disease. Cell. 2006;126:855–867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 2
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • G.W.Hart, M.P.Housley, C.Slawson. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature. 2007;446:1017–1022.
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 3
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: diversity, synthesis and function
    • K.W.Moremen, M.Tiemeyer, A.V.Nairn. Vertebrate protein glycosylation: diversity, synthesis and function. Nat Rev Mol Cell Biol. 2012;13:448–462.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 4
    • 31744447070 scopus 로고    scopus 로고
    • Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain
    • T.S.Raju, B.J.Scallon. Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain. Biochem Biophys Res Commun. 2006;341:797–803.
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 797-803
    • Raju, T.S.1    Scallon, B.J.2
  • 5
    • 68249094372 scopus 로고    scopus 로고
    • Site-selective chemical protein glycosylation protects from autolysis and proteolytic degradation
    • D.Russell, N.J.Oldham, B.G.Davis. Site-selective chemical protein glycosylation protects from autolysis and proteolytic degradation. Carbohydr Res. 2009;344:1508–1514.
    • (2009) Carbohydr Res , vol.344 , pp. 1508-1514
    • Russell, D.1    Oldham, N.J.2    Davis, B.G.3
  • 6
    • 84878758122 scopus 로고    scopus 로고
    • Engineering a monomeric Fc domain modality by N-glycosylation for the half-life extension of biotherapeutics
    • T.Ishino, M.Wang, L.Mosyak, et al. Engineering a monomeric Fc domain modality by N-glycosylation for the half-life extension of biotherapeutics. J Biol Chem. 2013;288:16529–16537.
    • (2013) J Biol Chem , vol.288 , pp. 16529-16537
    • Ishino, T.1    Wang, M.2    Mosyak, L.3
  • 7
    • 84862905517 scopus 로고    scopus 로고
    • Diseases of glycosylation beyond classical congenital disorders of glycosylation
    • T.Hennet. Diseases of glycosylation beyond classical congenital disorders of glycosylation. Biochim Biophys Acta - Gen Subj. 2012;1820:1306–1317.
    • (2012) Biochim Biophys Acta - Gen Subj , vol.1820 , pp. 1306-1317
    • Hennet, T.1
  • 8
    • 84930820543 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: a concise chart of glycocalyx dysfunction
    • T.Hennet, J.Cabalzar. Congenital disorders of glycosylation: a concise chart of glycocalyx dysfunction. Trends Biochem Sci. 2015;40:377–384.
    • (2015) Trends Biochem Sci , vol.40 , pp. 377-384
    • Hennet, T.1    Cabalzar, J.2
  • 9
    • 84904111497 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: new defects and still counting
    • K.Scott, T.Gadomski, T.Kozicz, et al. Congenital disorders of glycosylation: new defects and still counting. J Inherit Metab Dis. 2014;37:609–617.
    • (2014) J Inherit Metab Dis , vol.37 , pp. 609-617
    • Scott, K.1    Gadomski, T.2    Kozicz, T.3
  • 10
    • 84898914552 scopus 로고    scopus 로고
    • Impact of autoantibody glycosylation in autoimmune diseases
    • R.Goulabchand, T.Vincent, F.Batteux, et al. Impact of autoantibody glycosylation in autoimmune diseases. Autoimmun Rev. 2014;13:742–750.
    • (2014) Autoimmun Rev , vol.13 , pp. 742-750
    • Goulabchand, R.1    Vincent, T.2    Batteux, F.3
  • 11
    • 84946023390 scopus 로고    scopus 로고
    • Association of systemic lupus erythematosus with decreased immunosuppressive potential of the IgG glycome
    • F.Vučkovïć, J.Krištïć, I.Gudelj, et al. Association of systemic lupus erythematosus with decreased immunosuppressive potential of the IgG glycome. Arthritis Rheumatol. 2015;67:2978–2989.
    • (2015) Arthritis Rheumatol , vol.67 , pp. 2978-2989
    • Vučkovïć, F.1    Krištïć, J.2    Gudelj, I.3
  • 12
    • 58149391280 scopus 로고    scopus 로고
    • Glycosylation of serum proteins in inflammatory diseases
    • O.Gornik, G.Lauc. Glycosylation of serum proteins in inflammatory diseases. Dis Markers. 2008;25:267–278.
    • (2008) Dis Markers , vol.25 , pp. 267-278
    • Gornik, O.1    Lauc, G.2
  • 13
    • 84929900183 scopus 로고    scopus 로고
    • Inflammatory bowel disease associates with proinflammatory potential of the immunoglobulin G glycome
    • I.Trbojević Akmačić, N.T.Ventham, E.Theodoratou, et al. Inflammatory bowel disease associates with proinflammatory potential of the immunoglobulin G glycome. Inflamm Bowel Dis. 2015;21:1237–1247.
    • (2015) Inflamm Bowel Dis , vol.21 , pp. 1237-1247
    • Trbojević Akmačić, I.1    Ventham, N.T.2    Theodoratou, E.3
  • 14
    • 84898022102 scopus 로고    scopus 로고
    • Altered tumor-cell glycosylation promotes metastasis
    • I.Häuselmann, L.Borsig. Altered tumor-cell glycosylation promotes metastasis. Front Oncol. 2014;4:28.
    • (2014) Front Oncol , vol.4 , pp. 28
    • Häuselmann, I.1    Borsig, L.2
  • 16
    • 84863570384 scopus 로고    scopus 로고
    • Quantitative glycan profiling of normal human plasma derived immunoglobulin and its fragments Fab and Fc
    • K.R.Anumula. Quantitative glycan profiling of normal human plasma derived immunoglobulin and its fragments Fab and Fc. J Immunol Methods. 2012;382:167–176.
    • (2012) J Immunol Methods , vol.382 , pp. 167-176
    • Anumula, K.R.1
  • 17
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • J.N.Arnold, M.R.Wormald, R.B.Sim, et al. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol. 2007;25:21–50.
    • (2007) Annu Rev Immunol , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3
  • 18
    • 84922360962 scopus 로고    scopus 로고
    • Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding
    • J.Lu, J.Chu, Z.Zou, et al. Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding. Proc Natl Acad Sci. 2015;112:833–838.
    • (2015) Proc Natl Acad Sci , vol.112 , pp. 833-838
    • Lu, J.1    Chu, J.2    Zou, Z.3
  • 19
    • 84947032537 scopus 로고    scopus 로고
    • The structural role of antibody N-glycosylation in receptor interactions
    • G.P.Subedi, A.W.Barb. The structural role of antibody N-glycosylation in receptor interactions. Structure. 2015;23:1573–1583.
    • (2015) Structure , vol.23 , pp. 1573-1583
    • Subedi, G.P.1    Barb, A.W.2
  • 20
    • 84866104409 scopus 로고    scopus 로고
    • The role of sialic acid as a modulator of the anti-inflammatory activity of IgG
    • S.Böhm, I.Schwab, A.Lux, et al. The role of sialic acid as a modulator of the anti-inflammatory activity of IgG. Semin Immunopathol. 2012;34:443–453.
    • (2012) Semin Immunopathol , vol.34 , pp. 443-453
    • Böhm, S.1    Schwab, I.2    Lux, A.3
  • 21
    • 80054016444 scopus 로고    scopus 로고
    • High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations
    • M.Pucic, A.Knezevic, J.Vidic, et al. High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations. Mol Cell Proteomics. 2011;10:M111.010090–M111.010090.
    • (2011) Mol Cell Proteomics , vol.10
    • Pucic, M.1    Knezevic, A.2    Vidic, J.3
  • 22
    • 84861410115 scopus 로고    scopus 로고
    • Changes in plasma and IgG N-glycome during childhood and adolescence
    • M.Pučić, A.Mužinić, M.Novokmet, et al. Changes in plasma and IgG N-glycome during childhood and adolescence. Glycobiology. 2012;22:975–982.
