메뉴 건너뛰기




Volumn 9, Issue , 2016, Pages 223-247

Glycan Arrays: From Basic Biochemical Research to Bioanalytical and Biomedical Applications

Author keywords

Biomarkers; Cancer; Glycoconjugate vaccines; Infectious diseases; Lectins

Indexed keywords

BIOMARKERS; BIOMOLECULES; BIOPOLYMERS; CARBOHYDRATES; DISEASES; MEDICAL APPLICATIONS; PROTEINS; VACCINES;

EID: 84975462735     PISSN: 19361327     EISSN: 19361335     Source Type: Book Series    
DOI: 10.1146/annurev-anchem-071015-041641     Document Type: Review
Times cited : (68)

References (155)
  • 1
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • Mariño K, Bones J, Kattla JJ, Rudd PM. 2010. A systematic approach to protein glycosylation analysis: A path through the maze. Nat. Chem. Biol. 6(10):713-23
    • (2010) Nat. Chem. Biol. , vol.6 , Issue.10 , pp. 713-723
    • Mariño, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 5
    • 84903982909 scopus 로고    scopus 로고
    • Investigating virus-glycan interactions using glycan microarrays
    • SmithDF, Cummings RD. 2014. Investigating virus-glycan interactions using glycan microarrays. Curr. Opin. Virol. 7:79-87
    • (2014) Curr. Opin. Virol. , vol.7 , pp. 79-87
    • Smith, D.F.1    Cummings, R.D.2
  • 6
    • 77950480397 scopus 로고    scopus 로고
    • Carbohydrate vaccines: Developing solutions to sticky situations?
    • Astronomo RD, Burton DR. 2010. Carbohydrate vaccines: developing solutions to sticky situations? Nat. Rev. Drug Discov. 9(4):308-24
    • (2010) Nat. Rev. Drug Discov. , vol.9 , Issue.4 , pp. 308-324
    • Astronomo, R.D.1    Burton, D.R.2
  • 7
    • 77952148025 scopus 로고    scopus 로고
    • The promise of glycomics, glycan arrays and carbohydrate-based vaccines
    • Lepenies B, Seeberger PH. 2010. The promise of glycomics, glycan arrays and carbohydrate-based vaccines. Immunopharmacol. Immunotoxicol. 32(2):196-207
    • (2010) Immunopharmacol. Immunotoxicol. , vol.32 , Issue.2 , pp. 196-207
    • Lepenies, B.1    Seeberger, P.H.2
  • 8
    • 14844337835 scopus 로고    scopus 로고
    • Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: Cell signaling receptors, glycosylphosphatidylinositol (GPI) structural requirement, and regulation of GPI activity
    • Krishnegowda G,Hajjar AM, Zhu J, Douglass EJ, Uematsu S, et al. 2005. Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: cell signaling receptors, glycosylphosphatidylinositol (GPI) structural requirement, and regulation of GPI activity. J. Biol. Chem. 280(9):8606-16
    • (2005) J. Biol. Chem. , vol.280 , Issue.9 , pp. 8606-8616
    • Krishnegowda, G.1    Hajjar, A.M.2    Zhu, J.3    Douglass, E.J.4    Uematsu, S.5
  • 9
    • 80053133500 scopus 로고    scopus 로고
    • Human sperm binding is mediated by the sialyl-LewisX oligosaccharide on the zona pellucida
    • Pang P, Chiu PCN, Lee C, Chang L, Panico M, et al. 2011. Human sperm binding is mediated by the sialyl-LewisX oligosaccharide on the zona pellucida. Science 333(6050):1761-64
    • (2011) Science , vol.333 , Issue.6050 , pp. 1761-1764
    • Pang, P.1    Chiu, P.C.N.2    Lee, C.3    Chang, L.4    Panico, M.5
  • 10
    • 3042562999 scopus 로고    scopus 로고
    • Probing proteincarbohydrate interactions with microarrays of synthetic oligosaccharides
    • Ratner DM, Adams EW, Su J, O'Keefe BR, Mrksich M, Seeberger PH. 2004. Probing proteincarbohydrate interactions with microarrays of synthetic oligosaccharides. ChemBioChem 5(3):379-83
    • (2004) ChemBioChem , vol.5 , Issue.3 , pp. 379-383
    • Ratner, D.M.1    Adams, E.W.2    Su, J.3    O'Keefe, B.R.4    Mrksich, M.5    Seeberger, P.H.6
  • 11
    • 0036193564 scopus 로고    scopus 로고
    • Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells
    • Wang D, Liu S, Trummer BJ, Deng C, Wang A. 2002. Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells. Nat. Biotechnol. 20(3):275-81
    • (2002) Nat. Biotechnol. , vol.20 , Issue.3 , pp. 275-281
    • Wang, D.1    Liu, S.2    Trummer, B.J.3    Deng, C.4    Wang, A.5
  • 12
    • 0036788485 scopus 로고    scopus 로고
    • Oligosaccharide microarrays for highthroughput detection and specificity assignments of carbohydrate-protein interactions
    • Fukui S, Feizi T, Galustian C, Lawson AM, Chai W. 2002. Oligosaccharide microarrays for highthroughput detection and specificity assignments of carbohydrate-protein interactions. Nat. Biotechnol. 20(10):1011-17
    • (2002) Nat. Biotechnol. , vol.20 , Issue.10 , pp. 1011-1017
    • Fukui, S.1    Feizi, T.2    Galustian, C.3    Lawson, A.M.4    Chai, W.5
  • 13
    • 84901232121 scopus 로고    scopus 로고
    • Microbial glycan microarrays define key features of host-microbial interactions
    • Stowell SR, Arthur CM,McBride R, Berger O, Razi N, et al. 2014. Microbial glycan microarrays define key features of host-microbial interactions. Nat. Chem. Biol. 10(6):470-76
    • (2014) Nat. Chem. Biol. , vol.10 , Issue.6 , pp. 470-476
    • Stowell, S.R.1    Arthur, C.M.2    McBride, R.3    Berger, O.4    Razi, N.5
  • 14
    • 84926429839 scopus 로고    scopus 로고
    • Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
    • Palma AS, Liu Y, Zhang H, Zhang Y, McCleary BV, et al. 2015. Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry. Mol. Cell. Proteomics 14(4):974-88
    • (2015) Mol. Cell. Proteomics , vol.14 , Issue.4 , pp. 974-988
    • Palma, A.S.1    Liu, Y.2    Zhang, H.3    Zhang, Y.4    McCleary, B.V.5
  • 17
    • 79959464070 scopus 로고    scopus 로고
    • Glycan microarrays for decoding the glycome
    • Rillahan CD, Paulson JC. 2011. Glycan microarrays for decoding the glycome. Annu. Rev. Biochem. 80(1):797-823
    • (2011) Annu. Rev. Biochem. , vol.80 , Issue.1 , pp. 797-823
    • Rillahan, C.D.1    Paulson, J.C.2
  • 18
    • 10344233222 scopus 로고    scopus 로고
    • Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
    • Blixt O, Head S, Mondala T, Scanlan C, Huflejt ME, et al. 2004. Printed covalent glycan array for ligand profiling of diverse glycan binding proteins. PNAS 101(49):17033-38
    • (2004) PNAS , vol.101 , Issue.49 , pp. 17033-17038
    • Blixt, O.1    Head, S.2    Mondala, T.3    Scanlan, C.4    Huflejt, M.E.5
  • 19
    • 34247556420 scopus 로고    scopus 로고
    • Synthesis and medical applications of oligosaccharides
    • Seeberger PH, Werz DB. 2007. Synthesis and medical applications of oligosaccharides. Nature 446(7139):1046-51
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1046-1051
    • Seeberger, P.H.1    Werz, D.B.2
  • 20
    • 70350441377 scopus 로고    scopus 로고
    • Opportunities and challenges in synthetic oligosaccharide and glycoconjugate research
    • Boltje TJ, Buskas T, Boons GJ. 2009. Opportunities and challenges in synthetic oligosaccharide and glycoconjugate research. Nat. Chem. 1(8):611-22
    • (2009) Nat. Chem. , vol.1 , Issue.8 , pp. 611-622
    • Boltje, T.J.1    Buskas, T.2    Boons, G.J.3
  • 21
    • 84893437530 scopus 로고    scopus 로고
    • The neoglycolipid (NGL)-based oligosaccharide microarray system poised to decipher the meta-glycome
    • Palma AS, Feizi T, Childs RA, Chai W, Liu Y. 2014. The neoglycolipid (NGL)-based oligosaccharide microarray system poised to decipher the meta-glycome. Curr. Opin. Chem. Biol. 18:87-94
    • (2014) Curr. Opin. Chem. Biol. , vol.18 , pp. 87-94
    • Palma, A.S.1    Feizi, T.2    Childs, R.A.3    Chai, W.4    Liu, Y.5
  • 23
    • 84901830328 scopus 로고    scopus 로고
    • Shotgun glycomics of pig lung identifies natural endogenous receptors for influenza viruses
    • Byrd-Leotis L, Liu R, Bradley KC, Lasanajak Y, Cummings SF, et al. 2014. Shotgun glycomics of pig lung identifies natural endogenous receptors for influenza viruses. PNAS 111(22):E2241-50
    • (2014) PNAS , vol.111 , Issue.22 , pp. E2241-E2250
    • Byrd-Leotis, L.1    Liu, R.2    Bradley, K.C.3    Lasanajak, Y.4    Cummings, S.F.5
  • 25
    • 84870746348 scopus 로고    scopus 로고
    • Differential anti-glycan antibody responses in Schistosoma mansoni-infected children and adults studied by shotgun glycan microarray
