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Volumn 30, Issue 2, 2013, Pages 119-136

Targeting the glycoproteome

Author keywords

Attachment sites; Enrichment; Glycopeptide; Glycoproteomics; Hydrazide chemistry; Lectin affinity; Liquid chromatography; Tandem mass spectrometry

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN C3; BORONIC ACID DERIVATIVE; GLYCAN; GLYCOPEPTIDE; GLYCOPROTEIN; LECTIN; PROTEOME; SIALIC ACID;

EID: 84878823399     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-012-9438-6     Document Type: Article
Times cited : (36)

References (150)
  • 2
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • 18695988 1:CAS:528:DC%2BD1MXivFyrsbw%3D 10.1007/s10719-008-9162-4
    • Tian, E.; ten Hagen, K.G.: Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj. J. 26(3), 325-334 (2009)
    • (2009) Glycoconj. J. , vol.26 , Issue.3 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 3
    • 54949106904 scopus 로고    scopus 로고
    • Mammalian glycosylation in immunity
    • 18846099 1:CAS:528:DC%2BD1cXht12isLbE 10.1038/nri2417
    • Marth, J.D.; Grewal, P.K.: Mammalian glycosylation in immunity. Nat. Rev. Immunol. 8(11), 874-887 (2008)
    • (2008) Nat. Rev. Immunol. , vol.8 , Issue.11 , pp. 874-887
    • Marth, J.D.1    Grewal, P.K.2
  • 4
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • 16959566 1:CAS:528:DC%2BD28XpvVKitbo%3D 10.1016/j.cell.2006.08.019
    • Ohtsubo, K.; Marth, J.D.: Glycosylation in cellular mechanisms of health and disease. Cell 126(5), 855-867 (2006)
    • (2006) Cell , vol.126 , Issue.5 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 5
    • 70249135667 scopus 로고    scopus 로고
    • Glycosylation diseases: Quo vadis?
    • 19061954 1:CAS:528:DC%2BD1MXhtFGqsLjO 10.1016/j.bbadis.2008.11.002
    • Schachter, H.; Freeze, H.H.: Glycosylation diseases: quo vadis? Biochim. Biophys. Acta 1792(9), 925-930 (2009)
    • (2009) Biochim. Biophys. Acta , vol.1792 , Issue.9 , pp. 925-930
    • Schachter, H.1    Freeze, H.H.2
  • 6
    • 77956031216 scopus 로고    scopus 로고
    • Proteoglycomics: Recent progress and future challenges
    • 20450439 1:CAS:528:DC%2BC3cXhtlGlt77N 10.1089/omi.2009.0123
    • Ly, M.; Laremore, T.N.; Linhardt, R.J.: Proteoglycomics: recent progress and future challenges. Omics 14(4), 389-399 (2010)
    • (2010) Omics , vol.14 , Issue.4 , pp. 389-399
    • Ly, M.1    Laremore, T.N.2    Linhardt, R.J.3
  • 7
    • 79961141890 scopus 로고    scopus 로고
    • Structural remodeling, trafficking and functions of glycosylphosphatidylinositol-anchored proteins
    • 21658410 1:CAS:528:DC%2BC3MXht1OisL%2FK 10.1016/j.plipres.2011.05.002
    • Maeda, Y.; Kinoshita, T.: Structural remodeling, trafficking and functions of glycosylphosphatidylinositol-anchored proteins. Prog. Lipid Res. 50(4), 411-424 (2011)
    • (2011) Prog. Lipid Res. , vol.50 , Issue.4 , pp. 411-424
    • Maeda, Y.1    Kinoshita, T.2
  • 8
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • 21978957 1:CAS:528:DC%2BC3MXht12rtbvF 10.1016/j.sbi.2011.08.005
    • Schwarz, F.; Aebi, M.: Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 21(5), 576-582 (2011)
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , Issue.5 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 9
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation
    • 21614585 1:CAS:528:DC%2BC3MXptVOisro%3D 10.1007/s10545-011-9337-1
    • Mohorko, E.; Glockshuber, R.; Aebi, M.: Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation. J. Inherit. Metab. Dis. 34(4), 869-878 (2011)
    • (2011) J. Inherit. Metab. Dis. , vol.34 , Issue.4 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 10
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases
    • 12634319 10.1093/glycob/cwg007 1:CAS:528:DC%2BD3sXisFeqtL4%3D
    • Ten Hagen, K.G.; Fritz, T.A.; Tabak, L.A.: All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13(1), 1R-16R (2003)
    • (2003) Glycobiology , vol.13 , Issue.1
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 11
    • 79954612783 scopus 로고    scopus 로고
    • Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases
    • 21349845 1:CAS:528:DC%2BC3MXkslWisL0%3D 10.1074/jbc.M111.218701
    • Gerken, T.A.; Jamison, O.; Perrine, C.L.; Collette, J.C.; Moinova, H.; Ravi, L.; Markowitz, S.D.; Shen, W.; Patel, H.; Tabak, L.A.: Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases. J. Biol. Chem. 286(16), 14493-14507 (2011)
    • (2011) J. Biol. Chem. , vol.286 , Issue.16 , pp. 14493-14507
    • Gerken, T.A.1    Jamison, O.2    Perrine, C.L.3    Collette, J.C.4    Moinova, H.5    Ravi, L.6    Markowitz, S.D.7    Shen, W.8    Patel, H.9    Tabak, L.A.10
  • 12
    • 40749160803 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation and its potential use in drug and vaccine development
    • 17988798 1:CAS:528:DC%2BD1cXjsVSitrs%3D 10.1016/j.bbagen.2007.09.010
    • Tarp, M.A.; Clausen, H.: Mucin-type O-glycosylation and its potential use in drug and vaccine development. Biochim. Biophys. Acta 1780(3), 546-563 (2008)
    • (2008) Biochim. Biophys. Acta , vol.1780 , Issue.3 , pp. 546-563
    • Tarp, M.A.1    Clausen, H.2
  • 13
    • 77955279149 scopus 로고    scopus 로고
    • The role of mucin-type O-glycans in eukaryotic development
    • 20144722 1:CAS:528:DC%2BC3cXpvVOht70%3D 10.1016/j.semcdb.2010.02.001
    • Tabak, L.A.: The role of mucin-type O-glycans in eukaryotic development. Semin. Cell Dev. Biol. 21(6), 616-621 (2010)
    • (2010) Semin. Cell Dev. Biol. , vol.21 , Issue.6 , pp. 616-621
    • Tabak, L.A.1
  • 14
    • 79952106660 scopus 로고    scopus 로고
    • Location, location, location: New insights into O-GalNAc protein glycosylation
    • 21145746 1:CAS:528:DC%2BC3MXjs1Wksbs%3D 10.1016/j.tcb.2010.11.004
    • Gill, D.J.; Clausen, H.; Bard, F.: Location, location, location: new insights into O-GalNAc protein glycosylation. Trends Cell Biol. 21(3), 149-158 (2011)
    • (2011) Trends Cell Biol. , vol.21 , Issue.3 , pp. 149-158
    • Gill, D.J.1    Clausen, H.2    Bard, F.3
  • 15
    • 84860365843 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation - A classification of the polypeptide GalNAc-transferase gene family
    • Bennett, E.P.; Mandel, U.; Clausen, H.; Gerken, T.A.; Fritz, T.A.; Tabak, L.A.: Control of mucin-type O-glycosylation - a classification of the polypeptide GalNAc-transferase gene family. Glycobiology 22(6), 736-756 (2012)
    • (2012) Glycobiology , vol.22 , Issue.6 , pp. 736-756
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 16
    • 73649139554 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation - Putting the pieces together
    • 19919547 1:CAS:528:DC%2BC3cXhs1Gmtg%3D%3D 10.1111/j.1742-4658.2009.07429. x
    • Jensen, P.H.; Kolarich, D.; Packer, N.H.: Mucin-type O-glycosylation - putting the pieces together. FEBS J. 277(1), 81-94 (2010)
    • (2010) FEBS J. , vol.277 , Issue.1 , pp. 81-94
    • Jensen, P.H.1    Kolarich, D.2    Packer, N.H.3
  • 17
    • 0034737738 scopus 로고    scopus 로고
    • Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules
    • 10734111 1:CAS:528:DC%2BD3cXitlCqsrY%3D 10.1074/jbc.275.13.9604
    • Moloney, D.J.; Shair, L.H.; Lu, F.M.; Xia, J.; Locke, R.; Matta, K.L.; Haltiwanger, R.S.: Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules. J. Biol. Chem. 275(13), 9604-9611 (2000)
    • (2000) J. Biol. Chem. , vol.275 , Issue.13 , pp. 9604-9611
    • Moloney, D.J.1    Shair, L.H.2    Lu, F.M.3    Xia, J.4    Locke, R.5    Matta, K.L.6    Haltiwanger, R.S.7
  • 18
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • 11269319 1:CAS:528:DC%2BD3MXit1Knsb0%3D 10.1126/science.1058714
    • Wells, L.; Vosseller, K.; Hart, G.W.: Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291(5512), 2376-2378 (2001)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 19
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • 21850036 1:CAS:528:DC%2BC3MXhtVehs73E 10.1038/nrc3114
    • Slawson, C.; Hart, G.W.: O-GlcNAc signalling: implications for cancer cell biology. Nat. Rev. Cancer 11(9), 678-684 (2011)
    • (2011) Nat. Rev. Cancer , vol.11 , Issue.9 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 20
    • 0025672799 scopus 로고
    • Glycoconjugates: Overview and strategy
    • 2074835 1:CAS:528:DyaK3MXlslygsrs%3D 10.1016/0076-6879(90)93437-P
    • Laine, R.A.: Glycoconjugates: overview and strategy. Methods Enzymol. 193, 539-553 (1990)
    • (1990) Methods Enzymol. , vol.193 , pp. 539-553
    • Laine, R.A.1
  • 21
    • 7244258916 scopus 로고    scopus 로고
    • History of lectins: From hemagglutinins to biological recognition molecules
    • 15229195 1:CAS:528:DC%2BD2cXotVyqs7s%3D 10.1093/glycob/cwh122
    • Sharon, N.; Lis, H.: History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology 14(11), 53R-62R (2004)
    • (2004) Glycobiology , vol.14 , Issue.11
    • Sharon, N.1    Lis, H.2
  • 22
    • 0028178318 scopus 로고
    • Non-carbohydrate binding partners/domains of animal lectins