    • (2012) Glycobiology , vol.22 , pp. 975-982
    • Pučić, M.1    Mužinić, A.2    Novokmet, M.3
  • 23
    • 84902271562 scopus 로고    scopus 로고
    • Glycans are a novel biomarker of chronological and biological ages
    • J.Krištić, F.Vučković, C.Menni, et al. Glycans are a novel biomarker of chronological and biological ages. J Gerontol Ser Biol Sci Med Sci. 2014;69:779–789.
    • (2014) J Gerontol Ser Biol Sci Med Sci , vol.69 , pp. 779-789
    • Krištić, J.1    Vučković, F.2    Menni, C.3
  • 24
    • 84873404470 scopus 로고    scopus 로고
    • High-throughput IgG Fc N - glycosylation pro fi ling by mass spectrometry of glycopeptides
    • M.Baković, M.H.J.Selman, M.Ho, et al. High-throughput IgG Fc N - glycosylation pro fi ling by mass spectrometry of glycopeptides. J Proteome Res. 2013;12:821–831.
    • (2013) J Proteome Res , vol.12 , pp. 821-831
    • Baković, M.1    Selman, M.H.J.2    Ho, M.3
  • 25
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose
    • C.Ferrara, S.Grau, C.Jäger, et al. Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose. Proc Natl Acad Sci U S A. 2011;108:12669–12674.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12669-12674
    • Ferrara, C.1    Grau, S.2    Jäger, C.3
  • 26
    • 34247215987 scopus 로고    scopus 로고
    • Enhanced binding affinity for FcγRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity
    • K.Masuda, T.Kubota, E.Kaneko, et al. Enhanced binding affinity for FcγRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity. Mol Immunol. 2007;44:3122–3131.
    • (2007) Mol Immunol , vol.44 , pp. 3122-3131
    • Masuda, K.1    Kubota, T.2    Kaneko, E.3
  • 27
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Y.Kaneko, F.Nimmerjahn, J.V.Ravetch. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006;313:670–673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 28
    • 84875410765 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy: how does IgG modulate the immune system?
    • •• Extensive review of molecular and cellular pathways that are involved with intravenous immunoglobulin activity and its use in treatment of autoimmune diseases.
    • I.Schwab, F.Nimmerjahn. Intravenous immunoglobulin therapy: how does IgG modulate the immune system? Nat Rev Immunol. 2013;13:176–189.•• Extensive review of molecular and cellular pathways that are involved with intravenous immunoglobulin activity and its use in treatment of autoimmune diseases.
    • (2013) Nat Rev Immunol , vol.13 , pp. 176-189
    • Schwab, I.1    Nimmerjahn, F.2
  • 29
    • 84875749746 scopus 로고    scopus 로고
    • Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain
    • X.Yu, S.Vasiljevic, D.A.Mitchell, et al Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain. J Mol Biol. 2013;425:1253–1258.
    • (2013) J Mol Biol , vol.425 , pp. 1253-1258
    • Yu, X.1    Vasiljevic, S.2    Mitchell, D.A.3
  • 30
    • 84891921496 scopus 로고    scopus 로고
    • Treatment response in Kawasaki disease is associated with sialylation levels of endogenous but not therapeutic intravenous immunoglobulin G
    • S.Ogata, C.Shimizu, A.Franco, et al. Treatment response in Kawasaki disease is associated with sialylation levels of endogenous but not therapeutic intravenous immunoglobulin G. PLoS One. 2013;8:e81448.
    • (2013) PLoS One , vol.8 , pp. e81448
    • Ogata, S.1    Shimizu, C.2    Franco, A.3
  • 31
    • 80052225251 scopus 로고    scopus 로고
    • Genome-wide association study identifies two loci strongly affecting transferrin glycosylation
    • Z.Kutalik, B.Benyamin, S.Bergmann, et al. Genome-wide association study identifies two loci strongly affecting transferrin glycosylation. Hum Mol Genet. 2011;20:3710–3717.
    • (2011) Hum Mol Genet , vol.20 , pp. 3710-3717
    • Kutalik, Z.1    Benyamin, B.2    Bergmann, S.3
  • 32
    • 81855226434 scopus 로고    scopus 로고
    • Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults
    • J.E.Huffman, A.Knežević, V.Vitart, et al. Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults. Hum Mol Genet. 2011;20:5000–5011.
    • (2011) Hum Mol Genet , vol.20 , pp. 5000-5011
    • Huffman, J.E.1    Knežević, A.2    Vitart, V.3
  • 33
    • 84873495247 scopus 로고    scopus 로고
    • Loci associated with N-glycosylation of human immunoglobulin G Show pleiotropy with autoimmune diseases and haematological cancers
    • G.Lauc, J.E.Huffman, M.Pučić, et al. Loci associated with N-glycosylation of human immunoglobulin G Show pleiotropy with autoimmune diseases and haematological cancers. PLoS Genet. 2013;9(1):e1003225.
    • (2013) PLoS Genet , vol.91:e1003225
    • Lauc, G.1    Huffman, J.E.2    Pučić, M.3
  • 34
    • 84873743426 scopus 로고    scopus 로고
    • Aberrant PSA glycosylation–a sweet predictor of prostate cancer
    • S.Gilgunn, P.J.Conroy, R.Saldova, et al. Aberrant PSA glycosylation–a sweet predictor of prostate cancer. Nat Rev Urol. 2013;10:99–107.
    • (2013) Nat Rev Urol , vol.10 , pp. 99-107
    • Gilgunn, S.1    Conroy, P.J.2    Saldova, R.3
  • 35
    • 84901942411 scopus 로고    scopus 로고
    • Comparative performance of four methods for high-throughput glycosylation analysis of immunoglobulin G in genetic and epidemiological research
    • • Paper provides good comparison of methods used for the study of IgG N-glycans.
    • J.E.Huffman, M.Pučić-Baković, L.Klarić, et al. Comparative performance of four methods for high-throughput glycosylation analysis of immunoglobulin G in genetic and epidemiological research. Mol Cell Proteomics. 2014;13:1598–1610.• Paper provides good comparison of methods used for the study of IgG N-glycans.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1598-1610
    • Huffman, J.E.1    Pučić-Baković, M.2    Klarić, L.3
  • 36
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • W.Morelle, J.-C.Michalski. Analysis of protein glycosylation by mass spectrometry. Nat Protoc. 2007;2:1585–1602.
    • (2007) Nat Protoc , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.-C.2
  • 37
    • 83755224361 scopus 로고    scopus 로고
    • Enhanced sensitivity of LC-MS analysis of permethylated N-glycans through online purification
    • J.L.Desantos-Garcia, S.I.Khalil, A.Hussein, et al. Enhanced sensitivity of LC-MS analysis of permethylated N-glycans through online purification. Electrophoresis. 2011;32:3516–3525.
    • (2011) Electrophoresis , vol.32 , pp. 3516-3525
    • Desantos-Garcia, J.L.1    Khalil, S.I.2    Hussein, A.3
  • 38
    • 78650351800 scopus 로고    scopus 로고
    • Profiling of serum N -glycans for fast and efficient glycosylation
    • J.Bones, S.Mittermayr, N.O.Donoghue, et al. Profiling of serum N -glycans for fast and efficient glycosylation. Anal Chem. 2010;82:10208–10215.
    • (2010) Anal Chem , vol.82 , pp. 10208-10215
    • Bones, J.1    Mittermayr, S.2    Donoghue, N.O.3
  • 40
  • 41
    • 77950691184 scopus 로고    scopus 로고
    • Chemical and enzymatic N-glycan release comparison for N-glycan profiling of monoclonal antibodies expressed in plants
    • A.Triguero, G.Cabrera, L.Royle, et al. Chemical and enzymatic N-glycan release comparison for N-glycan profiling of monoclonal antibodies expressed in plants. Anal Biochem. 2010;400:173–183.
