메뉴 건너뛰기




Volumn 15, Issue 8-9, 1997, Pages 583-592

Modular organization of carbohydrate recognition domains in animal lectins

Author keywords

C type lectins; Carbohydrate recognition domains; Galectins; P type lectins

Indexed keywords

CARBOHYDRATE; GALECTIN; GLYCOCONJUGATE; LECTIN; OLIGOSACCHARIDE;

EID: 0030889185     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(97)90035-4     Document Type: Article
Times cited : (42)

References (64)
  • 5
    • 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
  • 6
    • 0025786162 scopus 로고
    • Endogenous muscle lectin inhibits myoblast adhesion to laminin
    • Cooper D.N., Massa S.M., Barondes S.H. Endogenous muscle lectin inhibits myoblast adhesion to laminin. J. Cell. Biol. 115:1991;1437-1448.
    • (1991) J. Cell. Biol. , vol.115 , pp. 1437-1448
    • Cooper, D.N.1    Massa, S.M.2    Barondes, S.H.3
  • 7
    • 0025569426 scopus 로고
    • LAMP-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin
    • Do K.Y., Smith D.F., Cummings R.D. LAMP-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin. Biochem. Biophys. Res. Commun. 173:1990;1123-1128.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 1123-1128
    • Do, K.Y.1    Smith, D.F.2    Cummings, R.D.3
  • 8
    • 0028566656 scopus 로고
    • A novel glycosaminoglycan attachment domain identification in two alternative splice variants of human versican
    • Dours-Zimmermann M.T., Zimmermann D.R. A novel glycosaminoglycan attachment domain identification in two alternative splice variants of human versican. J. Biol. Chem. 269:1994;32992-32998.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32992-32998
    • Dours-Zimmermann, M.T.1    Zimmermann, D.R.2
  • 9
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263:1988;9557-9560.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 10
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer K. Engineering galactose-binding activity into a C-type mannose-binding protein. Nature. 360:1992;183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 13
    • 0023373075 scopus 로고
    • Carbohydrates as antigenic determinants of glycoproteins
    • Feizi T., Childs R.A. Carbohydrates as antigenic determinants of glycoproteins. Biochem. J. 245:1987;1-11.
    • (1987) Biochem. J. , vol.245 , pp. 1-11
    • Feizi, T.1    Childs, R.A.2
  • 14
    • 0027338013 scopus 로고
    • Epsilon BP, a β-galactoside-binding animal lectin, recognizes IgE receptor (Fc epsilon RI) and activates mast cells
    • Frigeri L.G., Zuberi R.I., Liu F.T. Epsilon BP, a β-galactoside-binding animal lectin, recognizes IgE receptor (Fc epsilon RI) and activates mast cells. Biochemistry. 32:1993;7644-7649.
    • (1993) Biochemistry , vol.32 , pp. 7644-7649
    • Frigeri, L.G.1    Zuberi, R.I.2    Liu, F.T.3
  • 15
    • 0026089105 scopus 로고
    • Genomic sequence and organization of two members of a human lectin gene family
    • Gitt M.A., Barondes S.H. Genomic sequence and organization of two members of a human lectin gene family. Biochemistry. 30:1991;82-89.
    • (1991) Biochemistry , vol.30 , pp. 82-89
    • Gitt, M.A.1    Barondes, S.H.2
  • 17
    • 0026795018 scopus 로고
    • Genomic cloning of the gene for an IgE-binding lectin reveals unusual utilization of 5′ untranslated regions
    • Gritzmacher C.A., Mehl V.S., Liu F.T. Genomic cloning of the gene for an IgE-binding lectin reveals unusual utilization of 5′ untranslated regions. Biochemistry. 31:1992;9533-9538.
    • (1992) Biochemistry , vol.31 , pp. 9533-9538
    • Gritzmacher, C.A.1    Mehl, V.S.2    Liu, F.T.3
  • 18
    • 0028053242 scopus 로고
    • Selective modulation of the interaction of α7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation
    • Gu M., Wang W., Song W.K., Cooper D.N., Kaufman S.J. Selective modulation of the interaction of α7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation. J. Cell. Sci. 107:1994;175-181.
    • (1994) J. Cell. Sci. , vol.107 , pp. 175-181
    • Gu, M.1    Wang, W.2    Song, W.K.3    Cooper, D.N.4    Kaufman, S.J.5
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0027942208 scopus 로고
    • Further evidence by site-directed mutagenesis that conserved hydrophilic residues form a carbohydrate-binding site of human galectin-1
