메뉴 건너뛰기




Volumn 1572, Issue 2-3, 2002, Pages 232-254

Oligosaccharide specificity of galectins: A search by frontal affinity chromatography

Author keywords

Comparative glycomics; Dissociation constant; Frontal affinity chromatography; Galectin; Pyridylamination

Indexed keywords

CHICK GALECTIN PROTEIN; ECALECTIN; GALECTIN; GALECTIN 1; GALECTIN 2; GALECTIN 3; GALECTIN 7; GALECTIN 8; ISOPROTEIN; MUSHROOM GALECTIN PROTEIN; NEMATODE GALECTIN PROTEIN; OLIGOSACCHARIDE; PROTEIN; SPONGE GALECTIN PROTEIN; UNCLASSIFIED DRUG;

EID: 0037136406     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00311-2     Document Type: Review
Times cited : (866)

References (117)
  • 2
    • 0032509302 scopus 로고    scopus 로고
    • The C. elegans sequencing consortium, Genome sequence of the nematode Caenorhabditis elegans: a platform for investigating biology. Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 3
    • 23544461302 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams M.D., Celniker S.E., Holt R.A., Evans C.A.et al. The genome sequence of Drosophila melanogaster. Science. 291:2001;1304-1351.
    • (2001) Science , vol.291 , pp. 1304-1351
    • Adams, M.D.1    Celniker, S.E.2    Holt, R.A.3    Evans, C.A.4
  • 4
    • 0035825662 scopus 로고    scopus 로고
    • Functional annotation of a full-length mouse cDNA collection
    • Kawai J., Shinagawa A., Shibata V., Yoshino M.et al. Functional annotation of a full-length mouse cDNA collection. Nature. 409:2001;685-690.
    • (2001) Nature , vol.409 , pp. 685-690
    • Kawai, J.1    Shinagawa, A.2    Shibata, V.3    Yoshino, M.4
  • 6
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: A lesson in complexity
    • Cooper D.N.W. Galectinomics: a lesson in complexity. Biochim. Biophys. Acta. 1572:2002;209-231.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 7
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • Hirabayashi J., Kasai K. The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology. 3:1993;297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 9
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • Rabinovich G.A., Rubinstein N., Toscano M. Role of galectins in inflammatory and immunomodulatory processes. Biochim. Biophys. Acta. 1572:2002;274-284.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.3
  • 11
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • Brewer F.C., Dam T.K. Binding and cross-linking properties of galectins. Biochim. Biophys. Acta. 1572:2002;255-262.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 255-262
    • Brewer, F.C.1    Dam, T.K.2
  • 12
    • 0017295626 scopus 로고
    • Developmentally regulated lectin in embryonic chick muscle and a myogenic cell line
    • Nowak T.P., Haywood O.L., Barondes S.H. Developmentally regulated lectin in embryonic chick muscle and a myogenic cell line. Biochem. Biophys. Res. Commun. 69:1976;650-657.
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 650-657
    • Nowak, T.P.1    Haywood, O.L.2    Barondes, S.H.3
  • 13
    • 0023304892 scopus 로고
    • Complete amino acid sequence of 14 kDa β-galactoside-binding lectin of chick embryo
    • Hirabayashi J., Kawasaki H., Suzuki K., Kasai K. Complete amino acid sequence of 14 kDa β-galactoside-binding lectin of chick embryo. J. Biochem. (Tokyo). 101:1987;775-787.
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 775-787
    • Hirabayashi, J.1    Kawasaki, H.2    Suzuki, K.3    Kasai, K.4
  • 14
    • 0023318256 scopus 로고
    • Further characterization and structural studies on human placenta lectin
    • Hirabayashi J., Kawasaki H., Suzuki K., Kasai K. Further characterization and structural studies on human placenta lectin. J. Biochem. (Tokyo). 101:1987;987-995.
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 987-995
    • Hirabayashi, J.1    Kawasaki, H.2    Suzuki, K.3    Kasai, K.4
  • 15
    • 0026572371 scopus 로고
    • Characterization of carbohydrate-binding specificity of concanavalin A by competitive binding of pyridylamino sugar chains
    • Mega T., Oku H., Hase S. Characterization of carbohydrate-binding specificity of concanavalin A by competitive binding of pyridylamino sugar chains. J. Biochem. (Tokyo). 111:1992;396-400.