    • (2010) Anal Biochem , vol.400 , pp. 173-183
    • Triguero, A.1    Cabrera, G.2    Royle, L.3
  • 42
    • 0028070703 scopus 로고
    • Microbial endoglycosidases for analyses of oligosaccharide chains
    • K.Yamamoto. Microbial endoglycosidases for analyses of oligosaccharide chains. J Biochem. 1994;116:229–235.
    • (1994) J Biochem , vol.116 , pp. 229-235
    • Yamamoto, K.1
  • 43
    • 79961184231 scopus 로고    scopus 로고
    • Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry
    • E.P.Go, G.Hewawasam, H.-X.Liao, et al. Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol. 2011;85:8270–8284.
    • (2011) J Virol , vol.85 , pp. 8270-8284
    • Go, E.P.1    Hewawasam, G.2    Liao, H.-X.3
  • 44
    • 84862089456 scopus 로고    scopus 로고
    • An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling
    • J.J.Goodfellow, K.Baruah, K.Yamamoto, et al. An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling. J Am Chem Soc. 2012;134:8030–8033.
    • (2012) J Am Chem Soc , vol.134 , pp. 8030-8033
    • Goodfellow, J.J.1    Baruah, K.2    Yamamoto, K.3
  • 45
    • 84869398333 scopus 로고    scopus 로고
    • Fast and efficient online release of N-glycans from glycoproteins facilitating liquid chromatography–tandem mass spectrometry glycomic profiling
    • Y.Jmeian, L.A.Hammad, Y.Mechref. Fast and efficient online release of N-glycans from glycoproteins facilitating liquid chromatography–tandem mass spectrometry glycomic profiling. Anal Chem. 2012;84:8790–8796.
    • (2012) Anal Chem , vol.84 , pp. 8790-8796
    • Jmeian, Y.1    Hammad, L.A.2    Mechref, Y.3
  • 46
    • 84888432354 scopus 로고    scopus 로고
    • Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis
    • J.Krenkova, A.Szekrenyes, Z.Keresztessy, et al. Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis. J Chromatogr A. 2013;1322:54–61.
    • (2013) J Chromatogr A , vol.1322 , pp. 54-61
    • Krenkova, J.1    Szekrenyes, A.2    Keresztessy, Z.3
  • 47
    • 84861644702 scopus 로고    scopus 로고
    • PNGase F catalyzes de-N-glycosylation in a domestic microwave
    • H.Zhou, A.C.Briscoe, J.W.Froehlich, et al. PNGase F catalyzes de-N-glycosylation in a domestic microwave. Anal Biochem. 2012;427:33–35.
    • (2012) Anal Biochem , vol.427 , pp. 33-35
    • Zhou, H.1    Briscoe, A.C.2    Froehlich, J.W.3
  • 48
    • 77949778053 scopus 로고    scopus 로고
    • Rapid release of N-linked glycans from glycoproteins by pressure-cycling technology
    • Z.Szabo, A.Guttman, B.L.Karger. Rapid release of N-linked glycans from glycoproteins by pressure-cycling technology. Anal Chem. 2010;82:2588–2593.
    • (2010) Anal Chem , vol.82 , pp. 2588-2593
    • Szabo, Z.1    Guttman, A.2    Karger, B.L.3
  • 49
    • 84857948012 scopus 로고    scopus 로고
    • Detection of N-glycans on small amounts of glycoproteins in tissue samples and sodium dodecyl sulfate-polyacrylamide gels
    • T.Yoshimura, G.Yamada, M.Narumi, et al. Detection of N-glycans on small amounts of glycoproteins in tissue samples and sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem. 2012;423:253–260.
    • (2012) Anal Biochem , vol.423 , pp. 253-260
    • Yoshimura, T.1    Yamada, G.2    Narumi, M.3
  • 50
    • 41449087577 scopus 로고    scopus 로고
    • HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software
    • L.Royle, M.P.Campbell, C.M.Radcliffe, et al. HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software. Anal Biochem. 2008;376:1–12.
    • (2008) Anal Biochem , vol.376 , pp. 1-12
    • Royle, L.1    Campbell, M.P.2    Radcliffe, C.M.3
  • 51
    • 84858069690 scopus 로고    scopus 로고
    • Development and qualification of an antibody rapid deglycosylation method
    • K.S.Cook, K.Bullock, T.Sullivan. Development and qualification of an antibody rapid deglycosylation method. Biologicals. 2012;40:109–117.
    • (2012) Biologicals , vol.40 , pp. 109-117
    • Cook, K.S.1    Bullock, K.2    Sullivan, T.3
  • 52
    • 0031820069 scopus 로고    scopus 로고
    • High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid
    • K.R.Anumula, S.T.Dhume. High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid. Glycobiology. 1998;8:685–694.
    • (1998) Glycobiology , vol.8 , pp. 685-694
    • Anumula, K.R.1    Dhume, S.T.2
  • 53
    • 49449095723 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography-based high-throughput sample preparation method for N-glycan analysis from total human plasma glycoproteins
    • L.R.Ruhaak, C.Huhn, W.-J.Waterreus, et al. Hydrophilic interaction chromatography-based high-throughput sample preparation method for N-glycan analysis from total human plasma glycoproteins. Anal Chem. 2008;80:6119–6126.
    • (2008) Anal Chem , vol.80 , pp. 6119-6126
    • Ruhaak, L.R.1    Huhn, C.2    Waterreus, W.-J.3
  • 54
    • 41949083780 scopus 로고    scopus 로고
    • Two-dimensional hydrophilic interaction chromatography coupling anion-exchange and hydrophilic interaction columns for separation of 2-pyridylamino derivatives of neutral and sialylated N-glycans
    • K.Deguchi, T.Keira, K.Yamada, et al. Two-dimensional hydrophilic interaction chromatography coupling anion-exchange and hydrophilic interaction columns for separation of 2-pyridylamino derivatives of neutral and sialylated N-glycans. J Chromatogr A. 2008;1189:169–174.
    • (2008) J Chromatogr A , vol.1189 , pp. 169-174
    • Deguchi, K.1    Keira, T.2    Yamada, K.3
  • 55
    • 0034475474 scopus 로고    scopus 로고
    • Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatized at the reducing terminus
    • D.J.Harvey. Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatized at the reducing terminus. J Am Soc Mass Spectrom. 2000;11:900–915.
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 900-915
    • Harvey, D.J.1
  • 56
    • 13444304049 scopus 로고    scopus 로고
    • Separation of 2-aminobenzoic acid-derivatized glycosaminoglycans and asparagine-linked glycans by capillary electrophoresis
    • K.Sato, K.Sato, A.Okubo, et al. Separation of 2-aminobenzoic acid-derivatized glycosaminoglycans and asparagine-linked glycans by capillary electrophoresis. Anal Sci. 2005;21:21–24.
    • (2005) Anal Sci , vol.21 , pp. 21-24
    • Sato, K.1    Sato, K.2    Okubo, A.3
  • 57
    • 33749990332 scopus 로고    scopus 로고
    • Capillary electrophoresis with laser-induced fluorescence detection for detailed studies on N-linked oligosaccharide profile of therapeutic recombinant monoclonal antibodies
    • S.Kamoda, R.Ishikawa, K.Kakehi. Capillary electrophoresis with laser-induced fluorescence detection for detailed studies on N-linked oligosaccharide profile of therapeutic recombinant monoclonal antibodies. J Chromatogr A. 2006;1133:332–339.
