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Volumn 21, Issue 5, 2016, Pages 740-765

Challenges of glycosylation analysis and control: An integrated approach to producing optimal and consistent therapeutic drugs

Author keywords

[No Author keywords available]

Indexed keywords

ALEMTUZUMAB; CETUXIMAB; CHORIONIC GONADOTROPIN; FOLLITROPIN; GAMMA INTERFERON; GLYCOPROTEIN; LECTIN; MONOCLONAL ANTIBODY; TRASTUZUMAB;

EID: 84957922718     PISSN: 13596446     EISSN: 18785832     Source Type: Journal    
DOI: 10.1016/j.drudis.2016.01.006     Document Type: Review
Times cited : (171)

References (259)
  • 1
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • R. Apweiler, and et al. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database Biochim. Biophys. Acta 1473 1999 4 8
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1
  • 2
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • A.J. Parodi Protein glucosylation and its role in protein folding Annu. Rev. Biochem. 69 2000 69 93
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 3
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: Diversity, synthesis and function
    • K.W. Moremen, and et al. Vertebrate protein glycosylation: diversity, synthesis and function Nat. Rev. Mol. Cell Biol. 13 2012 448 462
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 448-462
    • Moremen, K.W.1
  • 4
    • 79953194818 scopus 로고    scopus 로고
    • Essential glycan-dependent interactions optimize MHC class i peptide loading
    • P.A. Wearsch, and et al. Essential glycan-dependent interactions optimize MHC class I peptide loading Proc. Natl. Acad. Sci. U. S. A. 108 2011 4950 4955
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 4950-4955
    • Wearsch, P.A.1
  • 5
    • 84922480109 scopus 로고    scopus 로고
    • The sweet spot: Defining virus-sialic acid interactions
    • J.E. Stencel-Baerenwald, and et al. The sweet spot: defining virus-sialic acid interactions Nat. Rev. Microbiol. 12 2014 739 749
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 739-749
    • Stencel-Baerenwald, J.E.1
  • 6
    • 84958524636 scopus 로고    scopus 로고
    • Glycosylation and Fc receptors
    • J.M. Hayes, and et al. Glycosylation and Fc receptors Curr. Top. Microbiol. Immunol. 382 2014 165 199
    • (2014) Curr. Top. Microbiol. Immunol. , vol.382 , pp. 165-199
    • Hayes, J.M.1
  • 7
    • 40849142102 scopus 로고    scopus 로고
    • Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose
    • C.H. Chung, and et al. Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose N. Engl. J. Med. 358 2008 1109 1117
    • (2008) N. Engl. J. Med. , vol.358 , pp. 1109-1117
    • Chung, C.H.1
  • 8
    • 84879923507 scopus 로고    scopus 로고
    • Erythropoiesis stimulating agents: Approaches to modulate activity
    • A.M. Sinclair Erythropoiesis stimulating agents: approaches to modulate activity Biologics 7 2013 161 174
    • (2013) Biologics , vol.7 , pp. 161-174
    • Sinclair, A.M.1
  • 9
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • T. Shinkawa, and et al. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity J. Biol. Chem. 278 2003 3466 3473
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1
  • 10
    • 84920502297 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2014
    • G. Walsh Biopharmaceutical benchmarks 2014 Nat. Biotechnol. 32 2014 992 1000
    • (2014) Nat. Biotechnol. , vol.32 , pp. 992-1000
    • Walsh, G.1
  • 11
    • 84921352030 scopus 로고    scopus 로고
    • The therapeutic monoclonal antibody market
    • D.M. Ecker, and et al. The therapeutic monoclonal antibody market MAbs 7 2015 9 14
    • (2015) MAbs , vol.7 , pp. 9-14
    • Ecker, D.M.1
  • 12
    • 84892170718 scopus 로고    scopus 로고
    • What's fueling the biotech engine-2012 to 2013
    • R.S. Aggarwal What's fueling the biotech engine-2012 to 2013 Nat. Biotechnol. 32 2014 32 39
    • (2014) Nat. Biotechnol. , vol.32 , pp. 32-39
    • Aggarwal, R.S.1
  • 13
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • J.N. Arnold, and et al. The impact of glycosylation on the biological function and structure of human immunoglobulins Annu. Rev. Immunol. 25 2007 21 50
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1
  • 14
    • 84873495247 scopus 로고    scopus 로고
    • Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers
    • G. Lauc, and et al. Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers PLoS Genet. 9 2013 e1003225
    • (2013) PLoS Genet. , vol.9 , pp. e1003225
    • Lauc, G.1
  • 15
    • 81055154923 scopus 로고    scopus 로고
    • 5-AZA-2′-deoxycytidine induced demethylation influences N-glycosylation of secreted glycoproteins in ovarian cancer
    • R. Saldova, and et al. 5-AZA-2′-deoxycytidine induced demethylation influences N-glycosylation of secreted glycoproteins in ovarian cancer Epigenetics 6 2011 1362 1372
    • (2011) Epigenetics , vol.6 , pp. 1362-1372
    • Saldova, R.1
  • 16
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • P. Hossler, and et al. Optimal and consistent protein glycosylation in mammalian cell culture Glycobiology 19 2009 936 949
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1
  • 17
    • 84958535852 scopus 로고    scopus 로고
    • Fc receptors as adaptive immunoreceptors
    • M. Daeron Fc receptors as adaptive immunoreceptors Curr. Top. Microbiol. Immunol. 382 2014 131 164
    • (2014) Curr. Top. Microbiol. Immunol. , vol.382 , pp. 131-164
    • Daeron, M.1
  • 18
    • 0016245356 scopus 로고
    • Primary structure of ° light chain from a human myeloma protein
    • C.P. Milstein, and E.V. Deverson Primary structure of ° light chain from a human myeloma protein Eur. J. Biochem. 49 1974 377 391
    • (1974) Eur. J. Biochem. , vol.49 , pp. 377-391
    • Milstein, C.P.1    Deverson, E.V.2
  • 19
    • 0027823753 scopus 로고
    • Construction and expression of two mouse-human chimeric antibodies with high specificity and affinity for carcinoembryonic antigen
    • F. Arakawa, and et al. Construction and expression of two mouse-human chimeric antibodies with high specificity and affinity for carcinoembryonic antigen Hybridoma 12 1993 365 379
    • (1993) Hybridoma , vol.12 , pp. 365-379
    • Arakawa, F.1
  • 20
    • 0028128038 scopus 로고
    • Accumulation enhancement of human monoclonal antibody HB4C5 to lung tumor xenografts by N-deglycosylation
    • K. Kusakabe, and et al. Accumulation enhancement of human monoclonal antibody HB4C5 to lung tumor xenografts by N-deglycosylation J. Nucl. Med. 35 1994 289 295
    • (1994) J. Nucl. Med. , vol.35 , pp. 289-295
    • Kusakabe, K.1
  • 21
    • 0023819528 scopus 로고
    • Glycosylation of a VH residue of a monoclonal antibody against alpha (1-6) dextran increases its affinity for antigen
    • S.C. Wallick, and et al. Glycosylation of a VH residue of a monoclonal antibody against alpha (1-6) dextran increases its affinity for antigen J. Exp. Med. 168 1988 1099 1109
    • (1988) J. Exp. Med. , vol.168 , pp. 1099-1109
    • Wallick, S.C.1
  • 22
    • 79960215653 scopus 로고    scopus 로고
    • Anti-galactose-[alpha]-1,3-galactose IgE from allergic patients does not bind [alpha]-galactosylated glycans on intact therapeutic antibody Fc domains
    • J.J.L. van Bueren, and et al. Anti-galactose-[alpha]-1,3-galactose IgE from allergic patients does not bind [alpha]-galactosylated glycans on intact therapeutic antibody Fc domains Nat. Biotechnol. 29 2011 574 576
    • (2011) Nat. Biotechnol. , vol.29 , pp. 574-576
    • Van Bueren, J.J.L.1
  • 23
    • 76649142720 scopus 로고    scopus 로고
    • Allergenicity of carbohydrates and their role in anaphylactic events
    • S.P. Commins, and T.A.E. Platts-Mills Allergenicity of carbohydrates and their role in anaphylactic events Curr. Allergy Asthma Rep. 10 2010 29 33
    • (2010) Curr. Allergy Asthma Rep. , vol.10 , pp. 29-33
    • Commins, S.P.1    Platts-Mills, T.A.E.2
  • 24
    • 0035937526 scopus 로고    scopus 로고
    • Glycosylation and the immune system
    • P.M. Rudd Glycosylation and the immune system Science 291 2001 2370 2376
    • (2001) Science , vol.291 , pp. 2370-2376
    • Rudd, P.M.1
  • 25
    • 84946233610 scopus 로고    scopus 로고
    • An intrinsic mechanism of secreted protein aging and turnover
    • W.H. Yang, and et al. An intrinsic mechanism of secreted protein aging and turnover Proc. Natl. Acad. Sci. U. S. A. 112 2015 13657 13662
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 13657-13662
    • Yang, W.H.1
  • 26
    • 0033571091 scopus 로고    scopus 로고
    • Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells
    • X. Dong, and et al. Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells J. Immunol. 163 1999 5427 5434
    • (1999) J. Immunol. , vol.163 , pp. 5427-5434
    • Dong, X.1
  • 27
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • R. Malhotra, and et al. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein Nat. Med. 1 1995 237 243
    • (1995) Nat. Med. , vol.1 , pp. 237-243
    • Malhotra, R.1
  • 28
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • A.M. Goetze, and et al. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans Glycobiology 21 2011 949 959
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1
  • 29
    • 84878758122 scopus 로고    scopus 로고
    • Engineering a monomeric Fc domain modality by N-glycosylation for the half-life extension of biotherapeutics
    • T. Ishino, and et al. Engineering a monomeric Fc domain modality by N-glycosylation for the half-life extension of biotherapeutics J. Biol. Chem. 288 2013 16529 16537
    • (2013) J. Biol. Chem. , vol.288 , pp. 16529-16537
    • Ishino, T.1
  • 30
    • 0030434866 scopus 로고    scopus 로고
    • Glycosylation and placental transport of immunoglobulin G
    • T. Kibe, and et al. Glycosylation and placental transport of immunoglobulin G J. Clin. Biochem. Nutr. 21 1996 57 63
    • (1996) J. Clin. Biochem. Nutr. , vol.21 , pp. 57-63
    • Kibe, T.1
  • 31
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals correlation between glycosylation and structural integrity
    • S. Krapp, and et al. Structural analysis of human IgG-Fc glycoforms reveals correlation between glycosylation and structural integrity J. Mol. Biol. 325 2003 979 989
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1
  • 32
    • 0035824579 scopus 로고    scopus 로고
    • Role of oligosaccharide residues of IgG1-Fc in Fc RIIb binding
    • Y. Mimura, and et al. Role of oligosaccharide residues of IgG1-Fc in Fc RIIb binding J. Biol. Chem. 276 2001 45539 45547
    • (2001) J. Biol. Chem. , vol.276 , pp. 45539-45547
    • Mimura, Y.1
  • 33
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc(RIII and antibodies lacking core fucose
    • C. Ferrara, and et al. Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc(RIII and antibodies lacking core fucose Proc. Natl. Acad. Sci. U. S. A. 108 2011 12669 12674
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12669-12674
    • Ferrara, C.1
  • 34
    • 0019867891 scopus 로고
    • The use of protein A and concanavalin A to examine the possible role of the carbohydrate of IgG in the binding of Clq
    • M.R. van Schravendijk, and R.A. Dwek The use of protein A and concanavalin A to examine the possible role of the carbohydrate of IgG in the binding of Clq Mol. Immunol. 18 1981 1079 1085
    • (1981) Mol. Immunol. , vol.18 , pp. 1079-1085
    • Van Schravendijk, M.R.1    Dwek, R.A.2
  • 35
    • 0019225569 scopus 로고
    • The Clq receptor site on immunoglobulin G
    • D.R. Burton, and et al. The Clq receptor site on immunoglobulin G Nature 288 1980 338 344
    • (1980) Nature , vol.288 , pp. 338-344
    • Burton, D.R.1
  • 36
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms
    • Y. Mimura, and et al. The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms Mol. Immunol. 37 2000 697 706
    • (2000) Mol. Immunol. , vol.37 , pp. 697-706
    • Mimura, Y.1
  • 37
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fc(RIII and antibody-dependent cellular toxicity