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 396-400
    • Mega, T.1    Oku, H.2    Hase, S.3
  • 16
    • 0022854422 scopus 로고
    • Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian β-galactosides
    • Leffler H., Barondes S.H. 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
  • 17
    • 0023664406 scopus 로고
    • Multiple soluble β-galactoside-binding lectins from human lung
    • Sparrow C.P., Leffler H., Barondes S.H. 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
  • 18
    • 0027457991 scopus 로고
    • Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain
    • Oda Y., Herrmann J., Gitt M.A., Turck C.W., Burlingame A.L., Barondes S.H., Leffler H. Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain. J. Biol. Chem. 268:1993;5929-5939.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5929-5939
    • Oda, Y.1    Herrmann, J.2    Gitt, M.A.3    Turck, C.W.4    Burlingame, A.L.5    Barondes, S.H.6    Leffler, H.7
  • 20
    • 0030447353 scopus 로고    scopus 로고
    • The primary structure and carbohydrate specificity of a β-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis
    • Ahmed H., Pohl J., Fink N.E., Strobel F., Vasta G.R. The primary structure and carbohydrate specificity of a β-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis. J. Biol. Chem. 271:1996;33083-33094.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33083-33094
    • Ahmed, H.1    Pohl, J.2    Fink, N.E.3    Strobel, F.4    Vasta, G.R.5
  • 21
    • 0028300654 scopus 로고
    • Kinetic measurement of the interaction between an oligosaccharide and lectins by a biosensor based on surface plasmon resonance
    • Shinohara Y., Kim F., Shimizu M., Goto M., Tosu M., Hasegawa Y. Kinetic measurement of the interaction between an oligosaccharide and lectins by a biosensor based on surface plasmon resonance. Eur. J. Biochem. 223:1994;189-194.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 189-194
    • Shinohara, Y.1    Kim, F.2    Shimizu, M.3    Goto, M.4    Tosu, M.5    Hasegawa, Y.6
  • 22
    • 0028287889 scopus 로고
    • Interaction of immobilized recombinant mouse C-type macrophage lectin with glycopeptides and oligosaccharides
    • Yamamoto K., Ishida C., Shinohara Y., Hasegawa Y., Konami Y., Osawa T., Irimura T. Interaction of immobilized recombinant mouse C-type macrophage lectin with glycopeptides and oligosaccharides. Biochemistry. 33:1994;8159-8166.
    • (1994) Biochemistry , vol.33 , pp. 8159-8166
    • Yamamoto, K.1    Ishida, C.2    Shinohara, Y.3    Hasegawa, Y.4    Konami, Y.5    Osawa, T.6    Irimura, T.7
  • 23
    • 0036160022 scopus 로고    scopus 로고
    • Determination of the affinity constants of recombinant human galectin-1 and -3 for simple saccharides by capillary affinophoresis
    • Shimura K., Arata Y., Uchiyama N., Hirabayashi J., Kasai K. Determination of the affinity constants of recombinant human galectin-1 and -3 for simple saccharides by capillary affinophoresis. J. Chromatogr., B, Biomed. Sci. Appl. 768:2002;199-210.
    • (2002) J. Chromatogr., B, Biomed. Sci. Appl. , vol.768 , pp. 199-210
    • Shimura, K.1    Arata, Y.2    Uchiyama, N.3    Hirabayashi, J.4    Kasai, K.5
  • 24
    • 0022467156 scopus 로고
    • Frontal affinity chromatography: Theory, for its application to studies on specific interaction of biomolecules
    • Kasai K., Oda Y., Nishikawa M., Ishii S. Frontal affinity chromatography: theory, for its application to studies on specific interaction of biomolecules. J. Chromatogr. 376:1986;33-47.
    • (1986) J. Chromatogr. , vol.376 , pp. 33-47
    • Kasai, K.1    Oda, Y.2    Nishikawa, M.3    Ishii, S.4
  • 25
    • 0034714622 scopus 로고    scopus 로고
    • Reinforcement of frontal affinity chromatography for effective analysis of lectin-oligosaccharide interactions
    • Hirabayashi J., Arata Y., Kasai K. Reinforcement of frontal affinity chromatography for effective analysis of lectin-oligosaccharide interactions. J. Chromatogr., A. 890:2000;261-271.
    • (2000) J. Chromatogr., A , vol.890 , pp. 261-271
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.3
  • 26
    • 0035793553 scopus 로고    scopus 로고
    • Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans: Detailed analysis by an improved frontal affinity chromatography method
    • Arata Y., Hirabayashi J., Kasai K. Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans: detailed analysis by an improved frontal affinity chromatography method. J. Biol. Chem. 276:2001;3068-3077.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3068-3077
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 28
    • 0031616461 scopus 로고    scopus 로고
    • Analysis of N- and O-glycans by pyridylamination
    • E.F. Hounsell. Totowa, NJ: Humana Press
    • Natsuka S., Hase S. Analysis of N- and O-glycans by pyridylamination. Hounsell E.F. Methods in Molecular Biology. vol. 76:1998;101-113 Humana Press, Totowa, NJ.
    • (1998) Methods in Molecular Biology , vol.76 , pp. 101-113
    • Natsuka, S.1    Hase, S.2
  • 29
    • 0032533672 scopus 로고    scopus 로고
    • Contribution of component monosaccharides to the coordinates of neutral and sialyl pyridylaminated N-glycans on a two-dimensional sugar map
    • Tomiya N., Takahashi N. Contribution of component monosaccharides to the coordinates of neutral and sialyl pyridylaminated N-glycans on a two-dimensional sugar map. Anal. Biochem. 264:1998;204-210.