    • 8013730 1:CAS:528:DyaK2cXltVajt7Y%3D 10.1016/0020-711X(94)90002-7
    • Gabius, H.J.: Non-carbohydrate binding partners/domains of animal lectins. Int. J. Biochem. 26(4), 469-477 (1994)
    • (1994) Int. J. Biochem. , vol.26 , Issue.4 , pp. 469-477
    • Gabius, H.J.1
  • 23
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • 9057819 1:CAS:528:DyaK2sXht1CjsLo%3D 10.1111/j.1432-1033.1997.t01-1- 00543.x
    • Gabius, H.J.: Animal lectins. Eur. J. Biochem. 243(3), 543-576 (1997)
    • (1997) Eur. J. Biochem. , vol.243 , Issue.3 , pp. 543-576
    • Gabius, H.J.1
  • 24
    • 77956014533 scopus 로고    scopus 로고
    • The lectin riddle: Glycoproteins fractionated from complex mixtures have similar glycomic profiles
    • 20726804 10.1089/omi.2010.0075 1:CAS:528:DC%2BC3cXhtlGlt77F
    • Lee, A.; Nakano, M.; Hincapie, M.; Kolarich, D.; Baker, M.S.; Hancock, W.S.; Packer, N.H.: The lectin riddle: glycoproteins fractionated from complex mixtures have similar glycomic profiles. Omics 14(4), 487-499 (2010)
    • (2010) Omics , vol.14 , Issue.4 , pp. 487-499
    • Lee, A.1    Nakano, M.2    Hincapie, M.3    Kolarich, D.4    Baker, M.S.5    Hancock, W.S.6    Packer, N.H.7
  • 25
    • 25844461911 scopus 로고    scopus 로고
    • Structural basis of high-affinity glycan recognition by bacterial and fungal lectins
    • 16140523 1:CAS:528:DC%2BD2MXhtVKjsLzM 10.1016/j.sbi.2005.08.003
    • Imberty, A.; Mitchell, E.P.; Wimmerová, M.: Structural basis of high-affinity glycan recognition by bacterial and fungal lectins. Curr. Opin. Struct. Biol. 15(5), 525-534 (2005)
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , Issue.5 , pp. 525-534
    • Imberty, A.1    Mitchell, E.P.2    Wimmerová, M.3
  • 26
    • 79958036381 scopus 로고    scopus 로고
    • From lectin structure to functional glycomics: Principles of the sugar code
    • 21458998 1:CAS:528:DC%2BC3MXnsVOqs7w%3D 10.1016/j.tibs.2011.01.005
    • Gabius, H.-J.; André, S.; Jiménez-Barbero, J.; Romero, A.; Solís, D.: From lectin structure to functional glycomics: principles of the sugar code. Trends Biochem. Sci. 36(6), 298-313 (2011)
    • (2011) Trends Biochem. Sci. , vol.36 , Issue.6 , pp. 298-313
    • Gabius, H.-J.1    André, S.2    Jiménez-Barbero, J.3    Romero, A.4    Solís, D.5
  • 27
    • 70349467181 scopus 로고    scopus 로고
    • Lectins as tools in glycoconjugate research
    • 18368479 1:CAS:528:DC%2BD1MXhsFChsL%2FL 10.1007/s10719-008-9119-7
    • Wu, A.M.; Lisowska, E.; Duk, M.; Yang, Z.: Lectins as tools in glycoconjugate research. Glycoconj. J. 26(8), 899-913 (2009)
    • (2009) Glycoconj. J. , vol.26 , Issue.8 , pp. 899-913
    • Wu, A.M.1    Lisowska, E.2    Duk, M.3    Yang, Z.4
  • 28
    • 0018786476 scopus 로고
    • Structural determinants of concanavalin A specificity for oligosaccharides
    • 85625 1:CAS:528:DyaE1MXktFyit7Y%3D
    • Baenziger, J.U.; Fiete, D.: Structural determinants of concanavalin A specificity for oligosaccharides. J. Biol. Chem. 254(7), 2400-2407 (1979)
    • (1979) J. Biol. Chem. , vol.254 , Issue.7 , pp. 2400-2407
    • Baenziger, J.U.1    Fiete, D.2
  • 29
    • 0016190847 scopus 로고
    • Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding
    • 4830237 1:CAS:528:DyaE2cXksF2ltrc%3D
    • Nagata, Y.; Burger, M.M.: Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J. Biol. Chem. 249(10), 3116-3122 (1974)
    • (1974) J. Biol. Chem. , vol.249 , Issue.10 , pp. 3116-3122
    • Nagata, Y.1    Burger, M.M.2
  • 30
    • 0018570913 scopus 로고
    • Interaction of wheat germ agglutinin with sialic acid
    • 92996 1:CAS:528:DyaL3cXksFWq 10.1021/bi00591a038
    • Peters, B.P.; Ebisu, S.; Goldstein, I.J.; Flashner, M.: Interaction of wheat germ agglutinin with sialic acid. Biochemistry 18(24), 5505-5511 (1979)
    • (1979) Biochemistry , vol.18 , Issue.24 , pp. 5505-5511
    • Peters, B.P.1    Ebisu, S.2    Goldstein, I.J.3    Flashner, M.4
  • 31
    • 0023644482 scopus 로고
    • The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence
    • 3805045 1:CAS:528:DyaL2sXhslWns7s%3D
    • Shibuya, N.; Goldstein, I.J.; Broekaert, W.F.; Nsimba-Lubaki, M.; Peeters, B.; Peumans, W.J.: The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence. J. Biol. Chem. 262(4), 1596-1601 (1987)
    • (1987) J. Biol. Chem. , vol.262 , Issue.4 , pp. 1596-1601
    • Shibuya, N.1    Goldstein, I.J.2    Broekaert, W.F.3    Nsimba-Lubaki, M.4    Peeters, B.5    Peumans, W.J.6
  • 32
    • 0026020575 scopus 로고
    • Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins
    • 1985926 1:CAS:528:DyaK3MXhvVSmur4%3D
    • Knibbs, R.N.; Goldstein, I.J.; Ratcliffe, R.M.; Shibuya, N.: Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins. J. Biol. Chem. 266(1), 83-88 (1991)
    • (1991) J. Biol. Chem. , vol.266 , Issue.1 , pp. 83-88
    • Knibbs, R.N.1    Goldstein, I.J.2    Ratcliffe, R.M.3    Shibuya, N.4
  • 33
    • 0034625394 scopus 로고    scopus 로고
    • An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides
    • 10747930 1:CAS:528:DC%2BD3cXktFaksbc%3D 10.1074/jbc.M000560200
    • Imberty, A.; Gautier, C.; Lescar, J.; Pérez, S.; Wyns, L.; Loris, R.: An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides. J. Biol. Chem. 275(23), 17541-17548 (2000)
    • (2000) J. Biol. Chem. , vol.275 , Issue.23 , pp. 17541-17548
    • Imberty, A.1    Gautier, C.2    Lescar, J.3    Pérez, S.4    Wyns, L.5    Loris, R.6
  • 34
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • 19674964 1:CAS:528:DC%2BD1MXhsVSms77M 10.1074/mcp.M900211-MCP200
    • Darula, Z.; Medzihradszky, K.F.: Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum. Mol. Cell Proteomics 8(11), 2515-2526 (2009)
    • (2009) Mol. Cell Proteomics , vol.8 , Issue.11 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 36
    • 0023953204 scopus 로고
    • Monosized, magnetic polymer particles: Their use in separation of cells and subcellular components, and in the study of lymphocyte function in vitro
    • 3078840 1:CAS:528:DyaL1cXmt1Oqurg%3D 10.1002/jmr.300010104
    • Lea, T.; Vartdal, F.; Nustad, K.; Funderud, S.; Berge, A.; Ellingsen, T.; Schmid, R.; Stenstad, P.; Ugelstad, J.: Monosized, magnetic polymer particles: their use in separation of cells and subcellular components, and in the study of lymphocyte function in vitro. J. Mol. Recognit. 1(1), 9-18 (1988)
    • (1988) J. Mol. Recognit. , vol.1 , Issue.1 , pp. 9-18
    • Lea, T.1    Vartdal, F.2    Nustad, K.3    Funderud, S.4    Berge, A.5    Ellingsen, T.6    Schmid, R.7    Stenstad, P.8    Ugelstad, J.9
  • 37
    • 84555178070 scopus 로고    scopus 로고
    • Liquid-phase-based separation systems for depletion, prefractionation and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis - An update covering the period 2008-2011
    • 22125262 1:CAS:528:DC%2BC3MXhsFalt7rL 10.1002/elps.201100431
    • Selvaraju, S.; Rassi, Z.E.: Liquid-phase-based separation systems for depletion, prefractionation and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis - an update covering the period 2008-2011. Electrophoresis 33(1), 74-88 (2012)
    • (2012) Electrophoresis , vol.33 , Issue.1 , pp. 74-88
    • Selvaraju, S.1    Rassi, Z.E.2
  • 38
    • 13244291497 scopus 로고    scopus 로고
    • Protein glycosylation analyzed by normal-phase nano-liquid chromatography-mass spectrometry of glycopeptides
    • 15679358 1:CAS:528:DC%2BD2cXhtFChsr7L 10.1021/ac048619x
    • Wuhrer, M.; Koeleman, C.A.; Hokke, C.H.; Deelder, A.M.: Protein glycosylation analyzed by normal-phase nano-liquid chromatography-mass spectrometry of glycopeptides. Anal. Chem. 77(3), 886-894 (2005)
    • (2005) Anal. Chem. , vol.77 , Issue.3 , pp. 886-894
    • Wuhrer, M.1    Koeleman, C.A.2    Hokke, C.H.3    Deelder, A.M.4
  • 39
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • 15538777 1:CAS:528:DC%2BD2cXosVSmt7k%3D 10.1021/ac049062o
    • Wada, Y.; Tajiri, M.; Yoshida, S.: Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal. Chem. 76(22), 6560-6565 (2004)
    • (2004) Anal. Chem. , vol.76 , Issue.22 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 40
    • 77950834205 scopus 로고    scopus 로고
    • Protein glycosylation analysis by HILIC-LC-MS of Proteinase K-generated N- and O-glycopeptides
    • 20222081 1:CAS:528:DC%2BC3cXkvFCnsr0%3D 10.1002/jssc.200900850
    • Zauner, G.; Koeleman, C.A.M.; Deelder, A.M.; Wuhrer, M.: Protein glycosylation analysis by HILIC-LC-MS of Proteinase K-generated N- and O-glycopeptides. J. Sep. Sci. 33(6-7), 903-910 (2010)
    • (2010) J. Sep. Sci. , vol.33 , Issue.6-7 , pp. 903-910
    • Zauner, G.1    Koeleman, C.A.M.2    Deelder, A.M.3    Wuhrer, M.4
  • 41
    • 65249134633 scopus 로고    scopus 로고
    • Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry
    • 18979527 1:CAS:528:DC%2BD1MXjs1KhtLo%3D 10.1002/mas.20195
    • Wuhrer, M.; de Boer, A.R.; Deelder, A.M.: Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry. Mass Spectrom. Rev. 28(2), 192-206 (2009)