    • R.L. Shields, and et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fc(RIII and antibody-dependent cellular toxicity J. Biol. Chem. 277 2002 26733 26740
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1
  • 38
    • 84904627207 scopus 로고    scopus 로고
    • Type i and type II Fc receptors regulate innate and adaptive immunity
    • A. Pincetic, and et al. Type I and type II Fc receptors regulate innate and adaptive immunity Nat. Immunol. 15 2014 707 716
    • (2014) Nat. Immunol. , vol.15 , pp. 707-716
    • Pincetic, A.1
  • 39
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • E.A. Padlan Anatomy of the antibody molecule Mol. Immunol. 31 1994 169 217
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 40
    • 84925324765 scopus 로고    scopus 로고
    • Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity
    • N. Washburn, and et al. Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity Proc. Natl. Acad. Sci. U. S. A. 112 2015 E1297 E1306
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E1297-E1306
    • Washburn, N.1
  • 41
    • 84956696215 scopus 로고    scopus 로고
    • At least two Fc Neu5Gc residues of monoclonal antibodies are required for binding to anti-Neu5Gc antibody
    • (article no. 20029)
    • C. Yu, and et al. At least two Fc Neu5Gc residues of monoclonal antibodies are required for binding to anti-Neu5Gc antibody Sci. Rep. 7 2016 10.1038/srep20029 (article no. 20029)
    • (2016) Sci. Rep. , vol.7
    • Yu, C.1
  • 42
    • 84891758097 scopus 로고    scopus 로고
    • Investigation of the correlation between charge and glycosylation of IgG1 variants by liquid chromatography-mass spectrometry
    • J-M. Yang, and et al. Investigation of the correlation between charge and glycosylation of IgG1 variants by liquid chromatography-mass spectrometry Anal. Biochem. 448 2014 82 91
    • (2014) Anal. Biochem. , vol.448 , pp. 82-91
    • Yang, J.-M.1
  • 43
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Y. Kaneko, and et al. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 313 2006 670 673
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1
  • 44
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • A. Samuelsson, and et al. Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor Science 291 2001 484 486
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1
  • 45
    • 84901251341 scopus 로고    scopus 로고
    • Therapeutic effect of IVIG on inflammatory arthritis in mice is dependent on the Fc portion and independent of sialylation or basophils
    • I.K. Campbell, and et al. Therapeutic effect of IVIG on inflammatory arthritis in mice is dependent on the Fc portion and independent of sialylation or basophils J. Immunol. 192 2014 5031 5038
    • (2014) J. Immunol. , vol.192 , pp. 5031-5038
    • Campbell, I.K.1
  • 46
    • 84938244540 scopus 로고    scopus 로고
    • Intravenous IgG (IVIG) and subcutaneous IgG (SCIG) preparations have comparable inhibitory effect on T cell activation, which is not dependent on IgG sialylation, monocytes or B cells
    • A.C. Issekutz, and et al. Intravenous IgG (IVIG) and subcutaneous IgG (SCIG) preparations have comparable inhibitory effect on T cell activation, which is not dependent on IgG sialylation, monocytes or B cells Clin. Immunol. 160 2015 123 132
    • (2015) Clin. Immunol. , vol.160 , pp. 123-132
    • Issekutz, A.C.1
  • 47
    • 84919723220 scopus 로고    scopus 로고
    • Inhibition of Fc(R-mediated phagocytosis by IVIg is independent of IgG-Fc sialylation and Fc(RIIb in human macrophages
    • S.Q. Nagelkerke, and et al. Inhibition of Fc(R-mediated phagocytosis by IVIg is independent of IgG-Fc sialylation and Fc(RIIb in human macrophages Blood 124 2014 3709 3718
    • (2014) Blood , vol.124 , pp. 3709-3718
    • Nagelkerke, S.Q.1
  • 48
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • R.M. Anthony, and et al. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway Nature 475 2011 110 113
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1
  • 49
    • 84856531046 scopus 로고    scopus 로고
    • Intravenous immunoglobulin expands regulatory T cells in autoimmune rheumatic disease
    • J. Bayry, and et al. Intravenous immunoglobulin expands regulatory T cells in autoimmune rheumatic disease J. Rheumatol. 39 2012 450 451
    • (2012) J. Rheumatol. , vol.39 , pp. 450-451
    • Bayry, J.1
  • 50
    • 38349137792 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy affects T regulatory cells by increasing their suppressive function
    • A. Kessel, and et al. Intravenous immunoglobulin therapy affects T regulatory cells by increasing their suppressive function J. Immunol. 179 2007 5571 5575
    • (2007) J. Immunol. , vol.179 , pp. 5571-5575
    • Kessel, A.1
  • 51
    • 84919873779 scopus 로고    scopus 로고
    • Fc-sialylated IgGs in intravenous immunoglobulins are not responsible for induction of regulatory T cells
    • C. Ramakrishna, and E.M. Cantin Fc-sialylated IgGs in intravenous immunoglobulins are not responsible for induction of regulatory T cells J. Allergy Clin. Immunol. 134 2014 1469
    • (2014) J. Allergy Clin. Immunol. , vol.134 , pp. 1469
    • Ramakrishna, C.1    Cantin, E.M.2
  • 52
    • 0036530010 scopus 로고    scopus 로고
    • Acquisition of potential N-glycosylation sites in the immunoglobulin variable region by somatic mutation is a distinctive feature of follicular lymphoma
    • D. Zhu, and et al. Acquisition of potential N-glycosylation sites in the immunoglobulin variable region by somatic mutation is a distinctive feature of follicular lymphoma Blood 99 2002 2562 2568
    • (2002) Blood , vol.99 , pp. 2562-2568
    • Zhu, D.1
  • 53
    • 61349137819 scopus 로고    scopus 로고
    • Immunoglobulin 1 (IgG1) Fc-glycosylation profiling of anti-citrullinated peptide antibodies from human serum
    • H.U. Scherer, and et al. Immunoglobulin 1 (IgG1) Fc-glycosylation profiling of anti-citrullinated peptide antibodies from human serum Proteomics Clin. Appl. 3 2009 106 115
    • (2009) Proteomics Clin. Appl. , vol.3 , pp. 106-115
    • Scherer, H.U.1
  • 55
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: Position effects on antigen binding and carbohydrate structure
    • A. Wright, and et al. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure EMBO J. 10 1991 2717
    • (1991) EMBO J. , vol.10 , pp. 2717
    • Wright, A.1
  • 56
    • 77953196497 scopus 로고    scopus 로고
    • Variable region heavy chain glycosylation determines the anticoagulant activity of a factor VIII antibody
    • M. Jacquemin Variable region heavy chain glycosylation determines the anticoagulant activity of a factor VIII antibody Haemophilia 16 2009 16 19
    • (2009) Haemophilia , vol.16 , pp. 16-19
    • Jacquemin, M.1
  • 57
    • 84887474033 scopus 로고    scopus 로고
    • Strategic addition of an N-linked glycan to a monoclonal antibody improves its HIV-1-neutralizing activity
    • R. Song, and et al. Strategic addition of an N-linked glycan to a monoclonal antibody improves its HIV-1-neutralizing activity Nat. Biotechnol. 31 2013 1047 1052
    • (2013) Nat. Biotechnol. , vol.31 , pp. 1047-1052
    • Song, R.1
  • 58
    • 84903459040 scopus 로고    scopus 로고
    • Redemption of autoantibodies on anergic B cells by variable-region glycosylation and mutation away from self-reactivity
    • Z. Sabouri, and et al. Redemption of autoantibodies on anergic B cells by variable-region glycosylation and mutation away from self-reactivity Proc. Natl. Acad. Sci. U. S. A. 111 2014 E2567 E2575
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E2567-E2575
    • Sabouri, Z.1
  • 59
    • 0026328063 scopus 로고
    • Glycosylation at the Fab portion of myeloma immunoglobulin G and increased fucosylated biantennary sugar chains: Structural analysis by high-performance liquid chromatography and antibody-lectin enzyme immunoassay using Lens culinaris agglutinin
    • N. Kinoshita, and et al. Glycosylation at the Fab portion of myeloma immunoglobulin G and increased fucosylated biantennary sugar chains: structural analysis by high-performance liquid chromatography and antibody-lectin enzyme immunoassay using Lens culinaris agglutinin Cancer Res. 51 1991 5888 5892
    • (1991) Cancer Res. , vol.51 , pp. 5888-5892
    • Kinoshita, N.1
  • 60
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • A. Youings, and et al. Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients Biochem. J. 314 1996 621 630
    • (1996) Biochem. J. , vol.314 , pp. 621-630
    • Youings, A.1
  • 61
    • 34247116573 scopus 로고    scopus 로고
    • Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor
    • C.M. Radcliffe, and et al. Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor J. Biol. Chem. 282 2007 7405 7415
    • (2007) J. Biol. Chem. , vol.282 , pp. 7405-7415
    • Radcliffe, C.M.1
  • 62
    • 78649840358 scopus 로고    scopus 로고
    • Glycosylation of surface Ig creates a functional bridge between human follicular lymphoma and microenvironmental lectins
    • V. Coelho, and et al. Glycosylation of surface Ig creates a functional bridge between human follicular lymphoma and microenvironmental lectins Proc. Natl. Acad. Sci. U. S. A. 107 2010 18587 18592
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 18587-18592
    • Coelho, V.1
  • 63
    • 0142059844 scopus 로고    scopus 로고
    • Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid
    • P. Tangvoranuntakul, and et al. Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid Proc. Natl. Acad. Sci. U. S. A. 100 2003 12045 12050
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12045-12050
    • Tangvoranuntakul, P.1
  • 64
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
    • D. Ghaderi, and et al. Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins Nat. Biotechnol. 28 2010 863 867
    • (2010) Nat. Biotechnol. , vol.28 , pp. 863-867
    • Ghaderi, D.1
  • 65
    • 0028798520 scopus 로고
    • Immunogenicity of N-glycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells
    • A. Noguchi, and et al. Immunogenicity of N-glycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells J. Biochem. 117 1995 59 62
    • (1995) J. Biochem. , vol.117 , pp. 59-62
    • Noguchi, A.1
  • 66
    • 78149290638 scopus 로고    scopus 로고
    • Chinese hamster ovary cells can produce galactose-α-1,3-galactose antigens on proteins
    • C.J. Bosques, and et al. Chinese hamster ovary cells can produce galactose-α-1,3-galactose antigens on proteins Nat. Biotechnol. 28 2010 1153 1156
    • (2010) Nat. Biotechnol. , vol.28 , pp. 1153-1156
    • Bosques, C.J.1
  • 67
    • 0001316176 scopus 로고
    • Hémagglutinines hétérogénétiques après injection de sérum de cheval
    • (in French)
    • M. Hanganutziu Hémagglutinines hétérogénétiques après injection de sérum de cheval CR Séances Soc. Biol. 91 1924 1457 1459 (in French)
    • (1924) CR Séances Soc. Biol. , vol.91 , pp. 1457-1459
    • Hanganutziu, M.1
  • 68
    • 0001202397 scopus 로고
    • Über die erzeugung heterospezifischer hämagglutinine durch injektion artfremden serums
    • (in German)
    • D.H. Deicher Über die erzeugung heterospezifischer hämagglutinine durch injektion artfremden serums Zeitschrift Hygiene Infektionskrankheiten 106 1926 561 579 (in German)
    • (1926) Zeitschrift Hygiene Infektionskrankheiten , vol.106 , pp. 561-579
    • Deicher, D.H.1
  • 69
    • 0015663485 scopus 로고
    • Foreign serum heterophile antibodies in patients receiving antithymocyte antisera
    • B. Pirofsky, and et al. Foreign serum heterophile antibodies in patients receiving antithymocyte antisera Blood 42 1973 385 393
    • (1973) Blood , vol.42 , pp. 385-393
    • Pirofsky, B.1
  • 70
    • 0017665490 scopus 로고
    • Antigen of serum sickness type of heterophile antibodies in human sera: Indentification as gangliosides with N-glycolylneuraminic acid
    • H. Higashi, and et al. Antigen of serum sickness type of heterophile antibodies in human sera: indentification as gangliosides with N-glycolylneuraminic acid Biochem. Biophys. Res. Commun. 79 1977 388 395