    • (2006) J Chromatogr A , vol.1133 , pp. 332-339
    • Kamoda, S.1    Ishikawa, R.2    Kakehi, K.3
  • 58
    • 77955155580 scopus 로고    scopus 로고
    • High throughput quantification of N-glycans using one-pot sialic acid modification and matrix assisted laser desorption ionization time-of-flight mass spectrometry
    • G.-C.Gil, B.Iliff, R.Cerny, et al. High throughput quantification of N-glycans using one-pot sialic acid modification and matrix assisted laser desorption ionization time-of-flight mass spectrometry. Anal Chem. 2010;82:6613–6620.
    • (2010) Anal Chem , vol.82 , pp. 6613-6620
    • Gil, G.-C.1    Iliff, B.2    Cerny, R.3
  • 59
    • 84864378010 scopus 로고    scopus 로고
    • N-glycosylation of colorectal cancer tissues: a liquid chromatography and mass spectrometry-based investigation
    • C.I.A.Balog, K.Stavenhagen, W.L.J.Fung, et al. N-glycosylation of colorectal cancer tissues: a liquid chromatography and mass spectrometry-based investigation. Mol Cell Proteomics. 2012;11:571–585.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 571-585
    • Balog, C.I.A.1    Stavenhagen, K.2    Fung, W.L.J.3
  • 60
    • 76849086981 scopus 로고    scopus 로고
    • Mass spectrometric-based stable isotopic 2-aminobenzoic acid glycan mapping for rapid glycan screening of biotherapeutics
    • J.M.Prien, B.D.Prater, Q.Qin, et al. Mass spectrometric-based stable isotopic 2-aminobenzoic acid glycan mapping for rapid glycan screening of biotherapeutics. Anal Chem. 2010;82:1498–1508.
    • (2010) Anal Chem , vol.82 , pp. 1498-1508
    • Prien, J.M.1    Prater, B.D.2    Qin, Q.3
  • 61
    • 32644474401 scopus 로고    scopus 로고
    • Advances in fluorescence derivatization methods for high-performance liquid chromatographic analysis of glycoprotein carbohydrates
    • K.R.Anumula. Advances in fluorescence derivatization methods for high-performance liquid chromatographic analysis of glycoprotein carbohydrates. Anal Biochem. 2006;350:1–23.
    • (2006) Anal Biochem , vol.350 , pp. 1-23
    • Anumula, K.R.1
  • 62
    • 84878411470 scopus 로고    scopus 로고
    • Reversed-phase liquid-chromatographic mass spectrometric N-glycan analysis of biopharmaceuticals
    • F.Higel, U.Demelbauer, A.Seidl, et al. Reversed-phase liquid-chromatographic mass spectrometric N-glycan analysis of biopharmaceuticals. Anal Bioanal Chem. 2013;405:2481–2493.
    • (2013) Anal Bioanal Chem , vol.405 , pp. 2481-2493
    • Higel, F.1    Demelbauer, U.2    Seidl, A.3
  • 63
    • 77954862775 scopus 로고    scopus 로고
    • The evaluation of a novel approach for the profiling and identification of N-linked glycan with a procainamide tag by HPLC with fluorescent and mass spectrometric detection
    • S.Klapoetke, J.Zhang, S.Becht, et al. The evaluation of a novel approach for the profiling and identification of N-linked glycan with a procainamide tag by HPLC with fluorescent and mass spectrometric detection. J Pharm Biomed Anal. 2010;53:315–324.
    • (2010) J Pharm Biomed Anal , vol.53 , pp. 315-324
    • Klapoetke, S.1    Zhang, J.2    Becht, S.3
  • 64
    • 84937622230 scopus 로고    scopus 로고
    • Comparison of procainamide and 2-aminobenzamide labeling for profiling and identification of glycans by liquid chromatography with fluorescence detection coupled to electrospray ionization–mass spectrometry
    • R.P.Kozak, C.B.Tortosa, D.L.Fernandes, et al. Comparison of procainamide and 2-aminobenzamide labeling for profiling and identification of glycans by liquid chromatography with fluorescence detection coupled to electrospray ionization–mass spectrometry. Anal Biochem. 2015;486:38–40.
    • (2015) Anal Biochem , vol.486 , pp. 38-40
    • Kozak, R.P.1    Tortosa, C.B.2    Fernandes, D.L.3
  • 65
    • 84939865360 scopus 로고    scopus 로고
    • 3)
    • •• Description of robotic platform for N-glycan analysis of 384 IgG samples using LC-FLR.
    • 3). Anal Chem. 2015;87:8316–8322.•• Description of robotic platform for N-glycan analysis of 384 IgG samples using LC-FLR.
    • (2015) Anal Chem , vol.87 , pp. 8316-8322
    • Stöckmann, H.1    Duke, R.M.2    Millán Martín, S.3
  • 66
    • 84929630799 scopus 로고    scopus 로고
    • Rapid preparation of released N-glycans for HILIC analysis using a labeling reagent that facilitates sensitive fluorescence and ESI-MS detection
    • M.A.Lauber, Y.-Q.Yu, D.W.Brousmiche, et al. Rapid preparation of released N-glycans for HILIC analysis using a labeling reagent that facilitates sensitive fluorescence and ESI-MS detection. Anal Chem. 2015;87:5401–5409.
    • (2015) Anal Chem , vol.87 , pp. 5401-5409
    • Lauber, M.A.1    Yu, Y.-Q.2    Brousmiche, D.W.3
  • 67
    • 31544451303 scopus 로고    scopus 로고
    • Application of the 6-aminoquinolyl-N-hydroxysccinimidyl carbamate (AQC) reagent to the RP-HPLC determination of amino acids in infant foods
    • L.Bosch, A.Alegría, R.Farré. Application of the 6-aminoquinolyl-N-hydroxysccinimidyl carbamate (AQC) reagent to the RP-HPLC determination of amino acids in infant foods. J Chromatogr B Anal Technol Biomed Life Sci. 2006;831:176–183.
    • (2006) J Chromatogr B Anal Technol Biomed Life Sci , vol.831 , pp. 176-183
    • Bosch, L.1    Alegría, A.2    Farré, R.3
  • 68
    • 33646236915 scopus 로고    scopus 로고
    • Derivatization by 6-aminoquinolyl- N-hydroxysuccinimidyl carbamate for enhancing the ionization yield of small peptides and glycopeptides in matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry
    • R.Ullmer, A.Plematl, A.Rizzi. Derivatization by 6-aminoquinolyl- N-hydroxysuccinimidyl carbamate for enhancing the ionization yield of small peptides and glycopeptides in matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry. Rapid Commun Mass Spectrom. 2006;20:1469–1479.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 1469-1479
    • Ullmer, R.1    Plematl, A.2    Rizzi, A.3
  • 69
    • 84937689016 scopus 로고    scopus 로고
    • High throughput glycomics: optimization of sample preparation
    • I.Trbojević Akmačić, I.Ugrina, J.Štambuk, et al. High throughput glycomics: optimization of sample preparation. Biochem. 2015;80:934–942.
    • (2015) Biochem , vol.80 , pp. 934-942
    • Trbojević Akmačić, I.1    Ugrina, I.2    Štambuk, J.3
  • 70
    • 34249989775 scopus 로고    scopus 로고
    • Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients
    • H.Nakagawa, M.Hato, Y.Takegawa, et al. Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients. J Chromatogr B Anal Technol Biomed Life Sci. 2007;853:133–137.
    • (2007) J Chromatogr B Anal Technol Biomed Life Sci , vol.853 , pp. 133-137
    • Nakagawa, H.1    Hato, M.2    Takegawa, Y.3
  • 71
    • 34447310112 scopus 로고    scopus 로고
    • Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions
    • L.Royle, C.M.Radcliffe, R.A.Dwek, et al Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions. Methods Mol Biol. 2006;347:125–143.
