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Volumn 5, Issue 1, 2009, Pages 52-68

Glycoprofiling of the human salivary proteome

Author keywords

Glycosylation; Human whole saliva; Lectin blotting; Two dimensional gel electrophoresis

Indexed keywords

GLYCAN; LECTIN; PROTEOME; SALIVA PROTEIN;

EID: 70349575991     PISSN: 15426416     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12014-008-9021-0     Document Type: Article
Times cited : (41)

References (111)
  • 1
    • 0032134726 scopus 로고    scopus 로고
    • Toward molecularly based diagnostics for the oral cavity
    • 9715016 1:STN:280:DyaK1czotVOnug%3D%3D
    • HC Slavkin 1998 Toward molecularly based diagnostics for the oral cavity J Am Dent Assoc 129 1138 1143 9715016 1:STN:280:DyaK1czotVOnug%3D%3D
    • (1998) J Am Dent Assoc , vol.129 , pp. 1138-1143
    • Slavkin, H.C.1
  • 2
    • 51349132896 scopus 로고    scopus 로고
    • The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions
    • 18361515 1:CAS:528:DC%2BD1cXjs1Ohtrg%3D
    • P Denny FK Hagen M Hardt, et al. 2008 The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions J Proteome Res 7 1994 2006 18361515 1:CAS:528:DC%2BD1cXjs1Ohtrg%3D
    • (2008) J Proteome Res , vol.7 , pp. 1994-2006
    • Denny, P.1    Hagen, F.K.2    Hardt, M.3
  • 3
  • 4
    • 33744981406 scopus 로고    scopus 로고
    • Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed-phase liquid chromatography coupled with ESI-tandem MS
    • 16739998 1:CAS:528:DC%2BD28Xkt1Ons7w%3D
    • T Guo PA Rudnick W Wang CS Lee DL Devoe BM Balgley 2006 Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed- phase liquid chromatography coupled with ESI-tandem MS J Proteome Res 5 1469 1478 16739998 1:CAS:528:DC%2BD28Xkt1Ons7w%3D
    • (2006) J Proteome Res , vol.5 , pp. 1469-1478
    • Guo, T.1    Rudnick, P.A.2    Wang, W.3    Lee, C.S.4    Devoe, D.L.5    Balgley, B.M.6
  • 5
    • 30744442098 scopus 로고    scopus 로고
    • Complexity of the human whole saliva proteome
    • 16440601 1:CAS:528:DC%2BD28Xit1Gqs7g%3D
    • C Hirtz F Chevalier D Centeno, et al. 2005 Complexity of the human whole saliva proteome J Physiol Biochem 61 469 480 16440601 1:CAS:528: DC%2BD28Xit1Gqs7g%3D
    • (2005) J Physiol Biochem , vol.61 , pp. 469-480
    • Hirtz, C.1    Chevalier, F.2    Centeno, D.3
  • 6
    • 33644634632 scopus 로고    scopus 로고
    • Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis
    • 16402355 1:CAS:528:DC%2BD28XivVWqs78%3D
    • A Walz K Stuhler A Wattenberg, et al. 2006 Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis Proteomics 6 1631 1639 16402355 1:CAS:528:DC%2BD28XivVWqs78%3D
    • (2006) Proteomics , vol.6 , pp. 1631-1639
    • Walz, A.1    Stuhler, K.2    Wattenberg, A.3
  • 8
    • 17844368916 scopus 로고    scopus 로고
    • Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry
    • 15800970 1:CAS:528:DC%2BD2MXktVWjsbo%3D
    • S Hu Y Xie P Ramachandran, et al. 2005 Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry Proteomics 5 1714 1728 15800970 1:CAS:528:DC%2BD2MXktVWjsbo%3D
    • (2005) Proteomics , vol.5 , pp. 1714-1728
    • Hu, S.1    Xie, Y.2    Ramachandran, P.3
  • 9
    • 14344257981 scopus 로고    scopus 로고
    • Toward defining the human parotid gland salivary proteome and peptidome: Identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry
    • 15723531 1:CAS:528:DC%2BD2MXosFWhtA%3D%3D
    • M Hardt LR Thomas SE Dixon, et al. 2005 Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry Biochemistry 44 2885 2899 15723531 1:CAS:528:DC%2BD2MXosFWhtA%3D%3D
    • (2005) Biochemistry , vol.44 , pp. 2885-2899
    • Hardt, M.1    Thomas, L.R.2    Dixon, S.E.3
  • 10
    • 5644277841 scopus 로고    scopus 로고
    • Comparative proteomic analysis of human whole saliva
    • 15485636 1:CAS:528:DC%2BD2cXos1aqtbY%3D
    • CM Huang 2004 Comparative proteomic analysis of human whole saliva Arch Oral Biol 49 951 962 15485636 1:CAS:528:DC%2BD2cXos1aqtbY%3D
    • (2004) Arch Oral Biol , vol.49 , pp. 951-962
    • Huang, C.M.1
  • 11
    • 7044241342 scopus 로고    scopus 로고
    • Two-dimensional liquid chromatography study of the human whole saliva proteome
    • 15473691 1:CAS:528:DC%2BD2cXnsVahsbg%3D
    • PA Wilmarth MA Riviere DL Rustvold JD Lauten TE Madden LL David 2004 Two-dimensional liquid chromatography study of the human whole saliva proteome J Proteome Res 3 1017 1023 15473691 1:CAS:528:DC%2BD2cXnsVahsbg%3D
    • (2004) J Proteome Res , vol.3 , pp. 1017-1023
    • Wilmarth, P.A.1    Riviere, M.A.2    Rustvold, D.L.3    Lauten, J.D.4    Madden, T.E.5    David, L.L.6
  • 12
    • 1842580707 scopus 로고    scopus 로고
    • Identification of human whole saliva protein components using proteomics
    • 15048992 1:CAS:528:DC%2BD2cXjt1SmtLg%3D
    • R Vitorino MJ Lobo AJ Ferrer-Correira, et al. 2004 Identification of human whole saliva protein components using proteomics Proteomics 4 1109 1115 15048992 1:CAS:528:DC%2BD2cXjt1SmtLg%3D
    • (2004) Proteomics , vol.4 , pp. 1109-1115
    • Vitorino, R.1    Lobo, M.J.2    Ferrer-Correira, A.J.3
  • 13
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • 16959566 1:CAS:528:DC%2BD28XpvVKitbo%3D
    • K Ohtsubo JD Marth 2006 Glycosylation in cellular mechanisms of health and disease Cell 126 855 867 16959566 1:CAS:528:DC%2BD28XpvVKitbo%3D
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 14
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • 17134948 1:CAS:528:DC%2BD28XhtlaltLzI
    • H Geyer R Geyer 2006 Strategies for analysis of glycoprotein glycosylation Biochim Biophys Acta 1764 1853 1869 17134948 1:CAS:528: DC%2BD28XhtlaltLzI
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 15
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • 12042244 1:CAS:528:DC%2BD38XltVyhtrY%3D
    • RG Spiro 2002 Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds Glycobiology 12 43R 56R 12042244 1:CAS:528:DC%2BD38XltVyhtrY%3D
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 16
    • 14744304617 scopus 로고    scopus 로고
    • Coming of age: Carbohydrates and immunity
    • 15682450 1:CAS:528:DC%2BD2MXhvFKmu70%3D
    • BA Cobb DL Kasper 2005 Coming of age: carbohydrates and immunity Eur J Immunol 35 352 356 15682450 1:CAS:528:DC%2BD2MXhvFKmu70%3D