    • van Diepen A, Smit CH, van Egmond L, Kabatereine NB, Pinot de Moira A, et al. 2012. Differential anti-glycan antibody responses in Schistosoma mansoni-infected children and adults studied by shotgun glycan microarray. PLOS Negl. Trop. Dis. 6(11):e1922
    • (2012) PLOS Negl. Trop. Dis. , vol.6 , Issue.11 , pp. e1922
    • Van Diepen, A.1    Smit, C.H.2    Van Egmond, L.3    Kabatereine, N.B.4    Pinot De Moira, A.5
  • 26
    • 84910642776 scopus 로고    scopus 로고
    • Human milk contains novel glycans that are potential decoy receptors for neonatal rotaviruses
    • Yu Y, Lasanajak Y, Song X, Hu L, Ramani S, et al. 2014. Human milk contains novel glycans that are potential decoy receptors for neonatal rotaviruses. Mol. Cell. Proteom. 13(11):2944-60
    • (2014) Mol. Cell. Proteom. , vol.13 , Issue.11 , pp. 2944-2960
    • Yu, Y.1    Lasanajak, Y.2    Song, X.3    Hu, L.4    Ramani, S.5
  • 27
    • 3042646556 scopus 로고    scopus 로고
    • Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology: Glycan-dependent gp120/protein interactions
    • Adams EW, Ratner DM, Bokesch HR, McMahon JB, O'Keefe BR, Seeberger PH. 2004. Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology: glycan-dependent gp120/protein interactions. Chem. Biol. 11(6):875-81
    • (2004) Chem. Biol. , vol.11 , Issue.6 , pp. 875-881
    • Adams, E.W.1    Ratner, D.M.2    Bokesch, H.R.3    McMahon, J.B.4    O'Keefe, B.R.5    Seeberger, P.H.6
  • 28
    • 50149097938 scopus 로고    scopus 로고
    • Glycan microarray of Globo H and related structures for quantitative analysis of breast cancer
    • Wang C, Huang Y, Ren C, Lin C, Hung J, et al. 2008. Glycan microarray of Globo H and related structures for quantitative analysis of breast cancer. PNAS 105(33):11661-66
    • (2008) PNAS , vol.105 , Issue.33 , pp. 11661-11666
    • Wang, C.1    Huang, Y.2    Ren, C.3    Lin, C.4    Hung, J.5
  • 30
    • 3242672218 scopus 로고    scopus 로고
    • Covalent display of oligosaccharide arrays in microtiter plates
    • Bryan MC, Fazio F, Lee H, Huang C, Chang A, et al. 2004. Covalent display of oligosaccharide arrays in microtiter plates. J. Am. Chem. Soc. 126(28):8640-41
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.28 , pp. 8640-8641
    • Bryan, M.C.1    Fazio, F.2    Lee, H.3    Huang, C.4    Chang, A.5
  • 31
    • 33750949914 scopus 로고    scopus 로고
    • Carbohydrate microarrays: Survey of fabrication techniques
    • Culf AS, Cuperlovic-Culf M, Ouellette RJ. 2006. Carbohydrate microarrays: survey of fabrication techniques. OMICS 10(3):289-310
    • (2006) OMICS , vol.10 , Issue.3 , pp. 289-310
    • Culf, A.S.1    Cuperlovic-Culf, M.2    Ouellette, R.J.3
  • 32
    • 84899877851 scopus 로고    scopus 로고
    • Crystallographic and glycan microarray analysis of human polyomavirus 9 VP1 identifies N-glycolyl neuraminic acid as a receptor candidate
    • Khan ZM, Liu Y, Neu U, Gilbert M, Ehlers B, et al. 2014. Crystallographic and glycan microarray analysis of human polyomavirus 9 VP1 identifies N-glycolyl neuraminic acid as a receptor candidate. J. Virol. 88(11):6100-11
    • (2014) J. Virol. , vol.88 , Issue.11 , pp. 6100-6111
    • Khan, Z.M.1    Liu, Y.2    Neu, U.3    Gilbert, M.4    Ehlers, B.5
  • 33
    • 84866443327 scopus 로고    scopus 로고
    • Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein
    • Klein F, Gaebler C,Mouquet H, Sather DN, Lehmann C, et al. 2012. Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein. J. Exp. Med. 209(8):1469-79
    • (2012) J. Exp. Med. , vol.209 , Issue.8 , pp. 1469-1479
    • Klein, F.1    Gaebler, C.2    Mouquet, H.3    Sather, D.N.4    Lehmann, C.5
  • 34
    • 84902192402 scopus 로고    scopus 로고
    • Carbohydrate sequence of the prostate cancer-associated antigen F77 assigned by a mucin O-glycome designer array
    • GaoC,Liu Y, ZhangH,Zhang Y, FukudaMN,et al. 2014. Carbohydrate sequence of the prostate cancer-associated antigen F77 assigned by a mucin O-glycome designer array. J. Biol. Chem. 289(23):16462-77
    • (2014) J. Biol. Chem. , vol.289 , Issue.23 , pp. 16462-16477
    • Gao, C.1    Liu, Y.2    Zhang, H.3    Zhang, Y.4    Fukuda, M.N.5
  • 35
    • 84934286887 scopus 로고    scopus 로고
    • Defining the interaction of human soluble lectin ZG16p and mycobacterial phosphatidylinositol mannosides
    • Hanashima S, Götze S, Liu Y, Ikeda A, Kojima-Aikawa K, et al. 2015. Defining the interaction of human soluble lectin ZG16p and mycobacterial phosphatidylinositol mannosides. ChemBioChem 16(10):1502-11
    • (2015) ChemBioChem , vol.16 , Issue.10 , pp. 1502-1511
    • Hanashima, S.1    Götze, S.2    Liu, Y.3    Ikeda, A.4    Kojima-Aikawa, K.5
  • 37
    • 82355193805 scopus 로고    scopus 로고
    • Neoglycolipid-based oligosaccharide microarray system: Preparation of NGLs and their noncovalent immobilization on nitrocellulose-coated glass slides for microarray analyses
    • Liu Y, Childs RA, Palma AS, Campanero-Rhodes MA, Stoll MS, et al. 2012. Neoglycolipid-based oligosaccharide microarray system: preparation of NGLs and their noncovalent immobilization on nitrocellulose-coated glass slides for microarray analyses. Methods Mol. Biol. 808:117-36
    • (2012) Methods Mol. Biol. , vol.808 , pp. 117-136
    • Liu, Y.1    Childs, R.A.2    Palma, A.S.3    Campanero-Rhodes, M.A.4    Stoll, M.S.5
  • 39
    • 84938953467 scopus 로고    scopus 로고
    • Chemical synthesis elucidates the immunological importance of a pyruvate modification in the capsular polysaccharide of Streptococcus pneumoniae serotype 4
    • Pereira CL, Geissner A, Anish C, Seeberger PH. 2015. Chemical synthesis elucidates the immunological importance of a pyruvate modification in the capsular polysaccharide of Streptococcus pneumoniae serotype 4. Angew. Chem. Int. Ed. 54(34):10016-19
    • (2015) Angew. Chem. Int. Ed. , vol.54 , Issue.34 , pp. 10016-10019
    • Pereira, C.L.1    Geissner, A.2    Anish, C.3    Seeberger, P.H.4
  • 40
    • 84915747394 scopus 로고    scopus 로고
    • Immunogenicity study of Globo H analogues with modification at the reducing or nonreducing end of the tumor antigen
    • Lee H, Chen C, Tsai T, Li S, Lin K, et al. 2014. Immunogenicity study of Globo H analogues with modification at the reducing or nonreducing end of the tumor antigen. J. Am. Chem. Soc. 136(48):16844-53
    • (2014) J. Am. Chem. Soc. , vol.136 , Issue.48 , pp. 16844-16853
    • Lee, H.1    Chen, C.2    Tsai, T.3    Li, S.4    Lin, K.5
  • 41
    • 84929192305 scopus 로고    scopus 로고
    • Total synthesis of legionaminic acid as basis for serological studies
    • Matthies S, Stallforth P, Seeberger PH. 2015. Total synthesis of legionaminic acid as basis for serological studies. J. Am. Chem. Soc. 137(8):2848-51
    • (2015) J. Am. Chem. Soc. , vol.137 , Issue.8 , pp. 2848-2851
    • Matthies, S.1    Stallforth, P.2    Seeberger, P.H.3
  • 42
    • 84898069380 scopus 로고    scopus 로고
    • Synthesis of conjugation-ready zwitterionic oligosaccharides by chemoselective thioglycoside activation
    • Schumann B, Pragani R, Anish C, Pereira CL, Seeberger PH. 2014. Synthesis of conjugation-ready zwitterionic oligosaccharides by chemoselective thioglycoside activation. Chem. Sci. 5(5):1992-2002
    • (2014) Chem. Sci. , vol.5 , Issue.5 , pp. 1992-2002
    • Schumann, B.1    Pragani, R.2    Anish, C.3    Pereira, C.L.4    Seeberger, P.H.5
  • 43
    • 84919344213 scopus 로고    scopus 로고
    • Diagnosis of toxoplasmosis using a synthetic glycosylphosphatidylinositol glycan
    • Götze S, Azzouz N, Tsai Y, Groß U, Reinhardt A, et al. 2014. Diagnosis of toxoplasmosis using a synthetic glycosylphosphatidylinositol glycan. Angew. Chem. Int. Ed. 53(50):13701-5
    • (2014) Angew. Chem. Int. Ed. , vol.53 , Issue.50 , pp. 13701-13705
    • Götze, S.1    Azzouz, N.2    Tsai, Y.3    Groß, U.4    Reinhardt, A.5
  • 44
    • 84943223077 scopus 로고    scopus 로고
    • Investigation of the protective properties of glycosylphosphatidylinositol-based vaccine candidates in a Toxoplasma gondii mouse challenge model
