메뉴 건너뛰기




Volumn 1810, Issue 7, 2011, Pages 643-651

The Galβ-(syn)-gauche configuration is required for galectin-recognition disaccharides

Author keywords

Carbohydrate binding specificity; Comparative glycomics; Dissociation constant; Frontal affinity chromatography; Galectin; Pyridylamination

Indexed keywords

BETA GALACTOSIDE; DISACCHARIDE; ECALECTIN; GALECTIN 1; GALECTIN 2; GALECTIN 3; GALECTIN 4; GALECTIN 7; GALECTIN 8; OLIGOSACCHARIDE;

EID: 79957657860     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.04.001     Document Type: Article
Times cited : (38)

References (67)
  • 1
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins; he made so many of them
    • DOI 10.1093/glycob/9.10.979
    • D.N. Cooper, S.H. Barondes, God must love galectins; he made so many of them, Glycobiology 9 (1999) 979-984. (Pubitemid 29473954)
    • (1999) Glycobiology , vol.9 , Issue.10 , pp. 979-984
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 2
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • J. Hirabayashi, K. Kasai, The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution, Glycobiology 3 (1993) 297-304. (Pubitemid 23281277)
    • (1993) Glycobiology , vol.3 , Issue.4 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.-I.2
  • 3
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • S.H. Barondes, D.N. Cooper, M.A. Gitt, H. Leffler, Galectins. Structure and function of a large family of animal lectins, J. Biol. Chem. 269 (1994) 20807-20810.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 4
    • 0037066780 scopus 로고    scopus 로고
    • Characterization of a novel Drosophila melanogaster galectin. Expression in developing immune, neural, and muscle tissues
    • K.E. Pace, T. Lebestky, T. Hummel, P. Arnoux, K. Kwan, L.G. Baum, Characterization of a novel Drosophila melanogaster galectin. Expression in developing immune, neural, and muscle tissues, J. Biol. Chem. 277 (2002) 13091-13098.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13091-13098
    • Pace, K.E.1    Lebestky, T.2    Hummel, T.3    Arnoux, P.4    Kwan, K.5    Baum, L.G.6
  • 5
    • 33847404009 scopus 로고    scopus 로고
    • Molecular characterization and oligosaccharide-binding properties of a galectin from the argasid tick Ornithodoros moubata
    • DOI 10.1093/glycob/cwl070
    • X. Huang, N. Tsuji, T. Miyoshi, S. Nakamura-Tsuruta, J. Hirabayashi, K. Fujisaki, Molecular characterization and oligosaccharide-binding properties of a galectin from the argasid tick Ornithodoros moubata, Glycobiology 17 (2007) 313-323. (Pubitemid 46344683)
    • (2007) Glycobiology , vol.17 , Issue.3 , pp. 313-323
    • Huang, X.1    Tsuji, N.2    Miyoshi, T.3    Nakamura-Tsuruta, S.4    Hirabayashi, J.5    Fujisaki, K.6
  • 6
    • 0026694658 scopus 로고
    • Evidence that Caenorhabditis elegans 32-kDa β-galactoside-binding protein is homologous to vertebrate β-galactoside-binding lectins. cDNA cloning and deduced amino acid sequence
    • J. Hirabayashi, M. Satoh, K. Kasai, Evidence that Caenorhabditis elegans 32-kDa β-galactoside-binding protein is homologous to vertebrate β-galactoside-binding lectins. cDNA cloning and deduced amino acid sequence, J. Biol. Chem. 267 (1992) 15485-15490.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15485-15490
    • Hirabayashi, J.1    Satoh, M.2    Kasai, K.3
  • 7
    • 0027161599 scopus 로고
    • S-type lectins occur also in invertebrates: High conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium
    • K. Pfeifer, M. Haasemann, V. Gamulin, H. Bretting, F. Fahrenholz, W.E. Muller, S-type lectins occur also in invertebrates: high conservation of the carbohydrate recognition domain in the lectin genes from themarine sponge Geodia cydonium, Glycobiology 3 (1993) 179-184. (Pubitemid 23132608)
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 179-184
    • Pfeifer, K.1    Haasemann, M.2    Gamulin, V.3    Bretting, H.4    Fahrenholz, F.5    Muller, W.E.G.6
  • 8