    • (1998) Anal. Biochem. , vol.264 , pp. 204-210
    • Tomiya, N.1    Takahashi, N.2
  • 30
    • 0023678267 scopus 로고
    • Complete amino acid sequence of a β-galactoside-binding lectin from human placenta
    • Hirabayashi J., Kasai K. Complete amino acid sequence of a β-galactoside-binding lectin from human placenta. J. Biochem. (Tokyo). 104:1988;1-4.
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 1-4
    • Hirabayashi, J.1    Kasai, K.2
  • 31
    • 0024382081 scopus 로고
    • Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa β-galactoside-binding lectin
    • Hirabayashi J., Ayaki H., Soma G., Kasai K. Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa β-galactoside-binding lectin. Biochim. Biophys. Acta. 1008:1989;85-91.
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 85-91
    • Hirabayashi, J.1    Ayaki, H.2    Soma, G.3    Kasai, K.4
  • 32
    • 0024356783 scopus 로고
    • Production and purification of a recombinant human 14 kDa β-galactoside-binding lectin
    • Hirabayashi J., Ayaki H., Soma G., Kasai K. Production and purification of a recombinant human 14 kDa β-galactoside-binding lectin. FEBS Lett. 250:1989;161-165.
    • (1989) FEBS Lett. , vol.250 , pp. 161-165
    • Hirabayashi, J.1    Ayaki, H.2    Soma, G.3    Kasai, K.4
  • 34
    • 0033555134 scopus 로고    scopus 로고
    • Identification and cloning of rat galectin-2: Expression is predominantly in epithelial cells of the stomach
    • Oka T., Murakami S., Arata Y., Hirabayashi J., Kasai K., Wada Y., Futai M. Identification and cloning of rat galectin-2: expression is predominantly in epithelial cells of the stomach. Arch. Biochem. Biophys. 364:1999;195-201.
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 195-201
    • Oka, T.1    Murakami, S.2    Arata, Y.3    Hirabayashi, J.4    Kasai, K.5    Wada, Y.6    Futai, M.7
  • 35
    • 0025859725 scopus 로고
    • Human breast carcinoma cDNA encoding a galactoside-binding lectin homologous to mouse Mac-2 antigen
    • Oda Y., Leffler H., Sakakura Y., Kasai K., Barondes S.H. Human breast carcinoma cDNA encoding a galactoside-binding lectin homologous to mouse Mac-2 antigen. Gene. 99:1991;279-283.
    • (1991) Gene , vol.99 , pp. 279-283
    • Oda, Y.1    Leffler, H.2    Sakakura, Y.3    Kasai, K.4    Barondes, S.H.5
  • 37
    • 0028923675 scopus 로고
    • Galectin-7, a human 14-kDa S-lectin, specifically expressed in keratinocytes and sensitive to retinoic acid
    • Magnaldo T., Bernerd F., Darmon M. Galectin-7, a human 14-kDa S-lectin, specifically expressed in keratinocytes and sensitive to retinoic acid. Dev. Biol. 168:1995;259-271.
    • (1995) Dev. Biol. , vol.168 , pp. 259-271
    • Magnaldo, T.1    Bernerd, F.2    Darmon, M.3
  • 39
    • 0042291641 scopus 로고    scopus 로고
    • Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease
    • Tureci O., Schmitt H., Fadle N., Pfreundschuh M., Sahin U. Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease. J. Biol. Chem. 272:1997;6416-6422.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6416-6422
    • Tureci, O.1    Schmitt, H.2    Fadle, N.3    Pfreundschuh, M.4    Sahin, U.5
  • 40
    • 0031048272 scopus 로고    scopus 로고
    • Identification and characterization of galectin-9, a novel β-galactoside-binding mammalian lectin
    • Wada J., Kanwar Y.S. Identification and characterization of galectin-9, a novel β-galactoside-binding mammalian lectin. J. Biol. Chem. 272:1997;6078-6086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6078-6086
    • Wada, J.1    Kanwar, Y.S.2
  • 43
    • 0025642403 scopus 로고
    • Structure of chicken 16-kDa β-galactoside-binding lectin: Complete amino acid sequence, cloning of cDNA and production of recombinant lectin
    • Sakakura Y., Hirabayashi J., Oda Y., Ohyama Y., Kasai K. Structure of chicken 16-kDa β-galactoside-binding lectin: complete amino acid sequence, cloning of cDNA and production of recombinant lectin. J. Biol. Chem. 265:1990;21573-21579.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21573-21579
    • Sakakura, Y.1    Hirabayashi, J.2    Oda, Y.3    Ohyama, Y.4    Kasai, K.5
  • 44
    • 0026694658 scopus 로고
    • Evidence that Caenorhabditis elegans 32-kDa β-galactoside-binding protein is homologous to vertebrate β-galactoside-binding lectins
    • Hirabayashi J., Satoh M., Kasai K. Evidence that Caenorhabditis elegans 32-kDa β-galactoside-binding protein is homologous to vertebrate β-galactoside-binding lectins. 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
  • 45
    • 0030705195 scopus 로고    scopus 로고
    • Structure of the 32-kDa galectin gene of the nematode Caenorhabditis elegans
    • Arata Y., Hirabayashi J., Kasai K. Structure of the 32-kDa galectin gene of the nematode Caenorhabditis elegans. J. Biol. Chem. 272:1997;26669-26677.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26669-26677
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 46
    • 0030023715 scopus 로고    scopus 로고
    • Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans
    • Hirabayashi J., Ubukata T., Kasai K. Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans. J. Biol. Chem. 271:1996;2497-2505.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2497-2505
    • Hirabayashi, J.1    Ubukata, T.2    Kasai, K.3
  • 47
    • 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
    • Pfeifer K., Haasemann M., Gamulin V., Bretting H., Fahrenholz F., Muller W.E.G. S-type lectins occur also in invertebrates: high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium. Glycobiology. 3:1993;179-184.