    • Götze S, ReinhardtA,Geissner A, Azzouz N, Tsai Y, et al. 2015. Investigation of the protective properties of glycosylphosphatidylinositol-based vaccine candidates in a Toxoplasma gondii mouse challenge model. Glycobiology 25(9):984-91
    • (2015) Glycobiology , vol.25 , Issue.9 , pp. 984-991
    • Götze, S.1    Reinhardt, A.2    Geissner, A.3    Azzouz, N.4    Tsai, Y.5
  • 45
    • 25444514510 scopus 로고    scopus 로고
    • Facile preparation of carbohydrate microarrays by site-specific, covalent immobilization of unmodified carbohydrates on hydrazide-coated glass slides
    • Lee M, Shin I. 2005. Facile preparation of carbohydrate microarrays by site-specific, covalent immobilization of unmodified carbohydrates on hydrazide-coated glass slides. Org. Lett. 7(19):4269-72
    • (2005) Org. Lett. , vol.7 , Issue.19 , pp. 4269-4272
    • Lee, M.1    Shin, I.2
  • 46
    • 84921528365 scopus 로고    scopus 로고
    • Antigenic potential of a highly conserved Neisseria meningitidis lipopolysaccharide inner core structure defined by chemical synthesis
    • Reinhardt A, Yang Y, ClausH, Pereira CL,Cox AD, et al. 2015. Antigenic potential of a highly conserved Neisseria meningitidis lipopolysaccharide inner core structure defined by chemical synthesis. Chem. Biol. 22(1):38-49
    • (2015) Chem. Biol. , vol.22 , Issue.1 , pp. 38-49
    • Reinhardt, A.1    Yang, Y.2    Claus, H.3    Pereira, C.L.4    Cox, A.D.5
  • 48
    • 53049085180 scopus 로고    scopus 로고
    • Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins
    • Tateno H, Mori A, Uchiyama N, Yabe R, Iwaki J, et al. 2008. Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins. Glycobiology 18(10):789-98
    • (2008) Glycobiology , vol.18 , Issue.10 , pp. 789-798
    • Tateno, H.1    Mori, A.2    Uchiyama, N.3    Yabe, R.4    Iwaki, J.5
  • 49
    • 84890350538 scopus 로고    scopus 로고
    • Presentation, presentation, presentation! Molecular-level insight into linker effects on glycan array screening data
    • Grant OC, Smith HM, Firsova D, Fadda E, Woods RJ. 2013. Presentation, presentation, presentation! Molecular-level insight into linker effects on glycan array screening data. Glycobiology 24(1):17-25
    • (2013) Glycobiology , vol.24 , Issue.1 , pp. 17-25
    • Grant, O.C.1    Smith, H.M.2    Firsova, D.3    Fadda, E.4    Woods, R.J.5
  • 50
    • 34548725053 scopus 로고    scopus 로고
    • Quantitative analysis of carbohydrate-protein interactions using glycan microarrays: Determination of surface and solution dissociation constants
    • Liang P, Wang S, Wong C. 2007. Quantitative analysis of carbohydrate-protein interactions using glycan microarrays: determination of surface and solution dissociation constants. J. Am. Chem. Soc. 129(36):11177-84
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.36 , pp. 11177-11184
    • Liang, P.1    Wang, S.2    Wong, C.3
  • 51
    • 67650351512 scopus 로고    scopus 로고
    • Microarrays with varying carbohydrate density reveal distinct subpopulations of serum antibodies
    • Oyelaran O, Li Q, Farnsworth D, Gildersleeve JC. 2009. Microarrays with varying carbohydrate density reveal distinct subpopulations of serum antibodies. J. Proteome Res. 8(7):3529-38
    • (2009) J. Proteome Res. , vol.8 , Issue.7 , pp. 3529-3538
    • Oyelaran, O.1    Li, Q.2    Farnsworth, D.3    Gildersleeve, J.C.4
  • 52
    • 84865150015 scopus 로고    scopus 로고
    • Synthesis of a library of fucosylated glycoclusters and determination of their binding toward Pseudomonas aeruginosa lectin B (PA-IIL) using a DNA-based carbohydrate microarray
    • Gerland B, Goudot A, Pourceau G, Meyer A, Dugas V, et al. 2012. Synthesis of a library of fucosylated glycoclusters and determination of their binding toward Pseudomonas aeruginosa lectin B (PA-IIL) using a DNA-based carbohydrate microarray. Bioconjug. Chem. 23(8):1534-47
    • (2012) Bioconjug. Chem. , vol.23 , Issue.8 , pp. 1534-1547
    • Gerland, B.1    Goudot, A.2    Pourceau, G.3    Meyer, A.4    Dugas, V.5
  • 53
    • 84868641932 scopus 로고    scopus 로고
    • Quantitative analysis (Kd and IC50) of glycoconjugates interactions with a bacterial lectin on a carbohydrate microarray with DNA direct immobilization (DDI)
    • Goudot A, Pourceau G, Meyer A, Gehin T, Vidal S, et al. 2013. Quantitative analysis (Kd and IC50) of glycoconjugates interactions with a bacterial lectin on a carbohydrate microarray with DNA direct immobilization (DDI). Biosens. Bioelectron. 40(1):153-60
    • (2013) Biosens. Bioelectron. , vol.40 , Issue.1 , pp. 153-160
    • Goudot, A.1    Pourceau, G.2    Meyer, A.3    Gehin, T.4    Vidal, S.5
  • 54
    • 78650336433 scopus 로고    scopus 로고
    • Surface characterization of carbohydrate microarrays
    • Scurr DJ, Horlacher T, Oberli MA,Werz DB, Kroeck L, et al. 2010. Surface characterization of carbohydrate microarrays. Langmuir 26(22):17143-55
    • (2010) Langmuir , vol.26 , Issue.22 , pp. 17143-17155
    • Scurr, D.J.1    Horlacher, T.2    Oberli, M.A.3    Werz, D.B.4    Kroeck, L.5
  • 55
    • 84971466507 scopus 로고    scopus 로고
    • Competition between serum IgG, IgM, and IgA anti-glycan antibodies
    • Muthana SM, Xia L, Campbell CT, Zhang Y, Gildersleeve JC. 2015. Competition between serum IgG, IgM, and IgA anti-glycan antibodies. PLOS ONE 10(3):e0119298
    • (2015) PLOS ONE , vol.10 , Issue.3 , pp. e0119298
    • Muthana, S.M.1    Xia, L.2    Campbell, C.T.3    Zhang, Y.4    Gildersleeve, J.C.5
  • 56
    • 84880347916 scopus 로고    scopus 로고
    • Glycan arrays containing synthetic Clostridium difficile lipoteichoic acid oligomers as tools toward a carbohydrate vaccine
    • Martin CE, Broecker F, Eller S, Oberli MA, Anish C, et al. 2013. Glycan arrays containing synthetic Clostridium difficile lipoteichoic acid oligomers as tools toward a carbohydrate vaccine. Chem. Commun. 49(64):7159
    • (2013) Chem. Commun. , vol.49 , Issue.64 , pp. 7159
    • Martin, C.E.1    Broecker, F.2    Eller, S.3    Oberli, M.A.4    Anish, C.5
  • 57
    • 33646843444 scopus 로고    scopus 로고
    • Ligands for the beta-glucan receptor, Dectin-1, assigned using "designer" microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides
    • Palma AS, Feizi T, Zhang Y, Stoll MS, Lawson AM, et al. 2006. Ligands for the beta-glucan receptor, Dectin-1, assigned using "designer" microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides. J. Biol. Chem. 281(9):5771-79
    • (2006) J. Biol. Chem. , vol.281 , Issue.9 , pp. 5771-5779
    • Palma, A.S.1    Feizi, T.2    Zhang, Y.3    Stoll, M.S.4    Lawson, A.M.5
  • 58
    • 84874109172 scopus 로고    scopus 로고
    • Vibrio cholerae cytolysin recognizes the heptasaccharide core of complex N-glycans with nanomolar affinity
    • Levan S, De S, Olson R. 2013. Vibrio cholerae cytolysin recognizes the heptasaccharide core of complex N-glycans with nanomolar affinity. J. Mol. Biol. 425(5):944-57
    • (2013) J. Mol. Biol. , vol.425 , Issue.5 , pp. 944-957
    • Levan, S.1    De, S.2    Olson, R.3
  • 59
    • 84859999995 scopus 로고    scopus 로고
    • Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity
    • Sulák O, Cioci G, Lameignère E, Balloy V, Round A, et al. 2011. Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. PLOS Pathog. 7(9):e1002238
    • (2011) PLOS Pathog. , vol.7 , Issue.9 , pp. e1002238
    • Sulák, O.1    Cioci, G.2    Lameignère, E.3    Balloy, V.4    Round, A.5
  • 60
    • 71749095164 scopus 로고    scopus 로고
    • Profiling carbohydrate-receptor interaction with recombinant innate immunity receptor-Fc fusion proteins
    • Hsu T, Cheng S, Yang W, Chin S, Chen B, et al. 2009. Profiling carbohydrate-receptor interaction with recombinant innate immunity receptor-Fc fusion proteins. J. Biol. Chem. 284(50):34479-89
    • (2009) J. Biol. Chem. , vol.284 , Issue.50 , pp. 34479-34489
    • Hsu, T.1    Cheng, S.2    Yang, W.3    Chin, S.4    Chen, B.5
  • 61
    • 84882266212 scopus 로고    scopus 로고