    • 0031002992 scopus 로고    scopus 로고
    • Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin
    • DOI 10.1023/A:1018558225454
    • F. Yagi, M. Miyamoto, T. Abe, Y. Minami, K. Tadera, I.J. Goldstein, Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin, Glycoconj. J. 14 (1997) 281-288. (Pubitemid 27144180)
    • (1997) Glycoconjugate Journal , vol.14 , Issue.2 , pp. 281-288
    • Yagi, F.1    Miyamoto, M.2    Abe, T.3    Minami, Y.4    Tadera, K.5    Goldstein, I.J.6
  • 9
    • 0035497421 scopus 로고    scopus 로고
    • Agrocybe cylindracea lectin is a member of the galectin family
    • DOI 10.1023/A:1021193432577
    • F. Yagi, H. Hiroyama, S. Kodama, Agrocybe cylindracea lectin is a member of the galectin family, Glycoconj. J. 18 (2001) 745-749. (Pubitemid 36071937)
    • (2001) Glycoconjugate Journal , vol.18 , Issue.10 , pp. 745-749
    • Yagi, F.1    Hiroyama, H.2    Kodama, S.3
  • 10
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • C. Fred Brewer, Binding and cross-linking properties of galectins, Biochim. Biophys. Acta 1572 (2002) 255-262.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 255-262
    • Fred Brewer, C.1
  • 11
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • DOI 10.1021/bi051144z
    • T.K. Dam, H.J. Gabius, S. Andre, H. Kaltner, M. Lensch, C.F. Brewer, Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants, Biochemistry 44 (2005) 12564-12571. (Pubitemid 41324347)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    Andre, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 12
    • 35548938481 scopus 로고    scopus 로고
    • Functions of cell surface galectin-glycoprotein lattices
    • DOI 10.1016/j.sbi.2007.09.002, PII S0959440X07001303, Carbohydrates and glycoconjugates / Biophysical methods
    • G.A. Rabinovich, M.A. Toscano, S.S. Jackson, G.R. Vasta, Functions of cell surface galectin-glycoprotein lattices, Curr. Opin. Struct. Biol. 17 (2007) 513-520. (Pubitemid 350019014)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.5 , pp. 513-520
    • Rabinovich, G.A.1    Toscano, M.A.2    Jackson, S.S.3    Vasta, G.R.4
  • 15
    • 0022854422 scopus 로고
    • Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian β-galactosides
    • H. Leffler, S.H. Barondes, Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian β-galactosides, J. Biol. Chem. 261 (1986) 10119-10126.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10119-10126
    • Leffler, H.1    Barondes, S.H.2
  • 16
    • 0032574694 scopus 로고    scopus 로고
    • Thermodynamics of bovine spleen galectin-1 binding to disaccharides: Correlation with structure and its effect on oligomerization at the denaturation temperature
    • DOI 10.1021/bi9716478
    • F.P. Schwarz, H. Ahmed, M.A. Bianchet, L.M. Amzel, G.R. Vasta, Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature, Biochemistry 37 (1998) 5867-5877. (Pubitemid 28196738)
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 5867-5877
    • Schwarz, F.P.1    Ahmed, H.2    Bianchet, M.A.3    Amzel, L.M.4    Vasta, G.R.5
  • 18
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galβ1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • DOI 10.1016/j.biochi.2004.03.007, PII S0300908404000392
    • A.M. Wu, J.H. Wu, J.H. Liu, T. Singh, S. Andre, H. Kaltner, H.J. Gabius, Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galβ1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N), Biochimie 86 (2004) 317-326. (Pubitemid 38780838)
    • (2004) Biochimie , vol.86 , Issue.4-5 , pp. 317-326
    • Wu, A.M.1    Wu, J.H.2    Liu, J.-H.3    Singh, T.4    Andre, S.5    Kaltner, H.6    Gabius, H.-J.7
  • 19
    • 4644260095 scopus 로고    scopus 로고
    • Fluorescence polarization as an analytical tool to evaluate galectin-ligand interactions
    • P. Sorme, B. Kahl-Knutsson, M. Huflejt, U.J. Nilsson, H. Leffler, Fluorescence polarization as an analytical tool to evaluate galectin-ligand interactions, Anal. Biochem. 334 (2004) 36-47.