    • (1993) Glycobiology , vol.3 , pp. 179-184
    • Pfeifer, K.1    Haasemann, M.2    Gamulin, V.3    Bretting, H.4    Fahrenholz, F.5    Muller, W.E.G.6
  • 48
    • 0031002992 scopus 로고    scopus 로고
    • Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin
    • Yagi F., Miyamoto M., Abe T., Minami Y., Tadera K., Goldstein I.J. Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin. Glycoconj. J. 14:1997;281-288.
    • (1997) Glycoconj. J. , vol.14 , pp. 281-288
    • Yagi, F.1    Miyamoto, M.2    Abe, T.3    Minami, Y.4    Tadera, K.5    Goldstein, I.J.6
  • 49
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein
    • Liao D.-I., Kapadia G., Ahmed H., Vasta G.R., Herzberg O. Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein. Proc. Natl. Acad. Sci. U. S. A. 91:1994;1428-1432.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1428-1432
    • Liao, D.-I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 51
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9 A resolution
    • Lobsanov Y.D., Gitt M.A., Leffler H., Barondes S.H., Rini J. X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9 A resolution. J. Biol. Chem. 268:1993;27034-27038.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3    Barondes, S.H.4    Rini, J.5
  • 52
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution
    • Seetharaman J., Kanigsberg A., Slaaby R., Leffler H., Barondes S.H., Rini M. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution. J. Biocl. Chem. 273:1998;13047-13052.
    • (1998) J. Biocl. Chem. , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, M.6
  • 54
    • 0033607322 scopus 로고    scopus 로고
    • The 2.15 A crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin
    • Varela P.F., Solis D., Diaz-Maurino T., Kaltner H., Gabius H.-J., Romero A. The 2.15 A crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin. J. Mol. Biol. 294:1999;537-549.
    • (1999) J. Mol. Biol. , vol.294 , pp. 537-549
    • Varela, P.F.1    Solis, D.2    Diaz-Maurino, T.3    Kaltner, H.4    Gabius, H.-J.5    Romero, A.6
  • 55
    • 0026007210 scopus 로고
    • Soluble 14-kDa β-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain
    • Abbott W.M., Feizi T. Soluble 14-kDa β-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain. J. Biol. Chem. 266:1989;5552-5557.
    • (1989) J. Biol. Chem. , vol.266 , pp. 5552-5557
    • Abbott, W.M.1    Feizi, T.2
  • 56
    • 0026344814 scopus 로고
    • Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside binding lectin
    • Hirabayashi J., Kasai K. Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside binding lectin. J. Biol. Chem. 266:1991;23648-23653.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23648-23653
    • Hirabayashi, J.1    Kasai, K.2
  • 57
    • 0029995399 scopus 로고    scopus 로고
    • Forssman disaccharide is the specific ligand of a galectin from the sponge Geodia cydonium but does not mediate its binding to nuclear protein np56
    • Hanisch F.G., Baldus S.E., Kummel T.A. Forssman disaccharide is the specific ligand of a galectin from the sponge Geodia cydonium but does not mediate its binding to nuclear protein np56. Glycobiology. 6:1996;321-336.
    • (1996) Glycobiology , vol.6 , pp. 321-336
    • Hanisch, F.G.1    Baldus, S.E.2    Kummel, T.A.3
  • 58
    • 0344995240 scopus 로고    scopus 로고
    • Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): A crystallographic study at 1.8 A resolution
    • Swaminathan G.J., Leonidas D.D., Savage M.P., Ackerman S.J., Acharya K.R. Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 38:1999;13837-13843.
    • (1999) Biochemistry , vol.38 , pp. 13837-13843
    • Swaminathan, G.J.1    Leonidas, D.D.2    Savage, M.P.3    Ackerman, S.J.4    Acharya, K.R.5
  • 59
    • 0021188441 scopus 로고
    • Photochemical cross-linking of β-galactoside-binding lectin to polylactosamino-proteoglycan of chick embryonic skin
    • Oda Y., Kasai K. Photochemical cross-linking of β-galactoside-binding lectin to polylactosamino-proteoglycan of chick embryonic skin. Biochem. Biophys. Res. Commun. 123:1984;1215-1220.