    • Hirabayashi J., Kasai K. Further evidence by site-directed mutagenesis that conserved hydrophilic residues form a carbohydrate-binding site of human galectin-1. Glycoconj. J. 11:1994;437-442.
    • (1994) Glycoconj. J. , vol.11 , pp. 437-442
    • Hirabayashi, J.1    Kasai, K.2
  • 23
    • 0028175514 scopus 로고
    • A three α-stranded helical bundle at the nucleation site of collagen triple-helix formation
    • Hoppe H.J., Barlow P.N., Reid K.B.M. A three α-stranded helical bundle at the nucleation site of collagen triple-helix formation. FEBS Lett. 344:1994;191-195.
    • (1994) FEBS Lett. , vol.344 , pp. 191-195
    • Hoppe, H.J.1    Barlow, P.N.2    Reid, K.B.M.3
  • 24
    • 0028169837 scopus 로고
    • Collectins soluble proteins containing collagenous regions and lectin domains and their roles on innate immunity
    • Hoppe H.J., Reid K.B.M. Collectins soluble proteins containing collagenous regions and lectin domains and their roles on innate immunity. Protein Sci. 3:1994;1143-1158.
    • (1994) Protein Sci. , vol.3 , pp. 1143-1158
    • Hoppe, H.J.1    Reid, K.B.M.2
  • 25
    • 0026770786 scopus 로고
    • Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin
    • Hsu D.K., Zuberi R.I., Liu F.T. Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin. J. Biol. Chem. 267:1992;14167-14174.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14167-14174
    • Hsu, D.K.1    Zuberi, R.I.2    Liu, F.T.3
  • 26
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo R.V., Murdoch A.D. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 10:1996;598-614.
    • (1996) FASEB J. , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 28
    • 0029791741 scopus 로고    scopus 로고
    • The α-helical neck region of human lung surfacatant protein D is essential for the binding of the carbohydrate recognition domains to lipopolysaccharide and phospholipids
    • Kishore U., Wang J.Y., Hoppe H.-J., Reid K.B.M. The α-helical neck region of human lung surfacatant protein D is essential for the binding of the carbohydrate recognition domains to lipopolysaccharide and phospholipids. Biochem. J. 318:1996;505-511.
    • (1996) Biochem. J. , vol.318 , pp. 505-511
    • Kishore, U.1    Wang, J.Y.2    Hoppe, H.-J.3    Reid, K.B.M.4
  • 30
    • 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
  • 31
    • 0029646108 scopus 로고
    • Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins
    • Leonidas D.D., Elbert B.L., Zhou Z., Leffler H., Ackerman S.J., Ravi Acharya K. Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 3:1995;1379-1393.
    • (1995) Structure , vol.3 , pp. 1379-1393
    • Leonidas, D.D.1    Elbert, B.L.2    Zhou, Z.3    Leffler, H.4    Ackerman, S.J.5    Ravi Acharya, K.6
  • 32
    • 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. USA. 91:1994;1428-1432.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 33
    • 0027508083 scopus 로고
    • S-type mammalian lectins in allergic inflammation
    • Liu F.T. S-type mammalian lectins in allergic inflammation. Immunol. Today. 14:1993;486-490.
    • (1993) Immunol. Today , vol.14 , pp. 486-490
    • Liu, F.T.1
  • 34
    • 0028874589 scopus 로고
    • Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages
    • Liu F.T., Hsu D.K., Zuberi R.I., Kuwabara I., Chi E.Y., Henderson W.R. Jr. Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages. Am. J. Pathol. 147:1995;1016-1028.
    • (1995) Am. J. Pathol. , vol.147 , pp. 1016-1028
    • Liu, F.T.1    Hsu, D.K.2    Zuberi, R.I.3    Kuwabara, I.4    Chi, E.Y.5    Henderson W.R., Jr.6
  • 35
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with lactose at 2.9-Å resolution
    • Lobsanov Y.D., Gitt M.A., Leffler H., Barondes S.H., Rini J.M. X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with lactose at 2.9-Å 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.M.5
  • 38
    • 0028229493 scopus 로고
    • Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism
    • Mahanthappa N.K., Cooper D.N., Barondes S.H., Schwarting G.A. Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism. Development. 120:1994;1373-1384.
    • (1994) Development , vol.120 , pp. 1373-1384