    • (2004) Anal. Biochem. , vol.334 , pp. 36-47
    • Sorme, P.1    Kahl-Knutsson, B.2    Huflejt, M.3    Nilsson, U.J.4    Leffler, H.5
  • 21
    • 41549129317 scopus 로고    scopus 로고
    • Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: A case study on galectins-1 and -3 and the impact of assay setting
    • DOI 10.1093/glycob/cwn009
    • E.M. Rapoport, S. Andre, O.V. Kurmyshkina, T.V. Pochechueva, V.V. Severov, G.V. Pazynina, H.J. Gabius, N.V. Bovin, Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: a case study on galectins-1 and -3 and the impact of assay setting, Glycobiology 18 (2008) 315-324. (Pubitemid 351461064)
    • (2008) Glycobiology , vol.18 , Issue.4 , pp. 315-324
    • Rapoport, E.M.1    Andre, S.2    Kurmyshkina, O.V.3    Pochechueva, T.V.4    Severov, V.V.5    Pazynina, G.V.6    Gabius, H.-J.7    Bovin, N.V.8
  • 24
    • 0025321165 scopus 로고
    • Binding characteristics of galactoside-binding lectin (galaptin) from human spleen
    • R.T. Lee, Y. Ichikawa, H.J. Allen, Y.C. Lee, Binding characteristics of galactoside-binding lectin (galaptin) from human spleen, J. Biol. Chem. 265 (1990) 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
  • 26
    • 33750985052 scopus 로고    scopus 로고
    • High-Throughput Analysis of Lectin-Oligosaccharide Interactions by Automated Frontal Affinity Chromatography
    • DOI 10.1016/S0076-6879(06)15019-3, PII S0076687906150193, Glycobiology
    • S. Nakamura-Tsuruta, N. Uchiyama, J. Hirabayashi, High-throughput analysis of lectin-oligosaccharide interactions by automated frontal affinity chromatography, Methods Enzymol. 415 (2006) 311-325. (Pubitemid 44751105)
    • (2006) Methods in Enzymology , vol.415 , pp. 311-325
    • Nakamura-Tsuruta, S.1    Uchiyama, N.2    Hirabayashi, J.3
  • 27
    • 38449103336 scopus 로고    scopus 로고
    • Frontal affinity chromatography: Sugar-protein interactions
    • H. Tateno, S. Nakamura-Tsuruta, J. Hirabayashi, Frontal affinity chromatography: sugar-protein interactions, Nat. Protoc. 2 (2007) 2529-2537.
    • (2007) Nat. Protoc. , vol.2 , pp. 2529-2537
    • Tateno, H.1    Nakamura-Tsuruta, S.2    Hirabayashi, J.3
  • 28
    • 0031616461 scopus 로고    scopus 로고
    • Analysis of N- and O-glycans by pyridylamination
    • S. Natsuka, S. Hase, Analysis of N- and O-glycans by pyridylamination, Methods Mol. Biol. 76 (1998) 101-113.