    • (2005) Eur J Immunol , vol.35 , pp. 352-356
    • Cobb, B.A.1    Kasper, D.L.2
  • 17
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • 10580125 1:CAS:528:DyaK1MXnsVKmt7o%3D
    • R Apweiler H Hermjakob N Sharon 1999 On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database Biochim Biophys Acta 1473 4 8 10580125 1:CAS:528:DyaK1MXnsVKmt7o%3D
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 18
    • 0027274715 scopus 로고
    • Abnormal glycosylation of alpha 2-macroglobulin, a non-acute-phase protein in patients with autoimmune diseases
    • 7691738 1:CAS:528:DyaK2cXhtVCrs7Y%3D
    • L Saso B Silvestrini A Guglielmotti R Lahita CY Cheng 1993 Abnormal glycosylation of alpha 2-macroglobulin, a non-acute-phase protein in patients with autoimmune diseases Inflammation 17 465 479 7691738 1:CAS:528: DyaK2cXhtVCrs7Y%3D
    • (1993) Inflammation , vol.17 , pp. 465-479
    • Saso, L.1    Silvestrini, B.2    Guglielmotti, A.3    Lahita, R.4    Cheng, C.Y.5
  • 19
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • 16033539 1:CAS:528:DC%2BD2MXpsVars78%3D
    • A Kobata J Amano 2005 Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours Immunol Cell Biol 83 429 439 16033539 1:CAS:528:DC%2BD2MXpsVars78%3D
    • (2005) Immunol Cell Biol , vol.83 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 20
    • 0344242000 scopus 로고    scopus 로고
    • Fetal fibronectin as a marker for an imminent (preterm) delivery. A new technique using the glycoprotein lectin immunosorbent assay
    • 10357204 1:CAS:528:DyaK1MXis1aqsbY%3D
    • DJ Hampel B Kottgen JW Dudenhausen E Kottgen 1999 Fetal fibronectin as a marker for an imminent (preterm) delivery. A new technique using the glycoprotein lectin immunosorbent assay J Immunol Methods 224 31 42 10357204 1:CAS:528:DyaK1MXis1aqsbY%3D
    • (1999) J Immunol Methods , vol.224 , pp. 31-42
    • Hampel, D.J.1    Kottgen, B.2    Dudenhausen, J.W.3    Kottgen, E.4
  • 21
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • 3927174 1:CAS:528:DyaL2MXltVehurY%3D
    • RB Parekh RA Dwek BJ Sutton, et al. 1985 Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG Nature 316 452 457 3927174 1:CAS:528:DyaL2MXltVehurY%3D
    • (1985) Nature , vol.316 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3
  • 22
    • 34248213619 scopus 로고    scopus 로고
    • Implications for diagnostics in the biochemistry and physiology of saliva
    • 17303829
    • A Van Nieuw Amerongen AJ Ligtenberg EC Veerman 2007 Implications for diagnostics in the biochemistry and physiology of saliva Ann N Y Acad Sci 1098 1 6 17303829
    • (2007) Ann N y Acad Sci , vol.1098 , pp. 1-6
    • Van Nieuw Amerongen, A.1    Ligtenberg, A.J.2    Veerman, E.C.3
  • 23
    • 2642515362 scopus 로고    scopus 로고
    • Salivary proteins: Protective and diagnostic value in cariology?
    • 15153696
    • A Van Nieuw Amerongen JG Bolscher EC Veerman 2004 Salivary proteins: protective and diagnostic value in cariology? Caries Res 38 247 253 15153696
    • (2004) Caries Res , vol.38 , pp. 247-253
    • Van Nieuw Amerongen, A.1    Bolscher, J.G.2    Veerman, E.C.3
  • 24
    • 34447619346 scopus 로고    scopus 로고
    • Interaction of salivary alpha-amylase and amylase-binding-protein A (AbpA) of Streptococcus gordonii with glucosyltransferase of S. gordonii and Streptococcus mutans
    • 17593303
    • B Chaudhuri J Rojek MM Vickerman JM Tanzer FA Scannapieco 2007 Interaction of salivary alpha-amylase and amylase-binding-protein A (AbpA) of Streptococcus gordonii with glucosyltransferase of S. gordonii and Streptococcus mutans BMC Microbiol 7 60 17593303
    • (2007) BMC Microbiol , vol.7 , pp. 60
    • Chaudhuri, B.1    Rojek, J.2    Vickerman, M.M.3    Tanzer, J.M.4    Scannapieco, F.A.5
  • 25
    • 0029620763 scopus 로고
    • Salivary mucins: Protective functions in relation to their diversity
    • 1:CAS:528:DyaK28XmtVSisg%3D%3D
    • A Van Nieuw Amerongen JG Bolscher EC Veerman 1995 Salivary mucins: protective functions in relation to their diversity Glycobiology 5 733 740 1:CAS:528:DyaK28XmtVSisg%3D%3D
    • (1995) Glycobiology , vol.5 , pp. 733-740
    • Van Nieuw Amerongen, A.1    Bolscher, J.G.2    Veerman, E.C.3
  • 26
    • 0028631078 scopus 로고
    • Saliva-bacterium interactions in oral microbial ecology
    • 7703323 1:STN:280:DyaK2M3hsl2qtg%3D%3D
    • FA Scannapieco 1994 Saliva-bacterium interactions in oral microbial ecology Crit Rev Oral Biol Med 5 203 248 7703323 1:STN:280:DyaK2M3hsl2qtg%3D%3D
    • (1994) Crit Rev Oral Biol Med , vol.5 , pp. 203-248
    • Scannapieco, F.A.1
  • 27
    • 0033214573 scopus 로고    scopus 로고
    • O-linked glycosylation occurs on basic parotid salivary proline-rich proteins
    • 10551158 1:CAS:528:DyaK1MXmsFeht7o%3D
    • GH Carpenter GB Proctor 1999 O-linked glycosylation occurs on basic parotid salivary proline-rich proteins Oral Microbiol Immunol 14 309 315 10551158 1:CAS:528:DyaK1MXmsFeht7o%3D
    • (1999) Oral Microbiol Immunol , vol.14 , pp. 309-315
    • Carpenter, G.H.1    Proctor, G.B.2
  • 28
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • 16740002 1:CAS:528:DC%2BD28Xktl2nsLs%3D
    • P Ramachandran P Boontheung Y Xie M Sondej DT Wong JA Loo 2006 Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry J Proteome Res 5 1493 1503 16740002 1:CAS:528: DC%2BD28Xktl2nsLs%3D
    • (2006) J Proteome Res , vol.5 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4    Wong, D.T.5    Loo, J.A.6
  • 29
    • 62549163033 scopus 로고    scopus 로고
    • Comparison of N-linked glycoproteins in human whole saliva, parotid, submandibular, and sublingual glandular secretions identified using hydrazide chemistry and mass spectrometry
    • 1:CAS:528:DC%2BD1cXhtlKis7rN
    • P Ramachandran P Boontheung E Pang W Yan DT Wong J Loo 2008 Comparison of N-linked glycoproteins in human whole saliva, parotid, submandibular, and sublingual glandular secretions identified using hydrazide chemistry and mass spectrometry Clin Proteomics 4 80 104 1:CAS:528:DC%2BD1cXhtlKis7rN
    • (2008) Clin Proteomics , vol.4 , pp. 80-104
    • Ramachandran, P.1    Boontheung, P.2    Pang, E.3    Yan, W.4    Wong, D.T.5    Loo, J.6
