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Volumn 21, Issue 5, 2016, Pages

Multivalent carbohydrate-lectin interactions: How synthetic chemistry enables insights into nanometric recognition

Author keywords

Agglutinin; Galectin; Glycocluster; Glycodendrimer; Glycophane; Glycoprotein; Liposomes; Oligosaccharides; Sugar code

Indexed keywords

CARBOHYDRATE; DENDRIMER; GALECTIN; GLYCOPROTEIN; POLYSACCHARIDE;

EID: 84973923068     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules21050629     Document Type: Review
Times cited : (59)

References (147)
  • 2
    • 0032953692 scopus 로고    scopus 로고
    • Eukaryotic glycosylation: Whim of nature or multipurpose tool?
    • Reuter, G.; Gabius, H.-J. Eukaryotic glycosylation: Whim of nature or multipurpose tool? Cell. Mol. Life Sci. 1999, 55, 368-422.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 368-422
    • Reuter, G.1    Gabius, H.-J.2
  • 3
    • 72249117511 scopus 로고    scopus 로고
    • N-Glycosylation
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Zuber, C.; Roth, J. N-Glycosylation. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 87-110.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 87-110
    • Zuber, C.1    Roth, J.2
  • 4
    • 77953778927 scopus 로고    scopus 로고
    • O-Glycosylation: Structural diversity and function
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Patsos, G.; Corfield, A. O-Glycosylation: Structural diversity and function. In The Sugar Code. Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 111-137.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 111-137
    • Patsos, G.1    Corfield, A.2
  • 5
    • 77953755681 scopus 로고    scopus 로고
    • Glycolipids
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Kopitz, J. Glycolipids. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 177-198.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 177-198
    • Kopitz, J.1
  • 6
    • 79958032980 scopus 로고    scopus 로고
    • Proteoglycans
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Buddecke, E. Proteoglycans. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 199-216.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 199-216
    • Buddecke, E.1
  • 7
    • 79958047641 scopus 로고    scopus 로고
    • Chitin: Structure, function and metabolism
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Merzendorfer, H. Chitin: Structure, function and metabolism. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 217-229.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 217-229
    • Merzendorfer, H.1
  • 8
    • 84930822109 scopus 로고    scopus 로고
    • Glycan variation and evolution in the eukaryotes
    • Corfield, A.P.; Berry, M. Glycan variation and evolution in the eukaryotes. Trends Biochem. Sci. 2015, 40, 351-359.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 351-359
    • Corfield, A.P.1    Berry, M.2
  • 10
    • 84930822983 scopus 로고    scopus 로고
    • The multi-tasked life of GM1 ganglioside, a true factotum of nature
    • Ledeen, R.W.; Wu, G. The multi-tasked life of GM1 ganglioside, a true factotum of nature. Trends Biochem. Sci. 2015, 40, 407-418.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 407-418
    • Ledeen, R.W.1    Wu, G.2
  • 11
    • 84930819900 scopus 로고    scopus 로고
    • Gangliosides: Glycosphingolipids essential for normal neural development and function
    • Schengrund, C.-L. Gangliosides: Glycosphingolipids essential for normal neural development and function. Trends Biochem. Sci. 2015, 40, 397-406.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 397-406
    • Schengrund, C.-L.1
  • 12
    • 84946606174 scopus 로고    scopus 로고
    • Do plant cell walls have a code?
    • Tavares, E.Q.; Buckeridge, M.S. Do plant cell walls have a code? Plant Sci. 2015, 241, 286-294.
    • (2015) Plant Sci. , vol.241 , pp. 286-294
    • Tavares, E.Q.1    Buckeridge, M.S.2
  • 13
    • 84930818143 scopus 로고    scopus 로고
    • Sugar coating: Bacterial protein glycosylation and host-microbe interactions
    • Tan, F.Y.; Tang, C.M.; Exley, R.M. Sugar coating: Bacterial protein glycosylation and host-microbe interactions. Trends Biochem. Sci. 2015, 40, 342-350.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 342-350
    • Tan, F.Y.1    Tang, C.M.2    Exley, R.M.3
  • 14
    • 0015521532 scopus 로고
    • The significance of glycosylated proteins
    • Winterburn, P.J.; Phelps, C.F. The significance of glycosylated proteins. Nature 1972, 236, 147-151.
    • (1972) Nature , vol.236 , pp. 147-151
    • Winterburn, P.J.1    Phelps, C.F.2
  • 15
    • 77149173217 scopus 로고    scopus 로고
    • The biochemical basis and coding capacity of the sugar code
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Rüdiger, H.; Gabius, H.-J. The biochemical basis and coding capacity of the sugar code. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 3-13.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 3-13
    • Rüdiger, H.1    Gabius, H.-J.2
  • 17
    • 77956661991 scopus 로고
    • The history of glycoprotein research, a personal view
    • Montreuil, J., Vliegenthart, J.F.G., Schachter, H., Eds.; Elsevier: Amsterdam, The Netherlands
    • Montreuil, J. The history of glycoprotein research, a personal view. In Glycoproteins; Montreuil, J., Vliegenthart, J.F.G., Schachter, H., Eds.; Elsevier: Amsterdam, The Netherlands, 1995; pp. 1-12.
    • (1995) Glycoproteins , pp. 1-12
    • Montreuil, J.1
  • 18
    • 0000149999 scopus 로고
    • Molecular modeling: An essential component in the structure determination of oligosaccharides and polysaccharides
    • Pérez, S.; Imberty, A.; Carver, J.P. Molecular modeling: An essential component in the structure determination of oligosaccharides and polysaccharides. Adv. Comput. Biol. 1994, 1, 147-202.
    • (1994) Adv. Comput. Biol. , vol.1 , pp. 147-202
    • Pérez, S.1    Imberty, A.2    Carver, J.P.3
  • 20
    • 0032985340 scopus 로고    scopus 로고
    • Structure and conformation of complex carbohydrates of glycoproteins, glycolipids, and bacterial polysaccharides
    • Bush, C.A.; Martin-Pastor, M.; Imberty, A. Structure and conformation of complex carbohydrates of glycoproteins, glycolipids, and bacterial polysaccharides. Annu. Rev. Biophys. Biomol. Struct. 1999, 28, 269-293.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 269-293
    • Bush, C.A.1    Martin-Pastor, M.2    Imberty, A.3
  • 21
    • 0037681028 scopus 로고    scopus 로고
    • Structure, conformation, and dynamics of bioactive oligosaccharides: Theoretical approaches and experimental validations
    • Imberty, A.; Pérez, S. Structure, conformation, and dynamics of bioactive oligosaccharides: Theoretical approaches and experimental validations. Chem. Rev. 2000, 100, 4567-4588.
    • (2000) Chem. Rev. , vol.100 , pp. 4567-4588
    • Imberty, A.1    Pérez, S.2
  • 22
    • 68149131940 scopus 로고    scopus 로고
    • From structural to functional glycomics: Core substitutions as molecular switches for shape and lectin affinity of N-glycans
    • André, S.; Kozár, T.; Kojima, S.; Unverzagt, C.; Gabius, H.-J. From structural to functional glycomics: Core substitutions as molecular switches for shape and lectin affinity of N-glycans. Biol. Chem. 2009, 390, 557-565.
    • (2009) Biol. Chem. , vol.390 , pp. 557-565
    • André, S.1    Kozár, T.2    Kojima, S.3    Unverzagt, C.4    Gabius, H.-J.5
  • 23
    • 84876782219 scopus 로고    scopus 로고
    • The third dimension of reading the sugar code by lectins: Design of glycoclusters with cyclic scaffolds as tools with the aim to define correlations between spatial presentation and activity
    • Murphy, P.V.; André, S.; Gabius, H.-J. The third dimension of reading the sugar code by lectins: Design of glycoclusters with cyclic scaffolds as tools with the aim to define correlations between spatial presentation and activity. Molecules 2013, 18, 4026-4053.