    • Mahanthappa, N.K.1    Cooper, D.N.2    Barondes, S.H.3    Schwarting, G.A.4
  • 39
    • 0028128857 scopus 로고
    • Possible interaction between animal lectins and bacterial carbohydrates
    • Mandrell R.E., Apicella M.A., Lindstedt R., Leffler H. Possible interaction between animal lectins and bacterial carbohydrates. Meth. Enzymol. 236:1994;231-254.
    • (1994) Meth. Enzymol. , vol.236 , pp. 231-254
    • Mandrell, R.E.1    Apicella, M.A.2    Lindstedt, R.3    Leffler, H.4
  • 40
    • 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
  • 41
    • 0028556893 scopus 로고
    • Characterization of the complete genomic structure of the human versican gene and functional analysis of its promoter
    • Naso M.F., Zimmermann D.R., Iozzo R.V. Characterization of the complete genomic structure of the human versican gene and functional analysis of its promoter. J. Biol. Chem. 269:1994;32999-33008.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32999-33008
    • Naso, M.F.1    Zimmermann, D.R.2    Iozzo, R.V.3
  • 42
    • 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
  • 43
    • 0025309457 scopus 로고
    • Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis
    • Offner H., Celnik B., Bringman T.S., Casentini Borocz D., Nedwin G.E., Vandenbark A.A. Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis. J. Neuroimmunol. 28:1990;177-184.
    • (1990) J. Neuroimmunol. , vol.28 , pp. 177-184
    • Offner, H.1    Celnik, B.2    Bringman, T.S.3    Casentini Borocz, D.4    Nedwin, G.E.5    Vandenbark, A.A.6
  • 44
    • 0027987812 scopus 로고
    • Chimeras of surfactant proteins A and D identify the carbohydrate recognition domains as essential for phospholipid interaction
    • Ogasawara Y., McCormack F.X., Mason R.J., Voelker D.R. Chimeras of surfactant proteins A and D identify the carbohydrate recognition domains as essential for phospholipid interaction. J. Biol. Chem. 269:1994;29785-29792.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29785-29792
    • Ogasawara, Y.1    McCormack, F.X.2    Mason, R.J.3    Voelker, D.R.4
  • 45
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson J.R., Ora A., Van P.N., Helenius A. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell. 6:1995;1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 46
    • 0026040605 scopus 로고
    • The sugared path to a normal lung: Soluble β-galactoside-specific lectins
    • Powell J.T., Harrison F.L. The sugared path to a normal lung: soluble β-galactoside-specific lectins. Am. J. Physiol. 261:1991;L236-L239.
    • (1991) Am. J. Physiol. , vol.261
    • Powell, J.T.1    Harrison, F.L.2
  • 47
    • 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
  • 49
    • 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
  • 50
    • 0027158038 scopus 로고
    • Lectin-carbohydrate complexes of plants and animals: An atomic view
    • Sharon N. Lectin-carbohydrate complexes of plants and animals: an atomic view. Trends Biochem. Sci. 18:1993;221-226.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 221-226
    • Sharon, N.1
  • 51
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple helical coiled-coil
    • Sheriff S., Chang C.Y.Y., Ezekowitz R.A.B. Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple helical coiled-coil. Nat. Struct. Biol. 1:1994;789-794.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.Y.2    Ezekowitz, R.A.B.3
  • 52
    • 0029822715 scopus 로고    scopus 로고
    • Interaction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssnus) allergens
    • Wang J.Y., Kishore U., Lim B.L., Strong P., Reid K.B.M. Interaction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssnus) allergens. Clin. Exp. Immunol. 106:1996;367-373.
    • (1996) Clin. Exp. Immunol. , vol.106 , pp. 367-373
    • Wang, J.Y.1    Kishore, U.2    Lim, B.L.3    Strong, P.4    Reid, K.B.M.5
  • 53
    • 0028824437 scopus 로고
    • A recombinant polypeptide, composed of the α-helical neck region and the carbohydrate recognition domain of conglutinin, self-associates to give a functionally intact homotrimer