    • (2009) Mass Spectrom. Rev. , vol.28 , Issue.2 , pp. 192-206
    • Wuhrer, M.1    De Boer, A.R.2    Deelder, A.M.3
  • 42
    • 79953292549 scopus 로고    scopus 로고
    • Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides
    • 21366235 1:CAS:528:DC%2BC3MXis1arsr4%3D 10.1021/ac1027116
    • Selman, M.H.J.; Hemayatkar, M.; Deelder, A.M.; Wuhrer, M.: Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides. Anal. Chem. 83(7), 2492-2499 (2011)
    • (2011) Anal. Chem. , vol.83 , Issue.7 , pp. 2492-2499
    • Selman, M.H.J.1    Hemayatkar, M.2    Deelder, A.M.3    Wuhrer, M.4
  • 43
    • 33645748520 scopus 로고    scopus 로고
    • Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles
    • 16522863
    • Sparbier, K.; Koch, S.; Kessler, I.; Wenzel, T.; Kostrzewa, M.: Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles. J. Biomol. Tech. 16(4), 407-413 (2005)
    • (2005) J. Biomol. Tech. , vol.16 , Issue.4 , pp. 407-413
    • Sparbier, K.1    Koch, S.2    Kessler, I.3    Wenzel, T.4    Kostrzewa, M.5
  • 44
    • 33746318976 scopus 로고    scopus 로고
    • Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles
    • 1:CAS:528:DC%2BD28Xns12ms7o%3D 10.1016/j.jchromb.2006.06.028
    • Sparbier, K.; Wenzel, T.; Kostrzewa, M.: Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles. J. Chromatogr. B 840(1), 29-36 (2006)
    • (2006) J. Chromatogr. B , vol.840 , Issue.1 , pp. 29-36
    • Sparbier, K.1    Wenzel, T.2    Kostrzewa, M.3
  • 45
    • 36048977494 scopus 로고    scopus 로고
    • Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection
    • 17916798
    • Sparbier, K.; Asperger, A.; Resemann, A.; Kessler, I.; Koch, S.; Wenzel, T.; Stein, G.; Vorwerg, L.; Suckau, D.; Kostrzewa, M.: Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection. J. Biomol. Tech. 18(4), 252-258 (2007)
    • (2007) J. Biomol. Tech. , vol.18 , Issue.4 , pp. 252-258
    • Sparbier, K.1    Asperger, A.2    Resemann, A.3    Kessler, I.4    Koch, S.5    Wenzel, T.6    Stein, G.7    Vorwerg, L.8    Suckau, D.9    Kostrzewa, M.10
  • 46
    • 58149464326 scopus 로고    scopus 로고
    • Highly specific enrichment of glycopeptides using boronic acid-functionalized mesoporous silica
    • 19117470 1:CAS:528:DC%2BD1cXhsVOnsLnO 10.1021/ac801912t
    • Xu, Y.; Wu, Z.; Zhang, L.; Lu, H.; Yang, P.; Webley, P.A.; Zhao, D.: Highly specific enrichment of glycopeptides using boronic acid-functionalized mesoporous silica. Anal. Chem. 81(1), 503-508 (2009)
    • (2009) Anal. Chem. , vol.81 , Issue.1 , pp. 503-508
    • Xu, Y.1    Wu, Z.2    Zhang, L.3    Lu, H.4    Yang, P.5    Webley, P.A.6    Zhao, D.7
  • 47
    • 79952250363 scopus 로고    scopus 로고
    • Boric acid gel enrichment of glycosylated proteins in human wound fluids
    • 21278005 1:CAS:528:DC%2BC3MXjsFCgsro%3D 10.1016/j.jprot.2011.01.005
    • Krisp, C.; Kubutat, C.; Kyas, A.; Steinstrasser, L.; Jacobsen, F.; Wolters, D.: Boric acid gel enrichment of glycosylated proteins in human wound fluids. J. Proteomics 74(4), 502-509 (2011)
    • (2011) J. Proteomics , vol.74 , Issue.4 , pp. 502-509
    • Krisp, C.1    Kubutat, C.2    Kyas, A.3    Steinstrasser, L.4    Jacobsen, F.5    Wolters, D.6
  • 48
    • 70949105966 scopus 로고    scopus 로고
    • On-plate-selective enrichment of glycopeptides using boronic acid-modified gold nanoparticles for direct MALDI-QIT-TOF MS analysis
    • 19834891 1:CAS:528:DC%2BD1MXhsVKhtLbK 10.1002/pmic.200900033
    • Tang, J.; Liu, Y.; Qi, D.; Yao, G.; Deng, C.; Zhang, X.: On-plate-selective enrichment of glycopeptides using boronic acid-modified gold nanoparticles for direct MALDI-QIT-TOF MS analysis. Proteomics 9(22), 5046-5055 (2009)
    • (2009) Proteomics , vol.9 , Issue.22 , pp. 5046-5055
    • Tang, J.1    Liu, Y.2    Qi, D.3    Yao, G.4    Deng, C.5    Zhang, X.6
  • 49
    • 0025344805 scopus 로고
    • Location and characterization of the three carbohydrate prosthetic groups of human protein HC
    • 1694784 1:CAS:528:DyaK3cXkvFemtrg%3D 10.1016/0014-5793(90)81531-R
    • Escribano, J.; Lopex-Otin, C.; Hjerpe, A.; Grubb, A.; Mendez, E.: Location and characterization of the three carbohydrate prosthetic groups of human protein HC. FEBS Lett. 266(1-2), 167-170 (1990)
    • (1990) FEBS Lett. , vol.266 , Issue.1-2 , pp. 167-170
    • Escribano, J.1    Lopex-Otin, C.2    Hjerpe, A.3    Grubb, A.4    Mendez, E.5
  • 50
    • 0026051641 scopus 로고
    • Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: The identification of Xaa-Pro-Xaa-Xaa as a motif for Thr-O-glycosylation
    • 1908233 1:CAS:528:DyaK3MXltlSgsro%3D 10.1016/0006-291X(91)91019-9
    • Gooley, A.A.; Classon, B.J.; Marschalek, R.; Williams, K.L.: Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: the identification of Xaa-Pro-Xaa-Xaa as a motif for Thr-O-glycosylation. Biochem. Biophys. Res. Commun. 178(3), 1194-1201 (1991)
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , Issue.3 , pp. 1194-1201
    • Gooley, A.A.1    Classon, B.J.2    Marschalek, R.3    Williams, K.L.4
  • 51
    • 0029148324 scopus 로고
    • Isolation and characterization of human milk bile salt-activated lipase C-tail fragment
    • 7654718 1:CAS:528:DyaK2MXnt1Kltro%3D 10.1021/bi00033a039
    • Wang, C.S.; Dashti, A.; Jackson, K.W.; Yeh, J.C.; Cummings, R.D.; Tang, J.: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry 34(33), 10639-10644 (1995)
    • (1995) Biochemistry , vol.34 , Issue.33 , pp. 10639-10644
    • Wang, C.S.1    Dashti, A.2    Jackson, K.W.3    Yeh, J.C.4    Cummings, R.D.5    Tang, J.6
  • 52
    • 0030924831 scopus 로고    scopus 로고
    • Phosphorylation and O-glycosylation sites of bovine chromogranin A from adrenal medullary chromaffin granules and their relationship with biological activities
    • 9115255 1:CAS:528:DyaK2sXivF2qs7s%3D 10.1074/jbc.272.18.11928
    • Strub, J.M.; Sorokine, O.; van Dorsselaer, A.; Aunis, D.; Metz-Boutigue, M.H.: Phosphorylation and O-glycosylation sites of bovine chromogranin A from adrenal medullary chromaffin granules and their relationship with biological activities. J. Biol. Chem. 272(18), 11928-11936 (1997)
    • (1997) J. Biol. Chem. , vol.272 , Issue.18 , pp. 11928-11936
    • Strub, J.M.1    Sorokine, O.2    Van Dorsselaer, A.3    Aunis, D.4    Metz-Boutigue, M.H.5
  • 53
    • 0034609578 scopus 로고    scopus 로고
    • Posttranslationally processed forms of the human chemokine HCC-1
    • 10978165 1:CAS:528:DC%2BD3cXlsV2itL0%3D 10.1021/bi992488q
    • Richter, R.; Schulz-Knappe, P.; John, H.; Forssmann, W.-G.: Posttranslationally processed forms of the human chemokine HCC-1. Biochemistry 39(35), 10799-10805 (2000)
    • (2000) Biochemistry , vol.39 , Issue.35 , pp. 10799-10805
    • Richter, R.1    Schulz-Knappe, P.2    John, H.3    Forssmann, W.-G.4
  • 54
    • 0024370669 scopus 로고
    • Glycosylation of human apolipoprotein E. The carbohydrate attachment site is threonine 194
    • 2498325 1:CAS:528:DyaL1MXktVaqtro%3D
    • Wernette-Hammond, M.E.; Lauer, S.J.; Corsini, A.; Walker, D.; Taylor, J.M.; Rall, S.C.: Glycosylation of human apolipoprotein E. The carbohydrate attachment site is threonine 194. J. Biol. Chem. 264(15), 9094-9101 (1989)
    • (1989) J. Biol. Chem. , vol.264 , Issue.15 , pp. 9094-9101
    • Wernette-Hammond, M.E.1    Lauer, S.J.2    Corsini, A.3    Walker, D.4    Taylor, J.M.5    Rall, S.C.6
  • 55
    • 77954203412 scopus 로고    scopus 로고
    • Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics
    • 20536156 1:CAS:528:DC%2BC3cXnt1GltL0%3D 10.1021/ac100530w
    • Mysling, S.; Palmisano, G.; Højrup, P.; Thaysen-Andersen, M.: Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics. Anal. Chem. 82(13), 5598-5609 (2010)
    • (2010) Anal. Chem. , vol.82 , Issue.13 , pp. 5598-5609
    • Mysling, S.1    Palmisano, G.2    Højrup, P.3    Thaysen-Andersen, M.4
  • 57
    • 77955440095 scopus 로고    scopus 로고
    • Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle
    • 20507882 1:CAS:528:DC%2BC3cXpvFSqsbk%3D 10.1093/glycob/cwq082
    • Nilsson, J.; Nilsson, J.; Larson, G.; Grahn, A.: Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle. Glycobiology 20(9), 1160-1169 (2010)
    • (2010) Glycobiology , vol.20 , Issue.9 , pp. 1160-1169
    • Nilsson, J.1    Nilsson, J.2    Larson, G.3    Grahn, A.4
  • 59
    • 78649907006 scopus 로고    scopus 로고
    • Further insight into the roles of the glycans attached to human blood protein C inhibitor
    • 21056543 1:CAS:528:DC%2BC3cXhsFGgs77M 10.1016/j.bbrc.2010.11.005
    • Sun, W.; Parry, S.; Ubhayasekera, W.; Engström, Å.; Dell, A.; Schedin-Weiss, S.: Further insight into the roles of the glycans attached to human blood protein C inhibitor. Biochem. Biophys. Res. Commun. 403(2), 198-202 (2010)
    • (2010) Biochem. Biophys. Res. Commun. , vol.403 , Issue.2 , pp. 198-202
    • Sun, W.1    Parry, S.2    Ubhayasekera, W.3    Engström, Å.4    Dell, A.5    Schedin-Weiss, S.6
  • 60
    • 79961077443 scopus 로고    scopus 로고
    • Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid {beta}-peptides in human cerebrospinal fluid
    • 21712440 1:CAS:528:DC%2BC3MXps1ektro%3D 10.1073/pnas.1102664108
    • Halim, A.; Brinkmalm, G.; Rüetschi, U.; Westman-Brinkmalm, A.; Portelius, E.; Zetterberg, H.; Blennow, K.; Larson, G.; Nilsson, J.: Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid {beta}-peptides in human cerebrospinal fluid. Proc. Natl. Acad. Sci. 108(29), 11848-11853 (2011)
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , Issue.29 , pp. 11848-11853
    • Halim, A.1    Brinkmalm, G.2    Rüetschi, U.3    Westman-Brinkmalm, A.4    Portelius, E.5    Zetterberg, H.6    Blennow, K.7    Larson, G.8    Nilsson, J.9
  • 61
    • 38649136201 scopus 로고    scopus 로고
    • Integrated analysis of the cerebrospinal fluid peptidome and proteome
    • 18052119 1:CAS:528:DC%2BD2sXhtlygsrrJ 10.1021/pr070501k
    • Zougman, A.; Pilch, B.; Podtelejnikov, A.; Kiehntopf, M.; Schnabel, C.; Kumar, C.; Mann, M.: Integrated analysis of the cerebrospinal fluid peptidome and proteome. J. Proteome Res. 7(1), 386-399 (2008)
    • (2008) J. Proteome Res. , vol.7 , Issue.1 , pp. 386-399
    • Zougman, A.1    Pilch, B.2    Podtelejnikov, A.3    Kiehntopf, M.4    Schnabel, C.5    Kumar, C.6    Mann, M.7
  • 62
    • 77956542058 scopus 로고    scopus 로고
    • Glycosylation and sialylation of macrophage-derived human apolipoprotein e analyzed by SDS-PAGE and mass spectrometry: Evidence for a novel site of glycosylation on Ser290
    • 20511397 1:CAS:528:DC%2BC3cXhtlegt7bI 10.1074/mcp.M900430-MCP200
    • Lee, Y.; Kockx, M.; Raftery, M.J.; Jessup, W.; Griffith, R.; Kritharides, L.: Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290. Mol. Cell Proteomics 9(9), 1968-1981 (2010)
    • (2010) Mol. Cell Proteomics , vol.9 , Issue.9 , pp. 1968-1981
    • Lee, Y.1    Kockx, M.2    Raftery, M.J.3    Jessup, W.4    Griffith, R.5    Kritharides, L.6
  • 63
    • 61849088987 scopus 로고    scopus 로고
    • Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation
    • 19093876 1:CAS:528:DC%2BD1cXhsFaisrjP 10.1021/pr800758g
    • Perdivara, I.; Petrovich, R.; Allinquant, B.; Deterding, L.J.; Tomer, K.B.; Przybylski, M.: Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation. J. Proteome Res. 8(2), 631-642 (2009)
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 631-642
    • Perdivara, I.1    Petrovich, R.2    Allinquant, B.3    Deterding, L.J.4    Tomer, K.B.5    Przybylski, M.6
  • 64
    • 77950631561 scopus 로고    scopus 로고
    • Mass spectrometric identification of aberrantly glycosylated human apolipoprotein C-III peptides in urine from schistosoma mansoni-infected individuals
    • 20071361 1:CAS:528:DC%2BC3cXlvFCjur8%3D 10.1074/mcp.M900537-MCP200
    • Balog, C.I.A.; Mayboroda, O.A.; Wuhrer, M.; Hokke, C.H.; Deelder, A.M.; Hensbergen, P.J.: Mass spectrometric identification of aberrantly glycosylated human apolipoprotein C-III peptides in urine from schistosoma mansoni-infected individuals. Mol. Cell Proteomics 9(4), 667-681 (2010)
    • (2010) Mol. Cell Proteomics , vol.9 , Issue.4 , pp. 667-681
    • Balog, C.I.A.1    Mayboroda, O.A.2    Wuhrer, M.3    Hokke, C.H.4    Deelder, A.M.5    Hensbergen, P.J.6
  • 66
    • 77952366352 scopus 로고    scopus 로고
    • Quantitative analysis of intact apolipoproteins in human HDL by top-down differential mass spectrometry
    • 20388904 1:CAS:528:DC%2BC3cXksFyqsrw%3D 10.1073/pnas.0910776107
    • Mazur, M.T.; Cardasis, H.L.; Spellman, D.S.; Liaw, A.; Yates, N.A.; Hendrickson, R.C.: Quantitative analysis of intact apolipoproteins in human HDL by top-down differential mass spectrometry. Proc. Natl. Acad. Sci. 107(17), 7728-7733 (2010)
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , Issue.17 , pp. 7728-7733
    • Mazur, M.T.1    Cardasis, H.L.2    Spellman, D.S.3    Liaw, A.4    Yates, N.A.5    Hendrickson, R.C.6
  • 68
    • 62349122640 scopus 로고    scopus 로고
    • Localization of O-glycans in MUC1 glycoproteins using electron-capture dissociation fragmentation mass spectrometry
    • 19095697 1:CAS:528:DC%2BD1MXivFSntbg%3D 10.1093/glycob/cwn144
    • Sihlbom, C.; van Dijk Härd, I.; Lidell, M.E.; Noll, T.; Hansson, G.C.; Backstrom, M.: Localization of O-glycans in MUC1 glycoproteins using electron-capture dissociation fragmentation mass spectrometry. Glycobiology 19(4), 375-381 (2009)
    • (2009) Glycobiology , vol.19 , Issue.4 , pp. 375-381
    • Sihlbom, C.1    Van Dijk Härd, I.2    Lidell, M.E.3    Noll, T.4    Hansson, G.C.5    Backstrom, M.6
  • 69
    • 0012252007 scopus 로고    scopus 로고
    • Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage
    • 12918977 1:CAS:528:DC%2BD3sXivVaqu7Y%3D 10.1021/ac026295b
    • Kjeldsen, F.; Haselmann, K.F.; Budnik, B.A.; Sørensen, E.S.; Zubarev, R.A.: Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage. Anal. Chem. 75(10), 2355-2361 (2003)
    • (2003) Anal. Chem. , vol.75 , Issue.10 , pp. 2355-2361
    • Kjeldsen, F.1    Haselmann, K.F.2    Budnik, B.A.3    Sørensen, E.S.4    Zubarev, R.A.5
  • 70
    • 21444448470 scopus 로고    scopus 로고
    • Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation fourier transform-ion cyclotron resonance mass spectrometry
    • 15728186 1:CAS:528:DC%2BD2MXjvFers70%3D 10.1074/jbc.M411368200
    • Renfrow, M.B.: Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation fourier transform-ion cyclotron resonance mass spectrometry. J. Biol. Chem. 280(19), 19136-19145 (2005)
    • (2005) J. Biol. Chem. , vol.280 , Issue.19 , pp. 19136-19145
    • Renfrow, M.B.1
  • 71
    • 35648929345 scopus 로고    scopus 로고
    • Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: Implications for IgA nephropathy
    • 17712550 1:CAS:528:DC%2BD2sXht1GhsLrF 10.1007/s00216-007-1500-z
    • Renfrow, M.B.; Mackay, C.L.; Chalmers, M.J.; Julian, B.A.; Mestecky, J.; Kilian, M.; Poulsen, K.; Emmett, M.R.; Marshall, A.G.; Novak, J.: Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: implications for IgA nephropathy. Anal. Bioanal. Chem. 389(5), 1397-1407 (2007)
    • (2007) Anal. Bioanal. Chem. , vol.389 , Issue.5 , pp. 1397-1407
    • Renfrow, M.B.1    Mackay, C.L.2    Chalmers, M.J.3    Julian, B.A.4    Mestecky, J.5    Kilian, M.6    Poulsen, K.7    Emmett, M.R.8    Marshall, A.G.9    Novak, J.10
  • 73
    • 0027586797 scopus 로고
    • Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: Methods for selective detection of glycopeptides in protein digests
    • 8470819 1:CAS:528:DyaK3sXht1Sgur4%3D 10.1021/ac00055a009
    • Huddleston, M.J.; Bean, M.F.; Carr, S.A.: Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: methods for selective detection of glycopeptides in protein digests. Anal. Chem. 65(7), 877-884 (1993)
    • (1993) Anal. Chem. , vol.65 , Issue.7 , pp. 877-884
    • Huddleston, M.J.1    Bean, M.F.2    Carr, S.A.3
  • 74
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
    • 11680880 1:CAS:528:DC%2BD3MXhvVCis7o%3D 10.1002/1615-9861(200102)1: 2<340: AID-PROT340>3.0.CO;2-B
    • Cooper, C.A.; Gasteiger, E.; Packer, N.H.: GlycoMod - a software tool for determining glycosylation compositions from mass spectrometric data. Proteomics 1(2), 340-349 (2001)
    • (2001) Proteomics , vol.1 , Issue.2 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.H.3
  • 76
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin
    • 8999917 1:CAS:528:DyaK2sXotVylsQ%3D%3D 10.1074/jbc.272.4.2156
    • Chiba, A.; Matsumura, K.; Yamada, H.; Inazu, T.; Shimizu, T.; Kusunoki, S.; Kanazawa, I.; Kobata, A.; Endo, T.: Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin. J. Biol. Chem. 272(4), 2156-2162 (1997)
    • (1997) J. Biol. Chem. , vol.272 , Issue.4 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 77
    • 84868028000 scopus 로고    scopus 로고
    • O-Mannose and O-GalNAc glycosylation of mammalian α-dystroglycan is conserved in a region-specific manner
    • doi: 10.1093/glycob/cws109
    • Gomez Toledo, A.; Raducu, M.; Cruzes, J.; Nilsson, J.; Halim, A.; Larson, G.; Ruetschi, U.; Grahn, A.: O-Mannose and O-GalNAc glycosylation of mammalian α-dystroglycan is conserved in a region-specific manner. Glycobiology. doi: 10.1093/glycob/cws109 (2012)
    • (2012) Glycobiology
    • Gomez Toledo, A.1    Raducu, M.2    Cruzes, J.3    Nilsson, J.4    Halim, A.5    Larson, G.6    Ruetschi, U.7    Grahn, A.8
  • 78
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • 17721543 1:CAS:528:DC%2BD2sXps12gsLY%3D 10.1038/nmeth1060
    • Olsen, J.V.; Macek, B.; Lange, O.; Makarov, A.; Horning, S.; Mann, M.: Higher-energy C-trap dissociation for peptide modification analysis. Nat. Methods 4(9), 709-712 (2007)
    • (2007) Nat. Methods , vol.4 , Issue.9 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 79
    • 34548186744 scopus 로고    scopus 로고
    • An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins
    • 17636988 10.1021/pr0700605 1:CAS:528:DC%2BD2sXnvVShsbg%3D