    • (2013) Molecules , vol.18 , pp. 4026-4053
    • Murphy, P.V.1    André, S.2    Gabius, H.-J.3
  • 24
  • 25
    • 0024159311 scopus 로고
    • Bifunctional properties of lectins: Lectins redefined
    • Barondes, S.H. Bifunctional properties of lectins: Lectins redefined. Trends Biochem. Sci. 1988, 13, 480-482.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 480-482
    • Barondes, S.H.1
  • 27
    • 0022555847 scopus 로고
    • Carbohydrate-binding proteins: Tertiary structures and protein-sugar interactions
    • Quiocho, F.A. Carbohydrate-binding proteins: Tertiary structures and protein-sugar interactions. Annu. Rev. Biochem. 1986, 55, 287-315.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 287-315
    • Quiocho, F.A.1
  • 30
    • 84930820197 scopus 로고    scopus 로고
    • The glycobiology of the CD system: A dictionary for translating marker designations into glycan/lectin structure and function
    • Gabius, H.-J.; Kaltner, H.; Kopitz, J.; André, S. The glycobiology of the CD system: A dictionary for translating marker designations into glycan/lectin structure and function. Trends Biochem. Sci. 2015, 40, 360-376.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 360-376
    • Gabius, H.-J.1    Kaltner, H.2    Kopitz, J.3    André, S.4
  • 31
    • 84860251714 scopus 로고    scopus 로고
    • Beyond glycoproteins as galectin counterreceptors: Tumor/effector T cell growth control via ganglioside GM1
    • Ledeen, R.W.; Wu, G.; André, S.; Bleich, D.; Huet, G.; Kaltner, H.; Kopitz, J.; Gabius, H.-J. Beyond glycoproteins as galectin counterreceptors: Tumor/effector T cell growth control via ganglioside GM1. Ann. N. Y. Acad. Sci. 2012, 1253, 206-221.
    • (2012) Ann. N. Y. Acad. Sci. , vol.1253 , pp. 206-221
    • Ledeen, R.W.1    Wu, G.2    André, S.3    Bleich, D.4    Huet, G.5    Kaltner, H.6    Kopitz, J.7    Gabius, H.-J.8
  • 34
    • 84867580385 scopus 로고    scopus 로고
    • INK4a: Anoikis-favoring decrease in N/O-glycan/cell surface sialylation by downregulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model
    • INK4a: Anoikis-favoring decrease in N/O-glycan/cell surface sialylation by downregulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model. FEBS J. 2012, 279, 4062-4080.
    • (2012) FEBS J , vol.279 , pp. 4062-4080
    • Amano, M.1    Eriksson, H.2    Manning, J.C.3    Detjen, K.M.4    André, S.5    Nishimura, S.-I.6    Lehtiö, J.7    Gabius, H.-J.8
  • 36
    • 15744367723 scopus 로고    scopus 로고
    • Thermodynamic, kinetic, and electron microscopy studies of concanavalin A and Dioclea grandiflora lectin cross-linked with synthetic divalent carbohydrates
    • Dam, T.K.; Oscarson, S.; Roy, R.; Das, S.K.; Page, D.; Macaluso, F.; Brewer, C.F. Thermodynamic, kinetic, and electron microscopy studies of concanavalin A and Dioclea grandiflora lectin cross-linked with synthetic divalent carbohydrates. J. Biol. Chem. 2005, 280, 8640-8646.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8640-8646
    • Dam, T.K.1    Oscarson, S.2    Roy, R.3    Das, S.K.4    Page, D.5    Macaluso, F.6    Brewer, C.F.7
  • 37
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • Dam, T.K.; Gabius, H.-J.; André, S.; Kaltner, H.; Lensch, M.; Brewer, C.F. Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry 2005, 44, 12564-12571.
    • (2005) Biochemistry , vol.44 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 38
    • 77955902749 scopus 로고    scopus 로고
    • Animal and human lectins
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Gabius, H.-J. Animal and human lectins. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 317-328.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 317-328
    • Gabius, H.-J.1
  • 39
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper, D.N.W. Galectinomics: Finding themes in complexity. Biochim. Biophys. Acta 2002, 1572, 209-231.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 40
    • 79955915952 scopus 로고    scopus 로고
    • Routes in lectin evolution: Case study on the C-type lectin-like domains
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Gready, J.N.; Zelensky, A.N. Routes in lectin evolution: Case study on the C-type lectin-like domains. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 329-346.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 329-346
    • Gready, J.N.1    Zelensky, A.N.2
  • 41
    • 78650001430 scopus 로고    scopus 로고
    • Evolution of CD33-related siglecs: Regulating host immune functions and escaping pathogen exploitation?
    • Cao, H.; Crocker, P.R. Evolution of CD33-related siglecs: Regulating host immune functions and escaping pathogen exploitation? Immunology 2011, 132, 18-26.
    • (2011) Immunology , vol.132 , pp. 18-26
    • Cao, H.1    Crocker, P.R.2
  • 43
    • 84857738686 scopus 로고    scopus 로고
    • A toolbox of lectins for translating the sugar code: The galectin network in phylogenesis and tumors
    • Kaltner, H.; Gabius, H.-J. A toolbox of lectins for translating the sugar code: The galectin network in phylogenesis and tumors. Histol. Histopathol. 2012, 27, 397-416.
    • (2012) Histol. Histopathol. , vol.27 , pp. 397-416
    • Kaltner, H.1    Gabius, H.-J.2
  • 44
    • 84887890030 scopus 로고    scopus 로고
    • Copy-number variation of functional galectin genes: Studying animal galectin-7 (p53-induced gene 1 in man) and tandem-repeat-type galectins-4 and -9
    • Kaltner, H.; Raschta, A.-S.; Manning, J.C.; Gabius, H.-J. Copy-number variation of functional galectin genes: Studying animal galectin-7 (p53-induced gene 1 in man) and tandem-repeat-type galectins-4 and -9. Glycobiology 2013, 23, 1152-1163.
    • (2013) Glycobiology , vol.23 , pp. 1152-1163
    • Kaltner, H.1    Raschta, A.-S.2    Manning, J.C.3    Gabius, H.-J.4
  • 45
    • 0021360008 scopus 로고
    • Soluble lectins: A new class of extracellular proteins
    • Barondes, S.H. Soluble lectins: A new class of extracellular proteins. Science 1984, 223, 1259-1264.
    • (1984) Science , vol.223 , pp. 1259-1264
    • Barondes, S.H.1
  • 46
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animal lectins that decipher glycocodes
    • Kasai, K.-I.; Hirabayashi, J. Galectins: A family of animal lectins that decipher glycocodes. J. Biochem. 1996, 119, 1-8.
    • (1996) J. Biochem. , vol.119 , pp. 1-8
    • Kasai, K.-I.1    Hirabayashi, J.2
  • 48
    • 84883302212 scopus 로고    scopus 로고
    • The growing galectin network in colon cancer and clinical relevance of cytoplasmic galectin-3 reactivity
    • Dawson, H.; André, S.; Karamitopoulou, E.; Zlobec, I.; Gabius, H.-J. The growing galectin network in colon cancer and clinical relevance of cytoplasmic galectin-3 reactivity. Anticancer Res. 2013, 33, 3053-3059.
    • (2013) Anticancer Res. , vol.33 , pp. 3053-3059
    • Dawson, H.1    André, S.2    Karamitopoulou, E.3    Zlobec, I.4    Gabius, H.-J.5
  • 49
    • 84917710465 scopus 로고    scopus 로고
    • Impact of sodium butyrate on the network of adhesion/growth-regulatory galectins in human colon cancer in vitro
    • Katzenmaier, E.-M.; André, S.; Kopitz, J.; Gabius, H.-J. Impact of sodium butyrate on the network of adhesion/growth-regulatory galectins in human colon cancer in vitro. Anticancer Res. 2014, 34, 5429-5438.