    • (1977) Biochem. Biophys. Res. Commun. , vol.79 , pp. 388-395
    • Higashi, H.1
  • 71
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • R.M. Anthony, and et al. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc Science 320 2008 373 376
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1
  • 72
    • 69949107840 scopus 로고    scopus 로고
    • A close look at human IgG sialylation and subclass distribution after lectin fractionation
    • J. Stadlmann, and et al. A close look at human IgG sialylation and subclass distribution after lectin fractionation Proteomics 9 2009 4143 4153
    • (2009) Proteomics , vol.9 , pp. 4143-4153
    • Stadlmann, J.1
  • 73
    • 77956187222 scopus 로고    scopus 로고
    • Analytical and functional aspects of antibody sialylation
    • J. Stadlmann, and et al. Analytical and functional aspects of antibody sialylation J. Clin. Immunol. 30 2010 15 19
    • (2010) J. Clin. Immunol. , vol.30 , pp. 15-19
    • Stadlmann, J.1
  • 74
    • 34548487155 scopus 로고    scopus 로고
    • High incidence of cetuximab-related infusion reactions in Tennessee and North Carolina and the association with atopic history
    • B.H. O'Neil, and et al. High incidence of cetuximab-related infusion reactions in Tennessee and North Carolina and the association with atopic history J. Clin. Oncol. 25 2007 3644 3648
    • (2007) J. Clin. Oncol. , vol.25 , pp. 3644-3648
    • O'Neil, B.H.1
  • 75
    • 0037075272 scopus 로고    scopus 로고
    • Pure red-cell aplasia and antierythropoietin antibodies in patients treated with recombinant erythropoietin
    • N. Casadevall, and et al. Pure red-cell aplasia and antierythropoietin antibodies in patients treated with recombinant erythropoietin N. Engl. J. Med. 346 2002 469 475
    • (2002) N. Engl. J. Med. , vol.346 , pp. 469-475
    • Casadevall, N.1
  • 76
    • 59449088566 scopus 로고    scopus 로고
    • Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-α-1,3-galactose
    • e422
    • S.P. Commins, and et al. Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-α-1,3-galactose J. Allergy Clin. Immunol. 123 2009 426 433 e422
    • (2009) J. Allergy Clin. Immunol. , vol.123 , pp. 426-433
    • Commins, S.P.1
  • 77
    • 79955613976 scopus 로고    scopus 로고
    • The relevance of tick bites to the production of IgE antibodies to the mammalian oligosaccharide galactose-α-1,3-galactose
    • e1286
    • S.P. Commins, and et al. The relevance of tick bites to the production of IgE antibodies to the mammalian oligosaccharide galactose-α-1,3-galactose J. Allergy Clin. Immunol. 127 2011 1286 1293 e1286
    • (2011) J. Allergy Clin. Immunol. , vol.127 , pp. 1286-1293
    • Commins, S.P.1
  • 80
    • 80051711268 scopus 로고    scopus 로고
    • Industry and regulatory experience of the glycosylation of monoclonal antibodies
    • E.K. Read, and et al. Industry and regulatory experience of the glycosylation of monoclonal antibodies Biotechnol. Appl. Biochem. 58 2011 213 219
    • (2011) Biotechnol. Appl. Biochem. , vol.58 , pp. 213-219
    • Read, E.K.1
  • 81
    • 79953861167 scopus 로고    scopus 로고
    • Acceptable changes in quality attributes of glycosylated biopharmaceuticals
    • M. Schiestl, and et al. Acceptable changes in quality attributes of glycosylated biopharmaceuticals Nat. Biotechnol. 29 2011 310 312
    • (2011) Nat. Biotechnol. , vol.29 , pp. 310-312
    • Schiestl, M.1
  • 82
    • 80053568475 scopus 로고    scopus 로고
    • A biosimilar industry view on the implementation of the WHO guidelines on evaluating similar biotherapeutic products
    • M. Schiestl A biosimilar industry view on the implementation of the WHO guidelines on evaluating similar biotherapeutic products Biologicals 39 2011 297 299
    • (2011) Biologicals , vol.39 , pp. 297-299
    • Schiestl, M.1
  • 84
    • 64549099901 scopus 로고    scopus 로고
    • N-linked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG
    • P.H.C. Van Berkel, and et al. N-linked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG Biotechnol. Prog. 25 2009 244 251
    • (2009) Biotechnol. Prog. , vol.25 , pp. 244-251
    • Van Berkel, P.H.C.1
  • 85
    • 60549102844 scopus 로고    scopus 로고
    • A study of monoclonal antibody-producing CHO cell lines: What makes a stable high producer?
    • J. Chusainow, and et al. A study of monoclonal antibody-producing CHO cell lines: what makes a stable high producer? Biotechnol. Bioeng. 102 2009 1182 1196
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 1182-1196
    • Chusainow, J.1
  • 86
    • 84922838909 scopus 로고    scopus 로고
    • Modulation of mAb quality attributes using microliter scale fed-batch cultures
    • Y. Rouiller, and et al. Modulation of mAb quality attributes using microliter scale fed-batch cultures Biotechnol. Prog. 30 2014 571 583
    • (2014) Biotechnol. Prog. , vol.30 , pp. 571-583
    • Rouiller, Y.1
  • 87
    • 84886241053 scopus 로고    scopus 로고
    • Automated disposable small scale reactor for high throughput bioprocess development: A proof of concept study
    • R. Bareither, and et al. Automated disposable small scale reactor for high throughput bioprocess development: a proof of concept study Biotechnol. Bioeng. 110 2013 3126 3138
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 3126-3138
    • Bareither, R.1
  • 88
    • 74849109030 scopus 로고    scopus 로고
    • Microwell engineering characterization for mammalian cell culture process development
    • T.A. Barrett, and et al. Microwell engineering characterization for mammalian cell culture process development Biotechnol. Bioeng. 105 2010 260 275
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 260-275
    • Barrett, T.A.1
  • 89
    • 84862212634 scopus 로고    scopus 로고
    • Quality attributes of recombinant therapeutic proteins: An assessment of impact on safety and efficacy as part of a quality by design development approach
    • A. Eon-Duval, and et al. Quality attributes of recombinant therapeutic proteins: an assessment of impact on safety and efficacy as part of a quality by design development approach Biotechnol. Prog. 28 2012 608 622
    • (2012) Biotechnol. Prog. , vol.28 , pp. 608-622
    • Eon-Duval, A.1
  • 90
    • 84902687071 scopus 로고    scopus 로고
    • Product quality considerations for mammalian cell culture process development and manufacturing
    • W. Zhou, A. Kantardjieff, Springer-Verlag Berlin
    • M.J. Gramer Product quality considerations for mammalian cell culture process development and manufacturing W. Zhou, A. Kantardjieff, Mammalian Cell Cultures for Biologics Manufacturing Vol. 139 2014 Springer-Verlag Berlin 123 166
    • (2014) Mammalian Cell Cultures for Biologics Manufacturing , vol.139 , pp. 123-166
    • Gramer, M.J.1
  • 91
    • 77953655955 scopus 로고    scopus 로고
    • Industrialization of mAb production technology: The bioprocessing industry at a crossroads
    • B. Kelley Industrialization of mAb production technology: the bioprocessing industry at a crossroads MAbs 1 2009 443 452
    • (2009) MAbs , vol.1 , pp. 443-452
    • Kelley, B.1
  • 92
    • 84903643820 scopus 로고    scopus 로고
    • Generation of monoclonal antibody-producing mammalian cell lines
    • S.C.L. Ho, and et al. Generation of monoclonal antibody-producing mammalian cell lines Pharm. Bioprocess. 1 2013 71 87
    • (2013) Pharm. Bioprocess. , vol.1 , pp. 71-87
    • Ho, S.C.L.1
  • 93
    • 84874173298 scopus 로고    scopus 로고
    • European perspective on biosimilars
    • M. Wadhwa, and R. Thorpe European perspective on biosimilars Bioanalysis 5 2013 521 524
    • (2013) Bioanalysis , vol.5 , pp. 521-524
    • Wadhwa, M.1    Thorpe, R.2
  • 94
    • 84872416874 scopus 로고    scopus 로고
    • Comments on the FDA draft guidance on biosimilar products
    • S-C. Chow, and et al. Comments on the FDA draft guidance on biosimilar products Statistics Med. 32 2013 364 369
    • (2013) Statistics Med. , vol.32 , pp. 364-369
    • Chow, S.-C.1
  • 95
    • 84877015785 scopus 로고    scopus 로고
    • Protein glycosylation control in mammalian cell culture: Past precedents and contemporary prospects
    • P. Hossler Protein glycosylation control in mammalian cell culture: past precedents and contemporary prospects Adv. Biochem. Eng. Biotechnol. 127 2012 187 219
    • (2012) Adv. Biochem. Eng. Biotechnol. , vol.127 , pp. 187-219
    • Hossler, P.1
  • 96
    • 84869878604 scopus 로고    scopus 로고
    • Functional heterogeneity and heritability in CHO cell populations
    • S.L. Davies, and et al. Functional heterogeneity and heritability in CHO cell populations Biotechnol. Bioeng. 110 2013 260 274
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 260-274
    • Davies, S.L.1
  • 97
    • 84855237715 scopus 로고    scopus 로고
    • IRES-mediated Tricistronic vectors for enhancing generation of high monoclonal antibody expressing CHO cell lines
    • S.C.L. Ho, and et al. IRES-mediated Tricistronic vectors for enhancing generation of high monoclonal antibody expressing CHO cell lines J. Biotechnol. 157 2012 130 139
    • (2012) J. Biotechnol. , vol.157 , pp. 130-139
    • Ho, S.C.L.1
  • 98
    • 84877354063 scopus 로고    scopus 로고
    • Control of IgG LC:HC ratio in stably transfected CHO cells and study of the impact on expression, aggregation, glycosylation and conformational stability
    • S.C.L. Ho, and et al. Control of IgG LC:HC ratio in stably transfected CHO cells and study of the impact on expression, aggregation, glycosylation and conformational stability J. Biotechnol. 165 2013 157 166
    • (2013) J. Biotechnol. , vol.165 , pp. 157-166
    • Ho, S.C.L.1
  • 99
    • 77958518175 scopus 로고    scopus 로고
    • Cell culture processes for monoclonal antibody production
    • F. Li, and et al. Cell culture processes for monoclonal antibody production MAbs 2 2010 466 479
    • (2010) MAbs , vol.2 , pp. 466-479
    • Li, F.1
  • 100
    • 75149112725 scopus 로고    scopus 로고
    • Recombinant glucocerebrosidase (imiglucerase) as a therapy for Gaucher disease
    • G.M. Pastores Recombinant glucocerebrosidase (imiglucerase) as a therapy for Gaucher disease BioDrugs 24 2010 41 47
    • (2010) BioDrugs , vol.24 , pp. 41-47
    • Pastores, G.M.1
  • 101
    • 84942919876 scopus 로고    scopus 로고
    • In vitro glycoengineering of IgG1 and its effect on Fc receptor binding and ADCC activity
    • M. Thomann, and et al. In vitro glycoengineering of IgG1 and its effect on Fc receptor binding and ADCC activity PLoS One 10 2015 e0134949
    • (2015) PLoS One , vol.10 , pp. e0134949
    • Thomann, M.1
  • 102
    • 84954373522 scopus 로고    scopus 로고
    • Enhanced sialylation of a human chimeric IgG1 variant produced in human and rodent cell lines
    • Y. Mimura, and et al. Enhanced sialylation of a human chimeric IgG1 variant produced in human and rodent cell lines J. Immunol. Methods 2015 10.1016/j.jim.2015.11.009
    • (2015) J. Immunol. Methods
    • Mimura, Y.1
  • 103
    • 33751002037 scopus 로고    scopus 로고
    • Lectin-resistant CHO glycosylation mutants
    • S.K. Patnaik, and P. Stanley Lectin-resistant CHO glycosylation mutants Methods Enzymol. 416 2006 159 182
    • (2006) Methods Enzymol. , vol.416 , pp. 159-182
    • Patnaik, S.K.1    Stanley, P.2
  • 104
    • 84879145733 scopus 로고    scopus 로고
    • CHO glycosylation mutants as potential host cells to produce therapeutic proteins with enhanced efficacy
    • P. Zhang, and et al. CHO glycosylation mutants as potential host cells to produce therapeutic proteins with enhanced efficacy Adv. Biochem. Eng. Biotechnol. 131 2013 63 87
    • (2013) Adv. Biochem. Eng. Biotechnol. , vol.131 , pp. 63-87
    • Zhang, P.1
  • 105
    • 84861376809 scopus 로고    scopus 로고
    • Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant
    • P. Zhang, and et al. Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant Glycobiology 22 2012 897 911
    • (2012) Glycobiology , vol.22 , pp. 897-911
    • Zhang, P.1
  • 106
    • 84903703251 scopus 로고    scopus 로고