    • Hägglund, P.; Matthiesen, R.; Elortza, F.; Højrup, P.; Roepstorff, P.; Jensen, O.N.; Bunkenborg, J.: An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins. J. Proteome Res. 6(8), 3021-3031 (2007)
    • (2007) J. Proteome Res. , vol.6 , Issue.8 , pp. 3021-3031
    • Hägglund, P.1    Matthiesen, R.2    Elortza, F.3    Højrup, P.4    Roepstorff, P.5    Jensen, O.N.6    Bunkenborg, J.7
  • 80
    • 70350735945 scopus 로고    scopus 로고
    • Enrichment of glycopeptides for glycan structure and attachment site identification
    • 19838169 1:CAS:528:DC%2BD1MXht1Ogsr%2FI 10.1038/nmeth.1392
    • Nilsson, J.; Rüetschi, U.; Halim, A.; Hesse, C.; Carlsohn, E.; Brinkmalm, G.; Larson, G.: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat. Methods 6(11), 809-811 (2009)
    • (2009) Nat. Methods , vol.6 , Issue.11 , pp. 809-811
    • Nilsson, J.1    Rüetschi, U.2    Halim, A.3    Hesse, C.4    Carlsohn, E.5    Brinkmalm, G.6    Larson, G.7
  • 81
    • 0035866603 scopus 로고    scopus 로고
    • Mass spectrometric determination of O-glycosylation sites using beta-elimination and partial acid hydrolysis
    • 11305661 1:CAS:528:DC%2BD3MXhtFWqtbc%3D 10.1021/ac001288d
    • Mirgorodskaya, E.; Hassan, H.; Clausen, H.; Roepstorff, P.: Mass spectrometric determination of O-glycosylation sites using beta-elimination and partial acid hydrolysis. Anal. Chem. 73(6), 1263-1269 (2001)
    • (2001) Anal. Chem. , vol.73 , Issue.6 , pp. 1263-1269
    • Mirgorodskaya, E.1    Hassan, H.2    Clausen, H.3    Roepstorff, P.4
  • 82
    • 0033541695 scopus 로고    scopus 로고
    • Partial vapor-phase hydrolysis of peptide bonds: A method for mass spectrometric determination of O-glycosylated sites in glycopeptides
    • 10094775 1:CAS:528:DyaK1MXitVWgt7k%3D 10.1006/abio.1998.3089
    • Mirgorodskaya, E.; Hassan, H.; Wandall, H.H.; Clausen, H.; Roepstorff, P.: Partial vapor-phase hydrolysis of peptide bonds: a method for mass spectrometric determination of O-glycosylated sites in glycopeptides. Anal. Biochem. 269(1), 54-65 (1999)
    • (1999) Anal. Biochem. , vol.269 , Issue.1 , pp. 54-65
    • Mirgorodskaya, E.1    Hassan, H.2    Wandall, H.H.3    Clausen, H.4    Roepstorff, P.5
  • 83
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry
    • 8742080 1:CAS:528:DyaK28Xps1eluw%3D%3D 10.1006/abio.1996.0047
    • Greis, K.D.; Hayes, B.K.; Comer, F.I.; Kirk, M.; Barnes, S.; Lowary, T.L.; Hart, G.W.: Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry. Anal. Biochem. 234(1), 38-49 (1996)
    • (1996) Anal. Biochem. , vol.234 , Issue.1 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4    Barnes, S.5    Lowary, T.L.6    Hart, G.W.7
  • 84
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • 12438562 1:CAS:528:DC%2BD38XovF2ktLo%3D 10.1074/mcp.M200048-MCP200
    • Wells, L.; Vosseller, K.; Cole, R.N.; Cronshaw, J.M.; Matunis, M.J.; Hart, G.W.: Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell Proteomics 1(10), 791-804 (2002)
    • (2002) Mol. Cell Proteomics , vol.1 , Issue.10 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 86
    • 22144482323 scopus 로고    scopus 로고
    • Protein identification using sequential ion/ion reactions and tandem mass spectrometry
    • 15983376 1:CAS:528:DC%2BD2MXmsVaksbg%3D 10.1073/pnas.0503189102
    • Coon, J.J.; Ueberheide, B.; Syka, J.E.P.; Dryhurst, D.D.; Ausio, J.; Shabanowitz, J.; Hunt, D.F.: Protein identification using sequential ion/ion reactions and tandem mass spectrometry. Proc. Natl. Acad. Sci. 102(27), 9463-9468 (2005)
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , Issue.27 , pp. 9463-9468
    • Coon, J.J.1    Ueberheide, B.2    Syka, J.E.P.3    Dryhurst, D.D.4    Ausio, J.5    Shabanowitz, J.6    Hunt, D.F.7
  • 87
    • 0032731855 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer
    • 10546526 1:CAS:528:DyaK1MXlvVSisr8%3D 10.1021/ac990578v
    • Mirgorodskaya, E.; Roepstorff, P.; Zubarev, R.A.: Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer. Anal. Chem. 71(20), 4431-4436 (1999)
    • (1999) Anal. Chem. , vol.71 , Issue.20 , pp. 4431-4436
    • Mirgorodskaya, E.1    Roepstorff, P.2    Zubarev, R.A.3
  • 88
    • 29144433431 scopus 로고    scopus 로고
    • Electron capture dissociation of O-glycosylated peptides: Radical site-induced fragmentation of glycosidic bonds
    • 1:CAS:528:DC%2BD2MXhtlegsrrK 10.1255/ejms.738
    • Mormann, M.; Paulsen, H.; Peter-Katalinić, J.: Electron capture dissociation of O-glycosylated peptides: radical site-induced fragmentation of glycosidic bonds. Eur. J. Mass Spectrom. 11(5), 497-511 (2005)
    • (2005) Eur. J. Mass Spectrom. , vol.11 , Issue.5 , pp. 497-511
    • Mormann, M.1    Paulsen, H.2    Peter-Katalinić, J.3
  • 89
    • 0030586369 scopus 로고    scopus 로고
    • The role of glycosylation in synthesis and secretion of beta-amyloid precursor protein by Chinese hamster ovary cells
    • 8660696 10.1006/abbi.1996.0296
    • Påhlsson, P.; Spitalnik, S.L.: The role of glycosylation in synthesis and secretion of beta-amyloid precursor protein by Chinese hamster ovary cells. Arch. Biochem. Biophys. 331(2), 177-186 (1996)
    • (1996) Arch. Biochem. Biophys. , vol.331 , Issue.2 , pp. 177-186
    • Påhlsson, P.1    Spitalnik, S.L.2
  • 90
    • 0032825983 scopus 로고    scopus 로고
    • Study of the sugar chains of recombinant human amyloid precursor protein produced by Chinese hamster ovary cells
    • 10572956 1:CAS:528:DyaK1MXnsFSrtrs%3D 10.1016/S0304-4165(99)00140-3
    • Sato, Y.; Liu, C.; Wojczyk, B.S.; Kobata, A.; Spitalnik, S.L.; Endo, T.: Study of the sugar chains of recombinant human amyloid precursor protein produced by Chinese hamster ovary cells. Biochim. Biophys. Acta 1472(1-2), 344-358 (1999)
    • (1999) Biochim. Biophys. Acta , vol.1472 , Issue.1-2 , pp. 344-358
    • Sato, Y.1    Liu, C.2    Wojczyk, B.S.3    Kobata, A.4    Spitalnik, S.L.5    Endo, T.6
  • 91
    • 53849139399 scopus 로고    scopus 로고
    • Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins
    • 18521746 1:CAS:528:DC%2BD1cXht1equrfI 10.1007/s10719-008-9140-x
    • Akasaka-Manya, K.; Manya, H.; Sakurai, Y.; Wojczyk, B.S.; Spitalnik, S.L.; Endo, T.: Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins. Glycoconj. J. 25(8), 775-786 (2008)
    • (2008) Glycoconj. J. , vol.25 , Issue.8 , pp. 775-786
    • Akasaka-Manya, K.1    Manya, H.2    Sakurai, Y.3    Wojczyk, B.S.4    Spitalnik, S.L.5    Endo, T.6
  • 92
    • 33645775230 scopus 로고    scopus 로고
    • Determination of beta-amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry
    • 16602710 1:CAS:528:DC%2BD28XitFOiur8%3D 10.1021/pr050475v
    • Portelius, E.; Westman-Brinkmalm, A.; Zetterberg, H.; Blennow, K.: Determination of beta-amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry. J. Proteome Res. 5(4), 1010-1016 (2006)
    • (2006) J. Proteome Res. , vol.5 , Issue.4 , pp. 1010-1016
    • Portelius, E.1    Westman-Brinkmalm, A.2    Zetterberg, H.3    Blennow, K.4
  • 94
    • 36348970121 scopus 로고    scopus 로고
    • Characterization of amyloid beta peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry
    • 17927230 1:CAS:528:DC%2BD2sXhtFegsrnE 10.1021/pr0703627
    • Portelius, E.; Tran, A.J.; Andreasson, U.; Persson, R.; Brinkmalm, G.; Zetterberg, H.; Blennow, K.; Westman-Brinkmalm, A.: Characterization of amyloid beta peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry. J. Proteome Res. 6(11), 4433-4439 (2007)
    • (2007) J. Proteome Res. , vol.6 , Issue.11 , pp. 4433-4439
    • Portelius, E.1    Tran, A.J.2    Andreasson, U.3    Persson, R.4    Brinkmalm, G.5    Zetterberg, H.6    Blennow, K.7    Westman-Brinkmalm, A.8
  • 95
    • 0023555539 scopus 로고
    • Molecular cloning of a human apoC-III variant: Thr 74 - Ala 74 mutation prevents O-glycosylation
    • 3123586 1:CAS:528:DyaL1cXhvF2iur0%3D
    • Maeda, H.; Hashimoto, R.K.; Ogura, T.; Hiraga, S.; Uzawa, H.: Molecular cloning of a human apoC-III variant: Thr 74 - Ala 74 mutation prevents O-glycosylation. J. Lipid Res. 28(12), 1405-1409 (1987)
    • (1987) J. Lipid Res. , vol.28 , Issue.12 , pp. 1405-1409
    • Maeda, H.1    Hashimoto, R.K.2    Ogura, T.3    Hiraga, S.4    Uzawa, H.5
  • 96
    • 0024854512 scopus 로고
    • Apolipoprotein C-III0 lacks carbohydrate residues: Use of mass spectrometry to study apolipoprotein structure
    • 2614277 1:CAS:528:DyaK3cXjt1elsg%3D%3D
    • Ito, Y.; Breslow, J.L.; Chait, B.T.: Apolipoprotein C-III0 lacks carbohydrate residues: use of mass spectrometry to study apolipoprotein structure. J. Lipid Res. 30(11), 1781-1787 (1989)
    • (1989) J. Lipid Res. , vol.30 , Issue.11 , pp. 1781-1787
    • Ito, Y.1    Breslow, J.L.2    Chait, B.T.3
  • 97
    • 36749040214 scopus 로고    scopus 로고
    • Reverse glycoblotting allows rapid-enrichment glycoproteomics of biopharmaceuticals and disease-related biomarkers
    • 17943939 1:CAS:528:DC%2BD2sXhsVWqtLzK 10.1002/anie.200702919