    • (2014) Anticancer Res. , vol.34 , pp. 5429-5438
    • Katzenmaier, E.-M.1    André, S.2    Kopitz, J.3    Gabius, H.-J.4
  • 50
    • 77956036448 scopus 로고    scopus 로고
    • Lectin microarrays for glycomic analysis
    • Gupta, G.; Surolia, A.; Sampathkumar, S.G. Lectin microarrays for glycomic analysis. Omics 2010, 14, 419-436.
    • (2010) Omics , vol.14 , pp. 419-436
    • Gupta, G.1    Surolia, A.2    Sampathkumar, S.G.3
  • 51
    • 84899822806 scopus 로고    scopus 로고
    • Glycan microarrays: New angles and new strategies
    • Donczo, B.; Kerekgyarto, J.; Szurmai, Z.; Guttman, A. Glycan microarrays: New angles and new strategies. Analyst 2014, 139, 2650-2657.
    • (2014) Analyst , vol.139 , pp. 2650-2657
    • Donczo, B.1    Kerekgyarto, J.2    Szurmai, Z.3    Guttman, A.4
  • 55
    • 0041289900 scopus 로고
    • A β-D-galactoside binding protein from electric organ tissue of Electrophorus electricus
    • Teichberg, V.I.; Silman, I.; Beitsch, D.D.; Resheff, G. A β-D-galactoside binding protein from electric organ tissue of Electrophorus electricus. Proc. Natl. Acad. Sci. USA 1975, 72, 1383-1387.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1383-1387
    • Teichberg, V.I.1    Silman, I.2    Beitsch, D.D.3    Resheff, G.4
  • 56
    • 0023664406 scopus 로고
    • Multiple soluble b-galactoside-binding lectins from human lung
    • Sparrow, C.; Leffler, H.; Barondes, S.H. Multiple soluble b-galactoside-binding lectins from human lung. J. Biol. Chem. 1987, 262, 7383-7390.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7383-7390
    • Sparrow, C.1    Leffler, H.2    Barondes, S.H.3
  • 57
    • 0025321107 scopus 로고
    • Human splenic galaptin: Carbohydrate-binding specificity and characterization of the combining site
    • Ahmed, H.; Allen, H.J.; Sharma, A.; Matta, K.L. Human splenic galaptin: Carbohydrate-binding specificity and characterization of the combining site. Biochemistry 1990, 29, 5315-5319.
    • (1990) Biochemistry , vol.29 , pp. 5315-5319
    • Ahmed, H.1    Allen, H.J.2    Sharma, A.3    Matta, K.L.4
  • 58
    • 0025321165 scopus 로고
    • Binding characteristics of galactoside-binding lectin (galaptin) from human spleen
    • Lee, R.T.; Ichikawa, Y.; Allen, H.J.; Lee, Y.C. Binding characteristics of galactoside-binding lectin (galaptin) from human spleen. J. Biol. Chem. 1990, 265, 7864-7871.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7864-7871
    • Lee, R.T.1    Ichikawa, Y.2    Allen, H.J.3    Lee, Y.C.4
  • 59
    • 0027260299 scopus 로고
    • Carbohydrate-binding protein 35. II. Analysis of the interaction of the recombinant polypeptide with saccharides
    • Knibbs, R.N.; Agrwal, N.; Wang, J.L.; Goldstein, I.J. Carbohydrate-binding protein 35. II. Analysis of the interaction of the recombinant polypeptide with saccharides. J. Biol. Chem. 1993, 268, 14940-14947.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14940-14947
    • Knibbs, R.N.1    Agrwal, N.2    Wang, J.L.3    Goldstein, I.J.4
  • 60
    • 0036436051 scopus 로고    scopus 로고
    • Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3 and -7. Evidence for differential binding specificities
    • Ahmad, N.; Gabius, H.-J.; Kaltner, H.; André, S.; Kuwabara, I.; Liu, F.-T.; Oscarson, S.; Norberg, T.; Brewer, C.F. Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3 and -7. Evidence for differential binding specificities. Can. J. Chem. 2002, 80, 1096-1104.
    • (2002) Can. J. Chem. , vol.80 , pp. 1096-1104
    • Ahmad, N.1    Gabius, H.-J.2    Kaltner, H.3    André, S.4    Kuwabara, I.5    Liu, F.-T.6    Oscarson, S.7    Norberg, T.8    Brewer, C.F.9
  • 62
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galb1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • Wu, A.M.; Wu, J.H.; Liu, J.-H.; Singh, T.; André, S.; Kaltner, H.; Gabius, H.-J. Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galb1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochimie 2004, 86, 317-326.
    • (2004) Biochimie , vol.86 , pp. 317-326
    • Wu, A.M.1    Wu, J.H.2    Liu, J.-H.3    Singh, T.4    André, S.5    Kaltner, H.6    Gabius, H.-J.7
  • 64
    • 78649773993 scopus 로고    scopus 로고
    • Human galectin-3 (Mac-2 antigen): Defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region
    • Krzeminski, M.; Singh, T.; André, S.; Lensch, M.; Wu, A.M.; Bonvin, A.M.; Gabius, H.-J. Human galectin-3 (Mac-2 antigen): Defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region. Biochim. Biophys. Acta 2011, 1810, 150-161.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 150-161
    • Krzeminski, M.1    Singh, T.2    André, S.3    Lensch, M.4    Wu, A.M.5    Bonvin, A.M.6    Gabius, H.-J.7
  • 66
    • 84919712126 scopus 로고    scopus 로고
    • Defining the potential of aglycone modifications for affinity/selectivity enhancement against medically relevant lectins: Synthesis, activity screening, and HSQC-based NMR analysis
    • Rauthu, S.R.; Shiao, T.C.; André, S.; Miller, M.C.; Madej, E.; Mayo, K.H.; Gabius, H.-J.; Roy, R. Defining the potential of aglycone modifications for affinity/selectivity enhancement against medically relevant lectins: Synthesis, activity screening, and HSQC-based NMR analysis. ChemBioChem 2015, 16, 126-139.
    • (2015) ChemBioChem , vol.16 , pp. 126-139
    • Rauthu, S.R.1    Shiao, T.C.2    André, S.3    Miller, M.C.4    Madej, E.5    Mayo, K.H.6    Gabius, H.-J.7    Roy, R.8
  • 67
    • 0023760470 scopus 로고
    • Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin
    • Merkle, R.K.; Cummings, R.D. Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin. J. Biol. Chem. 1988, 263, 16143-16149.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16143-16149
    • Merkle, R.K.1    Cummings, R.D.2
  • 68
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • Ideo, H.; Seko, A.; Ishizuka, I.; Yamashita, K. The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 2003, 13, 713-723.
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 70
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain
    • Stowell, S.R.; Arthur, C.M.; Slanina, K.A.; Horton, J.R.; Smith, D.F.; Cummings, R.D. Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain. J. Biol. Chem. 2008, 283, 20547-20559.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20547-20559
    • Stowell, S.R.1    Arthur, C.M.2    Slanina, K.A.3    Horton, J.R.4    Smith, D.F.5    Cummings, R.D.6
  • 71
    • 79953197242 scopus 로고    scopus 로고
    • Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans
    • Ideo, H.; Matsuzaka, T.; Nonaka, T.; Seko, A.; Yamashita, K. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. J. Biol. Chem. 2011, 286, 11346-11355.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11346-11355
    • Ideo, H.1    Matsuzaka, T.2    Nonaka, T.3    Seko, A.4    Yamashita, K.5
  • 72
    • 84895420067 scopus 로고    scopus 로고
    • Natural single amino acid polymorphism (F19Y) in human galectin-8: Detection of structural alterations and increased growth-regulatory activity on tumor cells
    • Ruiz, F.M.; Scholz, B.A.; Buzamet, E.; Kopitz, J.; André, S.; Menendez, M.; Romero, A.; Solís, D.; Gabius, H.-J. Natural single amino acid polymorphism (F19Y) in human galectin-8: Detection of structural alterations and increased growth-regulatory activity on tumor cells. FEBS J. 2014, 281, 1446-1464.