    • (1984) Biochem. Biophys. Res. Commun. , vol.123 , pp. 1215-1220
    • Oda, Y.1    Kasai, K.2
  • 60
    • 0026672573 scopus 로고
    • Identification of a 14-kDa laminin binding protein (HLBP14) in human melanoma cells that is identical to the 14-kDa galactoside binding lectin
    • Castronovo V., Luyten F., van den Brule F., Sobel M.E. Identification of a 14-kDa laminin binding protein (HLBP14) in human melanoma cells that is identical to the 14-kDa galactoside binding lectin. Arch. Biochem. Biophys. 297:1992;132-138.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 132-138
    • Castronovo, V.1    Luyten, F.2    Van den Brule, F.3    Sobel, M.E.4
  • 61
    • 0025317697 scopus 로고
    • The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2)
    • Woo H.J., Shaw L.M., Messier J.M., Mercurio A.M. The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2). J. Biol. Chem. 265:1990;7097-7099.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7097-7099
    • Woo, H.J.1    Shaw, L.M.2    Messier, J.M.3    Mercurio, A.M.4
  • 62
    • 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. 263:1988;16143-16149.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16143-16149
    • Merkle, R.K.1    Cummings, R.D.2
  • 63
    • 0032913440 scopus 로고    scopus 로고
    • Enzymatic synthesis of natural and 13C enriched linear poly-N-acetyllactosamines as ligands for galectin-1
    • Di Virgilio S., Glushka J., Moremen K., Pierce M. Enzymatic synthesis of natural and 13C enriched linear poly-N-acetyllactosamines as ligands for galectin-1. Glycobiology. 9:1999;353-364.
    • (1999) Glycobiology , vol.9 , pp. 353-364
    • Di Virgilio, S.1    Glushka, J.2    Moremen, K.3    Pierce, M.4
  • 67
    • 0035808666 scopus 로고    scopus 로고
    • Application of reinforced frontal affinity chromatography and advanced processing procedure to the study of the binding property of a Caenorhabditis elegans galectin
    • Arata Y., Hirabayashi J., Kasai K. Application of reinforced frontal affinity chromatography and advanced processing procedure to the study of the binding property of a Caenorhabditis elegans galectin. J. Chromatogr., A. 905:2001;337-343.
    • (2001) J. Chromatogr., A , vol.905 , pp. 337-343
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 68
    • 0022514861 scopus 로고
    • Oxidation and chemical modification of lung β-galactoside-specific lectin
    • Whitney P.L., Powell J.T., Sanford G.L. Oxidation and chemical modification of lung β-galactoside-specific lectin. Biochem. J. 238:1986;683-689.
    • (1986) Biochem. J. , vol.238 , pp. 683-689
    • Whitney, P.L.1    Powell, J.T.2    Sanford, G.L.3
  • 69
    • 0026739782 scopus 로고
    • Subunit molecular mass assignment of 14,654 Da to the soluble β-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation
    • Tracy B.M., Feizi T., Abbott W.M., Carruthers R.A., Green B.N., Lawson A.M. Subunit molecular mass assignment of 14,654 Da to the soluble β-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation. J. Biol. Chem. 267:1992;10342-10347.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10342-10347
    • Tracy, B.M.1    Feizi, T.2    Abbott, W.M.3    Carruthers, R.A.4    Green, B.N.5    Lawson, A.M.6
  • 70
    • 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. 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
  • 71
    • 0021772463 scopus 로고
    • New synthetic cluster ligands for galactose/N-acetylgalactosamine-specific lectin of mammalian liver
    • Lee R.T., Lin P., Lee Y.C. New synthetic cluster ligands for galactose/N-acetylgalactosamine-specific lectin of mammalian liver. Biochemistry. 23:1984;4255-4261.
    • (1984) Biochemistry , vol.23 , pp. 4255-4261
    • Lee, R.T.1    Lin, P.2    Lee, Y.C.3
  • 72
    • 0024418546 scopus 로고
    • Binding characteristics of N-acetylglucosamine-specific lectin of the isolated chicken hepatocytes: Similarities to mammalian hepatic galactose/N-acetylgalactosamine-specific lectin
    • Lee R.T., Rice K.G., Rao N.B., Ichikawa Y., Barthel T., Piskarev V., Lee Y.C. Binding characteristics of N-acetylglucosamine-specific lectin of the isolated chicken hepatocytes: similarities to mammalian hepatic galactose/N-acetylgalactosamine-specific lectin. Biochemistry. 28:1989;8351-8358.