    • (1998) Methods Mol. Biol. , vol.76 , pp. 101-113
    • Natsuka, S.1    Hase, S.2
  • 29
    • 57049185150 scopus 로고    scopus 로고
    • Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1
    • DOI 10.1093/glycob/cwn089
    • N. Nishi, A. Abe, J. Iwaki, H. Yoshida, A. Itoh, H. Shoji, S. Kamitori, J. Hirabayashi, T. Nakamura, Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1, Glycobiology 18 (2008) 1065-1073. (Pubitemid 352762841)
    • (2008) Glycobiology , vol.18 , Issue.12 , pp. 1065-1073
    • Nishi, N.1    Abe, A.2    Iwaki, J.3    Yoshida, H.4    Itoh, A.5    Shoji, H.6    Kamitori, S.7    Hirabayashi, J.8    Nakamura, T.9
  • 30
    • 0042027823 scopus 로고    scopus 로고
    • Frontal affinity chromatography as a tool for elucidation of sugar recognition properties of lectins
    • DOI 10.1016/S0076-6879(03)01025-5
    • J. Hirabayashi, Y. Arata, K. Kasai, Frontal affinity chromatography as a tool for elucidation of sugar recognition properties of lectins, Methods Enzymol. 362 (2003) 353-368. (Pubitemid 36993059)
    • (2003) Methods in Enzymology , vol.362 , pp. 353-368
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.-I.3
  • 31
    • 0023664406 scopus 로고
    • Multiple soluble β-galactoside-binding lectins from human lung
    • C.P. Sparrow, H. Leffler, S.H. Barondes, Multiple soluble β-galactoside-binding lectins from human lung, J. Biol. Chem. 262 (1987) 7383-7390.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7383-7390
    • Sparrow, C.P.1    Leffler, H.2    Barondes, S.H.3
  • 32
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • DOI 10.1093/glycob/cwg094
    • H. Ideo, A. Seko, I. Ishizuka, K. Yamashita, The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity, Glycobiology 13 (2003) 713-723. (Pubitemid 37337052)
    • (2003) Glycobiology , vol.13 , Issue.10 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 34
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain
    • S.R. Stowell, C.M. Arthur, K.A. Slanina, J.R. Horton, D.F. Smith, R.D. Cummings, Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain, J. Biol. Chem. 283 (2008) 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
  • 35
    • 53049085180 scopus 로고    scopus 로고
    • Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins
    • H. Tateno, A.Mori, N. Uchiyama, R. Yabe, J. Iwaki, T. Shikanai, T. Angata, H.Narimatsu, J. Hirabayashi, Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins, Glycobiology 18 (2008) 789-798.
    • (2008) Glycobiology , vol.18 , pp. 789-798
    • Tateno, H.1    Mori, A.2    Uchiyama, N.3    Yabe, R.4    Iwaki, J.5    Shikanai, T.6    Angata, T.7    Narimatsu, H.8    Hirabayashi, J.9
  • 36
    • 36348976981 scopus 로고    scopus 로고
    • Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue
    • M. Nagae, N. Nishi, S. Nakamura-Tsuruta, J. Hirabayashi, S. Wakatsuki, R. Kato, Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue, J. Mol. Biol. 375 (2008) 119-135.
    • (2008) J. Mol. Biol. , vol.375 , pp. 119-135
    • Nagae, M.1    Nishi, N.2    Nakamura-Tsuruta, S.3    Hirabayashi, J.4    Wakatsuki, S.5    Kato, R.6
  • 37
    • 0037124095 scopus 로고    scopus 로고
    • Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope
    • I. Pelletier, S. Sato, Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope, J. Biol. Chem. 277 (2002) 17663-17670.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17663-17670
    • Pelletier, I.1    Sato, S.2
  • 38
    • 0028358195 scopus 로고
    • Chemical characterization of sialyl oligosaccharides isolated from tammar wallaby (Macropus eugenii) milk
    • T. Urashima, T. Saito, Y. Tsuji, Y. Taneda, T. Takasawa, M. Messer, Chemical characterization of sialyl oligosaccharides isolated from tammar wallaby (Macropus eugenii) milk, Biochim. Biophys. Acta 1200 (1994) 64-72.