    • Precision genome editing: A small revolution for glycobiology
    • C. Steentoft, and et al. Precision genome editing: a small revolution for glycobiology Glycobiology 24 2014 663 680
    • (2014) Glycobiology , vol.24 , pp. 663-680
    • Steentoft, C.1
  • 107
    • 0024278423 scopus 로고
    • The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues
    • W.C. Wang, and R.D. Cummings The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues J. Biol. Chem. 263 1988 4576 4585
    • (1988) J. Biol. Chem. , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 108
    • 0026020575 scopus 로고
    • Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins
    • R.N. Knibbs, and et al. Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins J. Biol. Chem. 266 1991 83 88
    • (1991) J. Biol. Chem. , vol.266 , pp. 83-88
    • Knibbs, R.N.1
  • 109
    • 84860912187 scopus 로고    scopus 로고
    • Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation
    • D. Ghaderi, and et al. Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation Biotechnol. Genet. Eng. Rev. 28 2012 147 175
    • (2012) Biotechnol. Genet. Eng. Rev. , vol.28 , pp. 147-175
    • Ghaderi, D.1
  • 110
    • 54549083448 scopus 로고    scopus 로고
    • The Golgi CMP-sialic acid transporter: A new CHO mutant provides functional insights
    • S.F. Lim, and et al. The Golgi CMP-sialic acid transporter: a new CHO mutant provides functional insights Glycobiology 18 2008 851 860
    • (2008) Glycobiology , vol.18 , pp. 851-860
    • Lim, S.F.1
  • 111
    • 77953025411 scopus 로고    scopus 로고
    • RCA-I-resistant CHO mutant cells have dysfunctional GnT i and expression of normal GnT i in these mutants enhances sialylation of recombinant erythropoietin
    • J.S. Goh, and et al. RCA-I-resistant CHO mutant cells have dysfunctional GnT I and expression of normal GnT I in these mutants enhances sialylation of recombinant erythropoietin Metab. Eng. 12 2010 360 368
    • (2010) Metab. Eng. , vol.12 , pp. 360-368
    • Goh, J.S.1
  • 112
    • 84891945296 scopus 로고    scopus 로고
    • Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT i function
    • J.S. Goh, and et al. Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT I function Biotechnol. J. 9 2014 100 109
    • (2014) Biotechnol. J. , vol.9 , pp. 100-109
    • Goh, J.S.1
  • 113
    • 0032981699 scopus 로고    scopus 로고
    • Toward controlling gene expression at will: Selection and design of zinc finger domains recognizing each of the 5′-GNN-3′ DNA target sequences
    • D.J. Segal, and et al. Toward controlling gene expression at will: selection and design of zinc finger domains recognizing each of the 5′-GNN-3′ DNA target sequences Proc. Natl. Acad. Sci. U. S. A. 96 1999 2758 2763
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2758-2763
    • Segal, D.J.1
  • 114
    • 0034602243 scopus 로고    scopus 로고
    • Insights into the molecular recognition of the 5′-GNN-3′ family of DNA sequences by zinc finger domains
    • B. Dreier, and et al. Insights into the molecular recognition of the 5′-GNN-3′ family of DNA sequences by zinc finger domains J. Mol. Biol. 303 2000 489 502
    • (2000) J. Mol. Biol. , vol.303 , pp. 489-502
    • Dreier, B.1
  • 115
    • 0037040240 scopus 로고    scopus 로고
    • Validated zinc finger protein designs for all 16 GNN DNA triplet targets
    • Q. Liu, and et al. Validated zinc finger protein designs for all 16 GNN DNA triplet targets J. Biol. Chem. 277 2002 3850 3856
    • (2002) J. Biol. Chem. , vol.277 , pp. 3850-3856
    • Liu, Q.1
  • 116
    • 34547605763 scopus 로고    scopus 로고
    • Zinc finger targeter (ZiFiT): An engineered zinc finger/target site design tool
    • J.D. Sander, and et al. Zinc finger targeter (ZiFiT): an engineered zinc finger/target site design tool Nucleic Acids Res. 35 2007 W599 W605
    • (2007) Nucleic Acids Res. , vol.35 , pp. W599-W605
    • Sander, J.D.1
  • 117
    • 79960064013 scopus 로고    scopus 로고
    • Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting
    • T. Cermak, and et al. Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting Nucleic Acids Res. 39 2011 e82
    • (2011) Nucleic Acids Res. , vol.39 , pp. e82
    • Cermak, T.1
  • 118
    • 79551685675 scopus 로고    scopus 로고
    • A TALE nuclease architecture for efficient genome editing
    • J.C. Miller, and et al. A TALE nuclease architecture for efficient genome editing Nat. Biotechnol. 29 2011 143 148
    • (2011) Nat. Biotechnol. , vol.29 , pp. 143-148
    • Miller, J.C.1
  • 119
    • 72149110399 scopus 로고    scopus 로고
    • Breaking the code of DNA binding specificity of TAL-type III effectors
    • J. Boch, and et al. Breaking the code of DNA binding specificity of TAL-type III effectors Science 326 2009 1509 1512
    • (2009) Science , vol.326 , pp. 1509-1512
    • Boch, J.1
  • 120
    • 72149090954 scopus 로고    scopus 로고
    • A simple cipher governs DNA recognition by TAL effectors
    • M.J. Moscou, and A.J. Bogdanove A simple cipher governs DNA recognition by TAL effectors Science 326 2009 1501
    • (2009) Science , vol.326 , pp. 1501
    • Moscou, M.J.1    Bogdanove, A.J.2
  • 121
    • 84861170955 scopus 로고    scopus 로고
    • A transcription activator-like effector toolbox for genome engineering
    • N.E. Sanjana, and et al. A transcription activator-like effector toolbox for genome engineering Nat. Protocols 7 2012 171 192
    • (2012) Nat. Protocols , vol.7 , pp. 171-192
    • Sanjana, N.E.1
  • 122
    • 84860747716 scopus 로고    scopus 로고
    • FLASH assembly of TALENs for high-throughput genome editing
    • D. Reyon, and et al. FLASH assembly of TALENs for high-throughput genome editing Nat. Biotechnol. 30 2012 460 465
    • (2012) Nat. Biotechnol. , vol.30 , pp. 460-465
    • Reyon, D.1
  • 123
    • 84873729095 scopus 로고    scopus 로고
    • Multiplex genome engineering using CRISPR/Cas systems
    • L. Cong, and et al. Multiplex genome engineering using CRISPR/Cas systems Science 339 2013 819 823
    • (2013) Science , vol.339 , pp. 819-823
    • Cong, L.1
  • 124
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • P. Mali, and et al. RNA-guided human genome engineering via Cas9 Science 339 2013 823 826
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1
  • 125
    • 84940601641 scopus 로고    scopus 로고
    • One-step generation of triple knockout CHO cell lines using CRISPR/Cas9 and fluorescent enrichment
    • L.M. Grav, and et al. One-step generation of triple knockout CHO cell lines using CRISPR/Cas9 and fluorescent enrichment Biotechnol. J. 10 2015 1446 1456
    • (2015) Biotechnol. J. , vol.10 , pp. 1446-1456
    • Grav, L.M.1
  • 126
    • 84904813279 scopus 로고    scopus 로고
    • CHOPCHOP: A CRISPR/Cas9 and TALEN web tool for genome editing
    • T.G. Montague, and et al. CHOPCHOP: a CRISPR/Cas9 and TALEN web tool for genome editing Nucleic Acids Res. 42 2014 W401 W407
    • (2014) Nucleic Acids Res. , vol.42 , pp. W401-W407
    • Montague, T.G.1
  • 127
    • 84902095352 scopus 로고    scopus 로고
    • Genome-wide binding of the CRISPR endonuclease Cas9 in mammalian cells
    • X. Wu, and et al. Genome-wide binding of the CRISPR endonuclease Cas9 in mammalian cells Nat. Biotechnol. 32 2014 670 676
    • (2014) Nat. Biotechnol. , vol.32 , pp. 670-676
    • Wu, X.1
  • 128
    • 84903545084 scopus 로고    scopus 로고
    • Genome-wide analysis reveals characteristics of off-target sites bound by the Cas9 endonuclease
    • C. Kuscu, and et al. Genome-wide analysis reveals characteristics of off-target sites bound by the Cas9 endonuclease Nat. Biotechnol. 32 2014 677 683
    • (2014) Nat. Biotechnol. , vol.32 , pp. 677-683
    • Kuscu, C.1
  • 129
    • 84895925005 scopus 로고    scopus 로고
    • Applying quality by design to glycoprotein therapeutics: Experimental and computational efforts of process control
    • P.M.J. Jedrzejewski, and et al. Applying quality by design to glycoprotein therapeutics: experimental and computational efforts of process control Pharm. Bioprocess. 1 2013 51 69
    • (2013) Pharm. Bioprocess. , vol.1 , pp. 51-69
    • Jedrzejewski, P.M.J.1
  • 130
    • 68749083515 scopus 로고    scopus 로고
    • Roadmap for implementation of quality by design (QbD) for biotechnology products
    • A.S. Rathore Roadmap for implementation of quality by design (QbD) for biotechnology products Trends Biotechnol. 27 2009 546 553
    • (2009) Trends Biotechnol. , vol.27 , pp. 546-553
    • Rathore, A.S.1
  • 131
    • 78650201043 scopus 로고    scopus 로고
    • Towards the implementation of quality by design to the production of therapeutic monoclonal antibodies with desired glycosylation patterns
    • I.J. del Val, and et al. Towards the implementation of quality by design to the production of therapeutic monoclonal antibodies with desired glycosylation patterns Biotechnol. Prog. 26 2010 1505 1527
    • (2010) Biotechnol. Prog. , vol.26 , pp. 1505-1527
    • Del Val, I.J.1
  • 132
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • J. Hodoniczky, and et al. Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro Biotechnol. Prog. 21 2005 1644 1652
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1
  • 133
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • R.L. Shields, and et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity J. Biol. Chem. 277 2002 26733 26740
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1
  • 136
    • 84885636807 scopus 로고    scopus 로고
    • An automated robotic platform for rapid profiling oligosaccharide analysis of monoclonal antibodies directly from cell culture
    • M. Doherty, and et al. An automated robotic platform for rapid profiling oligosaccharide analysis of monoclonal antibodies directly from cell culture Anal. Biochem. 442 2013 10 18
    • (2013) Anal. Biochem. , vol.442 , pp. 10-18
    • Doherty, M.1
  • 137
    • 19944427570 scopus 로고    scopus 로고
    • High-throughput protein glycomics: Combined use of chemoselective glycoblotting and MALDI-TOF/TOF mass spectrometry
    • S. Nishimura, and et al. High-throughput protein glycomics: combined use of chemoselective glycoblotting and MALDI-TOF/TOF mass spectrometry Angew Chem. Int. Ed. Engl. 44 2004 91 96
    • (2004) Angew Chem. Int. Ed. Engl. , vol.44 , pp. 91-96
    • Nishimura, S.1
  • 138
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • H. Zhang, and et al. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 21 2003 660 666
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1
  • 139
    • 84884264843 scopus 로고    scopus 로고
    • Automated, high-throughput IgG-antibody glycoprofiling platform
    • H. Stockmann, and et al. Automated, high-throughput IgG-antibody glycoprofiling platform Anal. Chem. 85 2013 8841 8849
    • (2013) Anal. Chem. , vol.85 , pp. 8841-8849
    • Stockmann, H.1
  • 140
    • 84868553080 scopus 로고    scopus 로고
    • High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples
    • D. Reusch, and et al. High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples Anal. Biochem. 432 2013 82 89
    • (2013) Anal. Biochem. , vol.432 , pp. 82-89
    • Reusch, D.1
  • 141
    • 84893737131 scopus 로고    scopus 로고
    • Design of experiments applications in bioprocessing: Concepts and approach
    • V. Kumar, and et al. Design of experiments applications in bioprocessing: concepts and approach Biotechnol. Prog. 30 2014 86 99
    • (2014) Biotechnol. Prog. , vol.30 , pp. 86-99
    • Kumar, V.1
  • 142
    • 80054970831 scopus 로고    scopus 로고
    • On-line characterization of monoclonal antibody variants by liquid chromatography-mass spectrometry operating in a two-dimensional format
    • M. Alvarez, and et al. On-line characterization of monoclonal antibody variants by liquid chromatography-mass spectrometry operating in a two-dimensional format Anal. Biochem. 419 2011 17 25
    • (2011) Anal. Biochem. , vol.419 , pp. 17-25
    • Alvarez, M.1
  • 143
    • 79955591082 scopus 로고    scopus 로고
    • A high-throughput microchip-based glycan screening assay for antibody cell culture samples