    • (1989) Biochemistry , vol.28 , pp. 8351-8358
    • Lee, R.T.1    Rice, K.G.2    Rao, N.B.3    Ichikawa, Y.4    Barthel, T.5    Piskarev, V.6    Lee, Y.C.7
  • 73
    • 0025906415 scopus 로고
    • Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A): Homology of binding site architecture with mammalian and chicken hepatic lectins
    • Lee R.T., Ichikawa Y., Fay M., Drickamer K., Shao M.C., Lee Y.C. Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A): homology of binding site architecture with mammalian and chicken hepatic lectins. J. Biol. Chem. 266:1991;4810-4815.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4810-4815
    • Lee, R.T.1    Ichikawa, Y.2    Fay, M.3    Drickamer, K.4    Shao, M.C.5    Lee, Y.C.6
  • 74
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: An historical introduction and overview
    • Kilpatrick D.C. Animal lectins: an historical introduction and overview. Biochim. Biophys. Acta. 1572:2002;187-197.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 75
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondoroitin sulfate receptors
    • Weigel P.H., Yiki J.H.N. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondoroitin sulfate receptors. Biochim. Biophys. Acta. 1572:2002;341-363.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yiki, J.H.N.2
  • 77
    • 0032080122 scopus 로고    scopus 로고
    • Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • Kopitz J., von Reitzenstein C., Burchert M., Cantz M., Gabius H.-J. Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture. J. Biol. Chem. 273:1998;11205-11211.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11205-11211
    • Kopitz, J.1    Von Reitzenstein, C.2    Burchert, M.3    Cantz, M.4    Gabius, H.-J.5
  • 78
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3
    • Kopitz J., von Reitzenstein C., Andre S., Kaltner H., Uhl J., Ehemann V., Cantz M., Gabius H.-J. Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3. J. Biol. Chem. 276:2001;35917-35923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35917-35923
    • Kopitz, J.1    Von Reitzenstein, C.2    Andre, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6    Cantz, M.7    Gabius, H.-J.8
  • 79
    • 0023038671 scopus 로고
    • Evidence that a human soluble β-galactoside-binding lectin is encoded by a family of genes
    • Gitt M.A., Barondes S.H. Evidence that a human soluble β-galactoside-binding lectin is encoded by a family of genes. Proc. Natl. Acad. Sci. U. S. A. 83:1986;7603-7607.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 7603-7607
    • Gitt, M.A.1    Barondes, S.H.2
  • 80
    • 0026768317 scopus 로고
    • Isolation and expression of a gene encoding L-14-II, a new human soluble lactose-binding lectin
    • Gitt M.A., Massa S.M., Leffler H., Barondes S.H. Isolation and expression of a gene encoding L-14-II, a new human soluble lactose-binding lectin. J. Biol. Chem. 267:1992;10601-10606.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10601-10606
    • Gitt, M.A.1    Massa, S.M.2    Leffler, H.3    Barondes, S.H.4
  • 81
    • 0023488847 scopus 로고
    • Endogenous galactoside-binding lectins: A new class of functional tumor cell surface molecules related to metastasis
    • Raz A., Lotan R. Endogenous galactoside-binding lectins: a new class of functional tumor cell surface molecules related to metastasis. Cancer Metastasis Rev. 6:1987;433-452.
    • (1987) Cancer Metastasis Rev. , vol.6 , pp. 433-452
    • Raz, A.1    Lotan, R.2
  • 82
    • 0028047113 scopus 로고
    • Mac-2: A versatile galactose-binding protein of mammalian tissues
    • Hughes R.C. Mac-2: a versatile galactose-binding protein of mammalian tissues. Glycobiology. 4:1994;5-12.
    • (1994) Glycobiology , vol.4 , pp. 5-12
    • Hughes, R.C.1
  • 85
    • 0027492711 scopus 로고
    • L-29, an endogenous lectin, binds to glycoconjugate ligands with positive cooperativity
    • Massa S.M., Cooper D.N., Leffler H., Barondes S.H. L-29, an endogenous lectin, binds to glycoconjugate ligands with positive cooperativity. Biochemistry. 32:1993;260-267.
    • (1993) Biochemistry , vol.32 , pp. 260-267
    • Massa, S.M.1    Cooper, D.N.2    Leffler, H.3    Barondes, S.H.4
  • 86
    • 0026673762 scopus 로고
    • Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin
    • Sato S., Hughes R.C. Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. J. Biol. Chem. 267:1992;6983-6990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6983-6990
    • Sato, S.1    Hughes, R.C.2
  • 87
    • 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. 268:1993;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
  • 88
    • 0028217573 scopus 로고
    • Adhesive specificity of the soluble human lectin, IgE-binding protein (εBP), towards lipid-linked oligosaccharides. Presence of the blood group A, B, B-like and H monosaccharides confers a binding activity to tetrasaccharide (lacto-N- and lacto-N-neotetraose) backbones
    • Feizi T., Solomon J.C., Yuen C.-T., Jeng K.C.G., Frigeri L.G., Hsu D.K., Liu F.-T. Adhesive specificity of the soluble human lectin, IgE-binding protein (εBP), towards lipid-linked oligosaccharides. Presence of the blood group A, B, B-like and H monosaccharides confers a binding activity to tetrasaccharide (lacto-N- and lacto-N-neotetraose) backbones. Biochemistry. 33:1994;6342-6349.