    • Kurogochi, M.; Amano, M.; Fumoto, M.; Takimoto, A.; Kondo, H.; Nishimura, S.: Reverse glycoblotting allows rapid-enrichment glycoproteomics of biopharmaceuticals and disease-related biomarkers. Angew. Chem. Int. Ed. Engl. 46(46), 8808-8813 (2007)
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , Issue.46 , pp. 8808-8813
    • Kurogochi, M.1    Amano, M.2    Fumoto, M.3    Takimoto, A.4    Kondo, H.5    Nishimura, S.6
  • 98
    • 0038034116 scopus 로고    scopus 로고
    • Cleavage N-terminal to proline: Analysis of a database of peptide tandem mass spectra
    • 12720328 1:CAS:528:DC%2BD3sXitlGlsLo%3D 10.1021/ac026359i
    • Breci, L.A.; Tabb, D.L.; Yates, J.R.; Wysocki, V.H.: Cleavage N-terminal to proline: analysis of a database of peptide tandem mass spectra. Anal. Chem. 75(9), 1963-1971 (2003)
    • (2003) Anal. Chem. , vol.75 , Issue.9 , pp. 1963-1971
    • Breci, L.A.1    Tabb, D.L.2    Yates, J.R.3    Wysocki, V.H.4
  • 99
    • 84859862380 scopus 로고    scopus 로고
    • Human urinary glycoproteomics; Attachment site specific analysis of N-and O-linked glycosylations by CID and ECD
    • Halim, A.; Nilsson, J.; Rüetschi, U.; Hesse, C.; Larson, G.: Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD. Mol. Cell Proteomics 11(4), M111.013649 (2012)
    • (2012) Mol. Cell Proteomics , vol.11 , Issue.4
    • Halim, A.1    Nilsson, J.2    Rüetschi, U.3    Hesse, C.4    Larson, G.5
  • 100
    • 77956296123 scopus 로고    scopus 로고
    • Sialic acid-focused quantitative mouse serum glycoproteomics by multiple reaction monitoring assay
    • 20571061 1:CAS:528:DC%2BC3cXhsFWhs7vF 10.1074/mcp.M110.000430
    • Kurogochi, M.; Matsushista, T.; Amano, M.; Furukawa, J.; Shinohara, Y.; Aoshima, M.; Nishimura, S.: Sialic acid-focused quantitative mouse serum glycoproteomics by multiple reaction monitoring assay. Mol. Cell Proteomics 9(11), 2354-2368 (2010)
    • (2010) Mol. Cell Proteomics , vol.9 , Issue.11 , pp. 2354-2368
    • Kurogochi, M.1    Matsushista, T.2    Amano, M.3    Furukawa, J.4    Shinohara, Y.5    Aoshima, M.6    Nishimura, S.7
  • 101
    • 79960210781 scopus 로고    scopus 로고
    • Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities
    • 20652609 1:CAS:528:DC%2BC3MXmsFGgsLs%3D 10.1007/s00726-010-0692-2
    • Darula, Z.; Chalkley, R.J.; Lynn, A.; Baker, P.R.; Medzihradszky, K.F.: Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities. Amino Acids 41(2), 321-328 (2011)
    • (2011) Amino Acids , vol.41 , Issue.2 , pp. 321-328
    • Darula, Z.1    Chalkley, R.J.2    Lynn, A.3    Baker, P.R.4    Medzihradszky, K.F.5
  • 102
    • 77955482287 scopus 로고    scopus 로고
    • Mass spectrometric analysis, automated identification and complete annotation of O-linked glycopeptides
    • 1:CAS:528:DC%2BC3cXovVWqtrY%3D 10.1255/ejms.1028
    • Darula, Z.; Chalkley, R.J.; Baker, P.; Burlingame, A.L.; Medzihradszky, K.F.: Mass spectrometric analysis, automated identification and complete annotation of O-linked glycopeptides. Eur. J. Mass Spectrom. 16(3), 421-428 (2010)
    • (2010) Eur. J. Mass Spectrom. , vol.16 , Issue.3 , pp. 421-428
    • Darula, Z.1    Chalkley, R.J.2    Baker, P.3    Burlingame, A.L.4    Medzihradszky, K.F.5
  • 103
    • 84863789621 scopus 로고    scopus 로고
    • How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides
    • Darula, Z.; Sherman, J.; Medzihradszky, K.F.: How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides. Mol. Cell Proteomics 11(7), O111.016774 (2012)
    • (2012) Mol. Cell Proteomics , vol.11 , Issue.7
    • Darula, Z.1    Sherman, J.2    Medzihradszky, K.F.3
  • 105
    • 77952704489 scopus 로고    scopus 로고
    • Cosmc is an essential chaperone for correct protein O-glycosylation
    • 20439703 1:CAS:528:DC%2BC3cXmslGrtL4%3D 10.1073/pnas.0914004107
    • Wang, Y.; Ju, T.; Ding, X.; Xia, B.; Wang, W.; Xia, L.; He, M.; Cummings, R.D.: Cosmc is an essential chaperone for correct protein O-glycosylation. Proc. Natl. Acad. Sci. 107(20), 9228-9233 (2010)
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , Issue.20 , pp. 9228-9233
    • Wang, Y.1    Ju, T.2    Ding, X.3    Xia, B.4    Wang, W.5    Xia, L.6    He, M.7    Cummings, R.D.8
  • 107
    • 65349151261 scopus 로고    scopus 로고
    • Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry
    • 19288519 1:CAS:528:DC%2BD1MXltVertrY%3D 10.1002/pmic.200800249
    • Chu, C.S.; Ninonuevo, M.R.; Clowers, B.H.; Perkins, P.D.; An, H.J.; Yin, H.; Killeen, K.; Miyamoto, S.; Grimm, R.; Lebrilla, C.B.: Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry. Proteomics 9(7), 1939-1951 (2009)
    • (2009) Proteomics , vol.9 , Issue.7 , pp. 1939-1951
    • Chu, C.S.1    Ninonuevo, M.R.2    Clowers, B.H.3    Perkins, P.D.4    An, H.J.5    Yin, H.6    Killeen, K.7    Miyamoto, S.8    Grimm, R.9    Lebrilla, C.B.10
  • 108
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • 1358608 1:CAS:528:DyaK38Xls1Kjs7k%3D 10.1111/j.1432-1033.1992.tb17313.x
    • Kobata, A.: Structures and functions of the sugar chains of glycoproteins. Eur. J. Biochem. 209(2), 483-501 (1992)
    • (1992) Eur. J. Biochem. , vol.209 , Issue.2 , pp. 483-501
    • Kobata, A.1
  • 109
    • 2542487524 scopus 로고    scopus 로고
    • The third chains of living organisms - A trail of glycobiology that started from the third floor of building 4 in NIH
    • 15158661 1:CAS:528:DC%2BD2cXkt1Wrs78%3D 10.1016/j.abb.2004.01.023
    • Kobata, A.: The third chains of living organisms - a trail of glycobiology that started from the third floor of building 4 in NIH. Arch. Biochem. Biophys. 426(2), 107-121 (2004)
    • (2004) Arch. Biochem. Biophys. , vol.426 , Issue.2 , pp. 107-121
    • Kobata, A.1
  • 110
    • 21644459777 scopus 로고    scopus 로고
    • Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides
    • 15987113 1:CAS:528:DC%2BD2MXks1Sgtbs%3D 10.1021/ac050222l
    • Madera, M.; Mechref, Y.; Novotny, M.V.: Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides. Anal. Chem. 77(13), 4081-4090 (2005)
    • (2005) Anal. Chem. , vol.77 , Issue.13 , pp. 4081-4090
    • Madera, M.1    Mechref, Y.2    Novotny, M.V.3
  • 111
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • 17134948 1:CAS:528:DC%2BD28XhtlaltLzI 10.1016/j.bbapap.2006.10.007
    • Geyer, H.; Geyer, R.: Strategies for analysis of glycoprotein glycosylation. Biochim. Biophys. Acta 1764(12), 1853-1869 (2006)
    • (2006) Biochim. Biophys. Acta , vol.1764 , Issue.12 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 112
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • 14760718 1:CAS:528:DC%2BD2cXhs1Ciu78%3D 10.1002/pmic.200300556
    • Bunkenborg, J.; Pilch, B.J.; Podtelejnikov, A.V.; Wisniewski, J.R.: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 4(2), 454-465 (2004)
    • (2004) Proteomics , vol.4 , Issue.2 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wisniewski, J.R.4
  • 113
    • 33745827045 scopus 로고    scopus 로고
    • Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: Application to pancreatic cancer serum
    • 16823988 1:CAS:528:DC%2BD28XkvFGktbc%3D 10.1021/pr060034r
    • Zhao, J.; Simeone, D.M.; Heidt, D.; Anderson, M.A.; Lubman, D.M.: Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum. J. Proteome Res. 5(7), 1792-1802 (2006)
    • (2006) J. Proteome Res. , vol.5 , Issue.7 , pp. 1792-1802
    • Zhao, J.1    Simeone, D.M.2    Heidt, D.3    Anderson, M.A.4    Lubman, D.M.5
  • 114
    • 67650354379 scopus 로고    scopus 로고
    • Identification of glycoproteins carrying a target glycan-motif by liquid chromatography/multiple-stage mass spectrometry: Identification of Lewis x-conjugated glycoproteins in mouse kidney
    • 19453144 1:CAS:528:DC%2BD1MXntVyntLY%3D 10.1021/pr9000527
    • Hashii, N.; Kawasaki, N.; Itoh, S.; Nakajima, Y.; Harazono, A.; Kawanishi, T.; Yamaguchi, T.: Identification of glycoproteins carrying a target glycan-motif by liquid chromatography/multiple-stage mass spectrometry: identification of Lewis x-conjugated glycoproteins in mouse kidney. J. Proteome Res. 8(7), 3415-3429 (2009)
    • (2009) J. Proteome Res. , vol.8 , Issue.7 , pp. 3415-3429
    • Hashii, N.1    Kawasaki, N.2    Itoh, S.3    Nakajima, Y.4    Harazono, A.5    Kawanishi, T.6    Yamaguchi, T.7
  • 115
    • 35649011957 scopus 로고    scopus 로고
    • Exploring the sialiome using titanium dioxide chromatography and mass spectrometry
    • 17623646 1:CAS:528:DC%2BD2sXht1WksbrE 10.1074/mcp.M700086-MCP200
    • Larsen, M.R.; Jensen, S.S.; Jakobsen, L.A.; Heegaard, N.H.: Exploring the sialiome using titanium dioxide chromatography and mass spectrometry. Mol. Cell Proteomics 6(10), 1778-1787 (2007)
    • (2007) Mol. Cell Proteomics , vol.6 , Issue.10 , pp. 1778-1787
    • Larsen, M.R.1    Jensen, S.S.2    Jakobsen, L.A.3    Heegaard, N.H.4
  • 116
    • 78649961364 scopus 로고    scopus 로고
    • Selective enrichment of sialic acid-containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry
    • 21127490 1:CAS:528:DC%2BC3cXhsFSrsr7M 10.1038/nprot.2010.167