    • J. Primack, and et al. A high-throughput microchip-based glycan screening assay for antibody cell culture samples Electrophoresis 32 2011 1129 1132
    • (2011) Electrophoresis , vol.32 , pp. 1129-1132
    • Primack, J.1
  • 144
    • 70350633078 scopus 로고    scopus 로고
    • Characterization of IgG N-glycans employing a microfluidic chip that integrates glycan cleavage, sample purification, LC separation, and MS detection
    • M.A. Bynum, and et al. Characterization of IgG N-glycans employing a microfluidic chip that integrates glycan cleavage, sample purification, LC separation, and MS detection Anal. Chem. 81 2009 8818 8825
    • (2009) Anal. Chem. , vol.81 , pp. 8818-8825
    • Bynum, M.A.1
  • 145
    • 79961191745 scopus 로고    scopus 로고
    • The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line
    • X. Xu, and et al. The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line Nat. Biotechnol. 29 2011 735 741
    • (2011) Nat. Biotechnol. , vol.29 , pp. 735-741
    • Xu, X.1
  • 146
    • 70349978981 scopus 로고    scopus 로고
    • A mathematical model to derive N-glycan structures and cellular enzyme activities from mass spectrometric data
    • F.J. Krambeck, and et al. A mathematical model to derive N-glycan structures and cellular enzyme activities from mass spectrometric data Glycobiology 19 2009 1163 1175
    • (2009) Glycobiology , vol.19 , pp. 1163-1175
    • Krambeck, F.J.1
  • 147
    • 28844473175 scopus 로고    scopus 로고
    • A mathematical model of N-linked glycosylation
    • F.J. Krambeck, and M.J. Betenbaugh A mathematical model of N-linked glycosylation Biotechnol. Bioeng. 92 2005 711 728
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 711-728
    • Krambeck, F.J.1    Betenbaugh, M.J.2
  • 148
    • 0343581263 scopus 로고    scopus 로고
    • A mathematical model of N-linked glycoform biosynthesis
    • P. Umana, and J.E. Bailey A mathematical model of N-linked glycoform biosynthesis Biotechnol. Bioeng. 55 1997 890 908
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 890-908
    • Umana, P.1    Bailey, J.E.2
  • 149
    • 40249093192 scopus 로고    scopus 로고
    • Systems analysis of N-glycan processing in mammalian cells
    • P. Hossler, and et al. Systems analysis of N-glycan processing in mammalian cells PLoS One 2 2007 e713
    • (2007) PLoS One , vol.2 , pp. e713
    • Hossler, P.1
  • 150
    • 84896474989 scopus 로고    scopus 로고
    • Towards controlling the glycoform: A model framework linking extracellular metabolites to antibody glycosylation
    • P.M. Jedrzejewski, and et al. Towards controlling the glycoform: a model framework linking extracellular metabolites to antibody glycosylation Int. J. Mol. Sci. 15 2014 4492 4522
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 4492-4522
    • Jedrzejewski, P.M.1
  • 151
    • 82955237386 scopus 로고    scopus 로고
    • A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus
    • I. Jimenez del Val, and et al. A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus Biotechnol. Prog. 27 2011 1730 1743
    • (2011) Biotechnol. Prog. , vol.27 , pp. 1730-1743
    • Jimenez Del Val, I.1
  • 153
    • 84969679006 scopus 로고    scopus 로고
    • Bespoke affinity ligands for the purification of therapeutic proteins
    • G. El Khoury, and et al. Bespoke affinity ligands for the purification of therapeutic proteins Pharm. Bioprocess 3 2015 139 152
    • (2015) Pharm. Bioprocess , vol.3 , pp. 139-152
    • El Khoury, G.1
  • 154
    • 77958589701 scopus 로고    scopus 로고
    • Recovery and purification process development for monoclonal antibody production
    • H.F. Liu, and et al. Recovery and purification process development for monoclonal antibody production MAbs 2 2010 480 499
    • (2010) MAbs , vol.2 , pp. 480-499
    • Liu, H.F.1
  • 155
    • 84891371507 scopus 로고    scopus 로고
    • High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol
    • P. Gagnon, and et al. High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol J. Chromatogr. A 1324 2014 171 180
    • (2014) J. Chromatogr. A , vol.1324 , pp. 171-180
    • Gagnon, P.1
  • 156
    • 84916199227 scopus 로고    scopus 로고
    • Chromatin-mediated depression of fractionation performance on electronegative multimodal chromatography media, its prevention, and ramifications for purification of immunoglobulin G
    • P. Gagnon, and et al. Chromatin-mediated depression of fractionation performance on electronegative multimodal chromatography media, its prevention, and ramifications for purification of immunoglobulin G J. Chromatogr. A 1374 2014 145 155
    • (2014) J. Chromatogr. A , vol.1374 , pp. 145-155
    • Gagnon, P.1
  • 157
    • 84855441834 scopus 로고    scopus 로고
    • Technology trends in antibody purification
    • P. Gagnon Technology trends in antibody purification J. Chromatogr. A 1221 2012 57 70
    • (2012) J. Chromatogr. A , vol.1221 , pp. 57-70
    • Gagnon, P.1
  • 158
    • 84862987183 scopus 로고    scopus 로고
    • Using lectins to harvest the plasma/serum glycoproteome
    • S. Fanayan, and et al. Using lectins to harvest the plasma/serum glycoproteome Electrophoresis 33 2012 1746 1754
    • (2012) Electrophoresis , vol.33 , pp. 1746-1754
    • Fanayan, S.1
  • 159
    • 0029990425 scopus 로고    scopus 로고
    • Specificity of C-glycoside complexation by mannose/glucose specific lectins
    • R.V. Weatherman, and et al. Specificity of C-glycoside complexation by mannose/glucose specific lectins Biochemistry 35 1996 3619 3624
    • (1996) Biochemistry , vol.35 , pp. 3619-3624
    • Weatherman, R.V.1
  • 160
    • 0027317526 scopus 로고
    • Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins
    • A. Pusztai, and et al. Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins Br. J. Nutr. 70 1993 313 321
    • (1993) Br. J. Nutr. , vol.70 , pp. 313-321
    • Pusztai, A.1
  • 161
    • 0037093547 scopus 로고    scopus 로고
    • Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose
    • Y. Bourne, and et al. Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose Biochemical J 364 2002 173 180
    • (2002) Biochemical J , vol.364 , pp. 173-180
    • Bourne, Y.1
  • 162
    • 56249102761 scopus 로고    scopus 로고
    • Capture of cell culture-derived influenza virus by lectins: Strain independent, but host cell dependent
    • L. Opitz, and et al. Capture of cell culture-derived influenza virus by lectins: strain independent, but host cell dependent J. Virol. Methods 154 2008 61 68
    • (2008) J. Virol. Methods , vol.154 , pp. 61-68
    • Opitz, L.1
  • 163
    • 33845197089 scopus 로고    scopus 로고
    • Lectin-affinity chromatography for downstream processing of MDCK cell culture derived human influenza A viruses
    • L. Opitz, and et al. Lectin-affinity chromatography for downstream processing of MDCK cell culture derived human influenza A viruses Vaccine 25 2007 939 947
    • (2007) Vaccine , vol.25 , pp. 939-947
    • Opitz, L.1
  • 164
    • 84904311566 scopus 로고    scopus 로고
    • Phenylboronic acid as a multi-modal ligand for the capture of monoclonal antibodies: Development and optimization of a washing step
    • R. dos Santos, and et al. Phenylboronic acid as a multi-modal ligand for the capture of monoclonal antibodies: development and optimization of a washing step J. Chromatogr. A 1355 2014 115 124
    • (2014) J. Chromatogr. A , vol.1355 , pp. 115-124
    • Dos Santos, R.1
  • 165
    • 0037457414 scopus 로고    scopus 로고
    • Evaluation of phenylboronate agarose for industrial-scale purification of erythropoietin from mammalian cell cultures
    • D. Zanette, and et al. Evaluation of phenylboronate agarose for industrial-scale purification of erythropoietin from mammalian cell cultures J. Biotechnol. 101 2003 275 287
    • (2003) J. Biotechnol. , vol.101 , pp. 275-287
    • Zanette, D.1
  • 166
    • 78650380787 scopus 로고    scopus 로고
    • Synthesis of magnetic nanoparticles with immobilized aminophenylboronic acid for selective capture of glycoproteins
    • Z-A. Lin, and et al. Synthesis of magnetic nanoparticles with immobilized aminophenylboronic acid for selective capture of glycoproteins J. Mater. Chem. 21 2011 518 524
    • (2011) J. Mater. Chem. , vol.21 , pp. 518-524
    • Lin, Z.-A.1
  • 167
    • 45249112571 scopus 로고    scopus 로고
    • Using detonation nanodiamond for the specific capture of glycoproteins
    • W.S. Yeap, and et al. Using detonation nanodiamond for the specific capture of glycoproteins Anal. Chem. 80 2008 4659 4665
    • (2008) Anal. Chem. , vol.80 , pp. 4659-4665
    • Yeap, W.S.1
  • 168
    • 55849134876 scopus 로고    scopus 로고
    • Facile synthesis of aminophenylboronic acid-functionalized magnetic nanoparticles for selective separation of glycopeptides and glycoproteins
    • W. Zhou, and et al. Facile synthesis of aminophenylboronic acid-functionalized magnetic nanoparticles for selective separation of glycopeptides and glycoproteins Chem. Commun. 43 2008 5577 5579
    • (2008) Chem. Commun. , vol.43 , pp. 5577-5579
    • Zhou, W.1
  • 169
    • 84896812755 scopus 로고    scopus 로고
    • Facile synthesis of boronic acid-functionalized magnetic carbon nanotubes for highly specific enrichment of glycopeptides
    • R. Ma, and et al. Facile synthesis of boronic acid-functionalized magnetic carbon nanotubes for highly specific enrichment of glycopeptides Nanoscale 6 2014 3150 3156
    • (2014) Nanoscale , vol.6 , pp. 3150-3156
    • Ma, R.1
  • 170
    • 79959870210 scopus 로고    scopus 로고
    • A Wulff-type boronate for boronate affinity capture of cis-diol compounds at medium acidic pH condition
    • H. Li, and et al. A Wulff-type boronate for boronate affinity capture of cis-diol compounds at medium acidic pH condition Chem. Commun. 47 2011 8169 8171
    • (2011) Chem. Commun. , vol.47 , pp. 8169-8171
    • Li, H.1
  • 171
    • 84897536602 scopus 로고    scopus 로고
    • Benzoboroxole-functionalized magnetic core/shell microspheres for highly specific enrichment of glycoproteins under physiological conditions
    • Y. Zhang, and et al. Benzoboroxole-functionalized magnetic core/shell microspheres for highly specific enrichment of glycoproteins under physiological conditions Small 10 2014 1379 1386
    • (2014) Small , vol.10 , pp. 1379-1386
    • Zhang, Y.1
  • 172
    • 80155178883 scopus 로고    scopus 로고
    • Label-free detection of enhanced saccharide binding at pH 7.4 to nanoparticulate benzoboroxole based receptor units
    • S. Schumacher, and et al. Label-free detection of enhanced saccharide binding at pH 7.4 to nanoparticulate benzoboroxole based receptor units J. Mol. Recog. 24 2011 953 959
    • (2011) J. Mol. Recog. , vol.24 , pp. 953-959
    • Schumacher, S.1
  • 173
    • 59649120676 scopus 로고    scopus 로고
    • Glycoprotein synthesis: An update
    • D.P. Gamblin, and et al. Glycoprotein synthesis: an update Chem. Rev. 109 2009 131 163
    • (2009) Chem. Rev. , vol.109 , pp. 131-163
    • Gamblin, D.P.1
  • 174
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: Production and purification
    • A.C. Roque, and et al. Antibodies and genetically engineered related molecules: production and purification Biotechnol. Prog. 20 2004 639 654
    • (2004) Biotechnol. Prog. , vol.20 , pp. 639-654
    • Roque, A.C.1
  • 175
    • 84906732461 scopus 로고    scopus 로고
    • Affinity ligands for glycoprotein purification based on the multi-component Ugi reaction
    • C. Chen, and et al. Affinity ligands for glycoprotein purification based on the multi-component Ugi reaction J. Chromatogr. B 969 2014 171 180
    • (2014) J. Chromatogr. B , vol.969 , pp. 171-180
    • Chen, C.1
  • 176
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • K. Marino, and et al. A systematic approach to protein glycosylation analysis: a path through the maze Nat. Chem. Biol. 6 2010 713 723
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 713-723
    • Marino, K.1
  • 177
    • 74249106136 scopus 로고    scopus 로고
    • What does the future hold for top down mass spectrometry?