    • (1994) Biochim. Biophys. Acta , vol.1200 , pp. 64-72
    • Urashima, T.1    Saito, T.2    Tsuji, Y.3    Taneda, Y.4    Takasawa, T.5    Messer, M.6
  • 40
    • 33646863285 scopus 로고    scopus 로고
    • Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: Probing its fine specificity and the effect of naturally clustered ligand presentation
    • DOI 10.1093/glycob/cwj102
    • A.M. Wu, T. Singh, J.H. Wu, M. Lensch, S. Andre, H.J. Gabius, Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation, Glycobiology 16 (2006) 524-537. (Pubitemid 43779048)
    • (2006) Glycobiology , vol.16 , Issue.6 , pp. 524-537
    • Wu, A.M.1    Singh, T.2    Wu, J.H.3    Lensch, M.4    Andre, S.5    Gabius, H.-J.6
  • 41
    • 0037137247 scopus 로고    scopus 로고
    • Glycosidation of fructose-containing disaccharides using MCM-41 material as the catalyst
    • A.M. van der Heijden, T.C. Lee, F. van Rantwijk, H. van Bekkum, Glycosidation of fructose-containing disaccharides using MCM-41 material as the catalyst, Carbohydr. Res. 337 (2002) 1993-1998.
    • (2002) Carbohydr. Res. , vol.337 , pp. 1993-1998
    • Van Der Heijden, A.M.1    Lee, T.C.2    Van Rantwijk, F.3    Van Bekkum, H.4
  • 42
    • 71049177754 scopus 로고    scopus 로고
    • Caenorhabditis elegans galectins LEC-6 and LEC-1 recognize a chemically synthesized Galβ1-4Fuc disaccharide unit which is present in Protostomia glycoconjugates
    • T. Takeuchi, K. Nishiyama, K.I. Sugiura, M. Takahashi, A. Yamada, S. Kobayashi, H. Takahashi, H. Natsugari, K.I. Kasai, Caenorhabditis elegans galectins LEC-6 and LEC-1 recognize a chemically synthesized Galβ1-4Fuc disaccharide unit which is present in Protostomia glycoconjugates, Glycobiology 19 (2009) 1503-1510.
    • (2009) Glycobiology , vol.19 , pp. 1503-1510
    • Takeuchi, T.1    Nishiyama, K.2    Sugiura, K.I.3    Takahashi, M.4    Yamada, A.5    Kobayashi, S.6    Takahashi, H.7    Natsugari, H.8    Kasai, K.I.9
  • 43
    • 33748683137 scopus 로고    scopus 로고
    • Isomer and glycomer complexities of core GlcNAcs in Caenorhabditis elegans
    • DOI 10.1093/glycob/cwl011
    • A.J. Hanneman, J.C. Rosa, D. Ashline, V.N. Reinhold, Isomer and glycomer complexities of core GlcNAcs in Caenorhabditis elegans, Glycobiology 16 (2006) 874-890. (Pubitemid 44390931)
    • (2006) Glycobiology , vol.16 , Issue.9 , pp. 874-890
    • Hanneman, A.J.1    Rosa, J.C.2    Ashline, D.3    Reinhold, V.N.4
  • 48
    • 0036353416 scopus 로고    scopus 로고
    • High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlationwith thermodynamic binding data
    • C. Svensson, S. Teneberg, C.L. Nilsson, A. Kjellberg, F.P. Schwarz, N. Sharon, U. Krengel, High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlationwith thermodynamic binding data, J. Mol. Biol. 321 (2002) 69-83.
    • (2002) J. Mol. Biol. , vol.321 , pp. 69-83
    • Svensson, C.1    Teneberg, S.2    Nilsson, C.L.3    Kjellberg, A.4    Schwarz, F.P.5    Sharon, N.6    Krengel, U.7
  • 49
    • 0035874139 scopus 로고    scopus 로고
    • Crystal structures of the peanut lectin-lactose complexat acidicpH: Retention ofunusualquaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site
    • R. Ravishankar, C.J. Thomas, K. Suguna, A. Surolia, M. Vijayan, Crystal structures of the peanut lectin-lactose complexat acidicpH: retention ofunusualquaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site, Proteins 43 (2001) 260-270.