    • Palmisano, G.; Lendal, S.E.; Engholm-Keller, K.; Leth-Larsen, R.; Parker, B.L.; Larsen, M.R.: Selective enrichment of sialic acid-containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry. Nat. Protoc. 5(12), 1974-1982 (2010)
    • (2010) Nat. Protoc. , vol.5 , Issue.12 , pp. 1974-1982
    • Palmisano, G.1    Lendal, S.E.2    Engholm-Keller, K.3    Leth-Larsen, R.4    Parker, B.L.5    Larsen, M.R.6
  • 117
    • 14944367556 scopus 로고    scopus 로고
    • Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry
    • 15561728 1:CAS:528:DC%2BD2MXhvFKnt7o%3D
    • Larsen, M.R.; Hojrup, P.; Roepstorff, P.: Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry. Mol. Cell Proteomics 4(2), 107-119 (2005)
    • (2005) Mol. Cell Proteomics , vol.4 , Issue.2 , pp. 107-119
    • Larsen, M.R.1    Hojrup, P.2    Roepstorff, P.3
  • 118
    • 34247368120 scopus 로고    scopus 로고
    • Rapid and individual-specific glycoprofiling of the low abundance N-glycosylated protein tissue inhibitor of metalloproteinases-1
    • 17205978 1:CAS:528:DC%2BD2sXksVKgtbY%3D 10.1074/mcp.M600407-MCP200
    • Thaysen-Andersen, M.; Thogersen, I.B.; Nielsen, H.J.; Lademann, U.; Brunner, N.; Enghild, J.J.; Hojrup, P.: Rapid and individual-specific glycoprofiling of the low abundance N-glycosylated protein tissue inhibitor of metalloproteinases-1. Mol. Cell Proteomics 6(4), 638-647 (2007)
    • (2007) Mol. Cell Proteomics , vol.6 , Issue.4 , pp. 638-647
    • Thaysen-Andersen, M.1    Thogersen, I.B.2    Nielsen, H.J.3    Lademann, U.4    Brunner, N.5    Enghild, J.J.6    Hojrup, P.7
  • 119
    • 65249090285 scopus 로고    scopus 로고
    • Quantitative analysis of N-linked glycoproteins in tear fluid of climatic droplet keratopathy by glycopeptide capture and iTRAQ
    • 19714880 10.1021/pr800962q 1:CAS:528:DC%2BD1MXivFOltbs%3D
    • Lei, Z.; Beuerman, R.W.; Chew, A.P.; Koh, S.K.; Cafaro, T.A.; Urrets-Zavalia, E.A.; Urrets-Zavalia, J.A.; Li, S.F.; Serra, H.M.: Quantitative analysis of N-linked glycoproteins in tear fluid of climatic droplet keratopathy by glycopeptide capture and iTRAQ. J. Proteome Res. 8(4), 1992-2003 (2009)
    • (2009) J. Proteome Res. , vol.8 , Issue.4 , pp. 1992-2003
    • Lei, Z.1    Beuerman, R.W.2    Chew, A.P.3    Koh, S.K.4    Cafaro, T.A.5    Urrets-Zavalia, E.A.6    Urrets-Zavalia, J.A.7    Li, S.F.8    Serra, H.M.9
  • 120
    • 33644690335 scopus 로고    scopus 로고
    • Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach
    • 16263699 1:CAS:528:DC%2BD28XitVagsL8%3D
    • Lewandrowski, U.; Moebius, J.; Walter, U.; Sickmann, A.: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol. Cell Proteomics. 5(2), 226-233 (2006)
    • (2006) Mol. Cell Proteomics. , vol.5 , Issue.2 , pp. 226-233
    • Lewandrowski, U.1    Moebius, J.2    Walter, U.3    Sickmann, A.4
  • 121
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • 16335952 1:CAS:528:DC%2BD2MXhtFCitbvL 10.1021/pr0502065
    • Liu, T.; Qian, W.J.; Gritsenko, M.A.; Camp 2nd, D.G.; Monroe, M.E.; Moore, R.J.; Smith, R.D.: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 4(6), 2070-2080 (2005)
    • (2005) J. Proteome Res. , vol.4 , Issue.6 , pp. 2070-2080
    • Liu, T.1    Qian, W.J.2    Gritsenko, M.A.3    Camp II, D.G.4    Monroe, M.E.5    Moore, R.J.6    Smith, R.D.7
  • 122
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • 12754519 1:CAS:528:DC%2BD3sXktFSlu7s%3D 10.1038/nbt827
    • Zhang, H.; Li, X.J.; Martin, D.B.; Aebersold, R.: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21(6), 660-666 (2003)
    • (2003) Nat. Biotechnol. , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 123
    • 0021189137 scopus 로고
    • Demonstration of peptide: N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations
    • 6206060 1:CAS:528:DyaL2cXmt1Gmtbo%3D
    • Plummer Jr.; T.H.; Elder, J.H.; Alexander, S.; Phelan, A.W.; Tarentino, A.L.: Demonstration of peptide: N-glycosidase F activity in endo-beta-N- acetylglucosaminidase F preparations. J. Biol. Chem. 259(17), 10700-10704 (1984)
    • (1984) J. Biol. Chem. , vol.259 , Issue.17 , pp. 10700-10704
    • Plummer, Jr.T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 124
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • 2510544 1:CAS:528:DyaL1MXltFWkt7g%3D 10.1016/0003-2697(89)90115-2
    • Maley, F.; Trimble, R.B.; Tarentino, A.L.; Plummer Jr.; T.H.: Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem. 180(2), 195-204 (1989)
    • (1989) Anal. Biochem. , vol.180 , Issue.2 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer, Jr.T.H.4
  • 125
    • 18844434899 scopus 로고    scopus 로고
    • Structural determination of N-linked glycans by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry
    • 15832364 1:CAS:528:DC%2BD2MXkslejsrk%3D 10.1002/pmic.200401248
    • Harvey, D.J.: Structural determination of N-linked glycans by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry. Proteomics 5(7), 1774-1786 (2005)
    • (2005) Proteomics , vol.5 , Issue.7 , pp. 1774-1786
    • Harvey, D.J.1
  • 126
    • 77956303179 scopus 로고    scopus 로고
    • The N-glycome of human plasma
    • 20690605 1:CAS:528:DC%2BC3cXpslGqurc%3D 10.1021/pr100528k
    • Stumpo, K.A.; Reinhold, V.N.: The N-glycome of human plasma. J. Proteome Res. 9(9), 4823-4830 (2010)
    • (2010) J. Proteome Res. , vol.9 , Issue.9 , pp. 4823-4830
    • Stumpo, K.A.1    Reinhold, V.N.2
  • 127
    • 84857873715 scopus 로고    scopus 로고
    • Chemical deamidation: A common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses
    • 22256963 1:CAS:528:DC%2BC38XosFehtg%3D%3D 10.1021/pr2011268
    • Palmisano, G.; Melo-Braga, M.N.; Engholm-Keller, K.; Parker, B.L.; Larsen, M.R.: Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses. J. Proteome Res. 11(3), 1949-1957 (2012)
    • (2012) J. Proteome Res. , vol.11 , Issue.3 , pp. 1949-1957
    • Palmisano, G.1    Melo-Braga, M.N.2    Engholm-Keller, K.3    Parker, B.L.4    Larsen, M.R.5
  • 128
    • 80054030914 scopus 로고    scopus 로고
    • Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation
    • 21784994 10.1074/mcp.O111.009381 1:CAS:528:DC%2BC3MXhtlGmtrjK
    • Hao, P.; Ren, Y.; Alpert, A.J.; Sze, S.K.: Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation. Mol. Cell Proteomics 10(10), O111.009381 (2011)
    • (2011) Mol. Cell Proteomics , vol.10 , Issue.10 , pp. 111009381
    • Hao, P.1    Ren, Y.2    Alpert, A.J.3    Sze, S.K.4
  • 129
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • 12754521 1:CAS:528:DC%2BD3sXktFSlu7k%3D 10.1038/nbt829
    • Kaji, H.; Saito, H.; Yamauchi, Y.; Shinkawa, T.; Taoka, M.; Hirabayashi, J.; Kasai, K.-I.; Takahashi, N.; Isobe, T.: Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins. Nat. Biotechnol. 21(6), 667-672 (2003)
    • (2003) Nat. Biotechnol. , vol.21 , Issue.6 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3    Shinkawa, T.4    Taoka, M.5    Hirabayashi, J.6    Kasai, K.-I.7    Takahashi, N.8    Isobe, T.9
  • 130
    • 61849103543 scopus 로고    scopus 로고
    • Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics
    • 19072223 1:CAS:528:DC%2BD1cXhsV2hur7F 10.1021/pr800708h
    • Dodds, E.D.; Seipert, R.R.; Clowers, B.H.; German, J.B.; Lebrilla, C.B.: Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics. J. Proteome Res. 8(2), 502-512 (2009)
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 502-512
    • Dodds, E.D.1    Seipert, R.R.2    Clowers, B.H.3    German, J.B.4    Lebrilla, C.B.5
  • 131
    • 29244474577 scopus 로고    scopus 로고
    • Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry
    • 16321355 1:CAS:528:DC%2BD28Xks1Wq 10.1016/j.ab.2005.10.036
    • Harazono, A.; Kawasaki, N.; Itoh, S.; Hashii, N.; Ishii-Watabe, A.; Kawanishi, T.; Hayakawa, T.: Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry. Anal. Biochem. 348(2), 259-268 (2006)
    • (2006) Anal. Biochem. , vol.348 , Issue.2 , pp. 259-268
    • Harazono, A.1    Kawasaki, N.2    Itoh, S.3    Hashii, N.4    Ishii-Watabe, A.5    Kawanishi, T.6    Hayakawa, T.7
  • 132
    • 24044523213 scopus 로고    scopus 로고
    • Site-specific glycosylation analysis of human apolipoprotein B100 using LC/ESI MS/MS
    • 15616123 1:CAS:528:DC%2BD2MXjsl2hu7o%3D 10.1093/glycob/cwi033
    • Harazono, A.; Kawasaki, N.; Kawanishi, T.; Hayakawa, T.: Site-specific glycosylation analysis of human apolipoprotein B100 using LC/ESI MS/MS. Glycobiology 15(5), 447-462 (2005)
    • (2005) Glycobiology , vol.15 , Issue.5 , pp. 447-462
    • Harazono, A.1    Kawasaki, N.2    Kawanishi, T.3    Hayakawa, T.4
  • 133
    • 36148986496 scopus 로고    scopus 로고
    • Structure elucidation of glycoproteins by direct nanoESI MS and MS/MS analysis of proteolytic glycopeptides
    • 17960575 1:CAS:528:DC%2BD2sXhtlKktbzN 10.1002/jms.1265
    • Henning, S.; Peter-Katalinic, J.; Pohlentz, G.: Structure elucidation of glycoproteins by direct nanoESI MS and MS/MS analysis of proteolytic glycopeptides. J. Mass Spectrom. 42(11), 1415-1421 (2007)
    • (2007) J. Mass Spectrom. , vol.42 , Issue.11 , pp. 1415-1421