  • 30
    • 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
    • H Zhang XJ Li DB Martin R Aebersold 2003 Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat Biotechnol 21 660 666 12754519 1:CAS:528:DC%2BD3sXktFSlu7s%3D
    • (2003) Nat Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 31
    • 0037164021 scopus 로고    scopus 로고
    • Lectin structure-activity: The story is never over
    • 12381155 1:CAS:528:DC%2BD38Xnt1Sisr0%3D
    • IJ Goldstein 2002 Lectin structure-activity: the story is never over J Agric Food Chem 50 6583 6585 12381155 1:CAS:528:DC%2BD38Xnt1Sisr0%3D
    • (2002) J Agric Food Chem , vol.50 , pp. 6583-6585
    • Goldstein, I.J.1
  • 32
    • 7244258916 scopus 로고    scopus 로고
    • History of lectins: From hemagglutinins to biological recognition molecules
    • 15229195 1:CAS:528:DC%2BD2cXotVyqs7s%3D
    • N Sharon H Lis 2004 History of lectins: from hemagglutinins to biological recognition molecules Glycobiology 14 53R 62R 15229195 1:CAS:528: DC%2BD2cXotVyqs7s%3D
    • (2004) Glycobiology , vol.14
    • Sharon, N.1    Lis, H.2
  • 34
    • 0022555853 scopus 로고
    • Lectins as molecules and as tools
    • 3527046 1:CAS:528:DyaL28XkvFGlsro%3D
    • H Lis N Sharon 1986 Lectins as molecules and as tools Annu Rev Biochem 55 35 67 3527046 1:CAS:528:DyaL28XkvFGlsro%3D
    • (1986) Annu Rev Biochem , vol.55 , pp. 35-67
    • Lis, H.1    Sharon, N.2
  • 35
    • 0024969427 scopus 로고
    • Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity towards various glycopeptides and oligosaccharides
    • 2713870 1:CAS:528:DyaL1MXit1Oqtrg%3D
    • H Debray J Montreuil 1989 Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity towards various glycopeptides and oligosaccharides Carbohydr Res 185 15 26 2713870 1:CAS:528:DyaL1MXit1Oqtrg%3D
    • (1989) Carbohydr Res , vol.185 , pp. 15-26
    • Debray, H.1    Montreuil, J.2
  • 36
    • 0014672103 scopus 로고
    • Purification and characterization of an anti-H(O) phytohemagglutinin of Ulex europeus
    • 5353123 1:CAS:528:DyaE3cXhtV2mtg%3D%3D
    • I Matsumoto T Osawa 1969 Purification and characterization of an anti-H(O) phytohemagglutinin of Ulex europeus Biochim Biophys Acta 194 180 189 5353123 1:CAS:528:DyaE3cXhtV2mtg%3D%3D
    • (1969) Biochim Biophys Acta , vol.194 , pp. 180-189
    • Matsumoto, I.1    Osawa, T.2
  • 37
    • 0018096212 scopus 로고
    • Immunochemical studies on the combining site of the blood group H-specific lectin 1 from Ulex europeus seeds
    • 623479 1:CAS:528:DyaE1cXoslCktw%3D%3D
    • ME Pereira EC Kisailus F Gruezo EA Kabat 1978 Immunochemical studies on the combining site of the blood group H-specific lectin 1 from Ulex europeus seeds Arch Biochem Biophys 185 108 115 623479 1:CAS:528:DyaE1cXoslCktw%3D%3D
    • (1978) Arch Biochem Biophys , vol.185 , pp. 108-115
    • Pereira, M.E.1    Kisailus, E.C.2    Gruezo, F.3    Kabat, E.A.4
  • 38
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • 7262089 1:CAS:528:DyaL3MXkvFGhtb0%3D
    • H Debray D Decout G Strecker G Spik J Montreuil 1981 Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins Eur J Biochem 117 41 55 7262089 1:CAS:528:DyaL3MXkvFGhtb0%3D
    • (1981) Eur J Biochem , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, J.5
  • 39
    • 0023002029 scopus 로고
    • Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-D-Gal(1-3)D-GalNAc)
    • 3745164 1:CAS:528:DyaL28XlsVyms7c%3D
    • MV Sastry P Banarjee SR Patanjali MJ Swamy GV Swarnalatha A Surolia 1986 Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-D-Gal(1-3)D-GalNAc) J Biol Chem 261 11726 11733 3745164 1:CAS:528:DyaL28XlsVyms7c%3D
    • (1986) J Biol Chem , vol.261 , pp. 11726-11733
    • Sastry, M.V.1    Banarjee, P.2    Patanjali, S.R.3    Swamy, M.J.4    Swarnalatha, G.V.5    Surolia, A.6
  • 40
    • 0025141799 scopus 로고
    • Topography of the combining region of a Thomsen-Friedenreich-antigen- specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study
    • 2306217 1:CAS:528:DyaK3cXhslChtbw%3D
    • SK Mahanta MV Sastry A Surolia 1990 Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study Biochem J 265 831 840 2306217 1:CAS:528:DyaK3cXhslChtbw%3D
    • (1990) Biochem J , vol.265 , pp. 831-840
    • Mahanta, S.K.1    Sastry, M.V.2    Surolia, A.3
  • 41
    • 0024962069 scopus 로고
    • Further characterization and immunochemical studies on the carbohydrate specificity of jackfruit (Artocarpus integrifolia) lectin
    • 2722839 1:CAS:528:DyaL1MXksFalu7s%3D
    • H Ahmed BP Chatterjee 1989 Further characterization and immunochemical studies on the carbohydrate specificity of jackfruit (Artocarpus integrifolia) lectin J Biol Chem 264 9365 9372 2722839 1:CAS:528:DyaL1MXksFalu7s%3D
    • (1989) J Biol Chem , vol.264 , pp. 9365-9372
    • Ahmed, H.1    Chatterjee, B.P.2
  • 42
    • 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
    • RN Knibbs IJ Goldstein RM Ratcliffe N Shibuya 1991 Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins J Biol Chem 266 83 88 1985926 1:CAS:528:DyaK3MXhvVSmur4%3D
    • (1991) J Biol Chem , vol.266 , pp. 83-88
    • Knibbs, R.N.1    Goldstein, I.J.2    Ratcliffe, R.M.3    Shibuya, N.4
  • 43
    • 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
    • 3350806 1:CAS:528:DyaL1cXktValsLo%3D
    • WC Wang RD Cummings 1988 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 4576 4585 3350806 1:CAS:528: DyaL1cXktValsLo%3D
    • (1988) J Biol Chem , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 44
    • 0020727561 scopus 로고
    • Immunochemical and spectral studies on Vicia faba agglutinin
    • 1:CAS:528:DyaL3sXhsFyqt74%3D
    • I Matsumoto Y Uehara A Jimbo N Seno 1983 Immunochemical and spectral studies on Vicia faba agglutinin J Biochem (Tokyo) 93 763 769 1:CAS:528:DyaL3sXhsFyqt74%3D
    • (1983) J Biochem (Tokyo) , vol.93 , pp. 763-769
    • Matsumoto, I.1    Uehara, Y.2    Jimbo, A.3    Seno, N.4
  • 45
    • 0019877155 scopus 로고
    • The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant
    • 7240233 1:CAS:528:DyaL3MXltFeitr8%3D
    • K Kornfeld ML Reitman R Kornfeld 1981 The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant J Biol Chem 256 6633 6640 7240233 1:CAS:528:DyaL3MXltFeitr8%3D