    • Histopathologies, immunolocalization, and a glycan binding screen provide insights into Plasmodium falciparum interactions with the human placenta
    • Hromatka BS, Ngeleza S, Adibi JJ, Niles RK, Tshefu AK, Fisher SJ. 2013. Histopathologies, immunolocalization, and a glycan binding screen provide insights into Plasmodium falciparum interactions with the human placenta. Biol. Reprod. 88(6):154
    • (2013) Biol. Reprod. , vol.88 , Issue.6 , pp. 154
    • Hromatka, B.S.1    Ngeleza, S.2    Adibi, J.J.3    Niles, R.K.4    Tshefu, A.K.5    Fisher, S.J.6
  • 63
    • 84861146558 scopus 로고    scopus 로고
    • Difference in fine specificity to polysaccharides of Candida albicans mannoprotein between mouse SIGNR1 and human DC-SIGN
    • Takahara K, Arita T, Tokieda S, Shibata N, Okawa Y, et al. 2012. Difference in fine specificity to polysaccharides of Candida albicans mannoprotein between mouse SIGNR1 and human DC-SIGN. Infect. Immun. 80(5):1699-706
    • (2012) Infect. Immun. , vol.80 , Issue.5 , pp. 1699-1706
    • Takahara, K.1    Arita, T.2    Tokieda, S.3    Shibata, N.4    Okawa, Y.5
  • 64
    • 61849087823 scopus 로고    scopus 로고
    • Construction of carbohydrate microarrays by using one-step, direct immobilizations of diverse unmodified glycans on solid surfaces
    • Park S, LeeM, Shin I. 2009. Construction of carbohydrate microarrays by using one-step, direct immobilizations of diverse unmodified glycans on solid surfaces. Bioconjugate Chem. 20(1):155-62
    • (2009) Bioconjugate Chem. , vol.20 , Issue.1 , pp. 155-162
    • Park, S.1    Lee, M.2    Shin, I.3
  • 65
    • 34250207393 scopus 로고    scopus 로고
    • High-throughput mapping of cell-wall polymers within and between plants using novel microarrays
    • Moller I, Sørensen I, Bernal AJ, Blaukopf C, Lee K, et al. 2007. High-throughput mapping of cell-wall polymers within and between plants using novel microarrays. Plant J. 50(6):1118-28
    • (2007) Plant J. , vol.50 , Issue.6 , pp. 1118-1128
    • Moller, I.1    Sørensen, I.2    Bernal, A.J.3    Blaukopf, C.4    Lee, K.5
  • 67
    • 85012085322 scopus 로고    scopus 로고
    • Characterization of receptor binding profiles of influenza A viruses using an ellipsometry-based label-free glycan microarray assay platform
    • Fei Y, Sun Y, Li Y, Yu H, Lau K, et al. 2015. Characterization of receptor binding profiles of influenza A viruses using an ellipsometry-based label-free glycan microarray assay platform. Biomolecules 5(3):1480-98
    • (2015) Biomolecules , vol.5 , Issue.3 , pp. 1480-1498
    • Fei, Y.1    Sun, Y.2    Li, Y.3    Yu, H.4    Lau, K.5
  • 68
    • 84923790599 scopus 로고    scopus 로고
    • A diverse range of bacterial and eukaryotic chitinases hydrolyzes the LacNAc (Galβ1-4GlcNAc) and LacdiNAc (GalNAcβ1-4GlcNAc) motifs found on vertebrate and insect cells
    • Frederiksen RF, Yoshimura Y, Storgaard BG, Paspaliari DK, Petersen BO, et al. 2015. A diverse range of bacterial and eukaryotic chitinases hydrolyzes the LacNAc (Galβ1-4GlcNAc) and LacdiNAc (GalNAcβ1-4GlcNAc) motifs found on vertebrate and insect cells. J. Biol. Chem. 290(9):5354-66
    • (2015) J. Biol. Chem. , vol.290 , Issue.9 , pp. 5354-5366
    • Frederiksen, R.F.1    Yoshimura, Y.2    Storgaard, B.G.3    Paspaliari, D.K.4    Petersen, B.O.5
  • 69
    • 84926654892 scopus 로고    scopus 로고
    • A new versatile microarray-based method for high throughput screening of carbohydrate-active enzymes
    • Vidal-Melgosa S, Pedersen HL, Schückel J, Arnal G, Dumon C, et al. 2015. A new versatile microarray-based method for high throughput screening of carbohydrate-active enzymes. J. Biol. Chem. 290(14):9020-36
    • (2015) J. Biol. Chem. , vol.290 , Issue.14 , pp. 9020-9036
    • Vidal-Melgosa, S.1    Pedersen, H.L.2    Schückel, J.3    Arnal, G.4    Dumon, C.5
  • 70
    • 34248344690 scopus 로고    scopus 로고
    • Carbohydrate microarrays for assaying galactosyltransferase activity
    • Park S, Shin I. 2007. Carbohydrate microarrays for assaying galactosyltransferase activity. Org. Lett. 9(9):1675-78
    • (2007) Org. Lett. , vol.9 , Issue.9 , pp. 1675-1678
    • Park, S.1    Shin, I.2
  • 71
    • 84929576000 scopus 로고    scopus 로고
    • Synthesis and microarray-assisted binding studies of core xylose and fucose containing N-glycans
    • Brzezicka K, Echeverria B, Serna S, van Diepen A, Hokke CH, Reichardt N. 2015. Synthesis and microarray-assisted binding studies of core xylose and fucose containing N-glycans. ACS Chem. Biol. 10(5):1290-302
    • (2015) ACS Chem. Biol. , vol.10 , Issue.5 , pp. 1290-1302
    • Brzezicka, K.1    Echeverria, B.2    Serna, S.3    Van Diepen, A.4    Hokke, C.H.5    Reichardt, N.6
  • 72
    • 84880528724 scopus 로고    scopus 로고
    • Array-assisted characterization of a fucosyltransferase required for the biosynthesis of complex core modifications of nematode N-glycans
    • Yan S, Serna S, Reichardt N, Paschinger K, Wilson IBH. 2013. Array-assisted characterization of a fucosyltransferase required for the biosynthesis of complex core modifications of nematode N-glycans. J. Biol. Chem. 288(29):21015-28
    • (2013) J. Biol. Chem. , vol.288 , Issue.29 , pp. 21015-21028
    • Yan, S.1    Serna, S.2    Reichardt, N.3    Paschinger, K.4    Wilson, I.B.H.5
  • 73
    • 39049089497 scopus 로고    scopus 로고
    • Glycan microarrays for screening sialyltransferase specificities
    • Blixt O, Allin K, Bohorov O, Liu X, Andersson-Sand H, et al. 2008. Glycan microarrays for screening sialyltransferase specificities. Glycoconj. J. 25(1):59-68
    • (2008) Glycoconj. J. , vol.25 , Issue.1 , pp. 59-68
    • Blixt, O.1    Allin, K.2    Bohorov, O.3    Liu, X.4    Andersson-Sand, H.5
  • 74
    • 79951791809 scopus 로고    scopus 로고
    • MALDI-TOF mass spectrometric analysis of enzyme activity and lectin trapping on an array of N-glycans
    • Sanchez-Ruiz A, Serna S, Ruiz N, Martin-Lomas M, Reichardt N. 2011. MALDI-TOF mass spectrometric analysis of enzyme activity and lectin trapping on an array of N-glycans. Angew. Chem. Int. Ed. 50(8):1801-4
    • (2011) Angew. Chem. Int. Ed. , vol.50 , Issue.8 , pp. 1801-1804
    • Sanchez-Ruiz, A.1    Serna, S.2    Ruiz, N.3    Martin-Lomas, M.4    Reichardt, N.5
  • 75
    • 84865343780 scopus 로고    scopus 로고
    • Discovery of glycosyltransferases using carbohydrate arrays and mass spectrometry
    • BanL,PettitN,LiL, Stuparu AD, Cai L, et al. 2012. Discovery of glycosyltransferases using carbohydrate arrays and mass spectrometry. Nat. Chem. Biol. 8(9):769-73
    • (2012) Nat. Chem. Biol. , vol.8 , Issue.9 , pp. 769-773
    • Ban, L.1    Pettit, N.2    Li, L.3    Stuparu, A.D.4    Cai, L.5
  • 76
    • 70349117661 scopus 로고    scopus 로고
    • Glycan arrays: Recent advances and future challenges
    • Oyelaran O, Gildersleeve JC. 2009. Glycan arrays: recent advances and future challenges. Curr. Opin. Chem. Biol. 13(4):406-13
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , Issue.4 , pp. 406-413
    • Oyelaran, O.1    Gildersleeve, J.C.2
  • 77
    • 84878375746 scopus 로고    scopus 로고
    • A glyco-chip for the detection of ricin by an automated chemiluminescence read-out system
    • Huebner M, Wutz K, Szkola A, Niessner R, Seidel M. 2013. A glyco-chip for the detection of ricin by an automated chemiluminescence read-out system. Anal. Sci. 29(4):461-66
    • (2013) Anal. Sci. , vol.29 , Issue.4 , pp. 461-466
    • Huebner, M.1    Wutz, K.2    Szkola, A.3    Niessner, R.4    Seidel, M.5
  • 78
    • 84908004914 scopus 로고    scopus 로고
    • Rapid and simultaneous detection of ricin, staphylococcal enterotoxin B and saxitoxin by chemiluminescence-based microarray immunoassay
    • Szkola A, Linares EM, Worbs S,Dorner BG, Dietrich R, et al. 2014. Rapid and simultaneous detection of ricin, staphylococcal enterotoxin B and saxitoxin by chemiluminescence-based microarray immunoassay. Analyst 139(22):5885-92
    • (2014) Analyst , vol.139 , Issue.22 , pp. 5885-5892
    • Szkola, A.1    Linares, E.M.2    Worbs, S.3    Dorner, B.G.4    Dietrich, R.5