    • (2001) Proteins , vol.43 , pp. 260-270
    • Ravishankar, R.1    Thomas, C.J.2    Suguna, K.3    Surolia, A.4    Vijayan, M.5
  • 50
    • 0030720932 scopus 로고    scopus 로고
    • X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin
    • DOI 10.1021/bi971828+
    • L.R. Olsen, A. Dessen, D. Gupta, S. Sabesan, J.C. Sacchettini, C.F. Brewer, X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin, Biochemistry 36 (1997) 15073-15080. (Pubitemid 27527971)
    • (1997) Biochemistry , vol.36 , Issue.49 , pp. 15073-15080
    • Olsen, L.R.1    Dessen, A.2    Gupta, D.3    Sabesan, S.4    Sacchettini, J.C.5    Brewer, C.F.6
  • 51
    • 0037155263 scopus 로고    scopus 로고
    • 4. X-ray crystal structure of the complex and molecular dynamics characterization of the binding site
    • DOI 10.1074/jbc.M109919200
    • W. Tempel, S. Tschampel, R.J. Woods, The xenograft antigen bound to Griffonia simplicifolia lectin 1-B4. X-ray crystal structure of the complex and molecular dynamics characterization of the binding site, J. Biol. Chem. 277 (2002) 6615-6621. (Pubitemid 34968462)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6615-6621
    • Tempel, W.1    Tschampel, S.2    Woods, R.J.3
  • 52
    • 0034634584 scopus 로고    scopus 로고
    • Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor
    • H. Feinberg, D. Torgersen, K. Drickamer, W.I. Weis, Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor, J. Biol. Chem. 275 (2000) 35176-35184.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35176-35184
    • Feinberg, H.1    Torgersen, D.2    Drickamer, K.3    Weis, W.I.4
  • 55
    • 1342306229 scopus 로고    scopus 로고
    • Human galectin-1 recognition of poly-N-acetyllactosamine and chimeric polysaccharides
    • DOI 10.1093/glycob/cwh018
    • S.R. Stowell, M. Dias-Baruffi, L. Penttila, O. Renkonen, A.K. Nyame, R.D. Cummings, Human galectin-1 recognition of poly-N-acetyllactosamine and chimeric polysaccharides, Glycobiology 14 (2004) 157-167. (Pubitemid 38263100)
    • (2004) Glycobiology , vol.14 , Issue.2 , pp. 157-167
    • Stowell, S.R.1    Dias-Baruffi, M.2    Penttila, L.3    Renkonen, O.4    Nyame, A.K.5    Cummings, R.D.6
  • 56
    • 14044272136 scopus 로고    scopus 로고
    • Dimeric galectin-1 binds with high affinity to α2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans
    • DOI 10.1074/jbc.M412019200
    • A. Leppanen, S. Stowell, O. Blixt, R.D. Cummings, Dimeric galectin-1 binds with high affinity to α2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans, J. Biol. Chem. 280 (2005) 5549-5562. (Pubitemid 40280033)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5549-5562
    • Leppanen, A.1    Stowell, S.2    Blixt, O.3    Cummings, R.D.4
  • 57
    • 77956281991 scopus 로고    scopus 로고
    • Measurement of glycan-based interactions by frontal affinity chromatography and surface plasmon resonance
    • C. Sato, N. Yamakawa, K. Kitajima, Measurement of glycan-based interactions by frontal affinity chromatography and surface plasmon resonance, Methods Enzymol. 478 (2010) 219-232.
    • (2010) Methods Enzymol. , vol.478 , pp. 219-232
    • Sato, C.1    Yamakawa, N.2    Kitajima, K.3
  • 58
    • 54549113417 scopus 로고    scopus 로고
    • Caenorhabditis elegans N-glycans containing a Gal-Fuc disaccharide unit linked to the innermost GlcNAc residue are recognized by C. elegans galectin LEC-6
    • T. Takeuchi, K. Hayama, J. Hirabayashi, K. Kasai, Caenorhabditis elegans N-glycans containing a Gal-Fuc disaccharide unit linked to the innermost GlcNAc residue are recognized by C. elegans galectin LEC-6, Glycobiology 18 (2008) 882-890.