    • (1981) J Biol Chem , vol.256 , pp. 6633-6640
    • Kornfeld, K.1    Reitman, M.L.2    Kornfeld, R.3
  • 46
    • 0020349037 scopus 로고
    • Requirement of the core structure of a complex-type glycopeptide for the binding to immobilized lentil- and pea-lectins
    • 7151058 1:CAS:528:DyaL3sXjt1yitQ%3D%3D
    • K Yamamoto T Tsuji T Osawa 1982 Requirement of the core structure of a complex-type glycopeptide for the binding to immobilized lentil- and pea-lectins Carbohydr Res 110 283 289 7151058 1:CAS:528:DyaL3sXjt1yitQ%3D%3D
    • (1982) Carbohydr Res , vol.110 , pp. 283-289
    • Yamamoto, K.1    Tsuji, T.2    Osawa, T.3
  • 47
    • 0016813441 scopus 로고
    • Interaction of immunoglobulin glycopeptides with concanavalin A
    • 1123324 1:CAS:528:DyaE2MXhs1yltL4%3D
    • R Kornfeld C Ferris 1975 Interaction of immunoglobulin glycopeptides with concanavalin A J Biol Chem 250 2614 2619 1123324 1:CAS:528:DyaE2MXhs1yltL4%3D
    • (1975) J Biol Chem , vol.250 , pp. 2614-2619
    • Kornfeld, R.1    Ferris, C.2
  • 48
    • 0018786476 scopus 로고
    • Structural determinants of concanavalin A specificity for oligosaccharides
    • 85625 1:CAS:528:DyaE1MXktFyit7Y%3D
    • JU Baenziger D Fiete 1979 Structural determinants of concanavalin A specificity for oligosaccharides J Biol Chem 254 2400 2407 85625 1:CAS:528:DyaE1MXktFyit7Y%3D
    • (1979) J Biol Chem , vol.254 , pp. 2400-2407
    • Baenziger, J.U.1    Fiete, D.2
  • 49
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • 3335522 1:CAS:528:DyaL1cXhs1ent70%3D
    • N Shibuya IJ Goldstein EJ Van Damme WJ Peumans 1988 Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb J Biol Chem 263 728 734 3335522 1:CAS:528:DyaL1cXhs1ent70%3D
    • (1988) J Biol Chem , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.3    Peumans, W.J.4
  • 50
    • 0025333981 scopus 로고
    • Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins
    • 2350177 1:CAS:528:DyaK3cXktVahurg%3D
    • H Kaku EJ Van Damme WJ Peumans IJ Goldstein 1990 Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins Arch Biochem Biophys 279 298 304 2350177 1:CAS:528:DyaK3cXktVahurg%3D
    • (1990) Arch Biochem Biophys , vol.279 , pp. 298-304
    • Kaku, H.1    Van Damme, E.J.2    Peumans, W.J.3    Goldstein, I.J.4
  • 51
    • 0017831577 scopus 로고
    • Bauhinia purpurea agglutinin
    • 661593 1:CAS:528:DyaE1MXitVGguw%3D%3D
    • T Osawa T Irimura T Kawaguchi 1978 Bauhinia purpurea agglutinin Methods Enzymol 50 367 372 661593 1:CAS:528:DyaE1MXitVGguw%3D%3D
    • (1978) Methods Enzymol , vol.50 , pp. 367-372
    • Osawa, T.1    Irimura, T.2    Kawaguchi, T.3
  • 52
    • 0019326105 scopus 로고
    • Immunochemical studies on the combining site of the D-galactopyranose and 2-acetamido-2-deoxy-D-galactopyranose specific lectin isolated from Bauhinia purpurea alba seeds
    • 7447466 1:CAS:528:DyaL3cXmtlKlsLs%3D
    • AM Wu EA Kabat FG Gruezo HJ Allen 1980 Immunochemical studies on the combining site of the D-galactopyranose and 2-acetamido-2-deoxy-D- galactopyranose specific lectin isolated from Bauhinia purpurea alba seeds Arch Biochem Biophys 204 622 639 7447466 1:CAS:528:DyaL3cXmtlKlsLs%3D
    • (1980) Arch Biochem Biophys , vol.204 , pp. 622-639
    • Wu, A.M.1    Kabat, E.A.2    Gruezo, F.G.3    Allen, H.J.4
  • 53
    • 0019791108 scopus 로고
    • The specificity of the combining site of the lectin from Vicia villosa seeds which react with cytotoxic T-lymphoblasts
    • 6176850 1:CAS:528:DyaL38XhsVSqtLk%3D
    • PM Kaladas EA Kabat A Kimura B Ersson 1981 The specificity of the combining site of the lectin from Vicia villosa seeds which react with cytotoxic T-lymphoblasts Mol Immunol 18 969 977 6176850 1:CAS:528:DyaL38XhsVSqtLk%3D
    • (1981) Mol Immunol , vol.18 , pp. 969-977
    • Kaladas, P.M.1    Kabat, E.A.2    Kimura, A.3    Ersson, B.4
  • 54
    • 0021111871 scopus 로고
    • Isolation and characterization of lectins from Vicia villosa. Two distinct carbohydrate binding activities are present in seed extracts
    • 6833294 1:CAS:528:DyaL3sXitFeqsbs%3D
    • SE Tollefsen R Kornfeld 1983 Isolation and characterization of lectins from Vicia villosa. Two distinct carbohydrate binding activities are present in seed extracts J Biol Chem 258 5165 5171 6833294 1:CAS:528:DyaL3sXitFeqsbs%3D
    • (1983) J Biol Chem , vol.258 , pp. 5165-5171
    • Tollefsen, S.E.1    Kornfeld, R.2
  • 55
    • 0019604874 scopus 로고
    • Some properties of the lectin from Datura stramonium (thorn-apple) and the nature of its glycoprotein linkages
    • 7325959 1:CAS:528:DyaL38Xkslyr
    • NN Desai AK Allen A Neuberger 1981 Some properties of the lectin from Datura stramonium (thorn-apple) and the nature of its glycoprotein linkages Biochem J 197 345 353 7325959 1:CAS:528:DyaL38Xkslyr
    • (1981) Biochem J , vol.197 , pp. 345-353
    • Desai, N.N.1    Allen, A.K.2    Neuberger, A.3
  • 56
    • 0020015935 scopus 로고
    • Structural studies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubers and thorn-apple (Datura stramonium) seeds
    • 7082284 1:CAS:528:DyaL38Xhsl2ht74%3D
    • D Ashford NN Desai AK Allen A Neuberger MA O'Neill RR Selvendran 1982 Structural studies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubers and thorn-apple (Datura stramonium) seeds Biochem J 201 199 208 7082284 1:CAS:528:DyaL38Xhsl2ht74%3D
    • (1982) Biochem J , vol.201 , pp. 199-208
    • Ashford, D.1    Desai, N.N.2    Allen, A.K.3    Neuberger, A.4    O'Neill, M.A.5    Selvendran, R.R.6
  • 57
    • 0020010661 scopus 로고
    • Tomato (Lycopersicon esculentum) lectin
    • 7098939 1:CAS:528:DyaL38XkvFSisro%3D
    • MS Nachbar JD Oppenheim 1982 Tomato (Lycopersicon esculentum) lectin Methods Enzymol 83 363 368 7098939 1:CAS:528:DyaL38XkvFSisro%3D
    • (1982) Methods Enzymol , vol.83 , pp. 363-368
    • Nachbar, M.S.1    Oppenheim, J.D.2
  • 58
    • 0018843767 scopus 로고
    • Purification and some properties of a lectin from the fruit juice of the tomato (Lycopersicon esculentum)
    • 7378052 1:CAS:528:DyaL3cXhs1Smtro%3D
    • DC Kilpatrick 1980 Purification and some properties of a lectin from the fruit juice of the tomato (Lycopersicon esculentum) Biochem J 185 269 272 7378052 1:CAS:528:DyaL3cXhs1Smtro%3D