  • 79
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, Akira S. 2010. Pattern recognition receptors and inflammation. Cell 140(6):805-20
    • (2010) Cell , vol.140 , Issue.6 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 80
    • 45449112374 scopus 로고    scopus 로고
    • Galectins: Structure, function and therapeutic potential
    • Yang R, Rabinovich GA, Liu F. 2008. Galectins: structure, function and therapeutic potential. Expert Rev. Mol. Med. 10:e17
    • (2008) Expert Rev. Mol. Med. , vol.10 , pp. e17
    • Yang, R.1    Rabinovich, G.A.2    Liu, F.3
  • 81
    • 65249118801 scopus 로고    scopus 로고
    • Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: Contributions of an extended site and residue 343
    • Crouch E, Hartshorn K, Horlacher T, McDonald B, Smith K, et al. 2009. Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: contributions of an extended site and residue 343. Biochemistry 48(15):3335-45
    • (2009) Biochemistry , vol.48 , Issue.15 , pp. 3335-3345
    • Crouch, E.1    Hartshorn, K.2    Horlacher, T.3    McDonald, B.4    Smith, K.5
  • 83
    • 84859405717 scopus 로고    scopus 로고
    • Signaling by myeloid C-type lectin receptors in immunity and homeostasis
    • Sancho D, Reis e Sousa C. 2012. Signaling by myeloid C-type lectin receptors in immunity and homeostasis. Annu. Rev. Immunol. 30(1):491-529
    • (2012) Annu. Rev. Immunol. , vol.30 , Issue.1 , pp. 491-529
    • Sancho, D.1    Reis e Sousa, C.2
  • 84
    • 34548321364 scopus 로고    scopus 로고
    • Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins
    • Thiel S. 2007. Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins. Mol. Immunol. 44(16):3875-88
    • (2007) Mol. Immunol. , vol.44 , Issue.16 , pp. 3875-3888
    • Thiel, S.1
  • 86
    • 44649141897 scopus 로고    scopus 로고
    • Recognition of acetylated oligosaccharides by human L-ficolin
    • Krarup A, Mitchell DA, Sim RB. 2008. Recognition of acetylated oligosaccharides by human L-ficolin. Immunol. Lett. 118(2):152-56
    • (2008) Immunol. Lett. , vol.118 , Issue.2 , pp. 152-156
    • Krarup, A.1    Mitchell, D.A.2    Sim, R.B.3
  • 87
    • 77949878087 scopus 로고    scopus 로고
    • Carbohydrate recognition properties of human ficolins: Glycan array screening reveals the sialic acid binding specificity ofM-ficolin
    • Gout E, Garlatti V, Smith DF, Lacroix M, Dumestre-Pérard C, et al. 2010. Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity ofM-ficolin. J. Biol. Chem. 285(9):6612-22
    • (2010) J. Biol. Chem. , vol.285 , Issue.9 , pp. 6612-6622
    • Gout, E.1    Garlatti, V.2    Smith, D.F.3    Lacroix, M.4    Dumestre-Pérard, C.5
  • 88
    • 77955134905 scopus 로고    scopus 로고
    • Determination of carbohydratebinding preferences of human galectins with carbohydrate microarrays
    • Horlacher T, Oberli MA, Werz DB, Kröck L, Bufali S, et al. 2010. Determination of carbohydratebinding preferences of human galectins with carbohydrate microarrays. ChemBioChem 11(11):1563-73
    • (2010) ChemBioChem , vol.11 , Issue.11 , pp. 1563-1573
    • Horlacher, T.1    Oberli, M.A.2    Werz, D.B.3    Kröck, L.4    Bufali, S.5
  • 89
    • 44049104824 scopus 로고    scopus 로고
    • Galectin-1,-2, and-3 exhibit differential recognition of sialylated glycans and blood group antigens
    • Stowell SR, Arthur CM, Mehta P, Slanina KA, Blixt O, et al. 2008. Galectin-1,-2, and-3 exhibit differential recognition of sialylated glycans and blood group antigens. J. Biol. Chem. 283(15):10109-23
    • (2008) J. Biol. Chem. , vol.283 , Issue.15 , pp. 10109-10123
    • Stowell, S.R.1    Arthur, C.M.2    Mehta, P.3    Slanina, K.A.4    Blixt, O.5
  • 90
  • 91
    • 80051501538 scopus 로고    scopus 로고
    • Since there are PAMPs and DAMPs, there must be SAMPs? Glycan "self-associated molecular patterns" dampen innate immunity, but pathogens can mimic them
    • Varki A. 2011. Since there are PAMPs and DAMPs, there must be SAMPs? Glycan "self-associated molecular patterns" dampen innate immunity, but pathogens can mimic them. Glycobiology 21(9):1121-24
    • (2011) Glycobiology , vol.21 , Issue.9 , pp. 1121-1124
    • Varki, A.1
  • 92
    • 84891777645 scopus 로고    scopus 로고
    • A platform to screen for C-type lectin receptor-binding carbohydrates and their potential for cell-specific targeting and immune modulation
    • Maglinao M, Eriksson M, Schlegel MK, Zimmermann S, Johannssen T, et al. 2014. A platform to screen for C-type lectin receptor-binding carbohydrates and their potential for cell-specific targeting and immune modulation. J. Control. Release 175:36-42
    • (2014) J. Control. Release , vol.175 , pp. 36-42
    • Maglinao, M.1    Eriksson, M.2    Schlegel, M.K.3    Zimmermann, S.4    Johannssen, T.5
  • 93
    • 33745988599 scopus 로고    scopus 로고
    • Widely divergent biochemical properties of the complete set of mouse DC-SIGN-related proteins
    • Powlesland AS, Ward EM, Sadhu SK, Guo Y, Taylor ME, Drickamer K. 2006. Widely divergent biochemical properties of the complete set of mouse DC-SIGN-related proteins. J. Biol. Chem. 281(29):20440-49
    • (2006) J. Biol. Chem. , vol.281 , Issue.29 , pp. 20440-20449
    • Powlesland, A.S.1    Ward, E.M.2    Sadhu, S.K.3    Guo, Y.4    Taylor, M.E.5    Drickamer, K.6
  • 94
    • 84921786419 scopus 로고    scopus 로고
    • Siglec-mediated regulation of immune cell function in disease
    • Macauley MS, Crocker PR, Paulson JC. 2014. Siglec-mediated regulation of immune cell function in disease. Nat. Rev. Immunol. 14(10):653-66
    • (2014) Nat. Rev. Immunol. , vol.14 , Issue.10 , pp. 653-666
    • Macauley, M.S.1    Crocker, P.R.2    Paulson, J.C.3
  • 95
    • 33745171425 scopus 로고    scopus 로고
    • The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa
    • Diggle SP, Stacey RE, Dodd C, CamaraM,Williams P,Winzer K. 2006. The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa. Environ. Microbiol. 8(6):1095-104
    • (2006) Environ. Microbiol. , vol.8 , Issue.6 , pp. 1095-1104
    • Diggle, S.P.1    Stacey, R.E.2    Dodd, C.3    Camara, M.4    Williams, P.5    Winzer, K.6
  • 96
    • 53149111089 scopus 로고    scopus 로고
    • Structural basis of the preferential binding for Globo-series glycosphingolipids displayed by Pseudomonas aeruginosa lectin i
    • Blanchard B, Nurisso A, Hollville E, Tétaud C,Wiels J, et al. 2008. Structural basis of the preferential binding for Globo-series glycosphingolipids displayed by Pseudomonas aeruginosa lectin I. J. Mol. Biol. 383(4):837-53
    • (2008) J. Mol. Biol. , vol.383 , Issue.4 , pp. 837-853
    • Blanchard, B.1    Nurisso, A.2    Hollville, E.3    Tétaud, C.4    Wiels, J.5
  • 97
    • 42449095600 scopus 로고    scopus 로고
    • Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia
    • Lameignere E, MalinovskáL, SlávikováM,Duchaud E, Mitchell EP, et al. 2008. Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia. Biochem. J. 411(2):307
    • (2008) Biochem. J. , vol.411 , Issue.2 , pp. 307
    • Lameignere, E.1    Malinovskál2    Slávikovám3    Duchaud, E.4    Mitchell, E.P.5
  • 98
    • 84874418889 scopus 로고    scopus 로고
    • Staphylococcus aureus virulence factors in evasion from innate immune defenses in human and animal diseases
    • Zecconi A, Scali F. 2013. Staphylococcus aureus virulence factors in evasion from innate immune defenses in human and animal diseases. Immunol. Lett. 150(1-2):12-22
    • (2013) Immunol. Lett. , vol.150 , Issue.1-2 , pp. 12-22
    • Zecconi, A.1    Scali, F.2
  • 100
    • 79955728776 scopus 로고    scopus 로고
    • GPVI andGPIbαmediate staphylococcal superantigen-like protein 5 (SSL5) induced platelet activation and direct toward glycans as potential inhibitors
    • Hu H, Armstrong PCJ, Khalil E, Chen Y, Straub A, et al. 2011. GPVI andGPIbαmediate staphylococcal superantigen-like protein 5 (SSL5) induced platelet activation and direct toward glycans as potential inhibitors. PLOS ONE 6(4):e19190
    • (2011) PLOS ONE , vol.6 , Issue.4 , pp. e19190