    • (2014) FEBS J , vol.281 , pp. 1446-1464
    • Ruiz, F.M.1    Scholz, B.A.2    Buzamet, E.3    Kopitz, J.4    André, S.5    Menendez, M.6    Romero, A.7    Solís, D.8    Gabius, H.-J.9
  • 74
    • 84941599865 scopus 로고    scopus 로고
    • Combining crystallography and hydrogen-deuterium exchange to study galectin-ligand complexes
    • Ruiz, F.M.; Gilles, U.; Lindner, I.; André, S.; Romero, A.; Reusch, D.; Gabius, H.-J. Combining crystallography and hydrogen-deuterium exchange to study galectin-ligand complexes. Chem. Eur. J. 2015, 21, 13558-13568.
    • (2015) Chem. Eur. J. , vol.21 , pp. 13558-13568
    • Ruiz, F.M.1    Gilles, U.2    Lindner, I.3    André, S.4    Romero, A.5    Reusch, D.6    Gabius, H.-J.7
  • 75
    • 0032546511 scopus 로고    scopus 로고
    • Diversity of C-linked neoglycopeptides for the exploration of subsite-assisted carbohydrate binding interactions
    • Arya, P.; Kutterer, K.M.; Qin, H.; Roby, J.; Barnes, M.L.; Kim, J.M.; Roy, R. Diversity of C-linked neoglycopeptides for the exploration of subsite-assisted carbohydrate binding interactions. Bioorg. Med. Chem. Lett. 1998, 8, 1127-1132.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 1127-1132
    • Arya, P.1    Kutterer, K.M.2    Qin, H.3    Roby, J.4    Barnes, M.L.5    Kim, J.M.6    Roy, R.7
  • 76
    • 77957776922 scopus 로고    scopus 로고
    • Synthesis and screening of a small glycomimetic library for inhibitory activity on medically relevant galactoside-specific lectins in assays of increasing biorelevance
    • André, S.; Giguère, D.; Dam, T.K.; Brewer, C.F.; Gabius, H.-J.; Roy, R. Synthesis and screening of a small glycomimetic library for inhibitory activity on medically relevant galactoside-specific lectins in assays of increasing biorelevance. New J. Chem. 2010, 34, 2229-2240.
    • (2010) New J. Chem. , vol.34 , pp. 2229-2240
    • André, S.1    Giguère, D.2    Dam, T.K.3    Brewer, C.F.4    Gabius, H.-J.5    Roy, R.6
  • 77
    • 32144452076 scopus 로고    scopus 로고
    • Aryl O- and S-galactosides and lactosides as specific inhibitors of human galectins-1 and -3: Role of electrostatic potential at O-3
    • Giguère, D.; Sato, S.; St-Pierre, C.; Sirois, S.; Roy, R. Aryl O- and S-galactosides and lactosides as specific inhibitors of human galectins-1 and -3: Role of electrostatic potential at O-3. Bioorg. Med. Chem. Lett. 2006, 16, 1668-1672.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 1668-1672
    • Giguère, D.1    Sato, S.2    St-Pierre, C.3    Sirois, S.4    Roy, R.5
  • 79
    • 17544377102 scopus 로고    scopus 로고
    • Different architecture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives
    • Solís, D.; Romero, A.; Kaltner, H.; Gabius, H.-J.; Díaz-Mauriño, T. Different architecture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives. J. Biol. Chem. 1996, 271, 12744-12748.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solís, D.1    Romero, A.2    Kaltner, H.3    Gabius, H.-J.4    Díaz-Mauriño, T.5
  • 80
    • 0001084339 scopus 로고    scopus 로고
    • Anomeric group transformations under PTC
    • Roy, R.; Tropper, F.D.; Cao, S.; Kim, J.M. Anomeric group transformations under PTC. ACS Symp. Ser. 1997, 659, 163-180.
    • (1997) ACS Symp. Ser. , vol.659 , pp. 163-180
    • Roy, R.1    Tropper, F.D.2    Cao, S.3    Kim, J.M.4
  • 83
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • López-Lucendo, M.F.; Solís, D.; André, S.; Hirabayashi, J.; Kasai, K.-I.-I.; Kaltner, H.; Gabius, H.-J.; Romero, A. Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J. Mol. Biol. 2004, 343, 957-970.
    • (2004) J. Mol. Biol. , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.-I.-I.5    Kaltner, H.6    Gabius, H.-J.7    Romero, A.8
  • 86
    • 78651343256 scopus 로고    scopus 로고
    • Selenoglycosides in silico: Ab initio-derived reparameterization of MM4, conformational analysis using histo-blood group ABH antigens and lectin docking as indication for potential of bioactivity
    • Strino, F.; Lii, J.H.; Koppisetty, C.A.; Nyholm, P.G.; Gabius, H.-J. Selenoglycosides in silico: Ab initio-derived reparameterization of MM4, conformational analysis using histo-blood group ABH antigens and lectin docking as indication for potential of bioactivity. J. Comput. Aided Mol. Des. 2010, 24, 1009-1021.
    • (2010) J. Comput. Aided Mol. Des. , vol.24 , pp. 1009-1021
    • Strino, F.1    Lii, J.H.2    Koppisetty, C.A.3    Nyholm, P.G.4    Gabius, H.-J.5
  • 87
    • 84964219442 scopus 로고    scopus 로고
    • Thio- and selenoglycosides as ligands for biomedically relevant lectins: Valency-activity correlations for benzene-based dithiogalactoside clusters and first assessment for (di)selenodigalactosides
    • André, S.; Kover, K.E.; Gabius, H.-J.; Szilagyi, L. Thio- and selenoglycosides as ligands for biomedically relevant lectins: Valency-activity correlations for benzene-based dithiogalactoside clusters and first assessment for (di)selenodigalactosides. Bioorg. Med. Chem. Lett. 2015, 25, 931-935.
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 931-935
    • André, S.1    Kover, K.E.2    Gabius, H.-J.3    Szilagyi, L.4
  • 88
    • 78649967889 scopus 로고    scopus 로고
    • The chemist's way to synthesize glycosides
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Oscarson, S. The chemist's way to synthesize glycosides. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 31-51.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 31-51
    • Oscarson, S.1
  • 89
    • 84864989789 scopus 로고    scopus 로고
    • Bi- to tetravalent glycoclusters: Synthesis, structure-activity profiles as lectin inhibitors and impact of combining both valency and headgroup tailoring on selectivity
    • Wang, G.-N.; Andre, S.; Gabius, H.-J.; Murphy, P.V. Bi- to tetravalent glycoclusters: Synthesis, structure-activity profiles as lectin inhibitors and impact of combining both valency and headgroup tailoring on selectivity. Org. Biomol. Chem. 2012, 10, 6893-6907.
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 6893-6907
    • Wang, G.-N.1    Andre, S.2    Gabius, H.-J.3    Murphy, P.V.4
  • 90
    • 0002751972 scopus 로고
    • Synthetic studies in carbohydrates. 14. Synthesis of O-α-L-fucopyranosyl-(1-2)-O-β-D-galactopyranosyl-(1-4)-D-glucopyranose (2′-O-α-L-fucopyranosyl-lactose)
    • Abbas, S.A.; Barlow, J.J.; Matta, K.L. Synthetic studies in carbohydrates. 14. Synthesis of O-α-L-fucopyranosyl-(1-2)-O-β-D-galactopyranosyl-(1-4)-D-glucopyranose (2′-O-α-L-fucopyranosyl-lactose). Carbohydr. Res. 1981, 88, 51-60.