    • (1980) Biochem J , vol.185 , pp. 269-272
    • Kilpatrick, D.C.1
  • 59
    • 0015541815 scopus 로고
    • The purification, composition and specificity of wheat-germ agglutinin
    • 4737292 1:CAS:528:DyaE3sXptlyqtQ%3D%3D
    • AK Allen A Neuberger N Sharon 1973 The purification, composition and specificity of wheat-germ agglutinin Biochem J 131 155 162 4737292 1:CAS:528:DyaE3sXptlyqtQ%3D%3D
    • (1973) Biochem J , vol.131 , pp. 155-162
    • Allen, A.K.1    Neuberger, A.2    Sharon, N.3
  • 60
    • 0018387309 scopus 로고
    • The interaction of wheat germ agglutinin with sialoglycoproteins. the role of sialic acid
    • 108267 1:CAS:528:DyaE1MXksFCgtb0%3D
    • VP Bhavanandan AW Katlic 1979 The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid J Biol Chem 254 4000 4008 108267 1:CAS:528:DyaE1MXksFCgtb0%3D
    • (1979) J Biol Chem , vol.254 , pp. 4000-4008
    • Bhavanandan, V.P.1    Katlic, A.W.2
  • 61
    • 0016747954 scopus 로고
    • Precipitation and carbohydrate-binding specificity studies on wheat germ agglutinin
    • 1174568 1:CAS:528:DyaE2MXlsVGltrw%3D
    • IJ Goldstein S Hammarstrom G Sundblad 1975 Precipitation and carbohydrate-binding specificity studies on wheat germ agglutinin Biochim Biophys Acta 405 53 61 1174568 1:CAS:528:DyaE2MXlsVGltrw%3D
    • (1975) Biochim Biophys Acta , vol.405 , pp. 53-61
    • Goldstein, I.J.1    Hammarstrom, S.2    Sundblad, G.3
  • 62
    • 0028299382 scopus 로고
    • Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A
    • 8150094 1:CAS:528:DyaK2cXlsFWmsLk%3D
    • Y Konami K Yamamoto T Osawa T Irimura 1994 Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A FEBS Lett 342 334 338 8150094 1:CAS:528:DyaK2cXlsFWmsLk%3D
    • (1994) FEBS Lett , vol.342 , pp. 334-338
    • Konami, Y.1    Yamamoto, K.2    Osawa, T.3    Irimura, T.4
  • 63
    • 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
    • N Shibuya IJ Goldstein WF Broekaert M Nsimba-Lubaki B Peeters WJ Peumans 1987 The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence J Biol Chem 262 1596 1601 3805045 1:CAS:528: DyaL2sXhslWns7s%3D
    • (1987) J Biol Chem , vol.262 , 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
  • 64
    • 33751108967 scopus 로고    scopus 로고
    • Identification and analysis of altered alpha1,6-fucosylated glycoproteins associated with hepatocellular carcinoma metastasis
    • 17068759 1:CAS:528:DC%2BD28Xht1yqsbbI
    • Z Dai YK Liu JF Cui, et al. 2006 Identification and analysis of altered alpha1,6-fucosylated glycoproteins associated with hepatocellular carcinoma metastasis Proteomics 6 5857 5867 17068759 1:CAS:528:DC%2BD28Xht1yqsbbI
    • (2006) Proteomics , vol.6 , pp. 5857-5867
    • Dai, Z.1    Liu, Y.K.2    Cui, J.F.3
  • 65
    • 23944510667 scopus 로고    scopus 로고
    • Direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification of proteins on membrane detected by Western blotting and lectin blotting
    • 16083291 1:CAS:528:DC%2BD2MXltl2gtb0%3D
    • I Ohtsu T Nakanisi M Furuta E Ando O Nishimura 2005 Direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification of proteins on membrane detected by Western blotting and lectin blotting J Proteome Res 4 1391 1396 16083291 1:CAS:528:DC%2BD2MXltl2gtb0%3D
    • (2005) J Proteome Res , vol.4 , pp. 1391-1396
    • Ohtsu, I.1    Nakanisi, T.2    Furuta, M.3    Ando, E.4    Nishimura, O.5
  • 66
    • 8744227914 scopus 로고    scopus 로고
    • Identification of target proteins of N-acetylglucosaminyl-transferase v and fucosyltransferase 8 in human gastric tissues by glycomic approach
    • 15529413 1:CAS:528:DC%2BD2cXhtVaqsLfF
    • YS Kim SY Hwang S Oh, et al. 2004 Identification of target proteins of N-acetylglucosaminyl-transferase V and fucosyltransferase 8 in human gastric tissues by glycomic approach Proteomics 4 3353 3358 15529413 1:CAS:528:DC%2BD2cXhtVaqsLfF
    • (2004) Proteomics , vol.4 , pp. 3353-3358
    • Kim, Y.S.1    Hwang, S.Y.2    Oh, S.3
  • 67
    • 0036681949 scopus 로고    scopus 로고
    • A glycomic approach to hepatic tumors in N-acetylglucosaminyltransferase III (GnT-III) transgenic mice induced by diethylnitrosamine (DEN): Identification of haptoglobin as a target molecule of GnT-III
    • 12420740 1:CAS:528:DC%2BD3sXitlSlsrw%3D
    • A Ekuni E Miyoshi JH Ko, et al. 2002 A glycomic approach to hepatic tumors in N-acetylglucosaminyltransferase III (GnT-III) transgenic mice induced by diethylnitrosamine (DEN): identification of haptoglobin as a target molecule of GnT-III Free Radic Res 36 827 833 12420740 1:CAS:528:DC%2BD3sXitlSlsrw%3D
    • (2002) Free Radic Res , vol.36 , pp. 827-833
    • Ekuni, A.1    Miyoshi, E.2    Ko, J.H.3
  • 68
    • 0035260226 scopus 로고    scopus 로고
    • A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes
    • 11680870 1:CAS:528:DC%2BD3MXhvVCisro%3D
    • N Taniguchi A Ekuni JH Ko, et al. 2001 A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes Proteomics 1 239 247 11680870 1:CAS:528:DC%2BD3MXhvVCisro%3D
    • (2001) Proteomics , vol.1 , pp. 239-247
    • Taniguchi, N.1    Ekuni, A.2    Ko, J.H.3
  • 69
    • 33644668728 scopus 로고    scopus 로고
    • Molecular diversity in venom from the Australian Brown snake, Pseudonaja textilis
    • 16284125 1:CAS:528:DC%2BD28XitVagsbs%3D
    • GW Birrell S Earl PP Masci, et al. 2006 Molecular diversity in venom from the Australian Brown snake, Pseudonaja textilis Mol Cell Proteomics 5 379 389 16284125 1:CAS:528:DC%2BD28XitVagsbs%3D
    • (2006) Mol Cell Proteomics , vol.5 , pp. 379-389
    • Birrell, G.W.1    Earl, S.2    Masci, P.P.3
  • 70
    • 0032603137 scopus 로고    scopus 로고
    • Quantifying protein in 2-D PAGE solubilization buffers
    • 10027233 1:CAS:528:DyaK1cXotVGrsro%3D
    • LS Ramagli 1999 Quantifying protein in 2-D PAGE solubilization buffers Methods Mol Biol 112 99 103 10027233 1:CAS:528:DyaK1cXotVGrsro%3D
    • (1999) Methods Mol Biol , vol.112 , pp. 99-103
    • Ramagli, L.S.1
  • 72
    • 4444297375 scopus 로고    scopus 로고
    • Comparison of fluorescent stains: Relative photostability and differential staining of proteins in two-dimensional gels
    • 15300770 1:CAS:528:DC%2BD2cXmvFOjtL8%3D