    • Hu, H.1    Armstrong, P.C.J.2    Khalil, E.3    Chen, Y.4    Straub, A.5
  • 101
    • 36248995861 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition
    • Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD. 2007. The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol. Microbiol. 66(6):1342-55
    • (2007) Mol. Microbiol. , vol.66 , Issue.6 , pp. 1342-1355
    • Chung, M.C.1    Wines, B.D.2    Baker, H.3    Langley, R.J.4    Baker, E.N.5    Fraser, J.D.6
  • 102
    • 70449421592 scopus 로고    scopus 로고
    • Staphylococcal superantigen-like 5 activates platelets and supports platelet adhesion under flow conditions, which involves glycoprotein Ibαand αiIbβ3
    • de Haas CJC, Weeterings C, Vughs MM, de Groot PG, Van Strijp JA, Lisman T. 2009. Staphylococcal superantigen-like 5 activates platelets and supports platelet adhesion under flow conditions, which involves glycoprotein Ibαand αIIbβ3. J. Thromb. Haemost. 7(11):1867-74
    • (2009) J. Thromb. Haemost. , vol.7 , Issue.11 , pp. 1867-1874
    • De Haas, C.J.C.1    Weeterings, C.2    Vughs, M.M.3    De Groot, P.G.4    Van Strijp, J.A.5    Lisman, T.6
  • 103
    • 57349192094 scopus 로고    scopus 로고
    • Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin
    • Byres E, Paton AW, Paton JC, Löfling JC, Smith DF, et al. 2008. Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin. Nature 456(7222):648-52
    • (2008) Nature , vol.456 , Issue.7222 , pp. 648-652
    • Byres, E.1    Paton, A.W.2    Paton, J.C.3    Löfling, J.C.4    Smith, D.F.5
  • 105
    • 0020520729 scopus 로고
    • Receptor determinants of human and animal influenza virus isolates: Differences in receptor specificity of theH3hemagglutinin based on species of origin
    • Rogers GN, Paulson JC. 1983. Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of theH3hemagglutinin based on species of origin. Virology 127(2):361-73
    • (1983) Virology , vol.127 , Issue.2 , pp. 361-373
    • Rogers, G.N.1    Paulson, J.C.2
  • 106
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • Stevens J, Blixt O, Glaser L, Taubenberger JK, Palese P, et al. 2006. Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J. Mol. Biol. 355(5):1143-55
    • (2006) J. Mol. Biol. , vol.355 , Issue.5 , pp. 1143-1155
    • Stevens, J.1    Blixt, O.2    Glaser, L.3    Taubenberger, J.K.4    Palese, P.5
  • 107
    • 44949184685 scopus 로고    scopus 로고
    • Contemporary North American influenza H7 viruses possess human receptor specificity: Implications for virus transmissibility
    • Belser JA, Blixt O, Chen L, Pappas C, Maines TR, et al. 2008. Contemporary North American influenza H7 viruses possess human receptor specificity: implications for virus transmissibility. PNAS 105(21):7558-63
    • (2008) PNAS , vol.105 , Issue.21 , pp. 7558-7563
    • Belser, J.A.1    Blixt, O.2    Chen, L.3    Pappas, C.4    Maines, T.R.5
  • 108
    • 70249103855 scopus 로고    scopus 로고
    • Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray
    • Childs RA, Palma AS, Wharton S, Matrosovich T, Liu Y, et al. 2009. Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray. Nat. Biotechnol. 27(9):797-99
    • (2009) Nat. Biotechnol. , vol.27 , Issue.9 , pp. 797-799
    • Childs, R.A.1    Palma, A.S.2    Wharton, S.3    Matrosovich, T.4    Liu, Y.5
  • 109
    • 78049516347 scopus 로고    scopus 로고
    • Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus
    • Liu Y, Childs RA, Matrosovich T, Wharton S, Palma AS, et al. 2010. Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus. J. Virol. 84(22):12069-74
    • (2010) J. Virol. , vol.84 , Issue.22 , pp. 12069-12074
    • Liu, Y.1    Childs, R.A.2    Matrosovich, T.3    Wharton, S.4    Palma, A.S.5
  • 110
    • 79954632833 scopus 로고    scopus 로고
    • Comparison of the receptor binding properties of contemporary swine isolates and early human pandemicH1N1 isolates (novel 2009 H1N1)
    • Bradley KC, Jones CA, Tompkins SM, Tripp RA, Russell RJ, et al. 2011. Comparison of the receptor binding properties of contemporary swine isolates and early human pandemicH1N1 isolates (novel 2009 H1N1). Virology 413(2):169-82
    • (2011) Virology , vol.413 , Issue.2 , pp. 169-182
    • Bradley, K.C.1    Jones, C.A.2    Tompkins, S.M.3    Tripp, R.A.4    Russell, R.J.5
  • 111
    • 48749093648 scopus 로고    scopus 로고
    • Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity
    • Stevens J, Blixt O, Chen L, Donis RO, Paulson JC, Wilson IA. 2008. Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity. J. Mol. Biol. 381(5):1382-94
    • (2008) J. Mol. Biol. , vol.381 , Issue.5 , pp. 1382-1394
    • Stevens, J.1    Blixt, O.2    Chen, L.3    Donis, R.O.4    Paulson, J.C.5    Wilson, I.A.6
  • 112
    • 84886397294 scopus 로고    scopus 로고
    • Changes in the hemagglutinin of H5N1 viruses during human infection-influence on receptor binding
    • Crusat M, Liu J, Palma AS, Childs RA, Liu Y, et al. 2013. Changes in the hemagglutinin of H5N1 viruses during human infection-influence on receptor binding. Virology 447(1-2):326-37
    • (2013) Virology , vol.447 , Issue.1-2 , pp. 326-337
    • Crusat, M.1    Liu, J.2    Palma, A.S.3    Childs, R.A.4    Liu, Y.5
  • 113
    • 84890875708 scopus 로고    scopus 로고
    • Hemagglutinin receptor specificity and structural analyses of respiratory droplet transmissible H5N1 viruses
    • de Vries RP, Zhu X, McBride R, Rigter A, Hanson A, et al. 2014. Hemagglutinin receptor specificity and structural analyses of respiratory droplet transmissible H5N1 viruses. J. Virol. 88(1):768-73
    • (2014) J. Virol. , vol.88 , Issue.1 , pp. 768-773
    • De Vries, R.P.1    Zhu, X.2    McBride, R.3    Rigter, A.4    Hanson, A.5
  • 114
    • 84896142710 scopus 로고    scopus 로고
    • Characterization of the sialic acid binding activity of influenza A viruses using soluble variants of the H7 and H9 hemagglutinins
    • Sauer A, Liang C, Stech J, Peeters B, Quéré P, et al. 2014. Characterization of the sialic acid binding activity of influenza A viruses using soluble variants of the H7 and H9 hemagglutinins. PLOS ONE 9(2):e89529
    • (2014) PLOS ONE , vol.9 , Issue.2 , pp. e89529
    • Sauer, A.1    Liang, C.2    Stech, J.3    Peeters, B.4    Quéré, P.5
  • 115
    • 84926647098 scopus 로고    scopus 로고
    • Mammalian adaptation of influenza A(H7N9) virus is limited by a narrow genetic bottleneck
    • ZaraketH, Baranovich T, Kaplan BS, Carter R, SongM, et al. 2015. Mammalian adaptation of influenza A(H7N9) virus is limited by a narrow genetic bottleneck. Nat. Commun. 6:6553
    • (2015) Nat. Commun. , vol.6 , pp. 6553
    • Zaraket, H.1    Baranovich, T.2    Kaplan, B.S.3    Carter, R.4    Song, M.5
  • 116
    • 84926225986 scopus 로고    scopus 로고
    • A human-infecting H10N8 influenza virus retains a strong preference for avian-type receptors
    • ZhangH, de Vries RP, Tzarum N, Zhu X, YuW, et al. 2015. A human-infecting H10N8 influenza virus retains a strong preference for avian-type receptors. Cell Host Microbe 17(3):377-84
    • (2015) Cell Host Microbe , vol.17 , Issue.3 , pp. 377-384
    • Zhang, H.1    De Vries, R.P.2    Tzarum, N.3    Zhu, X.4    Yu, W.5
  • 117
    • 84875992488 scopus 로고    scopus 로고
    • Glycomic analysis of human respiratory tract tissues and correlation with influenza virus infection
    • Walther T, Karamanska R, Chan RWY, Chan MCW, Jia N, et al. 2013. Glycomic analysis of human respiratory tract tissues and correlation with influenza virus infection. PLOS Pathog. 9(3):e1003223
    • (2013) PLOS Pathog. , vol.9 , Issue.3 , pp. e1003223
    • Walther, T.1    Karamanska, R.2    Chan, R.W.Y.3    Chan, M.C.W.4    Jia, N.5
  • 118
    • 81255214348 scopus 로고    scopus 로고
    • Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein
    • Alymova IV, Portner A,MishinVP, McCullers JA, Freiden P,Taylor GL. 2012. Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein. Glycobiology 22(2):174-80
    • (2012) Glycobiology , vol.22 , Issue.2 , pp. 174-180