    • B.A. Garcia What does the future hold for top down mass spectrometry? J. Am. Soc. Mass Spectrom. 21 2010 193 202
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 193-202
    • Garcia, B.A.1
  • 178
    • 81255144037 scopus 로고    scopus 로고
    • Unit mass baseline resolution for an intact 148 kDa therapeutic monoclonal antibody by Fourier transform ion cyclotron resonance mass spectrometry
    • S.G. Valeja, and et al. Unit mass baseline resolution for an intact 148 kDa therapeutic monoclonal antibody by Fourier transform ion cyclotron resonance mass spectrometry Anal. Chem. 83 2011 8391 8395
    • (2011) Anal. Chem. , vol.83 , pp. 8391-8395
    • Valeja, S.G.1
  • 179
    • 59149092065 scopus 로고    scopus 로고
    • Mass spectrometry for structural characterization of therapeutic antibodies
    • Z. Zhang, and et al. Mass spectrometry for structural characterization of therapeutic antibodies Mass Spectrom. Rev. 28 2009 147 176
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 147-176
    • Zhang, Z.1
  • 180
    • 48349147103 scopus 로고    scopus 로고
    • Top-down identification and characterization of biomolecules by mass spectrometry
    • K. Breuker, and et al. Top-down identification and characterization of biomolecules by mass spectrometry J. Am. Soc. Mass Spectrom. 19 2008 1045 1053
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1045-1053
    • Breuker, K.1
  • 181
    • 20244385589 scopus 로고    scopus 로고
    • Characterization by liquid chromatography combined with mass spectrometry of monoclonal anti-IGF-1 receptor antibodies produced in CHO and NS0 cells
    • A. Beck, and et al. Characterization by liquid chromatography combined with mass spectrometry of monoclonal anti-IGF-1 receptor antibodies produced in CHO and NS0 cells J. Chromatogr. B 819 2005 203 218
    • (2005) J. Chromatogr. B , vol.819 , pp. 203-218
    • Beck, A.1
  • 182
    • 77958549515 scopus 로고    scopus 로고
    • Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies
    • H. Xie, and et al. Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies MAbs 2 2010 379 394
    • (2010) MAbs , vol.2 , pp. 379-394
    • Xie, H.1
  • 183
    • 34547751263 scopus 로고    scopus 로고
    • Characterization of variable regions of monoclonal antibodies by top-down mass spectrometry
    • Z. Zhang, and B. Shah Characterization of variable regions of monoclonal antibodies by top-down mass spectrometry Anal. Chem. 79 2007 5723 5729
    • (2007) Anal. Chem. , vol.79 , pp. 5723-5729
    • Zhang, Z.1    Shah, B.2
  • 184
    • 67650754060 scopus 로고    scopus 로고
    • Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer
    • P.V. Bondarenko, and et al. Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer J. Am. Soc. Mass Spectrom. 20 2009 1415 1424
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1415-1424
    • Bondarenko, P.V.1
  • 185
    • 84872503060 scopus 로고    scopus 로고
    • Characterization of therapeutic antibodies and related products
    • A. Beck, and et al. Characterization of therapeutic antibodies and related products Anal. Chem. 85 2013 715 736
    • (2013) Anal. Chem. , vol.85 , pp. 715-736
    • Beck, A.1
  • 186
    • 84873404470 scopus 로고    scopus 로고
    • High-throughput IgG Fc N-glycosylation profiling by mass spectrometry of glycopeptides
    • M.P. Bakovic, and et al. High-throughput IgG Fc N-glycosylation profiling by mass spectrometry of glycopeptides J. Proteome Res. 12 2013 821 831
    • (2013) J. Proteome Res. , vol.12 , pp. 821-831
    • Bakovic, M.P.1
  • 187
    • 33644841035 scopus 로고    scopus 로고
    • Tools for glycoproteomic analysis: Size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites
    • G. Alvarez-Manilla, and et al. Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites J. Proteome Res. 5 2006 701 708
    • (2006) J. Proteome Res. , vol.5 , pp. 701-708
    • Alvarez-Manilla, G.1
  • 188
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Y. Wada, and et al. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics Anal. Chem. 76 2004 6560 6565
    • (2004) Anal. Chem. , vol.76 , pp. 6560-6565
    • Wada, Y.1
  • 189
    • 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
    • P. Hagglund, and et al. 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
    • Hagglund, P.1
  • 190
    • 33646005544 scopus 로고    scopus 로고
    • Separation of isomeric 2-aminopyridine derivatized N-glycans and N-glycopeptides of human serum immunoglobulin G by using a zwitterionic type of hydrophilic-interaction chromatography
    • Y. Takegawa, and et al. Separation of isomeric 2-aminopyridine derivatized N-glycans and N-glycopeptides of human serum immunoglobulin G by using a zwitterionic type of hydrophilic-interaction chromatography J. Chromatogr. A 1113 2006 177 181
    • (2006) J. Chromatogr. A , vol.1113 , pp. 177-181
    • Takegawa, Y.1
  • 191
    • 26444476996 scopus 로고    scopus 로고
    • Protein glycosylation analysis by liquid chromatography-mass spectrometry
    • M. Wuhrer, and et al. Protein glycosylation analysis by liquid chromatography-mass spectrometry J. Chromatogr. B 825 2005 124 133
    • (2005) J. Chromatogr. B , vol.825 , pp. 124-133
    • Wuhrer, M.1
  • 192
    • 13244291497 scopus 로고    scopus 로고
    • Protein glycosylation analyzed by normal-phase nano-liquid chromatography - Mass spectrometry of glycopeptides
    • M. Wuhrer, and et al. Protein glycosylation analyzed by normal-phase nano-liquid chromatography - mass spectrometry of glycopeptides Anal. Chem. 77 2005 886 894
    • (2005) Anal. Chem. , vol.77 , pp. 886-894
    • Wuhrer, M.1
  • 193
    • 77951572809 scopus 로고    scopus 로고
    • Characterizing protein glycosylation sites through higher-energy C-trap dissociation
    • Z.M. Segu, and Y. Mechref Characterizing protein glycosylation sites through higher-energy C-trap dissociation Rapid Commun. Mass Spectrom. 24 2010 1217 1225
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 1217-1225
    • Segu, Z.M.1    Mechref, Y.2
  • 194
    • 34047164035 scopus 로고    scopus 로고
    • Glycoproteomics based on tandem mass spectrometry of glycopeptides
    • M. Wuhrer, and et al. Glycoproteomics based on tandem mass spectrometry of glycopeptides J. Chromatogr. B 849 2007 115 128
    • (2007) J. Chromatogr. B , vol.849 , pp. 115-128
    • Wuhrer, M.1
  • 195
    • 0035884155 scopus 로고    scopus 로고
    • Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information
    • K. Hakansson, and et al. Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information Anal. Chem. 73 2001 4530 4536
    • (2001) Anal. Chem. , vol.73 , pp. 4530-4536
    • Hakansson, K.1
  • 196
    • 0037084078 scopus 로고    scopus 로고
    • Internal residue loss: Rearrangements occurring during the fragmentation of carbohydrates derivatized at the reducing terminus
    • D.J. Harvey, and et al. Internal residue loss: rearrangements occurring during the fragmentation of carbohydrates derivatized at the reducing terminus Anal. Chem. 74 2002 734 740
    • (2002) Anal. Chem. , vol.74 , pp. 734-740
    • Harvey, D.J.1
  • 197
    • 33646927292 scopus 로고    scopus 로고
    • Mass spectrometry of proton adducts of fucosylated N-glycans: Fucose transfer between antennae gives rise to misleading fragments
    • M. Wuhrer, and et al. Mass spectrometry of proton adducts of fucosylated N-glycans: fucose transfer between antennae gives rise to misleading fragments Rapid Commun. Mass Spectrom. 20 2006 1747 1754
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 1747-1754
    • Wuhrer, M.1
  • 198
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • J.E. Syka, and et al. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry Proc. Natl. Acad. Sci. U. S. A. 101 2004 9528 9533
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9528-9533
    • Syka, J.E.1
  • 199
    • 33644839418 scopus 로고    scopus 로고
    • Infrared multiphoton dissociation and electron capture dissociation of high-mannose type glycopeptides
    • J.T. Adamson, and K. Hakansson Infrared multiphoton dissociation and electron capture dissociation of high-mannose type glycopeptides J. Proteome Res. 5 2006 493 501
    • (2006) J. Proteome Res. , vol.5 , pp. 493-501
    • Adamson, J.T.1    Hakansson, K.2
  • 200
    • 0038676364 scopus 로고    scopus 로고
    • Combined electron capture and infrared multiphoton dissociation for multistage MS/MS in a Fourier transform ion cyclotron resonance mass spectrometer
    • K. Hakansson, and et al. Combined electron capture and infrared multiphoton dissociation for multistage MS/MS in a Fourier transform ion cyclotron resonance mass spectrometer Anal. Chem. 75 2003 3256 3262
    • (2003) Anal. Chem. , vol.75 , pp. 3256-3262
    • Hakansson, K.1
  • 201
    • 29244474577 scopus 로고    scopus 로고
    • Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry
    • A. Harazono, and et al. Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry Anal. Biochem. 348 2006 259 268
    • (2006) Anal. Biochem. , vol.348 , pp. 259-268
    • Harazono, A.1
  • 202
    • 0037466992 scopus 로고    scopus 로고
    • Mechanism of charging and supercharging molecules in electrospray ionization
    • A.T. Iavarone, and E.R. Williams Mechanism of charging and supercharging molecules in electrospray ionization J. Am. Chem. Soc. 125 2003 2319 2327
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2319-2327
    • Iavarone, A.T.1    Williams, E.R.2
  • 203
    • 77956062358 scopus 로고    scopus 로고
    • Glycan labeling strategies and their use in identification and quantification
    • L.R. Ruhaak, and et al. Glycan labeling strategies and their use in identification and quantification Anal. Bioanal. Chem. 397 2010 3457 3481
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3457-3481
    • Ruhaak, L.R.1
  • 204
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • J. Zaia Mass spectrometry and the emerging field of glycomics Chem. Biol. 15 2008 881 892
    • (2008) Chem. Biol. , vol.15 , pp. 881-892
    • Zaia, J.1
  • 205
    • 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, and 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. 87 2015 5401 5409