    • (1994) Biochemistry , vol.33 , pp. 6342-6349
    • Feizi, T.1    Solomon, J.C.2    Yuen, C.-T.3    Jeng, K.C.G.4    Frigeri, L.G.5    Hsu, D.K.6    Liu, F.-T.7
  • 89
    • 0033661405 scopus 로고    scopus 로고
    • Molecular modeling and mutagenesis studies of the N-terminal domains of galectin-3: Evidence for participation with the C-terminal carbohydrate recognition domain in oligosaccharide binding
    • Barboni E.A., Bawumia S., Henrick K., Hughes R.C. Molecular modeling and mutagenesis studies of the N-terminal domains of galectin-3: evidence for participation with the C-terminal carbohydrate recognition domain in oligosaccharide binding. Glycobiology. 10:2000;1201-1208.
    • (2000) Glycobiology , vol.10 , pp. 1201-1208
    • Barboni, E.A.1    Bawumia, S.2    Henrick, K.3    Hughes, R.C.4
  • 90
    • 0033914833 scopus 로고    scopus 로고
    • β-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3
    • Fradin C., Poulain D., Jouault T. β-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3. Infect. Immun. 68:2000;4391-4398.
    • (2000) Infect. Immun. , vol.68 , pp. 4391-4398
    • Fradin, C.1    Poulain, D.2    Jouault, T.3
  • 91
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • Demetriou M., Granovsky M., Quaggin S., Dennis J.W. Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature. 409:2001;733-739.
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 92
    • 0033613211 scopus 로고    scopus 로고
    • Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes
    • Bernerd F., Sarasin A., Magnaldo T. Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes. Proc. Natl. Acad. Sci. U. S. A. 96:1999;11329-11334.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11329-11334
    • Bernerd, F.1    Sarasin, A.2    Magnaldo, T.3
  • 93
    • 0036479302 scopus 로고    scopus 로고
    • Galectin-7 (PIG1) exhibits pro-apoptotic function through JNK activation and mitochondrial cytochrome c release
    • Kuwabara I., Kuwabara Y., Yang R.Y., Schuler M., Green D.R., Zuraw B.L., Hsu D.K., Liu F.-T. Galectin-7 (PIG1) exhibits pro-apoptotic function through JNK activation and mitochondrial cytochrome c release. J. Biol. Chem. 277:2002;3487-3497.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3487-3497
    • Kuwabara, I.1    Kuwabara, Y.2    Yang, R.Y.3    Schuler, M.4    Green, D.R.5    Zuraw, B.L.6    Hsu, D.K.7    Liu, F.-T.8
  • 94
    • 0032579502 scopus 로고    scopus 로고
    • Galectin-4 and galectin-6 are two closely related lectins expressed in mouse gastrointestinal tract
    • Gitt M.A., Colnot C., Poirier F., Nani K.J., Barondes S.H., Leffler H. Galectin-4 and galectin-6 are two closely related lectins expressed in mouse gastrointestinal tract. J. Biol. Chem. 273:1998;2954-2960.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2954-2960
    • Gitt, M.A.1    Colnot, C.2    Poirier, F.3    Nani, K.J.4    Barondes, S.H.5    Leffler, H.6
  • 98
    • 0019152144 scopus 로고
    • Two lactose binding lectins from chicken tissues: Purified lectin from intestine is different from those in liver and muscle
    • Beyer E.C., Zweig S.E., Barondes S.H. Two lactose binding lectins from chicken tissues: purified lectin from intestine is different from those in liver and muscle. J. Biol. Chem. 255:1980;4236-4239.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4236-4239
    • Beyer, E.C.1    Zweig, S.E.2    Barondes, S.H.3
  • 100
    • 0028786452 scopus 로고
    • Differential binding of two chicken β-galactoside-specific lectins to homologous lymphocyte subpopulations and evidence for inhibitor activity of the dimeric lectin on stimulated T cells
    • Schneller M., Andre S., Cihak J., Kaltner H., Merkle H., Rademaker G.J., Haverkamp J., Thomas-Oates J.E., Losch U., Gabius H.-J. Differential binding of two chicken β-galactoside-specific lectins to homologous lymphocyte subpopulations and evidence for inhibitor activity of the dimeric lectin on stimulated T cells. Cell Immunol. 166:1995;35-43.