    • (1981) Carbohydr. Res. , vol.88 , pp. 51-60
    • Abbas, S.A.1    Barlow, J.J.2    Matta, K.L.3
  • 91
    • 0035913760 scopus 로고    scopus 로고
    • 1-Benzenesulfinyl piperidine/trifluoromethanesulfonic anhydride: A potent combination of shelf-stable reagents for the low-temperature conversion of thioglycosides to glycosyl triflates and for the formation of diverse glycosidic linkages
    • Crich, D.; Smith, M. 1-Benzenesulfinyl piperidine/trifluoromethanesulfonic anhydride: A potent combination of shelf-stable reagents for the low-temperature conversion of thioglycosides to glycosyl triflates and for the formation of diverse glycosidic linkages. J. Am. Chem. Soc. 2001, 123, 9015-9020.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9015-9020
    • Crich, D.1    Smith, M.2
  • 92
    • 84951291466 scopus 로고    scopus 로고
    • Lewis acid promoted anomerisation: Recent developments and applications
    • Murphy, P.V. Lewis acid promoted anomerisation: Recent developments and applications. Carbohydr. Chem. 2016, 41, 90-123.
    • (2016) Carbohydr. Chem. , vol.41 , pp. 90-123
    • Murphy, P.V.1
  • 93
    • 79956187792 scopus 로고    scopus 로고
    • Inhibitory potential of chemical substitutions at bioinspired sites of α-D-galactopyranose on neoglycoprotein/cell surface binding of two classes of medically relevant lectins
    • Giguère, D.; André, S.; Bonin, M.A.; Bellefleur, M.A.; Provencal, A.; Cloutier, P.; Pucci, B.; Roy, R.; Gabius, H.-J. Inhibitory potential of chemical substitutions at bioinspired sites of α-D-galactopyranose on neoglycoprotein/cell surface binding of two classes of medically relevant lectins. Bioorg. Med. Chem. 2011, 19, 3280-3287.
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 3280-3287
    • Giguère, D.1    André, S.2    Bonin, M.A.3    Bellefleur, M.A.4    Provencal, A.5    Cloutier, P.6    Pucci, B.7    Roy, R.8    Gabius, H.-J.9
  • 94
    • 13644272606 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on cation-p interactions in lectin-ligand complexes: High-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction
    • Sörme, P.; Arnoux, P.; Kahl-Knutsson, B.; Leffler, H.; Rini, J.M.; Nilsson, U.J. Structural and thermodynamic studies on cation-p interactions in lectin-ligand complexes: High-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction. J. Am. Chem. Soc. 2005, 127, 1737-1743.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1737-1743
    • Sörme, P.1    Arnoux, P.2    Kahl-Knutsson, B.3    Leffler, H.4    Rini, J.M.5    Nilsson, U.J.6
  • 95
  • 96
    • 0002773690 scopus 로고
    • Enhanced biochemical affinities of multivalent neoglycoconjugates
    • Lee, Y.C., Lee, R.T., Eds.; Academic Press: San Diego, CA, USA
    • Lee, R.T.; Lee, Y.C. Enhanced biochemical affinities of multivalent neoglycoconjugates. In Neoglycoconjugates, Preparation and Applications; Lee, Y.C., Lee, R.T., Eds.; Academic Press: San Diego, CA, USA, 1994; pp. 23-50.
    • (1994) Neoglycoconjugates, Preparation and Applications , pp. 23-50
    • Lee, R.T.1    Lee, Y.C.2
  • 97
    • 0347946755 scopus 로고    scopus 로고
    • A decade of glycodendrimer chemistry
    • Roy, R. A decade of glycodendrimer chemistry. Trends Glycosci. Glycotechnol. 2003, 15, 291-310.
    • (2003) Trends Glycosci. Glycotechnol , vol.15 , pp. 291-310
    • Roy, R.1
  • 98
    • 72249101901 scopus 로고    scopus 로고
    • The chemist's way to prepare multivalency
    • Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany
    • Chabre, Y.M.; Roy, R. The chemist's way to prepare multivalency. In The Sugar Code: Fundamentals of Glycosciences; Gabius, H.-J., Ed.; Wiley-VCH: Weinheim, Germany, 2009; pp. 53-70.
    • (2009) The Sugar Code: Fundamentals of Glycosciences , pp. 53-70
    • Chabre, Y.M.1    Roy, R.2
  • 99
    • 77954914845 scopus 로고    scopus 로고
    • Design and creativity in synthesis of multivalent neoglycoconjugates
    • Chabre, Y.M.; Roy, R. Design and creativity in synthesis of multivalent neoglycoconjugates. Adv. Carbohydr. Chem. Biochem. 2010, 63, 165-393.
    • (2010) Adv. Carbohydr. Chem. Biochem. , vol.63 , pp. 165-393
    • Chabre, Y.M.1    Roy, R.2
  • 100
    • 84877831631 scopus 로고    scopus 로고
    • Multivalent glycoconjugate syntheses and applications using aromatic scaffolds
    • Chabre, Y.M.; Roy, R. Multivalent glycoconjugate syntheses and applications using aromatic scaffolds. Chem. Soc. Rev. 2013, 42, 4657-4708.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 4657-4708
    • Chabre, Y.M.1    Roy, R.2
  • 101
    • 84930884115 scopus 로고    scopus 로고
    • Glyconanosynthons as powerful scaffolds and building blocks for the rapid construction of multifaceted, dense and chiral dendrimers
    • Roy, R.; Shiao, T.C. Glyconanosynthons as powerful scaffolds and building blocks for the rapid construction of multifaceted, dense and chiral dendrimers. Chem. Soc. Rev. 2015, 44, 3924-3941.
    • (2015) Chem. Soc. Rev. , vol.44 , pp. 3924-3941
    • Roy, R.1    Shiao, T.C.2
  • 102
    • 8744229693 scopus 로고    scopus 로고
    • Metathesis of structurally preorganized bivalent carbohydrates. Synthesis of macrocyclic and oligomeric scaffolds
    • Velasco-Torrijos, T.; Murphy, P.V. Metathesis of structurally preorganized bivalent carbohydrates. Synthesis of macrocyclic and oligomeric scaffolds. Org. Lett. 2004, 6, 3961-3964.
    • (2004) Org. Lett. , vol.6 , pp. 3961-3964
    • Velasco-Torrijos, T.1    Murphy, P.V.2
  • 103
    • 12344297355 scopus 로고    scopus 로고
    • Synthesis and conformational analysis of novel water soluble macrocycles incorporating carbohydrates, including a beta-cyclodextrin mimic
    • Velasco-Torrijos, T.; Murphy, P.V. Synthesis and conformational analysis of novel water soluble macrocycles incorporating carbohydrates, including a beta-cyclodextrin mimic. Tetrahedron Asymmetry 2005, 16, 261-272.