    • (2006) Methods Mol Biol , vol.347 , pp. 125-143
    • Royle, L.1    Radcliffe, C.M.2    Dwek, R.A.3
  • 72
    • 84857389958 scopus 로고    scopus 로고
    • Online nanoliquid chromatography-mass spectrometry and nanofluorescence detection for high-resolution quantitative N-glycan analysis
    • H.Kalay, M.Ambrosini, P.H.C.Van Berkel, et al. Online nanoliquid chromatography-mass spectrometry and nanofluorescence detection for high-resolution quantitative N-glycan analysis. Anal Biochem. 2012;423:153–162.
    • (2012) Anal Biochem , vol.423 , pp. 153-162
    • Kalay, H.1    Ambrosini, M.2    Van Berkel, P.H.C.3
  • 73
    • 56749173552 scopus 로고    scopus 로고
    • Comparison of fluorescent labels for oligosaccharides and introduction of a new postlabeling purification method
    • M.Pabst, D.Kolarich, G.Pöltl, et al. Comparison of fluorescent labels for oligosaccharides and introduction of a new postlabeling purification method. Anal Biochem. 2009;384:263–273.
    • (2009) Anal Biochem , vol.384 , pp. 263-273
    • Pabst, M.1    Kolarich, D.2    Pöltl, G.3
  • 74
    • 23844499696 scopus 로고    scopus 로고
    • A rapid sample preparation method for mass spectrometric characterization of N-linked glycans
    • Y.Q.Yu, M.Gilar, J.Kaska, et al. A rapid sample preparation method for mass spectrometric characterization of N-linked glycans. Rapid Commun Mass Spectrom. 2005;19:2331–2336.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 2331-2336
    • Yu, Y.Q.1    Gilar, M.2    Kaska, J.3
  • 75
    • 84881667954 scopus 로고    scopus 로고
    • A cost-effective plate-based sample preparation for antibody N-glycan analysis
    • I.Burnina, E.Hoyt, H.Lynaugh, et al. A cost-effective plate-based sample preparation for antibody N-glycan analysis. J Chromatogr A. 2013;1307:201–206.
    • (2013) J Chromatogr A , vol.1307 , pp. 201-206
    • Burnina, I.1    Hoyt, E.2    Lynaugh, H.3
  • 76
    • 34548475063 scopus 로고    scopus 로고
    • Automated sample preparation facilitated by PhyNexus MEA purification system for oligosaccharide mapping of glycoproteins
    • B.D.Prater, K.R.Anumula, J.T.Hutchins. Automated sample preparation facilitated by PhyNexus MEA purification system for oligosaccharide mapping of glycoproteins. Anal Biochem. 2007;369:202–209.
    • (2007) Anal Biochem , vol.369 , pp. 202-209
    • Prater, B.D.1    Anumula, K.R.2    Hutchins, J.T.3
  • 77
    • 84884264843 scopus 로고    scopus 로고
    • Automated, high-throughput IgG-antibody glycoprofiling platform
    • •• Explains the automatization of high-throughput sample preparation workflow for the study of IgG N-glycans.
    • H.Stöckmann, B.Adamczyk, J.Hayes, et al. Automated, high-throughput IgG-antibody glycoprofiling platform. Anal Chem. 2013;85:8841–8849.•• Explains the automatization of high-throughput sample preparation workflow for the study of IgG N-glycans.
    • (2013) Anal Chem , vol.85 , pp. 8841-8849
    • Stöckmann, H.1    Adamczyk, B.2    Hayes, J.3
  • 78
    • 74049141466 scopus 로고    scopus 로고
    • Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7μm sorbent
    • J.Ahn, J.Bones, Y.Q.Yu, et al. Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7μm sorbent. J Chromatogr B Anal Technol Biomed Life Sci. 2010;878:403–408.
    • (2010) J Chromatogr B Anal Technol Biomed Life Sci , vol.878 , pp. 403-408
    • Ahn, J.1    Bones, J.2    Yu, Y.Q.3
  • 79
    • 34848917542 scopus 로고    scopus 로고
    • Peak capacity in gradient reversed-phase liquid chromatography of biopolymers. Theoretical and practical implications for the separation of oligonucleotides
    • M.Gilar, U.D.Neue. Peak capacity in gradient reversed-phase liquid chromatography of biopolymers. Theoretical and practical implications for the separation of oligonucleotides. J Chromatogr A. 2007;1169:139–150.
    • (2007) J Chromatogr A , vol.1169 , pp. 139-150
    • Gilar, M.1    Neue, U.D.2
  • 80
    • 42649139214 scopus 로고    scopus 로고
    • GlycoBase and autoGU: tools for HPLC-based glycan analysis
    • M.P.Campbell, L.Royle, C.M.Radcliffe, et al. GlycoBase and autoGU: tools for HPLC-based glycan analysis. Bioinformatics. 2008;24:1214–1216.
    • (2008) Bioinformatics , vol.24 , pp. 1214-1216
    • Campbell, M.P.1    Royle, L.2    Radcliffe, C.M.3
  • 81
    • 84974620009 scopus 로고    scopus 로고
    • IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
    • A.Bondt, Y.Rombouts, M.H.J.Selman, et al. IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol Cell Proteomics. 2014;31:1–30.
    • (2014) Mol Cell Proteomics , vol.31 , pp. 1-30
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.J.3
  • 82
    • 84960109858 scopus 로고    scopus 로고
    • Extensive glycosylation of ACPA-IgG variable domains modulates binding to citrullinated antigens in rheumatoid arthritis
    • Y.Rombouts, A.Willemze, J.J.B.C.Van Beers, et al. Extensive glycosylation of ACPA-IgG variable domains modulates binding to citrullinated antigens in rheumatoid arthritis. Ann Rheum Dis. 2015;75:578–585.
    • (2015) Ann Rheum Dis , vol.75 , pp. 578-585
    • Rombouts, Y.1    Willemze, A.2    Van Beers, J.J.B.C.3
  • 83
    • 84922990828 scopus 로고    scopus 로고
    • A method for high-throughput, sensitive analysis of IgG Fc and Fab glycosylation by capillary electrophoresis
    • A.E.Mahan, J.Tedesco, K.Dionne, et al. A method for high-throughput, sensitive analysis of IgG Fc and Fab glycosylation by capillary electrophoresis. J Immunol Methods. 2015;417:34–44.
    • (2015) J Immunol Methods , vol.417 , pp. 34-44
    • Mahan, A.E.1    Tedesco, J.2    Dionne, K.3
  • 84
    • 84887664948 scopus 로고    scopus 로고
    • Capillary electrophoresis/mass spectrometry of APTS-labeled glycans for the identification of unknown glycan species in capillary electrophoresis/laser- induced fluorescence systems
    • S.-C.Bunz, E.Rapp, C.Neusüss. Capillary electrophoresis/mass spectrometry of APTS-labeled glycans for the identification of unknown glycan species in capillary electrophoresis/laser- induced fluorescence systems. Anal Chem. 2013;85:10218–10224.
    • (2013) Anal Chem , vol.85 , pp. 10218-10224
    • Bunz, S.-C.1    Rapp, E.2    Neusüss, C.3
  • 85
    • 84962541719 scopus 로고    scopus 로고
    • Fully automated sample preparation for ultrafast N-glycosylation analysis of antibody therapeutics
    • M.Szigeti, C.Lew, K.Roby, et al. Fully automated sample preparation for ultrafast N-glycosylation analysis of antibody therapeutics. J Lab Autom. 2016;21:281–286.
