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Volumn 535, Issue , 2002, Pages 107-124

Lectin domains on cytokines

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; CARBOHYDRATE BINDING PROTEIN; CD3 ANTIGEN; CD4 ANTIGEN; CYTOKINE; EPITOPE; GANGLIOSIDE GM3; GLYCAN; GLYCOSAMINOGLYCAN; HEMAGGLUTININ; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 2; INTERLEUKIN 2 RECEPTOR; INTERLEUKIN 2 RECEPTOR BETA; INTERLEUKIN 3; INTERLEUKIN 3 RECEPTOR; INTERLEUKIN 4; INTERLEUKIN 6; INTERLEUKIN 6 RECEPTOR; INTERLEUKIN 7; LECTIN; MANNOSE 6 PHOSPHATE; MUCIN; PERTUSSIS TOXIN; PROSTAGLANDIN; PROTEIN P56; PROTEOGLYCAN; T LYMPHOCYTE RECEPTOR;

EID: 1642440204     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (4)

References (92)
  • 1
    • 0025253851 scopus 로고
    • Expression of interleukin-2 receptor gamma chain on human neutrophils
    • Akira, S., Hirano, T., Taga, T., and Kishimoto, T., 1990, Expression of interleukin-2 receptor gamma chain on human neutrophils, FASEB J. 4:2860-2867.
    • (1990) FASEB J , vol.4 , pp. 2860-2867
    • Akira, S.1    Hirano, T.2    Taga, T.3    Kishimoto, T.4
  • 3
    • 0028926420 scopus 로고
    • ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells
    • Arar, C., Carpentier, V., Le Caer, J.P., Monsigny, M., Legrand, A., and Roche, A.C., 1995, ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells, J Biol Chem. 270:3551-3553.
    • (1995) J Biol Chem , vol.270 , pp. 3551-3553
    • Arar, C.1    Carpentier, V.2    Le Caer, J.P.3    Monsigny, M.4    Legrand, A.5    Roche, A.C.6
  • 4
    • 0024396981 scopus 로고
    • Membrane IL-1: IL-1 alpha precursor binds to the plasma membrane via a lectin-like interaction
    • Brody, D.T. and Durum, S.K., 1989, Membrane IL-1: IL-1 alpha precursor binds to the plasma membrane via a lectin-like interaction, J Immunol. 143:1183-1187.
    • (1989) J Immunol , vol.143 , pp. 1183-1187
    • Brody, D.T.1    Durum, S.K.2
  • 6
    • 0035937127 scopus 로고    scopus 로고
    • Recombinant human interleukins IL-1alpha, IL-1beta, IL-4, IL-6, and IL-7 show different and specific calcium-independent carbohydrate-binding properties
    • Cebo, C., Dambrouck, T., Maes, E., Laden, C., Strecker, G., Michalski, J.C., and Zanetta, J.P., 2001, Recombinant human interleukins IL-1alpha, IL-1beta, IL-4, IL-6, and IL-7 show different and specific calcium-independent carbohydrate-binding properties, J Biol Chem. 276:5685-5691.
    • (2001) J Biol Chem , vol.276 , pp. 5685-5691
    • Cebo, C.1    Dambrouck, T.2    Maes, E.3    Laden, C.4    Strecker, G.5    Michalski, J.C.6    Zanetta, J.P.7
  • 7
    • 0037023731 scopus 로고    scopus 로고
    • Function and molecular modelling of the interaction between human interleukin 6 and its HNK-1 oligosaccharide ligands
    • Cebo, C., Durier, V., Lagant, P., Maes, E., Florea, D., Lefebvre, T., Strecker, G., Vergoten, G., and Zanetta, J.P., 2002, Function and molecular modelling of the interaction between human interleukin 6 and its HNK-1 oligosaccharide ligands, J Biol Chem. 277:12246-12252.
    • (2002) J Biol Chem , vol.277 , pp. 12246-12252
    • Cebo, C.1    Durier, V.2    Lagant, P.3    Maes, E.4    Florea, D.5    Lefebvre, T.6    Strecker, G.7    Vergoten, G.8    Zanetta, J.P.9
  • 8
    • 0029016864 scopus 로고
    • Identification of a soluble, high affinity human interleukin 4 binding protein in normal human urine