    • Alymova, I.V.1    Portner, A.2    Mishin, V.P.3    McCullers, J.A.4    Freiden, P.5    Taylor, G.L.6
  • 119
    • 34547114495 scopus 로고    scopus 로고
    • Human parainfluenza viruses hPIV1 and hPIV3 bind oligosaccharides with α2-3-linked sialic acids that are distinct from those bound by H5 avian influenza virus hemagglutinin
    • Amonsen M, SmithDF, Cummings RD, AirGM. 2007. Human parainfluenza viruses hPIV1 and hPIV3 bind oligosaccharides with α2-3-linked sialic acids that are distinct from those bound by H5 avian influenza virus hemagglutinin. J. Virol. 81(15):8341-45
    • (2007) J. Virol. , vol.81 , Issue.15 , pp. 8341-8345
    • Amonsen, M.1    Smith, D.F.2    Cummings, R.D.3    Air, G.M.4
  • 120
    • 84896730363 scopus 로고    scopus 로고
    • Differential adeno-associated virus serotype-specific interaction patternswith synthetic heparins and other glycans
    • Mietzsch M, Broecker F, Reinhardt A, Seeberger PH, Heilbronn R. 2014. Differential adeno-associated virus serotype-specific interaction patternswith synthetic heparins and other glycans. J. Virol. 88(5):2991-3003
    • (2014) J. Virol. , vol.88 , Issue.5 , pp. 2991-3003
    • Mietzsch, M.1    Broecker, F.2    Reinhardt, A.3    Seeberger, P.H.4    Heilbronn, R.5
  • 121
    • 84939159972 scopus 로고    scopus 로고
    • Structural hot spots determine functional diversity of the Candida glabrata epithelial adhesin family
    • Diderrich R, Kock M, Maestre-ReynaM,Keller P, SteuberH, et al. 2015. Structural hot spots determine functional diversity of the Candida glabrata epithelial adhesin family. J. Biol. Chem. 290(32):19597-613
    • (2015) J. Biol. Chem. , vol.290 , Issue.32 , pp. 19597-19613
    • Diderrich, R.1    Kock, M.2    Maestre-Reyna, M.3    Keller, P.4    Steuber, H.5
  • 122
    • 84901833162 scopus 로고    scopus 로고
    • Glycan microarrays: Powerful tools for biomarker discovery
    • Muthana SM, Gildersleeve JC. 2014. Glycan microarrays: powerful tools for biomarker discovery. Cancer Biomark. 14(1):29-41
    • (2014) Cancer Biomark. , vol.14 , Issue.1 , pp. 29-41
    • Muthana, S.M.1    Gildersleeve, J.C.2
  • 123
    • 84927668143 scopus 로고    scopus 로고
    • Natural antibody repertoires: Development and functional role in inhibiting allergic airway disease
    • Kearney JF, Patel P, Stefanov EK, King RG. 2015. Natural antibody repertoires: development and functional role in inhibiting allergic airway disease. Annu. Rev. Immunol. 33(1):475-504
    • (2015) Annu. Rev. Immunol. , vol.33 , Issue.1 , pp. 475-504
    • Kearney, J.F.1    Patel, P.2    Stefanov, E.K.3    King, R.G.4
  • 124
    • 68749104303 scopus 로고    scopus 로고
    • Anti-carbohydrate antibodies of normal sera: Findings, surprises and challenges
    • Huflejt ME, Vuskovic M, Vasiliu D, Xu H, Obukhova P, et al. 2009. Anti-carbohydrate antibodies of normal sera: findings, surprises and challenges. Mol. Immunol. 46(15):3037-49
    • (2009) Mol. Immunol. , vol.46 , Issue.15 , pp. 3037-3049
    • Huflejt, M.E.1    Vuskovic, M.2    Vasiliu, D.3    Xu, H.4    Obukhova, P.5
  • 125
    • 84892633304 scopus 로고    scopus 로고
    • Chemical biology approaches to designing defined carbohydrate vaccines
    • Anish C, Schumann B, Pereira CL, Seeberger PH. 2014. Chemical biology approaches to designing defined carbohydrate vaccines. Chem. Biol. 21(1):38-50
    • (2014) Chem. Biol. , vol.21 , Issue.1 , pp. 38-50
    • Anish, C.1    Schumann, B.2    Pereira, C.L.3    Seeberger, P.H.4
  • 126
    • 84882791693 scopus 로고    scopus 로고
    • Recent mechanistic insights on glycoconjugate vaccines and future perspectives
    • Berti F, Adamo R. 2013. Recent mechanistic insights on glycoconjugate vaccines and future perspectives. ACS Chem. Biol. 8(8):1653-63
    • (2013) ACS Chem. Biol. , vol.8 , Issue.8 , pp. 1653-1663
    • Berti, F.1    Adamo, R.2
  • 127
    • 84959328955 scopus 로고    scopus 로고
    • Deciphering antigenic determinants of Streptococcus pneumoniae serotype 4 capsular polysaccharide using synthetic oligosaccharides
    • Geissner A, Pereira CL, Leddermann M, Anish C, Seeberger PH. 2016. Deciphering antigenic determinants of Streptococcus pneumoniae serotype 4 capsular polysaccharide using synthetic oligosaccharides. ACS Chem. Biol. 11(2)335-44
    • (2016) ACS Chem. Biol. , vol.11 , Issue.2 , pp. 35-44
    • Geissner, A.1    Pereira, C.L.2    Leddermann, M.3    Anish, C.4    Seeberger, P.H.5
  • 128
    • 84973402346 scopus 로고    scopus 로고
    • Multivalent display of minimal Clostridium difficile glycan epitopes mimics antigenic properties of larger glycans
    • Broecker F, Hanske J, Martin CE, Baek JY, Wahlbrink A, et al. 2016. Multivalent display of minimal Clostridium difficile glycan epitopes mimics antigenic properties of larger glycans. Nat. Commun. 7:11224
    • (2016) Nat. Commun. , vol.7 , pp. 11224
    • Broecker, F.1    Hanske, J.2    Martin, C.E.3    Baek, J.Y.4    Wahlbrink, A.5
  • 131
    • 84873714203 scopus 로고    scopus 로고
    • Carbohydrate-based vaccines with a glycolipid adjuvant for breast cancer
    • Huang YL, Hung JT, Cheung SK, Lee HY, Chu KC, et al. 2013. Carbohydrate-based vaccines with a glycolipid adjuvant for breast cancer. PNAS 110(7):2517-22
    • (2013) PNAS , vol.110 , Issue.7 , pp. 2517-2522
    • Huang, Y.L.1    Hung, J.T.2    Cheung, S.K.3    Lee, H.Y.4    Chu, K.C.5
  • 132
    • 76749087478 scopus 로고    scopus 로고
    • Cancer biomarkers defined by autoantibody signatures to aberrant O-glycopeptide epitopes
    • Wandall HH, Blixt O, Tarp MA, Pedersen JW, Bennett EP, et al. 2010. Cancer biomarkers defined by autoantibody signatures to aberrant O-glycopeptide epitopes. Cancer Res. 70(4):1306-13
    • (2010) Cancer Res. , vol.70 , Issue.4 , pp. 1306-1313
    • Wandall, H.H.1    Blixt, O.2    Tarp, M.A.3    Pedersen, J.W.4    Bennett, E.P.5
  • 133
    • 79951974583 scopus 로고    scopus 로고
    • Seromic profiling of colorectal cancer patients with novel glycopeptide microarray
    • Pedersen JW, Blixt O, Bennett EP, Tarp MA, Dar I, et al. 2011. Seromic profiling of colorectal cancer patients with novel glycopeptide microarray. Int. J. Cancer 128(8):1860-71
    • (2011) Int. J. Cancer , vol.128 , Issue.8 , pp. 1860-1871
    • Pedersen, J.W.1    Blixt, O.2    Bennett, E.P.3    Tarp, M.A.4    Dar, I.5
  • 134
    • 84896736154 scopus 로고    scopus 로고
    • Cancer-associated autoantibodies to MUC1 and MUC4-A blinded case-control study of colorectal cancer in UK collaborative trial of ovarian cancer screening
    • Pedersen JW, Gentry-Maharaj A, Nøstdal A, Fourkala E, Dawnay A, et al. 2014. Cancer-associated autoantibodies to MUC1 and MUC4-a blinded case-control study of colorectal cancer in UK collaborative trial of ovarian cancer screening. Int. J. Cancer 134(9):2180-88
    • (2014) Int. J. Cancer , vol.134 , Issue.9 , pp. 2180-2188
    • Pedersen, J.W.1    Gentry-Maharaj, A.2    Nøstdal, A.3    Fourkala, E.4    Dawnay, A.5
  • 135
    • 84900467152 scopus 로고    scopus 로고
    • Uncovering cryptic glycan markers inmultiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE)
    • Wang D, Bhat R, Sobel RA, HuangW,Wang L, et al. 2014. Uncovering cryptic glycan markers inmultiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). Drug Dev. Res. 75(3):172-88
    • (2014) Drug Dev. Res. , vol.75 , Issue.3 , pp. 172-188
    • Wang, D.1    Bhat, R.2    Sobel, R.A.3    Huang, W.4    Wang, L.5
  • 136
  • 137
    • 84928305375 scopus 로고    scopus 로고
    • Development of a Schistosoma mansoni shotgun O-glycan microarray and application to the discovery of new antigenic schistosome glycan motifs
    • van Diepen A, van der Plas AJ, Kozak RP, Royle L, Dunne DW, Hokke CH. 2015. Development of a Schistosoma mansoni shotgun O-glycan microarray and application to the discovery of new antigenic schistosome glycan motifs. Int. J. Parasitol. 45(7):465-75
    • (2015) Int. J. Parasitol. , vol.45 , Issue.7 , pp. 465-475
    • Van Diepen, A.1    Van Der Plas, A.J.2    Kozak, R.P.3    Royle, L.4    Dunne, D.W.5    Hokke, C.H.6
  • 138