    • (2016) J Lab Autom , vol.21 , pp. 281-286
    • Szigeti, M.1    Lew, C.2    Roby, K.3
  • 86
    • 77951151811 scopus 로고    scopus 로고
    • Improved sample preparation method for glycan analysis of glycoproteins by CE-LIF and CE-MS
    • Z.Szabo, A.Guttman, T.Rejtar, et al. Improved sample preparation method for glycan analysis of glycoproteins by CE-LIF and CE-MS. Electrophoresis. 2010;31:1389–1395.
    • (2010) Electrophoresis , vol.31 , pp. 1389-1395
    • Szabo, Z.1    Guttman, A.2    Rejtar, T.3
  • 87
    • 77953853129 scopus 로고    scopus 로고
    • 2-Picoline-borane: A non-toxic reducing agent for oligosaccharide labeling by reductive amination
    • L.R.Ruhaak, E.Steenvoorden, C.A.M.Koeleman, et al. 2-Picoline-borane: A non-toxic reducing agent for oligosaccharide labeling by reductive amination. Proteomics. 2010;10:2330–2336.
    • (2010) Proteomics , vol.10 , pp. 2330-2336
    • Ruhaak, L.R.1    Steenvoorden, E.2    Koeleman, C.A.M.3
  • 88
    • 84885308316 scopus 로고    scopus 로고
    • Analysis of native and APTS-labeled N-glycans by capillary electrophoresis/time-of-flight mass spectrometry
    • S.-C.Bunz, F.Cutillo, C.Neusüß. Analysis of native and APTS-labeled N-glycans by capillary electrophoresis/time-of-flight mass spectrometry. Anal Bioanal Chem. 2013;405:8277–8284.
    • (2013) Anal Bioanal Chem , vol.405 , pp. 8277-8284
    • Bunz, S.-C.1    Cutillo, F.2    Neusüß, C.3
  • 89
    • 84902789927 scopus 로고    scopus 로고
    • Rapid magnetic bead based sample preparation for automated and high throughput N-glycan analysis of therapeutic antibodies
    • C.Váradi, C.Lew, A.Guttman. Rapid magnetic bead based sample preparation for automated and high throughput N-glycan analysis of therapeutic antibodies. Anal Chem. 2014;86:5682–5687.
    • (2014) Anal Chem , vol.86 , pp. 5682-5687
    • Váradi, C.1    Lew, C.2    Guttman, A.3
  • 90
    • 78649869061 scopus 로고    scopus 로고
    • Optimized workflow for preparation of APTS-labeled N-glycans allowing high-throughput analysis of human plasma glycomes using 48-channel multiplexed CGE-LIF
    • L.R.Ruhaak, R.Hennig, C.Huhn, et al. Optimized workflow for preparation of APTS-labeled N-glycans allowing high-throughput analysis of human plasma glycomes using 48-channel multiplexed CGE-LIF. J Proteome Res. 2010;9:6655–6664.
    • (2010) J Proteome Res , vol.9 , pp. 6655-6664
    • Ruhaak, L.R.1    Hennig, R.2    Huhn, C.3
  • 91
    • 84860228629 scopus 로고    scopus 로고
    • Influence of molecular configuration and conformation on the electromigration of oligosaccharides in narrow bore capillaries
    • S.Mittermayr, A.Guttman. Influence of molecular configuration and conformation on the electromigration of oligosaccharides in narrow bore capillaries. Electrophoresis. 2012;33:1000–1007.
    • (2012) Electrophoresis , vol.33 , pp. 1000-1007
    • Mittermayr, S.1    Guttman, A.2
  • 92
    • 84954328603 scopus 로고    scopus 로고
    • GUcal: An integrated application for capillary electrophoresis based glycan analysis
    • G.Jarvas, M.Szigeti, A.Guttman. GUcal: An integrated application for capillary electrophoresis based glycan analysis. Electrophoresis. 2015;36:3094–3096.
    • (2015) Electrophoresis , vol.36 , pp. 3094-3096
    • Jarvas, G.1    Szigeti, M.2    Guttman, A.3
  • 93
    • 79961236820 scopus 로고    scopus 로고
    • Multiplexed analytical glycomics: rapid and confident IgG N-glycan structural elucidation
    • •• Description of a strategy for IgG glycan peak annotation using the CGE-LIF approach combining digestions with exoglycosidases and weak anion exchange fractionation.
    • S.Mittermayr, J.Bones, M.Doherty, et al. Multiplexed analytical glycomics: rapid and confident IgG N-glycan structural elucidation. J Proteome Res. 2011;10:3820–3829.•• Description of a strategy for IgG glycan peak annotation using the CGE-LIF approach combining digestions with exoglycosidases and weak anion exchange fractionation.
    • (2011) J Proteome Res , vol.10 , pp. 3820-3829
    • Mittermayr, S.1    Bones, J.2    Doherty, M.3
  • 94
    • 84877350385 scopus 로고    scopus 로고
    • Unraveling the glyco-puzzle: glycan structure identification by capillary electrophoresis
    • S.Mittermayr, J.Bones. Unraveling the glyco-puzzle: glycan structure identification by capillary electrophoresis. Anal Chem. 2013;85:4228–4238.
    • (2013) Anal Chem , vol.85 , pp. 4228-4238
    • Mittermayr, S.1    Bones, J.2
  • 95
    • 80051745436 scopus 로고    scopus 로고
    • A promising capillary electrophoresis-electrospray ionization-mass spectrometry method for carbohydrate analysis
    • E.J.Maxwell, C.Ratnayake, R.Jayo, et al. A promising capillary electrophoresis-electrospray ionization-mass spectrometry method for carbohydrate analysis. Electrophoresis. 2011;32:2161–2166.
    • (2011) Electrophoresis , vol.32 , pp. 2161-2166
    • Maxwell, E.J.1    Ratnayake, C.2    Jayo, R.3
  • 96
    • 84903726677 scopus 로고    scopus 로고
    • Simple capillary electrophoresis-mass spectrometry method for complex glycan analysis using a flow-through microvial interface
    • R.G.Jayo, M.Thaysen-Andersen, P.W.Lindenburg, et al. Simple capillary electrophoresis-mass spectrometry method for complex glycan analysis using a flow-through microvial interface. Anal Chem. 2014;86:6479–6486.
    • (2014) Anal Chem , vol.86 , pp. 6479-6486
    • Jayo, R.G.1    Thaysen-Andersen, M.2    Lindenburg, P.W.3
  • 97
    • 71749113776 scopus 로고    scopus 로고
    • Accelerated digestion for high-throughput proteomics analysis of whole bacterial proteomes
    • A.R.Vaezzadeh, J.M.P.Deshusses, P.Waridel, et al. Accelerated digestion for high-throughput proteomics analysis of whole bacterial proteomes. J Microbiol Methods. 2010;80:56–62.
    • (2010) J Microbiol Methods , vol.80 , pp. 56-62
    • Vaezzadeh, A.R.1    Deshusses, J.M.P.2    Waridel, P.3
  • 98
    • 84969988637 scopus 로고    scopus 로고
    • Characterization of immunoglobulins through analysis of N-glycopeptides by MALDI-TOF MS
    • • Comparison of different glycopeptide enrichment strategies for MALDI-TOF-MS analysis.
    • E.Komatsu, M.Buist, R.Roy, et al. Characterization of immunoglobulins through analysis of N-glycopeptides by MALDI-TOF MS. Methods. 2016 Jan 7. DOI:10.1016/j.ymeth.2016.01.005• Comparison of different glycopeptide enrichment strategies for MALDI-TOF-MS analysis.