    • GB Smejkal MH Robinson A Lazarev 2004 Comparison of fluorescent stains: relative photostability and differential staining of proteins in two-dimensional gels Electrophoresis 25 2511 2519 15300770 1:CAS:528:DC%2BD2cXmvFOjtL8%3D
    • (2004) Electrophoresis , vol.25 , pp. 2511-2519
    • Smejkal, G.B.1    Robinson, M.H.2    Lazarev, A.3
  • 73
    • 0033667456 scopus 로고    scopus 로고
    • A comparison of silver stain and SYPRO Ruby Protein Gel Stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling
    • 11271486 1:CAS:528:DC%2BD3cXos1SntLw%3D
    • MF Lopez K Berggren E Chernokalskaya A Lazarev M Robinson WF Patton 2000 A comparison of silver stain and SYPRO Ruby Protein Gel Stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling Electrophoresis 21 3673 3683 11271486 1:CAS:528:DC%2BD3cXos1SntLw%3D
    • (2000) Electrophoresis , vol.21 , pp. 3673-3683
    • Lopez, M.F.1    Berggren, K.2    Chernokalskaya, E.3    Lazarev, A.4    Robinson, M.5    Patton, W.F.6
  • 75
    • 34748895999 scopus 로고    scopus 로고
    • Diet and the evolution of human amylase gene copy number variation
    • 17828263 1:CAS:528:DC%2BD2sXhtV2isL7J
    • GH Perry NJ Dominy KG Claw, et al. 2007 Diet and the evolution of human amylase gene copy number variation Nat Genet 39 1256 1260 17828263 1:CAS:528:DC%2BD2sXhtV2isL7J
    • (2007) Nat Genet , vol.39 , pp. 1256-1260
    • Perry, G.H.1    Dominy, N.J.2    Claw, K.G.3
  • 76
    • 1842869336 scopus 로고    scopus 로고
    • 2D-electrophoresis. Detection of glycosylation and influence on spot pattern
    • 12029844 1:CAS:528:DC%2BD38XjvVKnu74%3D
    • K Loster C Kannicht 2002 2D-electrophoresis. Detection of glycosylation and influence on spot pattern Methods Mol Biol 194 301 316 12029844 1:CAS:528:DC%2BD38XjvVKnu74%3D
    • (2002) Methods Mol Biol , vol.194 , pp. 301-316
    • Loster, K.1    Kannicht, C.2
  • 77
    • 0031787807 scopus 로고    scopus 로고
    • Electrospray ionization mass analysis of normal and genetic variants of human serum albumin
    • 9799752 1:CAS:528:DyaK1cXnt1Oltrk%3D
    • SO Brennan 1998 Electrospray ionization mass analysis of normal and genetic variants of human serum albumin Clin Chem 44 2264 2269 9799752 1:CAS:528:DyaK1cXnt1Oltrk%3D
    • (1998) Clin Chem , vol.44 , pp. 2264-2269
    • Brennan, S.O.1
  • 78
    • 34447642991 scopus 로고    scopus 로고
    • Individual variation of mucin concentration in human saliva
    • PA Denny W Wu PC Denny 2002 Individual variation of mucin concentration in human saliva J Dent Res 81 A 501
    • (2002) J Dent Res , vol.81 , pp. 501
    • Denny, P.A.1    Wu, W.2    Denny, P.C.3
  • 79
    • 13844310831 scopus 로고    scopus 로고
    • A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: An approach to understanding venom proteomics
    • 15627971 1:CAS:528:DC%2BD2MXhs1OitbY%3D
    • SM Serrano JD Shannon D Wang AC Camargo JW Fox 2005 A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: an approach to understanding venom proteomics Proteomics 5 501 510 15627971 1:CAS:528:DC%2BD2MXhs1OitbY%3D
    • (2005) Proteomics , vol.5 , pp. 501-510
    • Serrano, S.M.1    Shannon, J.D.2    Wang, D.3    Camargo, A.C.4    Fox, J.W.5
  • 80
    • 4344645328 scopus 로고    scopus 로고
    • Glycosylation changes in Alzheimer's disease as revealed by a proteomic approach
    • 15331161 1:CAS:528:DC%2BD2cXntFWqt78%3D
    • K Kanninen G Goldsteins S Auriola I Alafuzoff J Koistinaho 2004 Glycosylation changes in Alzheimer's disease as revealed by a proteomic approach Neurosci Lett 367 235 240 15331161 1:CAS:528:DC%2BD2cXntFWqt78%3D
    • (2004) Neurosci Lett , vol.367 , pp. 235-240
    • Kanninen, K.1    Goldsteins, G.2    Auriola, S.3    Alafuzoff, I.4    Koistinaho, J.5
  • 82
    • 33646941555 scopus 로고    scopus 로고
    • Unique posttranslational modifications of chitin-binding lectins of Entamoeba invadens cyst walls
    • 16682461
    • KL Van Dellen A Chatterjee DM Ratner, et al. 2006 Unique posttranslational modifications of chitin-binding lectins of Entamoeba invadens cyst walls Eukaryot Cell 5 836 848 16682461
    • (2006) Eukaryot Cell , vol.5 , pp. 836-848
    • Van Dellen, K.L.1    Chatterjee, A.2    Ratner, D.M.3
  • 83
    • 35649011957 scopus 로고    scopus 로고
    • Exploring the sialiome using titanium dioxide chromatography and mass spectrometry
    • 17623646 1:CAS:528:DC%2BD2sXht1WksbrE
    • MR Larsen SS Jensen LA Jakobsen NH Heegaard 2007 Exploring the sialiome using titanium dioxide chromatography and mass spectrometry Mol Cell Proteomics 6 1778 1787 17623646 1:CAS:528:DC%2BD2sXht1WksbrE
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1778-1787
    • Larsen, M.R.1    Jensen, S.S.2    Jakobsen, L.A.3    Heegaard, N.H.4
  • 84
    • 4043094860 scopus 로고    scopus 로고
    • A proteomic analysis of human bile
    • 15084671 1:CAS:528:DC%2BD2cXlvFens7c%3D
    • TZ Kristiansen J Bunkenborg M Gronborg, et al. 2004 A proteomic analysis of human bile Mol Cell Proteomics 3 715 728 15084671 1:CAS:528: DC%2BD2cXlvFens7c%3D
    • (2004) Mol Cell Proteomics , vol.3 , pp. 715-728
    • Kristiansen, T.Z.1    Bunkenborg, J.2    Gronborg, M.3
  • 85
    • 0033872756 scopus 로고    scopus 로고
    • Glycosylated salivary alpha-amylases are capable of maltotriose hydrolysis and glucose formation
    • 11026667 1:STN:280:DC%2BD3cvns1Wgtw%3D%3D
    • I Koyama S Komine M Yakushijin S Hokari T Komoda 2000 Glycosylated salivary alpha-amylases are capable of maltotriose hydrolysis and glucose formation Comp Biochem Physiol B Biochem Mol Biol 126 553 560 11026667 1:STN:280:DC%2BD3cvns1Wgtw%3D%3D
    • (2000) Comp Biochem Physiol B Biochem Mol Biol , vol.126 , pp. 553-560
    • Koyama, I.1    Komine, S.2    Yakushijin, M.3    Hokari, S.4    Komoda, T.5
  • 86
    • 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
    • Z Yang WS Hancock 2004 Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column J Chromatogr A 1053 79 88 15543974 1:CAS:528:DC%2BD2cXos1yqtbk%3D
    • (2004) J Chromatogr A , vol.1053 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 87
    • 33751529259 scopus 로고    scopus 로고