    • (2005) Tetrahedron Asymmetry , vol.16 , pp. 261-272
    • Velasco-Torrijos, T.1    Murphy, P.V.2
  • 104
    • 70350690246 scopus 로고    scopus 로고
    • Phenylenediamine-based bivalent glycocyclophanes: Synthesis and analysis of the influence of scaffold rigidity and ligand spacing on lectin binding in cell systems with different glycomic profiles
    • André, S.; Velasco-Torrijos, T.; Leyden, R.; Gouin, S.; Tosin, M.; Murphy, P.V.; Gabius, H.-J. Phenylenediamine-based bivalent glycocyclophanes: Synthesis and analysis of the influence of scaffold rigidity and ligand spacing on lectin binding in cell systems with different glycomic profiles. Org. Biomol. Chem. 2009, 7, 4715-4725.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 4715-4725
    • André, S.1    Velasco-Torrijos, T.2    Leyden, R.3    Gouin, S.4    Tosin, M.5    Murphy, P.V.6    Gabius, H.-J.7
  • 105
    • 72249089323 scopus 로고    scopus 로고
    • Synthesis of bivalent lactosides based on terephthalamide, N,N′-diglucosylterephthalamide, and glycophane scaffolds and assessment of their inhibitory capacity on medically relevant lectins
    • Leyden, R.; Velasco-Torrijos, T.; André, S.; Gouin, S.; Gabius, H.-J.; Murphy, P.V. Synthesis of bivalent lactosides based on terephthalamide, N,N′-diglucosylterephthalamide, and glycophane scaffolds and assessment of their inhibitory capacity on medically relevant lectins. J. Org. Chem. 2009, 74, 9010-9026.
    • (2009) J. Org. Chem. , vol.74 , pp. 9010-9026
    • Leyden, R.1    Velasco-Torrijos, T.2    André, S.3    Gouin, S.4    Gabius, H.-J.5    Murphy, P.V.6
  • 106
    • 84655170133 scopus 로고    scopus 로고
    • Synthesis of bivalent lactosides and their activity as sensors for differences between lectins in inter- and intrafamily comparisons
    • André, S.; Jarikote, D.V.; Yan, D.; Vincenz, L.; Wang, G.N.; Kaltner, H.; Murphy, P.V.; Gabius, H.-J. Synthesis of bivalent lactosides and their activity as sensors for differences between lectins in inter- and intrafamily comparisons. Bioorg. Med. Chem. Lett. 2012, 22, 313-318.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 313-318
    • André, S.1    Jarikote, D.V.2    Yan, D.3    Vincenz, L.4    Wang, G.N.5    Kaltner, H.6    Murphy, P.V.7    Gabius, H.-J.8
  • 107
    • 84899658349 scopus 로고    scopus 로고
    • Combining glycocluster synthesis with protein engineering: An approach to probe into the significance of linker length in a tandem-repeat-type lectin (galectin-4)
    • André, S.; Wang, G.N.; Gabius, H.-J.; Murphy, P.V. Combining glycocluster synthesis with protein engineering: An approach to probe into the significance of linker length in a tandem-repeat-type lectin (galectin-4). Carbohydr. Res. 2014, 389, 25-38.
    • (2014) Carbohydr. Res. , vol.389 , pp. 25-38
    • André, S.1    Wang, G.N.2    Gabius, H.-J.3    Murphy, P.V.4
  • 108
    • 3342915857 scopus 로고    scopus 로고
    • Glycosidation reactions of silyl ethers with conformationally inverted donors derived from glucuronic acid: Stereoselective synthesis of glycosides and 2-deoxyglycosides
    • Poláková, M.; Pitt, N.; Tosin, M.; Murphy, P.V. Glycosidation reactions of silyl ethers with conformationally inverted donors derived from glucuronic acid: Stereoselective synthesis of glycosides and 2-deoxyglycosides. Angew. Chem. Int. Ed. 2004, 43, 2518-2521.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 2518-2521
    • Poláková, M.1    Pitt, N.2    Tosin, M.3    Murphy, P.V.4
  • 110
  • 111
    • 0344515363 scopus 로고    scopus 로고
    • First demonstration of differential inhibition of lectin binding by synthetic tri-and tetravalent glycoclusters from cross-coupling of rigidified 2-propynyl lactoside
    • André, S.; Liu, B.; Gabius, H.-J.; Roy, R. First demonstration of differential inhibition of lectin binding by synthetic tri-and tetravalent glycoclusters from cross-coupling of rigidified 2-propynyl lactoside. Org. Biomol. Chem. 2003, 1, 3909-3916.
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3909-3916
    • André, S.1    Liu, B.2    Gabius, H.-J.3    Roy, R.4
  • 112
    • 0035844649 scopus 로고    scopus 로고
    • Tris-bipyridine ruthenium complex-based glycoclusters: Amplified luminescence and enhanced lectin affinities
    • Hasegawa, T.; Yonemura, T.; Matsuura, K.; Kobayashi, K. Tris-bipyridine ruthenium complex-based glycoclusters: Amplified luminescence and enhanced lectin affinities. Tetrahedron Lett. 2001, 42, 3989-3992.
    • (2001) Tetrahedron Lett. , vol.42 , pp. 3989-3992
    • Hasegawa, T.1    Yonemura, T.2    Matsuura, K.3    Kobayashi, K.4
  • 113
    • 0037620667 scopus 로고    scopus 로고
    • Cu(II)-self-assembling bipyridyl-glycoclusters and dendrimers bearing the Tn-antigen cancer marker: Syntheses and lectin binding properties
    • Roy, R.; Kim, J.M. Cu(II)-self-assembling bipyridyl-glycoclusters and dendrimers bearing the Tn-antigen cancer marker: Syntheses and lectin binding properties. Tetrahedron 2003, 59, 3881-3893.
    • (2003) Tetrahedron , vol.59 , pp. 3881-3893
    • Roy, R.1    Kim, J.M.2
  • 114
    • 57249115761 scopus 로고    scopus 로고
    • Recent advances on cyclopeptide-based glycoclusters
    • Renaudet, O. Recent advances on cyclopeptide-based glycoclusters. Mini Rev. Org. Chem. 2008, 5, 274-286.
    • (2008) Mini Rev. Org. Chem. , vol.5 , pp. 274-286
    • Renaudet, O.1
  • 115
    • 79955888952 scopus 로고    scopus 로고
    • Cyclic neoglycodecapeptides: How to increase their inhibitory activity and selectivity on lectin/toxin binding to a glycoprotein and cells
    • André, S.; Renaudet, O.; Bossu, I.; Dumy, P.; Gabius, H.-J. Cyclic neoglycodecapeptides: How to increase their inhibitory activity and selectivity on lectin/toxin binding to a glycoprotein and cells. J. Pept. Sci. 2011, 17, 427-437.
    • (2011) J. Pept. Sci. , vol.17 , pp. 427-437
    • André, S.1    Renaudet, O.2    Bossu, I.3    Dumy, P.4    Gabius, H.-J.5
  • 116
    • 48649102319 scopus 로고    scopus 로고
    • Calix[n]arene-based glycoclusters: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins
    • André, S.; Sansone, F.; Kaltner, H.; Casnati, A.; Kopitz, J.; Gabius, H.-J.; Ungaro, R. Calix[n]arene-based glycoclusters: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins. ChemBioChem 2008, 9, 1649-1661.
    • (2008) ChemBioChem , vol.9 , pp. 1649-1661
    • André, S.1    Sansone, F.2    Kaltner, H.3    Casnati, A.4    Kopitz, J.5    Gabius, H.-J.6    Ungaro, R.7
  • 117
    • 79956088428 scopus 로고    scopus 로고
    • Combining carbohydrate substitutions at bioinspired positions with multivalent presentation towards optimising lectin inhibitors: Case study with calixarenes
    • André, S.; Grandjean, C.; Gautier, F.M.; Bernardi, S.; Sansone, F.; Gabius, H.-J.; Ungaro, R. Combining carbohydrate substitutions at bioinspired positions with multivalent presentation towards optimising lectin inhibitors: Case study with calixarenes. Chem. Commun. 2011, 47, 6126-6128.