    • (2015) Anal. Chem. , vol.87 , pp. 5401-5409
    • Lauber, M.A.1
  • 206
    • 84939865360 scopus 로고    scopus 로고
    • Ultrahigh throughput, ultrafiltration-based N-glycomics platform for ultraperformance liquid chromatography (ULTRA(3))
    • H. Stockmann, and et al. Ultrahigh throughput, ultrafiltration-based N-glycomics platform for ultraperformance liquid chromatography (ULTRA(3)) Anal. Chem. 87 2015 8316 8322
    • (2015) Anal. Chem. , vol.87 , pp. 8316-8322
    • Stockmann, H.1
  • 207
    • 77953476888 scopus 로고    scopus 로고
    • New trends in fast and high-resolution liquid chromatography: A critical comparison of existing approaches
    • D. Guillarme, and et al. New trends in fast and high-resolution liquid chromatography: a critical comparison of existing approaches Anal. Bioanal. Chem. 397 2010 1069 1082
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 1069-1082
    • Guillarme, D.1
  • 208
    • 30144444985 scopus 로고    scopus 로고
    • Advantages of application of UPLC in pharmaceutical analysis
    • L. Novakova, and et al. Advantages of application of UPLC in pharmaceutical analysis Talanta 68 2006 908 918
    • (2006) Talanta , vol.68 , pp. 908-918
    • Novakova, L.1
  • 209
    • 74049141466 scopus 로고    scopus 로고
    • Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 microm sorbent
    • J. Ahn, and et al. Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 microm sorbent J. Chromatogr. B 878 2010 403 408
    • (2010) J. Chromatogr. B , vol.878 , pp. 403-408
    • Ahn, J.1
  • 210
    • 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, and 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 10 2011 10.1074/mcp.M111.010090
    • (2011) Mol. Cell. Proteomics , vol.10
    • Pucic, M.1
  • 211
    • 84924632685 scopus 로고    scopus 로고
    • GlycoBase and autoGU: Resources for interpreting HPLC-glycan data
    • M.P. Campbell, and et al. GlycoBase and autoGU: resources for interpreting HPLC-glycan data Methods Mol. Biol. 1273 2015 17 28
    • (2015) Methods Mol. Biol. , vol.1273 , pp. 17-28
    • Campbell, M.P.1
  • 212
    • 84936743358 scopus 로고    scopus 로고
    • GlycoProfileAssigner: Automated structural assignment with error estimation for glycan LC data
    • F.J. Duffy, and P.M. Rudd GlycoProfileAssigner: automated structural assignment with error estimation for glycan LC data Bioinformatics 31 2015 2220 2221
    • (2015) Bioinformatics , vol.31 , pp. 2220-2221
    • Duffy, F.J.1    Rudd, P.M.2
  • 213
    • 84975742481 scopus 로고    scopus 로고
    • Genomics meets glycomics- The first GWAS study of human N-glycome identifies HNF1alpha as a master regulator of plasma protein fucosylation
    • G. Lauc, and et al. Genomics meets glycomics-the first GWAS study of human N-glycome identifies HNF1alpha as a master regulator of plasma protein fucosylation PLoS Genet. 6 2010 e1001256
    • (2010) PLoS Genet. , vol.6 , pp. e1001256
    • Lauc, G.1
  • 214
    • 79961236820 scopus 로고    scopus 로고
    • Multiplexed analytical glycomics: Rapid and confident IgG N-glycan structural elucidation
    • S. Mittermayr, and et al. Multiplexed analytical glycomics: rapid and confident IgG N-glycan structural elucidation J. Proteome Res. 10 2011 3820 3829
    • (2011) J. Proteome Res. , vol.10 , pp. 3820-3829
    • Mittermayr, S.1
  • 215
    • 84892577275 scopus 로고    scopus 로고
    • High-throughput glycosylation analysis of therapeutic immunoglobulin G by capillary gel electrophoresis using a DNA analyzer
    • D. Reusch, and et al. High-throughput glycosylation analysis of therapeutic immunoglobulin G by capillary gel electrophoresis using a DNA analyzer MAbs 6 2014 185 196
    • (2014) MAbs , vol.6 , pp. 185-196
    • Reusch, D.1
  • 216
    • 84859396316 scopus 로고    scopus 로고
    • Effective use of mass spectrometry for glycan and glycopeptide structural analysis
    • N. Leymarie, and J. Zaia Effective use of mass spectrometry for glycan and glycopeptide structural analysis Anal. Chem. 84 2012 3040 3048
    • (2012) Anal. Chem. , vol.84 , pp. 3040-3048
    • Leymarie, N.1    Zaia, J.2
  • 217
    • 84905457591 scopus 로고    scopus 로고
    • Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core
    • D.J. Harvey, and et al. Fragmentation of negative ions from N-linked carbohydrates: part 6. Glycans containing one N-acetylglucosamine in the core Rapid Commun. Mass Spectrom. 28 2014 2008 2018
    • (2014) Rapid Commun. Mass Spectrom. , vol.28 , pp. 2008-2018
    • Harvey, D.J.1
  • 218
    • 84881610706 scopus 로고    scopus 로고
    • Travelling wave ion mobility and negative ion fragmentation for the structural determination of N-linked glycans
    • D.J. Harvey, and et al. Travelling wave ion mobility and negative ion fragmentation for the structural determination of N-linked glycans Electrophoresis 34 2013 2368 2378
    • (2013) Electrophoresis , vol.34 , pp. 2368-2378
    • Harvey, D.J.1
  • 219
    • 84887678119 scopus 로고    scopus 로고
    • Detailed glycan structural characterization by electronic excitation dissociation
    • X. Yu, and et al. Detailed glycan structural characterization by electronic excitation dissociation Anal. Chem. 85 2013 10017 10021
    • (2013) Anal. Chem. , vol.85 , pp. 10017-10021
    • Yu, X.1
  • 220
    • 77951837705 scopus 로고    scopus 로고
    • Negative electron transfer dissociation of glycosaminoglycans
    • J.J. Wolff, and et al. Negative electron transfer dissociation of glycosaminoglycans Anal. Chem. 82 2010 3460 3466
    • (2010) Anal. Chem. , vol.82 , pp. 3460-3466
    • Wolff, J.J.1
  • 221
    • 84874134892 scopus 로고    scopus 로고
    • Analytical platform for glycomic characterization of recombinant erythropoietin biotherapeutics and biosimilars by MS
    • M.J. Oh, and et al. Analytical platform for glycomic characterization of recombinant erythropoietin biotherapeutics and biosimilars by MS Bioanalysis 5 2013 545 559
    • (2013) Bioanalysis , vol.5 , pp. 545-559
    • Oh, M.J.1
  • 222
    • 84908573066 scopus 로고    scopus 로고
    • Estimating collision cross sections of negatively charged N-glycans using traveling wave ion mobility-mass spectrometry
    • J. Hofmann, and et al. Estimating collision cross sections of negatively charged N-glycans using traveling wave ion mobility-mass spectrometry Anal. Chem. 86 2014 10789 10795
    • (2014) Anal. Chem. , vol.86 , pp. 10789-10795
    • Hofmann, J.1
  • 223
    • 84868637049 scopus 로고    scopus 로고
    • Confident identification of isomeric N-glycan structures by combined ion mobility mass spectrometry and hydrophilic interaction liquid chromatography
    • Y. Yamaguchi, and et al. Confident identification of isomeric N-glycan structures by combined ion mobility mass spectrometry and hydrophilic interaction liquid chromatography Rapid Commun. Mass Spectrom. 26 2012 2877 2884
    • (2012) Rapid Commun. Mass Spectrom. , vol.26 , pp. 2877-2884
    • Yamaguchi, Y.1
  • 224
    • 41449103126 scopus 로고    scopus 로고
    • Separation-based glycoprofiling approaches using fluorescent labels
    • P.J. Domann, and et al. Separation-based glycoprofiling approaches using fluorescent labels Proteomics 7 Suppl. 1 2007 70 76
    • (2007) Proteomics , vol.7 , pp. 70-76
    • Domann, P.J.1
  • 225
    • 79954545117 scopus 로고    scopus 로고
    • UniCarb-DB: A database resource for glycomic discovery
    • C.A. Hayes, and et al. UniCarb-DB: a database resource for glycomic discovery Bioinformatics 27 2011 1343 1344
    • (2011) Bioinformatics , vol.27 , pp. 1343-1344
    • Hayes, C.A.1
  • 226
    • 84864129235 scopus 로고    scopus 로고
    • Databases and tools in glycobiology
    • N.V. Artemenko, and et al. Databases and tools in glycobiology Methods Mol. Biol. 899 2012 325 350
    • (2012) Methods Mol. Biol. , vol.899 , pp. 325-350
    • Artemenko, N.V.1
  • 227
    • 84862668247 scopus 로고    scopus 로고
    • Glycomic mass spectrometric analysis and data interpretation tools
    • C.-W. von der Lieth, John Wiley & Sons
    • N.G. Karlsson, and N.H. Packer Glycomic mass spectrometric analysis and data interpretation tools C.-W. von der Lieth, Bioinformatics for Glycobiology and Glycomics 2009 John Wiley & Sons 223 256
    • (2009) Bioinformatics for Glycobiology and Glycomics , pp. 223-256
    • Karlsson, N.G.1    Packer, N.H.2
  • 228
    • 84901273059 scopus 로고    scopus 로고
    • Toolboxes for a standardised and systematic study of glycans
    • M.P. Campbell, and et al. Toolboxes for a standardised and systematic study of glycans BMC Bioinformatics 15 Suppl. 1 2014 S9
    • (2014) BMC Bioinformatics , vol.15 , pp. S9
    • Campbell, M.P.1
  • 229
    • 33947192955 scopus 로고    scopus 로고
    • Comparison of the methods for profiling glycoprotein glycans-HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study
    • Y. Wada, and et al. Comparison of the methods for profiling glycoprotein glycans-HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study Glycobiology 17 2007 411 422
    • (2007) Glycobiology , vol.17 , pp. 411-422
    • Wada, Y.1
  • 230
    • 33646108830 scopus 로고    scopus 로고
    • The role of informatics in glycobiology research with special emphasis on automatic interpretation of MS spectra
    • C.W. von der Lieth, and et al. The role of informatics in glycobiology research with special emphasis on automatic interpretation of MS spectra Biochim. Biophys. Acta 1760 2006 568 577
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 568-577
    • Von Der Lieth, C.W.1
  • 231
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
    • C.A. Cooper, and et al. GlycoMod - a software tool for determining glycosylation compositions from mass spectrometric data Proteomics 1 2001 340 349
    • (2001) Proteomics , vol.1 , pp. 340-349
    • Cooper, C.A.1
  • 232
    • 2942568109 scopus 로고    scopus 로고
    • Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data
    • H.J. Joshi, and et al. Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data Proteomics 4 2004 1650 1664
    • (2004) Proteomics , vol.4 , pp. 1650-1664