    • Henning, S.1    Peter-Katalinic, J.2    Pohlentz, G.3
  • 134
    • 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
    • 11575803 1:CAS:528:DC%2BD3MXlvFanur4%3D 10.1021/ac0103470
    • Hakansson, K.; Cooper, H.J.; Emmett, M.R.; Costello, C.E.; Marshall, A.G.; Nilsson, C.L.: Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information. Anal. Chem. 73(18), 4530-4536 (2001)
    • (2001) Anal. Chem. , vol.73 , Issue.18 , pp. 4530-4536
    • Hakansson, K.1    Cooper, H.J.2    Emmett, M.R.3    Costello, C.E.4    Marshall, A.G.5    Nilsson, C.L.6
  • 135
    • 77954203412 scopus 로고    scopus 로고
    • Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics
    • 20536156 1:CAS:528:DC%2BC3cXnt1GltL0%3D 10.1021/ac100530w
    • Mysling, S.; Palmisano, G.; Hojrup, P.; Thaysen-Andersen, M.: Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics. Anal. Chem. 82(13), 5598-5609 (2010)
    • (2010) Anal. Chem. , vol.82 , Issue.13 , pp. 5598-5609
    • Mysling, S.1    Palmisano, G.2    Hojrup, P.3    Thaysen-Andersen, M.4
  • 136
    • 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
    • 16503336 1:CAS:528:DC%2BD28Xjs1ygt7c%3D
    • Takegawa, Y.; Deguchi, K.; Keira, T.; Ito, H.; Nakagawa, H.; Nishimura, S.: 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(1-2), 177-181 (2006)
    • (2006) J. Chromatogr. A , vol.1113 , Issue.1-2 , pp. 177-181
    • Takegawa, Y.1    Deguchi, K.2    Keira, T.3    Ito, H.4    Nakagawa, H.5    Nishimura, S.6
  • 137
    • 60149111900 scopus 로고    scopus 로고
    • Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data
    • 19065542 1:CAS:528:DC%2BD1MXptVykug%3D%3D 10.1002/rcm.3850
    • Alley Jr.; W.R.; Mechref, Y.; Novotny, M.V.: Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data. Rapid Commun. Mass Spectrom. 23(1), 161-170 (2009)
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , Issue.1 , pp. 161-170
    • Alley, Jr.W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 138
    • 43949117767 scopus 로고    scopus 로고
    • Analysis of glycopeptides using lectin affinity chromatography with MALDI-TOF mass spectrometry
    • 18410132 1:CAS:528:DC%2BD1cXks1emsrw%3D 10.1021/ac800070d
    • Kubota, K.; Sato, Y.; Suzuki, Y.; Goto-Inoue, N.; Toda, T.; Suzuki, M.; Hisanaga, S.-I.; Suzuki, A.; Endo, T.: Analysis of glycopeptides using lectin affinity chromatography with MALDI-TOF mass spectrometry. Anal. Chem. 80(10), 3693-3698 (2008)
    • (2008) Anal. Chem. , vol.80 , Issue.10 , pp. 3693-3698
    • Kubota, K.1    Sato, Y.2    Suzuki, Y.3    Goto-Inoue, N.4    Toda, T.5    Suzuki, M.6    Hisanaga, S.-I.7    Suzuki, A.8    Endo, T.9
  • 139
    • 33645100367 scopus 로고    scopus 로고
    • Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms
    • 16622833 1:CAS:528:DC%2BD28Xmt1artLo%3D 10.1002/pmic.200500751
    • Kolarich, D.; Weber, A.; Turecek, P.L.; Schwarz, H.-P.; Altmann, F.: Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms. Proteomics 6(11), 3369-3380 (2006)
    • (2006) Proteomics , vol.6 , Issue.11 , pp. 3369-3380
    • Kolarich, D.1    Weber, A.2    Turecek, P.L.3    Schwarz, H.-P.4    Altmann, F.5
  • 140
    • 84857043221 scopus 로고    scopus 로고
    • Characterization of transferrin glycopeptide structures in human cerebrospinal fluid
    • 22408387 1:CAS:528:DC%2BC38XitFOksrY%3D 10.1016/j.ijms.2011.06.021
    • Brown, K.J.; Vanderver, A.; Hoffman, E.P.; Schiffmann, R.; Hathout, Y.: Characterization of transferrin glycopeptide structures in human cerebrospinal fluid. Int. J. Mass Spectrom. 312, 97-106 (2012)
    • (2012) Int. J. Mass Spectrom. , vol.312 , pp. 97-106
    • Brown, K.J.1    Vanderver, A.2    Hoffman, E.P.3    Schiffmann, R.4    Hathout, Y.5
  • 141
    • 29144502243 scopus 로고    scopus 로고
    • Prefractionation of cerebrospinal fluid to enhance glycoprotein concentration prior to structural determination with FT-ICR mass spectrometry
    • 16335978 1:CAS:528:DC%2BD2MXhtVKmtb%2FL 10.1021/pr050210g
    • Sihlbom, C.; Davidsson, P.; Nilsson, C.L.: Prefractionation of cerebrospinal fluid to enhance glycoprotein concentration prior to structural determination with FT-ICR mass spectrometry. J. Proteome Res. 4(6), 2294-2301 (2005)
    • (2005) J. Proteome Res. , vol.4 , Issue.6 , pp. 2294-2301
    • Sihlbom, C.1    Davidsson, P.2    Nilsson, C.L.3
  • 142
    • 34047164035 scopus 로고    scopus 로고
    • Glycoproteomics based on tandem mass spectrometry of glycopeptides
    • 1:CAS:528:DC%2BD2sXjvFeisLs%3D 10.1016/j.jchromb.2006.09.041
    • Wuhrer, M.; Catalina, M.I.; Deelder, A.M.; Hokke, C.H.: Glycoproteomics based on tandem mass spectrometry of glycopeptides. J. Chromatogr. B 849(1-2), 115-128 (2007)
    • (2007) J. Chromatogr. B , vol.849 , Issue.1-2 , pp. 115-128
    • Wuhrer, M.1    Catalina, M.I.2    Deelder, A.M.3    Hokke, C.H.4
  • 143
    • 33646873090 scopus 로고    scopus 로고
    • Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electrospray linear ion trap-Fourier transform mass spectrometry
    • 16497783 1:CAS:528:DC%2BD28XkvVSrs7o%3D 10.1093/glycob/cwj091
    • Wang, Y.; Wu, S.L.; Hancock, W.S.: Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electrospray linear ion trap-Fourier transform mass spectrometry. Glycobiology 16(6), 514-523 (2006)
    • (2006) Glycobiology , vol.16 , Issue.6 , pp. 514-523
    • Wang, Y.1    Wu, S.L.2    Hancock, W.S.3
  • 144
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • 15543974 1:CAS:528:DC%2BD2cXos1yqtbk%3D
    • Yang, Z.; Hancock, W.S.: Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J. Chromatogr. A 1053(1-2), 79-88 (2004)
    • (2004) J. Chromatogr. A , vol.1053 , Issue.1-2 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 145
    • 29244474601 scopus 로고    scopus 로고
    • High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis
    • 16170054 1:CAS:528:DC%2BD2MXhtlWqsb%2FP 10.1074/mcp.M500203-MCP200
    • Uematsu, R.; Furukawa, J.; Nakagawa, H.; Shinohara, Y.; Deguchi, K.; Monde, K.; Nishimura, S.: High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis. Mol. Cell Proteomics 4(12), 1977-1989 (2005)
    • (2005) Mol. Cell Proteomics , vol.4 , Issue.12 , pp. 1977-1989
    • Uematsu, R.1    Furukawa, J.2    Nakagawa, H.3    Shinohara, Y.4    Deguchi, K.5    Monde, K.6    Nishimura, S.7
  • 146
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • 20360033
    • Scott, N.E.; Parker, B.L.; Connolly, A.M.; Paulech, J.; Edwards, A.V.G.; Crossett, B.; Falconer, L.; Kolarich, D.; Djordjevic, S.P.; Højrup, P.; Packer, N.H.; Larsen, M.R.; Cordwell, S.J.: Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol. Cell Proteomics 10(2), M000031-MCP000201 (2011)
    • (2011) Mol. Cell Proteomics , vol.10 , Issue.2
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.G.5    Crossett, B.6    Falconer, L.7    Kolarich, D.8    Djordjevic, S.P.9    Højrup, P.10    Packer, N.H.11    Larsen, M.R.12    Cordwell, S.J.13
  • 147
    • 79954616758 scopus 로고    scopus 로고
    • Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.d. porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry
    • 21338062 1:CAS:528:DC%2BC3MXit1Wjsbk%3D 10.1021/ac102825g
    • Wang, D.; Hincapie, M.; Rejtar, T.; Karger, B.L.: Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.d. porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry. Anal. Chem. 83(6), 2029-2037 (2011)
    • (2011) Anal. Chem. , vol.83 , Issue.6 , pp. 2029-2037
    • Wang, D.1    Hincapie, M.2    Rejtar, T.3    Karger, B.L.4
  • 148
    • 17444375706 scopus 로고    scopus 로고
    • Complementary structural information from a tryptic N-linked glycopeptide via electron transfer ion/ion reactions and collision-induced dissociation
    • 15822944 1:CAS:528:DC%2BD2MXitVClurc%3D 10.1021/pr049770q
    • Hogan, J.M.; Pitteri, S.J.; Chrisman, P.A.; McLuckey, S.A.: Complementary structural information from a tryptic N-linked glycopeptide via electron transfer ion/ion reactions and collision-induced dissociation. J. Proteome Res. 4(2), 628-632 (2005)
    • (2005) J. Proteome Res. , vol.4 , Issue.2 , pp. 628-632
    • Hogan, J.M.1    Pitteri, S.J.2    Chrisman, P.A.3    McLuckey, S.A.4
  • 149
    • 77955714199 scopus 로고    scopus 로고
    • Bioinformatics and molecular modeling in glycobiology
    • 20364395 1:CAS:528:DC%2BC3cXpsVGisLs%3D 10.1007/s00018-010-0352-4
    • Frank, M.; Schloissnig, S.: Bioinformatics and molecular modeling in glycobiology. Cell. Mol. Life Sci. 67(16), 2749-2772 (2010)
    • (2010) Cell. Mol. Life Sci. , vol.67 , Issue.16 , pp. 2749-2772
    • Frank, M.1    Schloissnig, S.2
  • 150
    • 58849120468 scopus 로고    scopus 로고
    • Web resources for the glycoscientist
    • 18693281 10.1002/cbic.200800338 1:CAS:528:DC%2BD1cXhtFansrjJ
    • Lütteke, T.: Web resources for the glycoscientist. ChemBioChem 9(13), 2155-2160 (2008)
    • (2008) ChemBioChem , vol.9 , Issue.13 , pp. 2155-2160
    • Lütteke, T.1


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