    • (2011) Chem. Commun. , vol.47 , pp. 6126-6128
    • André, S.1    Grandjean, C.2    Gautier, F.M.3    Bernardi, S.4    Sansone, F.5    Gabius, H.-J.6    Ungaro, R.7
  • 118
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • Ahmad, N.; Gabius, H.-J.; André, S.; Kaltner, H.; Sabesan, S.; Roy, R.; Liu, B.; Macaluso, F.; Brewer, C.F. Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J. Biol. Chem. 2004, 279, 10841-10847.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.7    Macaluso, F.8    Brewer, C.F.9
  • 119
    • 84905463032 scopus 로고    scopus 로고
    • Human chimera-type galectin-3: Defining the critical tail length for high-affinity glycoprotein/cell surface binding and functional competition with galectin-1 in neuroblastoma cell growth regulation
    • Kopitz, J.; Vértesy, S.; André, S.; Fiedler, S.; Schnölzer, M.; Gabius, H.-J. Human chimera-type galectin-3: Defining the critical tail length for high-affinity glycoprotein/cell surface binding and functional competition with galectin-1 in neuroblastoma cell growth regulation. Biochimie 2014, 104, 90-99.
    • (2014) Biochimie , vol.104 , pp. 90-99
    • Kopitz, J.1    Vértesy, S.2    André, S.3    Fiedler, S.4    Schnölzer, M.5    Gabius, H.-J.6
  • 120
    • 0012061680 scopus 로고    scopus 로고
    • Lactose-containing starburst dendrimers: Influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties
    • André, S.; Cejas Ortega, P.J.; Perez, M.A.; Roy, R.; Gabius, H.-J. Lactose-containing starburst dendrimers: Influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties. Glycobiology 1999, 9, 1253-1261.
    • (1999) Glycobiology , vol.9 , pp. 1253-1261
    • André, S.1    Cejas Ortega, P.J.2    Perez, M.A.3    Roy, R.4    Gabius, H.-J.5
  • 121
    • 48249154964 scopus 로고    scopus 로고
    • Expeditive synthesis of glycodendrimer scaffolds based on versatile TRIS and mannoside derivatives
    • Chabre, Y.M.; Contino-Pepin, C.; Placide, V.; Shiao, T.C.; Roy, R. Expeditive synthesis of glycodendrimer scaffolds based on versatile TRIS and mannoside derivatives. J. Org. Chem. 2008, 73, 5602-5605.
    • (2008) J. Org. Chem. , vol.73 , pp. 5602-5605
    • Chabre, Y.M.1    Contino-Pepin, C.2    Placide, V.3    Shiao, T.C.4    Roy, R.5
  • 122
    • 78651495413 scopus 로고    scopus 로고
    • Hexaphenylbenzene as a rigid template for the straightforward syntheses of "star-shaped" glycodendrimers
    • Chabre, Y.M.; Brisebois, P.P.; Abbassi, L.; Kerr, S.C.; Fahy, J.V.; Marcotte, I.; Roy, R. Hexaphenylbenzene as a rigid template for the straightforward syntheses of "star-shaped" glycodendrimers. J. Org. Chem. 2011, 76, 724-727.
    • (2011) J. Org. Chem. , vol.76 , pp. 724-727
    • Chabre, Y.M.1    Brisebois, P.P.2    Abbassi, L.3    Kerr, S.C.4    Fahy, J.V.5    Marcotte, I.6    Roy, R.7
  • 123
    • 84923253165 scopus 로고    scopus 로고
    • A fast track strategy toward highly functionalized dendrimers with different structural layers: An "onion peel approach"
    • Sharma, R.; Zhang, I.; Abbassi, L.; Rej, R.; Maysinger, D.; Roy, R. A fast track strategy toward highly functionalized dendrimers with different structural layers: An "onion peel approach". Polym. Chem. 2015, 6, 1436-1444.
    • (2015) Polym. Chem. , vol.6 , pp. 1436-1444
    • Sharma, R.1    Zhang, I.2    Abbassi, L.3    Rej, R.4    Maysinger, D.5    Roy, R.6
  • 124
    • 84902675108 scopus 로고    scopus 로고
    • "Onion peel" dendrimers: A straightforward synthetic approach towards highly diversified architectures
    • Sharma, R.; Naresh, K.; Chabre, Y.M.; Rej, R.; Saadeh, N.K.; Roy, R. "Onion peel" dendrimers: A straightforward synthetic approach towards highly diversified architectures. Polym. Chem. 2014, 5, 4321-4331.
    • (2014) Polym. Chem. , vol.5 , pp. 4321-4331
    • Sharma, R.1    Naresh, K.2    Chabre, Y.M.3    Rej, R.4    Saadeh, N.K.5    Roy, R.6
  • 125
    • 84923242416 scopus 로고    scopus 로고
    • A highly versatile convergent/divergent "onion peel" synthetic strategy toward potent multivalent glycodendrimers
    • Sharma, R.; Kottari, N.; Chabre, Y.M.; Abbassi, L.; Shiao, T.C.; Roy, R. A highly versatile convergent/divergent "onion peel" synthetic strategy toward potent multivalent glycodendrimers. Chem. Commun. 2014, 50, 13300-13303.
    • (2014) Chem. Commun. , vol.50 , pp. 13300-13303
    • Sharma, R.1    Kottari, N.2    Chabre, Y.M.3    Abbassi, L.4    Shiao, T.C.5    Roy, R.6
  • 126
    • 84946747356 scopus 로고    scopus 로고
    • Multifaceted glycodendrimers with programmable bioactivity through convergent, divergent, and accelerated approaches using polyfunctional cyclotriphosphazenes
    • Abbassi, L.; Chabre, Y.M.; Kottari, N.; Arnold, A.A.; André, S.; Josserand, J.; Gabius, H.-J.; Roy, R. Multifaceted glycodendrimers with programmable bioactivity through convergent, divergent, and accelerated approaches using polyfunctional cyclotriphosphazenes. Polym. Chem. 2015, 6, 7666-7683.
    • (2015) Polym. Chem. , vol.6 , pp. 7666-7683
    • Abbassi, L.1    Chabre, Y.M.2    Kottari, N.3    Arnold, A.A.4    André, S.5    Josserand, J.6    Gabius, H.-J.7    Roy, R.8
  • 127
    • 84879348746 scopus 로고    scopus 로고
    • Modular synthesis of amphiphilic Janus glycodendrimers and their self-assembly into glycodendrimersomes and other complex architectures with bioactivity to biomedically relevant lectins
    • Percec, V.; Leowanawat, P.; Sun, H.J.; Kulikov, O.; Nusbaum, C.D.; Tran, T.M.; Bertin, A.; Wilson, D.A.; Peterca, M.; Zhang, S.; et al. Modular synthesis of amphiphilic Janus glycodendrimers and their self-assembly into glycodendrimersomes and other complex architectures with bioactivity to biomedically relevant lectins. J. Am. Chem. Soc. 2013, 135, 9055-9077.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 9055-9077
    • Percec, V.1    Leowanawat, P.2    Sun, H.J.3    Kulikov, O.4    Nusbaum, C.D.5    Tran, T.M.6    Bertin, A.7    Wilson, D.A.8    Peterca, M.9    Zhang, S.10
  • 130
    • 84945280400 scopus 로고    scopus 로고
    • Glycodendrimersomes from sequence-defined Janus glycodendrimers reveal high activity and sensor capacity for the agglutination by natural variants of human lectins
    • Zhang, S.; Xiao, Q.; Sherman, S.E.; Muncan, A.; Vicente, A.D.R.; Wang, Z.; Hammer, D.A.; Williams, D.; Chen, Y.; Pochan, D.J.; et al. Glycodendrimersomes from sequence-defined Janus glycodendrimers reveal high activity and sensor capacity for the agglutination by natural variants of human lectins. J. Am. Chem. Soc. 2015, 137, 13334-13344.