    • Methods
    • Komatsu, E.1    Buist, M.2    Roy, R.3
  • 99
    • 84861844024 scopus 로고    scopus 로고
    • Centrifugation assisted microreactor enables facile integration of trypsin digestion, hydrophilic interaction chromatography enrichment, and on-column deglycosylation for rapid and sensitive N-glycoproteome analysis
    • J.Zhu, F.Wang, R.Chen, et al. Centrifugation assisted microreactor enables facile integration of trypsin digestion, hydrophilic interaction chromatography enrichment, and on-column deglycosylation for rapid and sensitive N-glycoproteome analysis. Anal Chem. 2012;84:5146–5153.
    • (2012) Anal Chem , vol.84 , pp. 5146-5153
    • Zhu, J.1    Wang, F.2    Chen, R.3
  • 100
    • 76749088472 scopus 로고    scopus 로고
    • Digestion completeness of microwave-assisted and conventional trypsin-catalyzed reactions
    • P.M.Reddy, W.-Y.Hsu, J.-F.Hu, et al. Digestion completeness of microwave-assisted and conventional trypsin-catalyzed reactions. J Am Soc Mass Spectrom. 2010;21:421–424.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 421-424
    • Reddy, P.M.1    Hsu, W.-Y.2    Hu, J.-F.3
  • 101
    • 70349113034 scopus 로고    scopus 로고
    • Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
    • H.J.An, J.W.Froehlich, C.B.Lebrilla. Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. Curr Opin Chem Biol. 2009;13:421–426.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 421-426
    • An, H.J.1    Froehlich, J.W.2    Lebrilla, C.B.3
  • 102
    • 84948469789 scopus 로고    scopus 로고
    • Site-specific protein N- and O-glycosylation analysis by a C18-porous graphitized carbon-liquid chromatography-electrospray ionization mass spectrometry approach using pronase treated glycopeptides
    • K.Stavenhagen, R.Plomp, M.Wuhrer. Site-specific protein N- and O-glycosylation analysis by a C18-porous graphitized carbon-liquid chromatography-electrospray ionization mass spectrometry approach using pronase treated glycopeptides. Anal Chem. 2015;87:11691–11699.
    • (2015) Anal Chem , vol.87 , pp. 11691-11699
    • Stavenhagen, K.1    Plomp, R.2    Wuhrer, M.3
  • 103
    • 84937432796 scopus 로고    scopus 로고
    • Carbohydrates on proteins: site-specific glycosylation analysis by mass spectrometry
    • Z.Zhu, H.Desaire. Carbohydrates on proteins: site-specific glycosylation analysis by mass spectrometry. Annu Rev Anal Chem. 2015;8:463–483.
    • (2015) Annu Rev Anal Chem , vol.8 , pp. 463-483
    • Zhu, Z.1    Desaire, H.2
  • 104
    • 84862238705 scopus 로고    scopus 로고
    • Determination of site-specific glycan heterogeneity on glycoproteins
    • D.Kolarich, P.H.Jensen, F.Altmann, et al. Determination of site-specific glycan heterogeneity on glycoproteins. Nat Protoc. 2012;7:1285–1298.
    • (2012) Nat Protoc , vol.7 , pp. 1285-1298
    • Kolarich, D.1    Jensen, P.H.2    Altmann, F.3
  • 105
    • 79953292549 scopus 로고    scopus 로고
    • Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides
    • M.H.J.Selman, M.Hemayatkar, A.M.Deelder, et al. Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides. Anal Chem. 2011;83:2492–2499.
    • (2011) Anal Chem , vol.83 , pp. 2492-2499
    • Selman, M.H.J.1    Hemayatkar, M.2    Deelder, A.M.3
  • 106
    • 84902814201 scopus 로고    scopus 로고
    • High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification
    • • Development and optimization of a linkage-specific high-throughput derivatization strategy of sialylated glycans for MALDI-TOF-MS glycan analysis.
    • K.R.Reiding, D.Blank, D.M.Kuijper, et al. High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification. Anal Chem. 2014;86:5784–5793.• Development and optimization of a linkage-specific high-throughput derivatization strategy of sialylated glycans for MALDI-TOF-MS glycan analysis.
    • (2014) Anal Chem , vol.86 , pp. 5784-5793
    • Reiding, K.R.1    Blank, D.2    Kuijper, D.M.3
  • 107
    • 84905714910 scopus 로고    scopus 로고
    • Highly selective and ultra fast solid-phase extraction of N - glycoproteome by oxime click chemistry using aminooxy- functionalized magnetic nanoparticles
    • Y.Zhang, M.Yu, C.Zhang, et al. Highly selective and ultra fast solid-phase extraction of N - glycoproteome by oxime click chemistry using aminooxy- functionalized magnetic nanoparticles. Anal Chem. 2014;86:7920–7924.
    • (2014) Anal Chem , vol.86 , pp. 7920-7924
    • Zhang, Y.1    Yu, M.2    Zhang, C.3
  • 108
    • 84925355788 scopus 로고    scopus 로고
    • Highly specific enrichment of N-glycoproteome through a nonreductive amination reaction using Fe3O4@SiO2-aniline nanoparticles
    • Y.Zhang, M.Yu, C.Zhang, et al. Highly specific enrichment of N-glycoproteome through a nonreductive amination reaction using Fe3O4@SiO2-aniline nanoparticles. Chem Commun (Cambridge, United Kingdom). 2015;51:5982–5985.
    • (2015) Chem Commun (Cambridge, United Kingdom) , vol.51 , pp. 5982-5985
    • Zhang, Y.1    Yu, M.2    Zhang, C.3
  • 109
    • 84890846517 scopus 로고    scopus 로고
    • Highly specific enrichment of N-linked glycopeptides based on hydrazide functionalized soluble nanopolymers
    • L.Zhang, H.Jiang, J.Yao, et al. Highly specific enrichment of N-linked glycopeptides based on hydrazide functionalized soluble nanopolymers. Chem Commun. 2014;50:1027–1029.
    • (2014) Chem Commun , vol.50 , pp. 1027-1029
    • Zhang, L.1    Jiang, H.2    Yao, J.3
  • 110
    • 84878630101 scopus 로고    scopus 로고
    • Glycopeptide enrichment for MALDI-TOF mass spectrometry analysis by hydrophilic interaction liquid chromatography solid phase extraction (HILIC SPE)
    • P.H.Jensen, S.Mysling, P.Højrup, et al. Glycopeptide enrichment for MALDI-TOF mass spectrometry analysis by hydrophilic interaction liquid chromatography solid phase extraction (HILIC SPE). Methods Mol Biol. 2013;951:131–144.
    • (2013) Methods Mol Biol , vol.951 , pp. 131-144
    • Jensen, P.H.1    Mysling, S.2    Højrup, P.3
  • 111
    • 84859861608 scopus 로고    scopus 로고
    • N-glycoproteomics: mass spectrometry-based glycosylation site annotation
    • Y.Pasing, A.Sickmann, U.Lewandrowski. N-glycoproteomics: mass spectrometry-based glycosylation site annotation. Biol Chem. 2012;393:249–258.
    • (2012) Biol Chem , vol.393 , pp. 249-258
    • Pasing, Y.1    Sickmann, A.2    Lewandrowski, U.3
  • 112
    • 84903771833 scopus 로고    scopus 로고
    • Mass spectrometry-based N-glycoproteomics for cancer biomarker discovery
    • Y.Zhang, J.Jiao, P.Yang, et al. Mass spectrometry-based N-glycoproteomics for cancer biomarker discovery. Clin Proteomics. 2014;11:1–14.
    • (2014) Clin Proteomics , vol.11 , pp. 1-14
    • Zhang, Y.1    Jiao, J.2    Yang, P.3
  • 113
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • J.Stadlmann, M.Pabst, D.Kolarich, et al. Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics. 2008;8:2858–2871.
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3
  • 114
    • 84921395878 scopus 로고    scopus 로고
    • Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles–part 1: separation-based methods
    • D.Reusch, M.Haberger, B.Maier, et al. Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles–part 1: separation-based methods. MAbs. 2015;7:732–742.