    • 0037102205 scopus 로고    scopus 로고
    • Synthetic GPI as a candidate antitoxic vaccine in a model of malaria
    • Schofield L, Hewitt MC, Evans K, Siomos M, Seeberger PH. 2002. Synthetic GPI as a candidate antitoxic vaccine in a model of malaria. Nature 418(6899):785-89
    • (2002) Nature , vol.418 , Issue.6899 , pp. 785-789
    • Schofield, L.1    Hewitt, M.C.2    Evans, K.3    Siomos, M.4    Seeberger, P.H.5
  • 140
    • 84883010128 scopus 로고    scopus 로고
    • Synthesis of Neisseria meningitidis serogroup W135 capsular oligosaccharides for immunogenicity comparison and vaccine development
    • Wang C, Li S, Lin T, Cheng Y, Sun T, et al. 2013. Synthesis of Neisseria meningitidis serogroup W135 capsular oligosaccharides for immunogenicity comparison and vaccine development. Angew. Chem. Int. Ed. 52(35):9157-61
    • (2013) Angew. Chem. Int. Ed. , vol.52 , Issue.35 , pp. 9157-9161
    • Wang, C.1    Li, S.2    Lin, T.3    Cheng, Y.4    Sun, T.5
  • 141
    • 79957532830 scopus 로고    scopus 로고
    • A possible oligosaccharide-conjugate vaccine candidate for Clostridium difficile is antigenic and immunogenic
    • Oberli MA, Hecht M, Bindschädler P, Adibekian A, Adam T, Seeberger PH. 2011. A possible oligosaccharide-conjugate vaccine candidate for Clostridium difficile is antigenic and immunogenic. Chem. Biol. 18(5):580-88
    • (2011) Chem. Biol. , vol.18 , Issue.5 , pp. 580-588
    • Oberli, M.A.1    Hecht, M.2    Bindschädler, P.3    Adibekian, A.4    Adam, T.5    Seeberger, P.H.6
  • 142
    • 84879776854 scopus 로고    scopus 로고
    • Immunological evaluation of a synthetic Clostridium difficile oligosaccharide conjugate vaccine candidate and identification of a minimal epitope
    • Martin CE, Broecker F, Oberli MA, Komor J, Mattner J, et al. 2013. Immunological evaluation of a synthetic Clostridium difficile oligosaccharide conjugate vaccine candidate and identification of a minimal epitope. J. Am. Chem. Soc. 135(26):9713-22
    • (2013) J. Am. Chem. Soc. , vol.135 , Issue.26 , pp. 9713-9722
    • Martin, C.E.1    Broecker, F.2    Oberli, M.A.3    Komor, J.4    Mattner, J.5
  • 143
    • 84897019003 scopus 로고    scopus 로고
    • HIV-1 envelope-receptor interactions required for macrophage infection and implications for current HIV-1 cure strategies
    • Gorry PR, Francella N, Lewin SR, Collman RG. 2014. HIV-1 envelope-receptor interactions required for macrophage infection and implications for current HIV-1 cure strategies. J. Leukoc. Biol. 95(1):71-81
    • (2014) J. Leukoc. Biol. , vol.95 , Issue.1 , pp. 71-81
    • Gorry, P.R.1    Francella, N.2    Lewin, S.R.3    Collman, R.G.4
  • 144
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, Huber M, Doores KJ, Falkowska E, Pejchal R, et al. 2011. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477(7365):466-70
    • (2011) Nature , vol.477 , Issue.7365 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3    Falkowska, E.4    Pejchal, R.5
  • 145
    • 84869831194 scopus 로고    scopus 로고
    • Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies
    • Mouquet H, Scharf L, Euler Z, Liu Y, Eden C, et al. 2012. Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies. PNAS 109(47):E3268
    • (2012) PNAS , vol.109 , Issue.47 , pp. E3268
    • Mouquet, H.1    Scharf, L.2    Euler, Z.3    Liu, Y.4    Eden, C.5
  • 146
    • 84878519611 scopus 로고    scopus 로고
    • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans
    • Julien J, Sok D, Khayat R, Lee JH, Doores KJ, et al. 2013. Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans. PLOS Pathog. 9(5):e1003342
    • (2013) PLOS Pathog. , vol.9 , Issue.5 , pp. e1003342
    • Julien, J.1    Sok, D.2    Khayat, R.3    Lee, J.H.4    Doores, K.J.5
  • 147
    • 84907548228 scopus 로고    scopus 로고
    • Pectic-β(1,4)-galactan, extensin and arabinogalactan-protein epitopes differentiate ripening stages in wine and table grape cell walls
    • Moore JP, Fangel JU, Willats WGT, Vivier MA. 2014. Pectic-β(1,4)-galactan, extensin and arabinogalactan-protein epitopes differentiate ripening stages in wine and table grape cell walls. Ann. Bot. 114(6):1279-94
    • (2014) Ann. Bot. , vol.114 , Issue.6 , pp. 1279-1294
    • Moore, J.P.1    Fangel, J.U.2    Willats, W.G.T.3    Vivier, M.A.4
  • 148
    • 84925003047 scopus 로고    scopus 로고
    • Following the compositional changes of fresh grape skin cell walls during the fermentation process in the presence and absence of maceration enzymes
    • Zietsman AJJ, Moore JP, Fangel JU, WillatsWGT, Trygg J, VivierMA. 2015. Following the compositional changes of fresh grape skin cell walls during the fermentation process in the presence and absence of maceration enzymes. J. Agric. Food Chem. 63(10):2798-810
    • (2015) J. Agric. Food Chem. , vol.63 , Issue.10 , pp. 2798-2810
    • Zietsman, A.J.J.1    Moore, J.P.2    Fangel, J.U.3    Willats, W.G.T.4    Trygg, J.5    Vivier, M.A.6
  • 149
    • 84919483188 scopus 로고    scopus 로고
    • Non-cellulosic polysaccharides from cotton fibre are differently impacted by textile processing
    • Runavot J, Guo X, Willats WGT, Knox JP, Goubet F, Meulewaeter F. 2014. Non-cellulosic polysaccharides from cotton fibre are differently impacted by textile processing. PLOS ONE 9(12):e115150
    • (2014) PLOS ONE , vol.9 , Issue.12 , pp. e115150
    • Runavot, J.1    Guo, X.2    Willats, W.G.T.3    Knox, J.P.4    Goubet, F.5    Meulewaeter, F.6
  • 150
    • 84925389893 scopus 로고    scopus 로고
    • Automated synthesis of arabinoxylan-oligosaccharides enables characterization of antibodies that recognize plant cell wall glycans
    • Schmidt D, Schuhmacher F, Geissner A, Seeberger PH, Pfrengle F. 2015. Automated synthesis of arabinoxylan-oligosaccharides enables characterization of antibodies that recognize plant cell wall glycans. Chem. Eur. J. 21(15):5709-13
    • (2015) Chem. Eur. J. , vol.21 , Issue.15 , pp. 5709-5713
    • Schmidt, D.1    Schuhmacher, F.2    Geissner, A.3    Seeberger, P.H.4    Pfrengle, F.5
  • 151
    • 33846564998 scopus 로고    scopus 로고
    • Photogenerated glycan arrays identify immunogenic sugar moieties of Bacillus anthracis exosporium
    • Wang D, Carroll GT, Turro NJ, Koberstein JT, Kovác P, et al. 2007. Photogenerated glycan arrays identify immunogenic sugar moieties of Bacillus anthracis exosporium. Proteomics 7(2):180-84
    • (2007) Proteomics , vol.7 , Issue.2 , pp. 180-184
    • Wang, D.1    Carroll, G.T.2    Turro, N.J.3    Koberstein, J.T.4    Kovác, P.5
  • 152
    • 77949885066 scopus 로고    scopus 로고
    • Dual specificity of langerin to sulfated and mannosylated glycans via a single C-type carbohydrate recognition domain
    • Tateno H, Ohnishi K, Yabe R,Hayatsu N, Sato T, et al. 2010. Dual specificity of langerin to sulfated and mannosylated glycans via a single C-type carbohydrate recognition domain. J. Biol. Chem. 285(9):6390-400
    • (2010) J. Biol. Chem. , vol.285 , Issue.9 , pp. 6390-6400
    • Tateno, H.1    Ohnishi, K.2    Yabe, R.3    Hayatsu, N.4    Sato, T.5
  • 153
    • 84862911453 scopus 로고    scopus 로고
    • Human ZG16p recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system
    • Tateno H, Yabe R, Sato T, Shibazaki A, Shikanai T, et al. 2012. Human ZG16p recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system. Glycobiology 22(2):210-20
    • (2012) Glycobiology , vol.22 , Issue.2 , pp. 210-220
    • Tateno, H.1    Yabe, R.2    Sato, T.3    Shibazaki, A.4    Shikanai, T.5
  • 154
    • 79952451633 scopus 로고    scopus 로고
    • An expression system for screening of proteins for glycan and protein interactions
    • Otto DM, Campanero-Rhodes MA, Karamanska R, Powell AK, Bovin N, et al. 2011. An expression system for screening of proteins for glycan and protein interactions. Anal. Biochem. 411(2):261-70
    • (2011) Anal. Biochem. , vol.411 , Issue.2 , pp. 261-270
    • Otto, D.M.1    Campanero-Rhodes, M.A.2    Karamanska, R.3    Powell, A.K.4    Bovin, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.