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 13334-13344
    • Zhang, S.1    Xiao, Q.2    Sherman, S.E.3    Muncan, A.4    Vicente, A.D.R.5    Wang, Z.6    Hammer, D.A.7    Williams, D.8    Chen, Y.9    Pochan, D.J.10
  • 131
    • 84928975425 scopus 로고    scopus 로고
    • Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface
    • Zhang, S.; Moussodia, R.-O.; Vértesy, S.; André, S.; Klein, M.L.; Gabius, H.-J.; Percec, V. Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface. Proc. Natl. Acad. Sci. USA 2015, 112, 5585-5590.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 5585-5590
    • Zhang, S.1    Moussodia, R.-O.2    Vértesy, S.3    André, S.4    Klein, M.L.5    Gabius, H.-J.6    Percec, V.7
  • 132
    • 0034669526 scopus 로고    scopus 로고
    • Differences in zero-force and force-driven kinetics of ligand dissociation from β-galactoside-specific proteins (plant and animal lectins, immunoglobulin G) monitored by plasmon resonance and dynamic single molecule force microscopy
    • Dettmann, W.; Grandbois, M.; André, S.; Benoit, M.; Wehle, A.K.; Kaltner, H.; Gabius, H.-J.; Gaub, H.E. Differences in zero-force and force-driven kinetics of ligand dissociation from β-galactoside-specific proteins (plant and animal lectins, immunoglobulin G) monitored by plasmon resonance and dynamic single molecule force microscopy. Arch. Biochem. Biophys. 2000, 383, 157-170.
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 157-170
    • Dettmann, W.1    Grandbois, M.2    André, S.3    Benoit, M.4    Wehle, A.K.5    Kaltner, H.6    Gabius, H.-J.7    Gaub, H.E.8
  • 133
    • 0003090129 scopus 로고    scopus 로고
    • Induction of T lymphocyte apoptosis: A novel function for galectin-1
    • Pace, K.E.; Baum, L.G. Induction of T lymphocyte apoptosis: A novel function for galectin-1. Trends Glycosci. Glycotechnol. 1997, 9, 21-29.
    • (1997) Trends Glycosci. Glycotechnol , vol.9 , pp. 21-29
    • Pace, K.E.1    Baum, L.G.2
  • 134
    • 0035107949 scopus 로고    scopus 로고
    • Galectin-1 is highly expressed in human gliomas with relevance for modulation of invasion of tumor astrocytes into the brain parenchyma
    • Rorive, S.; Belot, N.; Decaestecker, C.; Lefranc, F.; Gordower, L.; Micik, S.; Maurage, C.-A.; Kaltner, H.; Ruchoux, M.-M.; Danguy, A.; et al. Galectin-1 is highly expressed in human gliomas with relevance for modulation of invasion of tumor astrocytes into the brain parenchyma. Glia 2001, 33, 241-255.
    • (2001) Glia , vol.33 , pp. 241-255
    • Rorive, S.1    Belot, N.2    Decaestecker, C.3    Lefranc, F.4    Gordower, L.5    Micik, S.6    Maurage, C.-A.7    Kaltner, H.8    Ruchoux, M.-M.9    Danguy, A.10
  • 136
    • 84860228899 scopus 로고    scopus 로고
    • Galectins in acute and chronic inflammation
    • Liu, F.-T.; Yang, R.Y.; Hsu, D.K. Galectins in acute and chronic inflammation. Ann. N. Y. Acad. Sci. 2012, 1253, 80-91.
    • (2012) Ann. N. Y. Acad. Sci. , vol.1253 , pp. 80-91
    • Liu, F.-T.1    Yang, R.Y.2    Hsu, D.K.3
  • 137
    • 84922161299 scopus 로고    scopus 로고
    • Human osteoarthritic knee cartilage: Fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration
    • Toegel, S.; Bieder, D.; André, S.; Kayser, K.; Walzer, S.M.; Hobusch, G.; Windhager, R.; Gabius, H.-J. Human osteoarthritic knee cartilage: Fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration. Histochem. Cell Biol. 2014, 142, 373-388.
    • (2014) Histochem. Cell Biol. , vol.142 , pp. 373-388
    • Toegel, S.1    Bieder, D.2    André, S.3    Kayser, K.4    Walzer, S.M.5    Hobusch, G.6    Windhager, R.7    Gabius, H.-J.8
  • 138
    • 84969900633 scopus 로고    scopus 로고
    • Galectins and immune responses-Just how do they do those things they do?
    • Thiemann, S.; Baum, L.G. Galectins and immune responses-Just how do they do those things they do? Annu. Rev. Immunol. 2016, 34, 243-264.
    • (2016) Annu. Rev. Immunol. , vol.34 , pp. 243-264
    • Thiemann, S.1    Baum, L.G.2
  • 140
    • 84863438780 scopus 로고    scopus 로고
    • Non-synonymous single nucleotide polymorphisms in genes for immunoregulatory galectins: Association of galectin-8 (F19Y) occurrence with autoimmune diseases in a Caucasian population
    • Pál, Z.; Antal, P.; Srivastava, S.K.; Hullám, G.; Semsei, A.F.; Gál, J.; Svébis, M.; Soós, G.; Szalai, C.; André, S.; et al. Non-synonymous single nucleotide polymorphisms in genes for immunoregulatory galectins: Association of galectin-8 (F19Y) occurrence with autoimmune diseases in a Caucasian population. Biochim. Biophys. Acta 2012, 1820, 1512-1518.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 1512-1518
    • Pál, Z.1    Antal, P.2    Srivastava, S.K.3    Hullám, G.4    Semsei, A.F.5    Gál, J.6    Svébis, M.7    Soós, G.8    Szalai, C.9    André, S.10
  • 142
    • 84937704546 scopus 로고    scopus 로고
    • X-ray reflectivity and grazing incidence diffraction studies of interaction between huma adhesion/growth-regulatory galectin-1 and DPPE:GM1 lipid monolayer at the air/water interface
    • Majewski, J.; André, S.; Jones, E.; Chi, E.; Gabius, H.-J. X-ray reflectivity and grazing incidence diffraction studies of interaction between huma adhesion/growth-regulatory galectin-1 and DPPE:GM1 lipid monolayer at the air/water interface. Biochemistry 2015, 80, 943-956.
    • (2015) Biochemistry , vol.80 , pp. 943-956
    • Majewski, J.1    André, S.2    Jones, E.3    Chi, E.4    Gabius, H.-J.5
  • 144
    • 84957840736 scopus 로고    scopus 로고
    • Merging carbohydrate chemistry with lectin histochemistry to study inhibition of lectin binding by glycoclusters in the natural tissue context
    • André, S.; Kaltner, H.; Kayser, K.; Murphy, P.V.; Gabius, H.-J. Merging carbohydrate chemistry with lectin histochemistry to study inhibition of lectin binding by glycoclusters in the natural tissue context. Histochem. Cell Biol. 2016, 145, 185-199.
    • (2016) Histochem. Cell Biol. , vol.145 , pp. 185-199
    • André, S.1    Kaltner, H.2    Kayser, K.3    Murphy, P.V.4    Gabius, H.-J.5
  • 145
    • 84905226184 scopus 로고    scopus 로고
    • Low-molecular weight inhibitors of galectins
    • Leffler, H.; Nilsson, U. Low-molecular weight inhibitors of galectins. ACS Symp. Ser. 2012, 1115, 47-59.
    • (2012) ACS Symp. Ser. , vol.1115 , pp. 47-59
    • Leffler, H.1    Nilsson, U.2
  • 146
    • 79952576615 scopus 로고    scopus 로고
    • Inhibition of galectins with small molecules
    • Oeberg, C.T.; Leffler, H.; Nilsson, U.J. Inhibition of galectins with small molecules. Chimia 2011, 65, 18-23.
    • (2011) Chimia , vol.65 , pp. 18-23
    • Oeberg, C.T.1    Leffler, H.2    Nilsson, U.J.3


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