    • Joshi, H.J.1
  • 233
    • 0142213540 scopus 로고    scopus 로고
    • GLYCO-FRAGMENT: A web tool to support the interpretation of mass spectra of complex carbohydrates
    • K.K. Lohmann, and C.W. von der Lieth GLYCO-FRAGMENT: a web tool to support the interpretation of mass spectra of complex carbohydrates Proteomics 3 2003 2028 2035
    • (2003) Proteomics , vol.3 , pp. 2028-2035
    • Lohmann, K.K.1    Von Der Lieth, C.W.2
  • 234
    • 3242890883 scopus 로고    scopus 로고
    • GlycoFragment and GlycoSearchMS: Web tools to support the interpretation of mass spectra of complex carbohydrates
    • K.K. Lohmann, and C.W. von der Lieth GlycoFragment and GlycoSearchMS: web tools to support the interpretation of mass spectra of complex carbohydrates Nucleic Acids Res. 32 2004 W261 W266
    • (2004) Nucleic Acids Res. , vol.32 , pp. W261-W266
    • Lohmann, K.K.1    Von Der Lieth, C.W.2
  • 235
    • 33847203661 scopus 로고    scopus 로고
    • GlycoPep DB: A tool for glycopeptide analysis using a Smart Search
    • E.P. Go, and et al. GlycoPep DB: a tool for glycopeptide analysis using a Smart Search Anal. Chem. 79 2007 1708 1713
    • (2007) Anal. Chem. , vol.79 , pp. 1708-1713
    • Go, E.P.1
  • 236
    • 76149084829 scopus 로고    scopus 로고
    • GlycoSpectrumScan: Fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA
    • N. Deshpande, and et al. GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA J. Proteome Res. 9 2010 1063 1075
    • (2010) J. Proteome Res. , vol.9 , pp. 1063-1075
    • Deshpande, N.1
  • 237
    • 16344380985 scopus 로고    scopus 로고
    • Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra
    • D. Goldberg, and et al. Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra Proteomics 5 2005 865 875
    • (2005) Proteomics , vol.5 , pp. 865-875
    • Goldberg, D.1
  • 238
    • 33745004837 scopus 로고    scopus 로고
    • Automatic determination of O-glycan structure from fragmentation spectra
    • D. Goldberg, and et al. Automatic determination of O-glycan structure from fragmentation spectra J. Proteome Res. 5 2006 1429 1434
    • (2006) J. Proteome Res. , vol.5 , pp. 1429-1434
    • Goldberg, D.1
  • 239
    • 35648943348 scopus 로고    scopus 로고
    • Automated N-glycopeptide identification using a combination of single- and tandem-MS
    • D. Goldberg, and et al. Automated N-glycopeptide identification using a combination of single- and tandem-MS J. Proteome Res. 6 2007 3995 4005
    • (2007) J. Proteome Res. , vol.6 , pp. 3995-4005
    • Goldberg, D.1
  • 240
    • 34247328263 scopus 로고    scopus 로고
    • Simplification of mass spectral analysis of acidic glycopeptides using GlycoPep ID
    • J. Irungu, and et al. Simplification of mass spectral analysis of acidic glycopeptides using GlycoPep ID Anal. Chem. 79 2007 3065 3074
    • (2007) Anal. Chem. , vol.79 , pp. 3065-3074
    • Irungu, J.1
  • 241
    • 84861839252 scopus 로고    scopus 로고
    • GlycoPep grader: A web-based utility for assigning the composition of N-linked glycopeptides
    • C.L. Woodin, and et al. GlycoPep grader: a web-based utility for assigning the composition of N-linked glycopeptides Anal. Chem. 84 2012 4821 4829
    • (2012) Anal. Chem. , vol.84 , pp. 4821-4829
    • Woodin, C.L.1
  • 242
    • 84881172533 scopus 로고    scopus 로고
    • Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search
    • K.B. Chandler, and et al. Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search J. Proteome Res. 12 2013 3652 3666
    • (2013) J. Proteome Res. , vol.12 , pp. 3652-3666
    • Chandler, K.B.1
  • 243
    • 84878297205 scopus 로고    scopus 로고
    • GlycoPep Detector: A tool for assigning mass spectrometry data of N-linked glycopeptides on the basis of their electron transfer dissociation spectra
    • Z. Zhu, and et al. GlycoPep Detector: a tool for assigning mass spectrometry data of N-linked glycopeptides on the basis of their electron transfer dissociation spectra Anal. Chem. 85 2013 5023 5032
    • (2013) Anal. Chem. , vol.85 , pp. 5023-5032
    • Zhu, Z.1
  • 244
    • 84914128997 scopus 로고    scopus 로고
    • GlycoMaster DB: Software to assist the automated identification of N-linked glycopeptides by tandem mass spectrometry
    • L. He, and et al. GlycoMaster DB: software to assist the automated identification of N-linked glycopeptides by tandem mass spectrometry J. Proteome Res. 13 2014 3881 3895
    • (2014) J. Proteome Res. , vol.13 , pp. 3881-3895
    • He, L.1
  • 245
    • 0034214358 scopus 로고    scopus 로고
    • STAT: A saccharide topology analysis tool used in combination with tandem mass spectrometry
    • S.P. Gaucher, and et al. STAT: a saccharide topology analysis tool used in combination with tandem mass spectrometry Anal. Chem. 72 2000 2331 2336
    • (2000) Anal. Chem. , vol.72 , pp. 2331-2336
    • Gaucher, S.P.1
  • 246
    • 84860544131 scopus 로고    scopus 로고
    • Automated interpretation of MS/MS spectra of oligosaccharides
    • H. Tang, and et al. Automated interpretation of MS/MS spectra of oligosaccharides Bioinformatics 21 Suppl. 1 2005 431 439
    • (2005) Bioinformatics , vol.21 , pp. 431-439
    • Tang, H.1
  • 247
    • 38049036318 scopus 로고    scopus 로고
    • Glyco-peakfinder - De novo composition analysis of glycoconjugates
    • K. Maass, and et al. Glyco-peakfinder - de novo composition analysis of glycoconjugates Proteomics 7 2007 4435 4444
    • (2007) Proteomics , vol.7 , pp. 4435-4444
    • Maass, K.1
  • 248
    • 47749097124 scopus 로고    scopus 로고
    • Regulation of glycan structures in animal tissues: Transcript profiling of glycan-related genes
    • A.V. Nairn, and et al. Regulation of glycan structures in animal tissues: transcript profiling of glycan-related genes J. Biol. Chem. 283 2008 17298 17313
    • (2008) J. Biol. Chem. , vol.283 , pp. 17298-17313
    • Nairn, A.V.1
  • 249
    • 33845247062 scopus 로고    scopus 로고
    • GlycoVis: Visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells
    • P. Hossler, and et al. GlycoVis: visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells Biotechnol. Bioeng. 95 2006 946 960
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 946-960
    • Hossler, P.1
  • 250
    • 38549146892 scopus 로고    scopus 로고
    • Glycoconjugate Data Bank: Structures - An annotated glycan structure database and N-glycan primary structure verification service
    • T. Nakahara, and et al. Glycoconjugate Data Bank: structures - an annotated glycan structure database and N-glycan primary structure verification service Nucleic Acids Res. 36 2008 D368 D371
    • (2008) Nucleic Acids Res. , vol.36 , pp. D368-D371
    • Nakahara, T.1
  • 251
    • 84875991393 scopus 로고    scopus 로고
    • Bioinformatics analysis of glycan structures from a genomic perspective
    • T. Luetteke, M. Frank, John Wiley & Sons
    • K.F. Aoki-kinoshita, and M. Kanehisa Bioinformatics analysis of glycan structures from a genomic perspective T. Luetteke, M. Frank, Bioinformatics for Glycobiology and Glycomics 2009 John Wiley & Sons 125 141
    • (2009) Bioinformatics for Glycobiology and Glycomics , pp. 125-141
    • Aoki-Kinoshita, K.F.1    Kanehisa, M.2
  • 252
    • 33646149392 scopus 로고    scopus 로고
    • KEGG as a glycome informatics resource
    • K. Hashimoto, and et al. KEGG as a glycome informatics resource Glycobiology 16 2006 63 70R
    • (2006) Glycobiology , vol.16 , pp. 63-70R
    • Hashimoto, K.1
  • 253
    • 33644874819 scopus 로고    scopus 로고
    • From genomics to chemical genomics: New developments in KEGG
    • M. Kanehisa, and et al. From genomics to chemical genomics: new developments in KEGG Nucleic Acids Res. 34 2006 D354 D357
    • (2006) Nucleic Acids Res. , vol.34 , pp. D354-D357
    • Kanehisa, M.1
  • 254
    • 44049091490 scopus 로고    scopus 로고
    • GlycoVault: A bioinformatics infrastructure for glycan pathway visualization, analysis and modeling. Information Technology: New Generations
    • S. Nimmagadda, and et al. GlycoVault: a bioinformatics infrastructure for glycan pathway visualization, analysis and modeling. Information Technology: New Generations Fifth International Conference 2008 692 697
    • (2008) Fifth International Conference , pp. 692-697
    • Nimmagadda, S.1
  • 255
    • 34848927484 scopus 로고    scopus 로고
    • The GlycanBuilder: A fast, intuitive and flexible software tool for building and displaying glycan structures
    • A. Ceroni, and et al. The GlycanBuilder: a fast, intuitive and flexible software tool for building and displaying glycan structures Source Code Biol. Med. 2 2007 3
    • (2007) Source Code Biol. Med. , vol.2 , pp. 3
    • Ceroni, A.1
  • 256
    • 84924565611 scopus 로고    scopus 로고
    • Analyzing glycan structure synthesis with the Glycan Pathway Predictor (GPP) tool
    • K.F. Aoki-Kinoshita Analyzing glycan structure synthesis with the Glycan Pathway Predictor (GPP) tool Methods Mol. Biol. 1273 2015 139 147
    • (2015) Methods Mol. Biol. , vol.1273 , pp. 139-147
    • Aoki-Kinoshita, K.F.1
  • 257
    • 75749136871 scopus 로고    scopus 로고
    • Complex genetic regulation of protein glycosylation
    • G. Lauc, and et al. Complex genetic regulation of protein glycosylation Mol. Biosyst. 6 2010 329 335
    • (2010) Mol. Biosyst. , vol.6 , pp. 329-335
    • Lauc, G.1
  • 258
    • 77951561987 scopus 로고    scopus 로고
    • Increasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell-mediated B-cell cytotoxicity
    • E. Mossner, and et al. Increasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell-mediated B-cell cytotoxicity Blood 115 2010 4393 4402
    • (2010) Blood , vol.115 , pp. 4393-4402
    • Mossner, E.1
  • 259
    • 0033522647 scopus 로고    scopus 로고
    • 1.9 A structure of the therapeutic antibody CAMPATH-1H Fab in complex with a synthetic peptide antigen
    • L.C. James, and et al. 1.9 A structure of the therapeutic antibody CAMPATH-1H Fab in complex with a synthetic peptide antigen J. Mol. Biol. 289 1999 293 301
    • (1999) J. Mol. Biol. , vol.289 , pp. 293-301
    • James, L.C.1


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