    • High-sensitivity profiling of glycoproteins from human blood serum through multiple-lectin affinity chromatography and liquid chromatography/tandem mass spectrometry
    • 16987717 1:CAS:528:DC%2BD28Xht12ktrzE
    • M Madera Y Mechref I Klouckova MV Novotny 2007 High-sensitivity profiling of glycoproteins from human blood serum through multiple-lectin affinity chromatography and liquid chromatography/tandem mass spectrometry J Chromatogr B Analyt Technol Biomed Life Sci 845 121 137 16987717 1:CAS:528: DC%2BD28Xht12ktrzE
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.845 , pp. 121-137
    • Madera, M.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 88
    • 33847339730 scopus 로고    scopus 로고
    • Combination of abundant protein depletion and multi-lectin affinity chromatography (M-LAC) for plasma protein biomarker discovery
    • 17269723 1:CAS:528:DC%2BD28XhtlCit73K
    • T Plavina E Wakshull WS Hancock M Hincapie 2007 Combination of abundant protein depletion and multi-lectin affinity chromatography (M-LAC) for plasma protein biomarker discovery J Proteome Res 6 662 671 17269723 1:CAS:528:DC%2BD28XhtlCit73K
    • (2007) J Proteome Res , vol.6 , pp. 662-671
    • Plavina, T.1    Wakshull, E.2    Hancock, W.S.3    Hincapie, M.4
  • 89
    • 33748294165 scopus 로고    scopus 로고
    • Semiautomated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry
    • 16944947 1:CAS:528:DC%2BD28Xns1ajsLw%3D
    • M Madera Y Mechref I Klouckova MV Novotny 2006 Semiautomated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry J Proteome Res 5 2348 2363 16944947 1:CAS:528:DC%2BD28Xns1ajsLw%3D
    • (2006) J Proteome Res , vol.5 , pp. 2348-2363
    • Madera, M.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 90
    • 18144419694 scopus 로고    scopus 로고
    • Use of multidimensional lectin affinity chromatography in differential glycoproteomics
    • 15859596 1:CAS:528:DC%2BD2MXisleqsr8%3D
    • R Qiu FE Regnier 2005 Use of multidimensional lectin affinity chromatography in differential glycoproteomics Anal Chem 77 2802 2809 15859596 1:CAS:528:DC%2BD2MXisleqsr8%3D
    • (2005) Anal Chem , vol.77 , pp. 2802-2809
    • Qiu, R.1    Regnier, F.E.2
  • 91
    • 0028280439 scopus 로고
    • Structural analysis of the N-glycans from human immunoglobulin A1: Comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis
    • 8166649 1:CAS:528:DyaK2cXjt1Whsr4%3D
    • MC Field S Amatayakul-Chantler TW Rademacher PM Rudd RA Dwek 1994 Structural analysis of the N-glycans from human immunoglobulin A1: comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis Biochem J 299 Pt 1 261 275 8166649 1:CAS:528: DyaK2cXjt1Whsr4%3D
    • (1994) Biochem J , vol.299 , Issue.PT 1 , pp. 261-275
    • Field, M.C.1    Amatayakul-Chantler, S.2    Rademacher, T.W.3    Rudd, P.M.4    Dwek, R.A.5
  • 92
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions
    • 9442070 1:CAS:528:DyaK1cXnsVGktw%3D%3D
    • TS Mattu RJ Pleass AC Willis, et al. 1998 The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions J Biol Chem 273 2260 2272 9442070 1:CAS:528:DyaK1cXnsVGktw%3D%3D
    • (1998) J Biol Chem , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3
  • 93
    • 0034686416 scopus 로고    scopus 로고
    • The N-glycans determine the differential blood clearance and hepatic uptake of human immunoglobulin (Ig)A1 and IgA2 isotypes
    • 10859341 1:CAS:528:DC%2BD3cXkt1WrurY%3D
    • A Rifai K Fadden SL Morrison KR Chintalacharuvu 2000 The N-glycans determine the differential blood clearance and hepatic uptake of human immunoglobulin (Ig)A1 and IgA2 isotypes J Exp Med 191 2171 2182 10859341 1:CAS:528:DC%2BD3cXkt1WrurY%3D
    • (2000) J Exp Med , vol.191 , pp. 2171-2182
    • Rifai, A.1    Fadden, K.2    Morrison, S.L.3    Chintalacharuvu, K.R.4
  • 94
    • 0028998769 scopus 로고
    • The asialoglycoprotein receptor: Relationships between structure, function, and expression
    • 7624395 1:CAS:528:DyaK2MXnslSlu7c%3D
    • RJ Stockert 1995 The asialoglycoprotein receptor: relationships between structure, function, and expression Physiol Rev 75 591 609 7624395 1:CAS:528:DyaK2MXnslSlu7c%3D
    • (1995) Physiol Rev , vol.75 , pp. 591-609
    • Stockert, R.J.1
  • 95
    • 0034753207 scopus 로고    scopus 로고
    • Progress in molecular and genetic studies of IgA nephropathy
    • 11720004 1:CAS:528:DC%2BD3MXovFSjurY%3D
    • J Novak BA Julian M Tomana J Mesteck 2001 Progress in molecular and genetic studies of IgA nephropathy J Clin Immunol 21 310 327 11720004 1:CAS:528:DC%2BD3MXovFSjurY%3D
    • (2001) J Clin Immunol , vol.21 , pp. 310-327
    • Novak, J.1    Julian, B.A.2    Tomana, M.3    Mesteck, J.4
  • 96
    • 0036145758 scopus 로고    scopus 로고
    • Increased sialylation of polymeric lambda-IgA1 in patients with IgA nephropathy
    • 11835525 1:CAS:528:DC%2BD38Xht1Wru74%3D
    • JC Leung SC Tang DT Chan SL Lui KN Lai 2002 Increased sialylation of polymeric lambda-IgA1 in patients with IgA nephropathy J Clin Lab Anal 16 11 19 11835525 1:CAS:528:DC%2BD38Xht1Wru74%3D
    • (2002) J Clin Lab Anal , vol.16 , pp. 11-19
    • Leung, J.C.1    Tang, S.C.2    Chan, D.T.3    Lui, S.L.4    Lai, K.N.5
  • 97
    • 0029001438 scopus 로고
    • Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy
    • 7774058 1:STN:280:DyaK2M3pt1eqtA%3D%3D
    • AC Allen SJ Harper J Feehally 1995 Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy Clin Exp Immunol 100 470 474 7774058 1:STN:280:DyaK2M3pt1eqtA%3D%3D
    • (1995) Clin Exp Immunol , vol.100 , pp. 470-474
    • Allen, A.C.1    Harper, S.J.2    Feehally, J.3
  • 98
    • 0027339137 scopus 로고
    • Carbohydrates in cell recognition
    • 7678182 1:CAS:528:DyaK3sXlsVCisA%3D%3D
    • N Sharon H Lis 1993 Carbohydrates in cell recognition Sci Am 268 82 89 7678182 1:CAS:528:DyaK3sXlsVCisA%3D%3D
    • (1993) Sci Am , vol.268 , pp. 82-89
    • Sharon, N.1    Lis, H.2
  • 99
    • 0028787845 scopus 로고
    • Microbial recognition of target-cell glycoconjugates
    • 8574698 1:CAS:528:DyaK2MXptFWrtrc%3D
    • KA Karlsson 1995 Microbial recognition of target-cell glycoconjugates Curr Opin Struct Biol 5 622 635 8574698 1:CAS:528:DyaK2MXptFWrtrc%3D
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 622-635
    • Karlsson, K.A.1
  • 100