    • Wang J.Y., Kishore U., Reid K.B.M. A recombinant polypeptide, composed of the α-helical neck region and the carbohydrate recognition domain of conglutinin, self-associates to give a functionally intact homotrimer. FEBS Lett. 376:1995;6-10.
    • (1995) FEBS Lett. , vol.376 , pp. 6-10
    • Wang, J.Y.1    Kishore, U.2    Reid, K.B.M.3
  • 54
    • 0026523484 scopus 로고
    • Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex
    • Wang J.L., Werner E.A., Laing J.G., Patterson R.J. Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex. Biochem. Soc. Trans. 20:1992;269-274.
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 269-274
    • Wang, J.L.1    Werner, E.A.2    Laing, J.G.3    Patterson, R.J.4
  • 55
    • 0025718593 scopus 로고
    • Physical characterization and crystallization of the carbohydrate-recognition domain of a mannose-binding protein from rat
    • Weis W.I., Crichlow G.V., Murthy H.M., Hendrickson W.A., Drickamer K. Physical characterization and crystallization of the carbohydrate-recognition domain of a mannose-binding protein from rat. J. Biol. Chem. 266:1991;20678-20686.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20678-20686
    • Weis, W.I.1    Crichlow, G.V.2    Murthy, H.M.3    Hendrickson, W.A.4    Drickamer, K.5
  • 56
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis W.I., Drickamer K. Trimeric structure of a C-type mannose-binding protein. Structure. 2:1994;1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 57
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis W.I., Drickamer K. Structural basis of lectin-carbohydrate recognition. Ann. Rev. Biochem. 65:1996;441-473.
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 58
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis W.I., Drickamer K., Hendrickson W.A. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature. 360:1992;127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 59
    • 0026079139 scopus 로고
    • Identification of an autocrine negative growth factor: Mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator
    • Wells V., Mallucci L. Identification of an autocrine negative growth factor: mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator. Cell. 64:1991;91-97.
    • (1991) Cell , vol.64 , pp. 91-97
    • Wells, V.1    Mallucci, L.2
  • 60
    • 0024473752 scopus 로고
    • Synthesis of a truncated 46 kD mannose 6-phosphate receptor that is secreted and retains ligand binding
    • Wendland M., Hille A., Nagel G., Waheed A., von Figura K., Pohlman R. Synthesis of a truncated 46 kD mannose 6-phosphate receptor that is secreted and retains ligand binding. Biochem. J. 260:1989;201-206.
    • (1989) Biochem. J. , vol.260 , pp. 201-206
    • Wendland, M.1    Hille, A.2    Nagel, G.3    Waheed, A.4    Von Figura, K.5    Pohlman, R.6
  • 61
    • 0026352780 scopus 로고
    • The bovine mannose 6-phosphate/insulin-like growth factor II receptor: Localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region
    • Westlund B., Dahms N.M., Kornfeld S. The bovine mannose 6-phosphate/insulin-like growth factor II receptor: localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region. J. Biol. Chem. 266:1991;23233-23239.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23233-23239
    • Westlund, B.1    Dahms, N.M.2    Kornfeld, S.3
  • 62
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White T.K., Zhu Q., Tanzer M.L. Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J. Biol. Chem. 270:1995;15926-15929.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15926-15929
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 63
    • 0025372418 scopus 로고
    • The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin
    • Zhou Q., Cummings R.D. The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin. Arch. Biochem. Biophys. 281:1990;27-35.
    • (1990) Arch. Biochem. Biophys. , vol.281 , pp. 27-35
    • Zhou, Q.1    Cummings, R.D.2
  • 64
    • 0027162467 scopus 로고
    • L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion
    • Zhou Q., Cummings R.D. L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion. Arch. Biochem. Biophys. 300:1993;6-17.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 6-17
    • Zhou, Q.1    Cummings, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.