    • (2008) Glycobiology , vol.18 , pp. 882-890
    • Takeuchi, T.1    Hayama, K.2    Hirabayashi, J.3    Kasai, K.4
  • 60
    • 0034663733 scopus 로고    scopus 로고
    • Soluble β-galactosyl-binding lectin (galectin) from toad ovary: Crystallographic studies of two protein-sugar complexes
    • DOI 10.1002/1097-0134(20000815)40:3<378::AID-PROT40>3.0.CO;2-7
    • M.A. Bianchet, H. Ahmed, G.R. Vasta, L.M. Amzel, Soluble β-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes, Proteins 40 (2000) 378-388. (Pubitemid 30624446)
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , Issue.3 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3    Amzel, L.M.4
  • 61
    • 33845987092 scopus 로고    scopus 로고
    • Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition
    • M. Nagae, N. Nishi, T. Murata, T. Usui, T. Nakamura, S. Wakatsuki, R. Kato, Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition, J. Biol. Chem. 281 (2006) 35884-35893.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35884-35893
    • Nagae, M.1    Nishi, N.2    Murata, T.3    Usui, T.4    Nakamura, T.5    Wakatsuki, S.6    Kato, R.7
  • 62
    • 23444442426 scopus 로고    scopus 로고
    • Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate
    • M. Ban, H.J. Yoon, E. Demirkan, S. Utsumi, B. Mikami, F. Yagi, Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate, J. Mol. Biol. 351 (2005) 695-706.
    • (2005) J. Mol. Biol. , vol.351 , pp. 695-706
    • Ban, M.1    Yoon, H.J.2    Demirkan, E.3    Utsumi, S.4    Mikami, B.5    Yagi, F.6
  • 63
    • 77949904604 scopus 로고    scopus 로고
    • A motif-based analysis of glycan array data to determine the specificities of glycan-binding proteins
    • A. Porter, T. Yue, L. Heeringa, S. Day, E. Suh, B.B. Haab, A motif-based analysis of glycan array data to determine the specificities of glycan-binding proteins, Glycobiology 20 (2010) 369-380.
    • (2010) Glycobiology , vol.20 , pp. 369-380
    • Porter, A.1    Yue, T.2    Heeringa, L.3    Day, S.4    Suh, E.5    Haab, B.B.6
  • 64
    • 0018578870 scopus 로고
    • Colorectal carcinoma antigens detected by hybridoma antibodies
    • H. Koprowski, Z. Steplewski, K. Mitchell, M. Herlyn, D. Herlyn, P. Fuhrer, Colorectal carcinoma antigens detected by hybridoma antibodies, Somatic Cell Genet. 5 (1979) 957-971. (Pubitemid 10132218)
    • (1979) Somatic Cell Genetics , vol.5 , Issue.6 , pp. 957-971
    • Koprowski, H.1    Steplewski, Z.2    Mitchell, K.3
  • 65
    • 0033568542 scopus 로고    scopus 로고
    • The human embryonal carcinoma marker antigen TRA-1-60 is a sialylated keratan sulfate proteoglycan
    • G. Badcock, C. Pigott, J. Goepel, P.W. Andrews, The human embryonal carcinoma marker antigen TRA-1-60 is a sialylated keratan sulfate proteoglycan, Cancer Res. 59 (1999) 4715-4719. (Pubitemid 29428981)
    • (1999) Cancer Research , vol.59 , Issue.18 , pp. 4715-4719
    • Badcock, G.1    Pigott, C.2    Goepel, J.3    Andrews, P.W.4
  • 67
    • 34447523910 scopus 로고    scopus 로고
    • Targeting the glycans of glycoproteins: A novel paradigm for antiviral therapy
    • DOI 10.1038/nrmicro1707, PII NRMICRO1707
    • J. Balzarini, Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy, Nat. Rev. Microbiol. 5 (2007) 583-597. (Pubitemid 47074114)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.8 , pp. 583-597
    • Balzarini, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.