    • (1995) Cell Immunol. , vol.166 , pp. 35-43
    • Schneller, M.1    Andre, S.2    Cihak, J.3    Kaltner, H.4    Merkle, H.5    Rademaker, G.J.6    Haverkamp, J.7    Thomas-Oates, J.E.8    Losch, U.9    Gabius, H.-J.10
  • 101
    • 17544377102 scopus 로고    scopus 로고
    • Differentital architecture of the combining site of the two chicken galectins revealed by chemical mapping studies with synthetic ligand derivatives
    • Solis D., Romero A., Kaltner H., Gabius H.-J., Diaz-Maurino T. Differentital architecture of the combining site of the two chicken galectins revealed by chemical mapping studies with synthetic ligand derivatives. J. Biol. Chem. 271:1996;12744-12748.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solis, D.1    Romero, A.2    Kaltner, H.3    Gabius, H.-J.4    Diaz-Maurino, T.5
  • 102
    • 0035884413 scopus 로고    scopus 로고
    • Carbohydrate specificity of a galectin from chicken liver (CG-16)
    • Wu A.M., Wu J.H., Tsai M.S., Kaltner H., Gabius H.J. Carbohydrate specificity of a galectin from chicken liver (CG-16). Biochem. J. 358:2001;529-538.
    • (2001) Biochem. J. , vol.358 , pp. 529-538
    • Wu, A.M.1    Wu, J.H.2    Tsai, M.S.3    Kaltner, H.4    Gabius, H.J.5
  • 103
    • 0031523724 scopus 로고    scopus 로고
    • Galectins from the nematode Caenorhabditis elegans and the genome project
    • Hirabayashi J., Arata Y., Kasai K. Galectins from the nematode Caenorhabditis elegans and the genome project. Trends Glycosci. Glycotechnol. 9:1997;113-122.
    • (1997) Trends Glycosci. Glycotechnol. , vol.9 , pp. 113-122
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.3
  • 105
    • 0030758114 scopus 로고    scopus 로고
    • The two lectin domains of the tandem-repeat 32-kDa galectin of the nematode Caenorhabditis elegans have different binding properties: Studies with recombinant protein
    • Arata Y., Hirabayashi J., Kasai K. The two lectin domains of the tandem-repeat 32-kDa galectin of the nematode Caenorhabditis elegans have different binding properties: studies with recombinant protein. J. Biochem. (Tokyo). 121:1997;1002-1009.
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 1002-1009
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 107
    • 0026530019 scopus 로고
    • Purification and characterization of β-galactoside-binding proteins from Caenorhabditis elegans
    • Hirabayashi J., Satoh M., Ohyama Y., Kasai K. Purification and characterization of β-galactoside-binding proteins from Caenorhabditis elegans. J. Biochem. (Tokyo). 111:1992;553-555.
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 553-555
    • Hirabayashi, J.1    Satoh, M.2    Ohyama, Y.3    Kasai, K.4
  • 109
    • 0029908797 scopus 로고    scopus 로고
    • Thermodynamics of carbohydrate binding to galectin-1 from Chinese hamster ovary cells and two mutants: A comparison with four galactose-specific plant lectins
    • Gupta D., Cho M., Cummings R.D., Brewer C.F. Thermodynamics of carbohydrate binding to galectin-1 from Chinese hamster ovary cells and two mutants: a comparison with four galactose-specific plant lectins. Biochemistry. 35:1996;15236-15243.
    • (1996) Biochemistry , vol.35 , pp. 15236-15243
    • Gupta, D.1    Cho, M.2    Cummings, R.D.3    Brewer, C.F.4
  • 111
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris R. Principles of structures of animal and plant lectins. Biochim. Biophys. Acta. 1572:2002;198-208.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 114
    • 0033215424 scopus 로고    scopus 로고
    • Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1
    • Pace K.E., Lee C., Stewart P.L., Baum L.G. Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1. J. Immunol. 163:1999;3801-3811.
    • (1999) J. Immunol. , vol.163 , pp. 3801-3811
    • Pace, K.E.1    Lee, C.2    Stewart, P.L.3    Baum, L.G.4
  • 115
    • 0035852973 scopus 로고    scopus 로고
    • Multivalent protein-carbohydrate interactions: A new paradigm for supermolecular assembly and signal transduction
    • Sacchettini J.C., Baum L.G., Brewer C.F. Multivalent protein-carbohydrate interactions: a new paradigm for supermolecular assembly and signal transduction. Biochemistry. 40:2001;3009-3015.
    • (2001) Biochemistry , vol.40 , pp. 3009-3015
    • Sacchettini, J.C.1    Baum, L.G.2    Brewer, C.F.3
  • 116
    • 0035260267 scopus 로고    scopus 로고
    • Glycome project: Concept, strategy and preliminary application to C. elegans
    • Hirabayashi J., Arata Y., Kasai K. Glycome project: concept, strategy and preliminary application to C. elegans. Proteomics. 1:2001;295-303.
    • (2001) Proteomics , vol.1 , pp. 295-303
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.3
  • 117
    • 0030236933 scopus 로고    scopus 로고
    • On the origin of elementary hexoses
    • Hirabayashi J. On the origin of elementary hexoses. Q. Rev. Biol. 71:1996;365-380.
    • (1996) Q. Rev. Biol. , vol.71 , pp. 365-380
    • Hirabayashi, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.