    • (2015) MAbs , vol.7 , pp. 732-742
    • Reusch, D.1    Haberger, M.2    Maier, B.3
  • 115
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N- and O-glycans released from glycoproteins
    • P.H.Jensen, N.G.Karlsson, D.Kolarich, et al. Structural analysis of N- and O-glycans released from glycoproteins. Nat Protoc. 2012;7:1299–1310.
    • (2012) Nat Protoc , vol.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3
  • 116
    • 84925504413 scopus 로고    scopus 로고
    • High-throughput analysis and automation for glycomics studies
    • • Recent review that includes detailed overview of sialic acid derivatization strategies for MS analysis of glycans.
    • A.Shubhakar, K.R.Reiding, R.A.Gardner, et al. High-throughput analysis and automation for glycomics studies. Chromatographia. 2015;78:321–333.• Recent review that includes detailed overview of sialic acid derivatization strategies for MS analysis of glycans.
    • (2015) Chromatographia , vol.78 , pp. 321-333
    • Shubhakar, A.1    Reiding, K.R.2    Gardner, R.A.3
  • 117
    • 77957318349 scopus 로고    scopus 로고
    • Methylamidation for sialoglycomics by MALDI-MS: a facile derivatization strategy for both α2,3- and α2,6-linked sialic acids
    • X.Liu, H.Qiu, R.Kuo Lee, et al. Methylamidation for sialoglycomics by MALDI-MS: a facile derivatization strategy for both α2,3- and α2,6-linked sialic acids. Anal Chem. 2010;82:8300–8306.
    • (2010) Anal Chem , vol.82 , pp. 8300-8306
    • Liu, X.1    Qiu, H.2    Kuo Lee, R.3
  • 118
    • 34250313689 scopus 로고    scopus 로고
    • Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry
    • Y.Miura, Y.Shinohara, J.I.Furukawa, et al. Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry. Chem - A Eur J. 2007;13:4797–4804.
    • (2007) Chem - A Eur J , vol.13 , pp. 4797-4804
    • Miura, Y.1    Shinohara, Y.2    Furukawa, J.I.3
  • 119
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • R.M.Anthony, F.Nimmerjahn, D.J.Ashline, et al. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science. 2008;320:373–376.
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3
  • 120
    • 84941060330 scopus 로고    scopus 로고
    • Automation of high-throughput mass spectrometry-based plasma N -glycome analysis with linkage-specific sialic acid esterification
    • M.R.Bladergroen, K.R.Reiding, A.L.Hipgrave Ederveen, et al. Automation of high-throughput mass spectrometry-based plasma N -glycome analysis with linkage-specific sialic acid esterification. J Proteome Res. 2015;14:4080–4086.
    • (2015) J Proteome Res , vol.14 , pp. 4080-4086
    • Bladergroen, M.R.1    Reiding, K.R.2    Hipgrave Ederveen, A.L.3
  • 121
    • 84939865371 scopus 로고    scopus 로고
    • Linkage-specific sialic acid derivatization for MALDI-TOF-MS profiling of IgG glycopeptides
    • N.De Haan, K.R.Reiding, M.Haberger, et al. Linkage-specific sialic acid derivatization for MALDI-TOF-MS profiling of IgG glycopeptides. Anal Chem. 2015;87:8284–8291.
    • (2015) Anal Chem , vol.87 , pp. 8284-8291
    • De Haan, N.1    Reiding, K.R.2    Haberger, M.3
  • 122
    • 79955629718 scopus 로고    scopus 로고
    • Negative-ion MALDI-MS2 for discrimination of α2,3- and α2,6-sialylation on glycopeptides labeled with a pyrene derivative
    • T.Nishikaze, T.Nakamura, H.Jinmei, et al. Negative-ion MALDI-MS2 for discrimination of α2,3- and α2,6-sialylation on glycopeptides labeled with a pyrene derivative. J Chromatogr B Anal Technol Biomed Life Sci. 2011;879:1419–1428.
    • (2011) J Chromatogr B Anal Technol Biomed Life Sci , vol.879 , pp. 1419-1428
    • Nishikaze, T.1    Nakamura, T.2    Jinmei, H.3
  • 123
    • 84901800096 scopus 로고    scopus 로고
    • In-depth structural characterization of N -linked glycopeptides using complete derivatization for carboxyl groups followed by positive- and negative-ion tandem mass spectrometry
    • T.Nishikaze, S.-I.Kawabata, K.Tanaka. In-depth structural characterization of N -linked glycopeptides using complete derivatization for carboxyl groups followed by positive- and negative-ion tandem mass spectrometry. Anal Chem. 2014;86:5360–5369.
    • (2014) Anal Chem , vol.86 , pp. 5360-5369
    • Nishikaze, T.1    Kawabata, S.-I.2    Tanaka, K.3
  • 124
    • 84884273245 scopus 로고    scopus 로고
    • Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring
    • Q.Hong, C.B.Lebrilla, S.Miyamoto, et al. Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring. Anal Chem. 2013;85:8585–8593.
    • (2013) Anal Chem , vol.85 , pp. 8585-8593
    • Hong, Q.1    Lebrilla, C.B.2    Miyamoto, S.3
  • 125
    • 84900675178 scopus 로고    scopus 로고
    • Label free absolute quantitation of oligosaccharides using multiple reaction monitoring
    • Q.Hong, L.R.Ruhaak, S.M.Totten, et al. Label free absolute quantitation of oligosaccharides using multiple reaction monitoring. Anal Chem. 2014;86:2640−2647.
    • (2014) Anal Chem , vol.86 , pp. 2640-2647
    • Hong, Q.1    Ruhaak, L.R.2    Totten, S.M.3
  • 126
    • 84925486059 scopus 로고    scopus 로고
    • Applications of multiple reaction monitoring to clinical glycomics
    • L.R.Ruhaak, C.B.Lebrilla. Applications of multiple reaction monitoring to clinical glycomics. Chromatographia. 2015;78:335–342.
    • (2015) Chromatographia , vol.78 , pp. 335-342
    • Ruhaak, L.R.1    Lebrilla, C.B.2
  • 127
    • 84949034098 scopus 로고    scopus 로고
    • A method for comprehensive glycosite-mapping and direct quantitation of serum glycoproteins
    • Q.Hong, L.R.Ruhaak, C.Stroble, et al. A method for comprehensive glycosite-mapping and direct quantitation of serum glycoproteins. J Proteome Res. 2015;14:5179–5192.
    • (2015) J Proteome Res , vol.14 , pp. 5179-5192
    • Hong, Q.1    Ruhaak, L.R.2    Stroble, C.3
  • 128
    • 84960461505 scopus 로고    scopus 로고
    • Protein-specific differential glycosylation of immunoglobulins in serum of ovarian cancer patients
    • L.R.Ruhaak, K.Kim, C.Stroble, et al. Protein-specific differential glycosylation of immunoglobulins in serum of ovarian cancer patients. J Proteome Res. 2016;15:1002–1010.
    • (2016) J Proteome Res , vol.15 , pp. 1002-1010
    • Ruhaak, L.R.1    Kim, K.2    Stroble, C.3
  • 129
    • 84864762633 scopus 로고    scopus 로고
    • Quantification of glycopeptides by multiple reaction monitoring liquid chromatography/tandem mass spectrometry
    • E.Song, S.Pyreddy, Y.Mechref. Quantification of glycopeptides by multiple reaction monitoring liquid chromatography/tandem mass spectrometry. Rapid Commun Mass Spectrom. 2012;26:1941–1954.
    • (2012) Rapid Commun Mass Spectrom , vol.26 , pp. 1941-1954
    • Song, E.1    Pyreddy, S.2    Mechref, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.