    • 13544251395 scopus 로고    scopus 로고
    • Highly glycosylated human salivary molecules present oligosaccharides that mediate adhesion of leukocytes and Helicobacter pylori
    • 15697247 1:CAS:528:DC%2BD2MXjs1Krsw%3D%3D
    • A Prakobphol T Boren W Ma P Zhixiang SJ Fisher 2005 Highly glycosylated human salivary molecules present oligosaccharides that mediate adhesion of leukocytes and Helicobacter pylori Biochemistry 44 2216 2224 15697247 1:CAS:528:DC%2BD2MXjs1Krsw%3D%3D
    • (2005) Biochemistry , vol.44 , pp. 2216-2224
    • Prakobphol, A.1    Boren, T.2    Ma, W.3    Zhixiang, P.4    Fisher, S.J.5
  • 101
    • 33746501942 scopus 로고    scopus 로고
    • Pathogenesis of Helicobacter pylori infection
    • 16847081 1:CAS:528:DC%2BD28XosVaqsrg%3D
    • JG Kusters AH van Vliet EJ Kuipers 2006 Pathogenesis of Helicobacter pylori infection Clin Microbiol Rev 19 449 490 16847081 1:CAS:528: DC%2BD28XosVaqsrg%3D
    • (2006) Clin Microbiol Rev , vol.19 , pp. 449-490
    • Kusters, J.G.1    Van Vliet, A.H.2    Kuipers, E.J.3
  • 102
    • 15444357984 scopus 로고    scopus 로고
    • Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging
    • 9430586 1:CAS:528:DyaK1cXmtlyqtQ%3D%3D
    • D Ilver A Arnqvist J Ogren, et al. 1998 Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging Science 279 373 377 9430586 1:CAS:528:DyaK1cXmtlyqtQ%3D%3D
    • (1998) Science , vol.279 , pp. 373-377
    • Ilver, D.1    Arnqvist, A.2    Ogren, J.3
  • 103
    • 0027749278 scopus 로고
    • Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens
    • 8018146 1:CAS:528:DyaK2cXlt1ajsA%3D%3D
    • T Boren P Falk KA Roth G Larson S Normark 1993 Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens Science 262 1892 1895 8018146 1:CAS:528:DyaK2cXlt1ajsA%3D%3D
    • (1993) Science , vol.262 , pp. 1892-1895
    • Boren, T.1    Falk, P.2    Roth, K.A.3    Larson, G.4    Normark, S.5
  • 104
    • 0025948394 scopus 로고
    • Structure and bacterial receptor activity of a human salivary proline-rich glycoprotein
    • 1894623 1:CAS:528:DyaK3MXmtVCkurc%3D
    • BL Gillece-Castro A Prakobphol AL Burlingame H Leffler SJ Fisher 1991 Structure and bacterial receptor activity of a human salivary proline-rich glycoprotein J Biol Chem 266 17358 17368 1894623 1:CAS:528:DyaK3MXmtVCkurc%3D
    • (1991) J Biol Chem , vol.266 , pp. 17358-17368
    • Gillece-Castro, B.L.1    Prakobphol, A.2    Burlingame, A.L.3    Leffler, H.4    Fisher, S.J.5
  • 105
    • 0033983470 scopus 로고    scopus 로고
    • A role for Lewis a antigens on salivary agglutinin in binding to Streptococcus mutans
    • 10696874 1:CAS:528:DC%2BD3cXhvFWmt7g%3D
    • AJ Ligtenberg EC Veerman AV Nieuw Amerongen 2000 A role for Lewis a antigens on salivary agglutinin in binding to Streptococcus mutans Antonie Van Leeuwenhoek 77 21 30 10696874 1:CAS:528:DC%2BD3cXhvFWmt7g%3D
    • (2000) Antonie Van Leeuwenhoek , vol.77 , pp. 21-30
    • Ligtenberg, A.J.1    Veerman, E.C.2    Nieuw Amerongen, A.V.3
  • 106
    • 0030018567 scopus 로고    scopus 로고
    • Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans
    • 8836444 1:CAS:528:DyaK28XltVals7Y%3D
    • J Groenink AJ Ligtenberg EC Veerman JG Bolscher AV Nieuw Amerongen 1996 Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans Antonie Van Leeuwenhoek 70 79 87 8836444 1:CAS:528:DyaK28XltVals7Y%3D
    • (1996) Antonie Van Leeuwenhoek , vol.70 , pp. 79-87
    • Groenink, J.1    Ligtenberg, A.J.2    Veerman, E.C.3    Bolscher, J.G.4    Nieuw Amerongen, A.V.5
  • 107
    • 0033602996 scopus 로고    scopus 로고
    • Separate oligosaccharide determinants mediate interactions of the low-molecular-weight salivary mucin with neutrophils and bacteria
    • 10346903 1:CAS:528:DyaK1MXivVKku70%3D
    • A Prakobphol K Tangemann SD Rosen CI Hoover H Leffler SJ Fisher 1999 Separate oligosaccharide determinants mediate interactions of the low-molecular-weight salivary mucin with neutrophils and bacteria Biochemistry 38 6817 6825 10346903 1:CAS:528:DyaK1MXivVKku70%3D
    • (1999) Biochemistry , vol.38 , pp. 6817-6825
    • Prakobphol, A.1    Tangemann, K.2    Rosen, S.D.3    Hoover, C.I.4    Leffler, H.5    Fisher, S.J.6
  • 108
    • 0036123711 scopus 로고    scopus 로고
    • The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse
    • 11825880 1:CAS:528:DC%2BD38XhslOqtb0%3D
    • KA Thomsson A Prakobphol H Leffler, et al. 2002 The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse Glycobiology 12 1 14 11825880 1:CAS:528:DC%2BD38XhslOqtb0%3D
    • (2002) Glycobiology , vol.12 , pp. 1-14
    • Thomsson, K.A.1    Prakobphol, A.2    Leffler, H.3
  • 109
    • 22844433667 scopus 로고    scopus 로고
    • The chemistry and biology of mucin-type O-linked glycosylation
    • 16005634 1:CAS:528:DC%2BD2MXmvVKhtrk%3D
    • HC Hang CR Bertozzi 2005 The chemistry and biology of mucin-type O-linked glycosylation Bioorg Med Chem 13 5021 5034 16005634 1:CAS:528: DC%2BD2MXmvVKhtrk%3D
    • (2005) Bioorg Med Chem , vol.13 , pp. 5021-5034
    • Hang, H.C.1    Bertozzi, C.R.2
  • 110
    • 0026748190 scopus 로고
    • The broad diversity of neutral and sialylated oligosaccharides derived from human salivary mucins
    • 1627559 1:CAS:528:DyaK38Xkt1aisbY%3D
    • A Klein C Carnoy JM Wieruszeski, et al. 1992 The broad diversity of neutral and sialylated oligosaccharides derived from human salivary mucins Biochemistry 31 6152 6165 1627559 1:CAS:528:DyaK38Xkt1aisbY%3D
    • (1992) Biochemistry , vol.31 , pp. 6152-6165
    • Klein, A.1    Carnoy, C.2    Wieruszeski, J.M.3
  • 111
    • 0028980976 scopus 로고
    • Distinct populations of high-M(r) mucins secreted by different human salivary glands discriminated by density-gradient electrophoresis
    • 7639696 1:CAS:528:DyaK2MXnt1yjurs%3D
    • J Bolscher E Veerman A Van Nieuw Amerongen A Tulp D Verwoerd 1995 Distinct populations of high-M(r) mucins secreted by different human salivary glands discriminated by density-gradient electrophoresis Biochem J 309 Pt 3 801 806 7639696 1:CAS:528:DyaK2MXnt1yjurs%3D
    • (1995) Biochem J , vol.309 , Issue.PT 3 , pp. 801-806
    • Bolscher, J.1    Veerman, E.2    Van Nieuw Amerongen, A.3    Tulp, A.4    Verwoerd, D.5


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