    • Christie, G., Dacey, I., and Weston, J., 1995, Identification of a soluble, high affinity human interleukin 4 binding protein in normal human urine, Cytokine. 7:305-310.
    • (1995) Cytokine , vol.7 , pp. 305-310
    • Christie, G.1    Dacey, I.2    Weston, J.3
  • 9
    • 0028965864 scopus 로고
    • Gangliosides interact with interleukin-4 and inhibit interleukin-4- stimulated helper T-cell proliferation
    • Chu, J.W. and Sharom, F., 1995, Gangliosides interact with interleukin-4 and inhibit interleukin-4-stimulated helper T-cell proliferation, Immunology. 84:396-403.
    • (1995) Immunology , vol.84 , pp. 396-403
    • Chu, J.W.1    Sharom, F.2
  • 10
    • 0029010483 scopus 로고
    • Interaction of interleukin 7 (IL-7) with glycosaminoglycans and its biological relevance
    • Clarke, D., Katoh, O., Gibbs, R.V., Griffiths, S.D., and Gordon, M.Y., 1995, Interaction of interleukin 7 (IL-7) with glycosaminoglycans and its biological relevance, Cytokine. 7:325-330.
    • (1995) Cytokine , vol.7 , pp. 325-330
    • Clarke, D.1    Katoh, O.2    Gibbs, R.V.3    Griffiths, S.D.4    Gordon, M.Y.5
  • 12
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper, D.N.W., 2002, Galectinomics: finding themes in complexity, Biochim Biophys Acta. 1572:209-231.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 13
    • 0028675659 scopus 로고
    • The interleukin-1 family: 10 Years of discovery
    • Dinarello, C.A., 1994, The interleukin-1 family: 10 years of discovery, FASEB J. 8:1314-1325.
    • (1994) FASEB J , vol.8 , pp. 1314-1325
    • Dinarello, C.A.1
  • 14
    • 0028972101 scopus 로고
    • N-glycosylation of the human granulocyte-macrophage colony-stimulating factor receptor alpha subunit is essential for ligand binding and signal transduction
    • Ding, D.X., Vera, J.C., Heaney, M.L., and Golde, D.W., 1995, N-glycosylation of the human granulocyte-macrophage colony-stimulating factor receptor alpha subunit is essential for ligand binding and signal transduction, J Biol Chem. 270:24580-24584.
    • (1995) J Biol Chem , vol.270 , pp. 24580-24584
    • Ding, D.X.1    Vera, J.C.2    Heaney, M.L.3    Golde, D.W.4
  • 15
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • Dodd, R.B. and Drickamer, K., 2001, Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity, Glycobiology. 11:71-79.
    • (2001) Glycobiology , vol.11 , pp. 71-79
    • Dodd, R.B.1    Drickamer, K.2
  • 16
    • 0031569879 scopus 로고    scopus 로고
    • Making a fitting choice: Common aspects of sugar-binding sites in plant and animal lectins
    • Drickamer, K., 1997, Making a fitting choice: common aspects of sugar-binding sites in plant and animal lectins, Structure. 5:465-468.
    • (1997) Structure , vol.5 , pp. 465-468
    • Drickamer, K.1
  • 18
    • 0023373075 scopus 로고
    • Carbohydrates as antigenic determinants of glycoproteins
    • Feizi, T. and Childs, R.A., 1987, Carbohydrates as antigenic determinants of glycoproteins, Biochem J. 245:1-11.
    • (1987) Biochem J , vol.245 , pp. 1-11
    • Feizi, T.1    Childs, R.A.2
  • 19
    • 0025362240 scopus 로고
    • A soluble, high-affinity, interleukin-4-binding protein is present in the biological fluids of mice
    • Fernandez-Botran, R. and Vitetta, E.S., 1990, A soluble, high-affinity, interleukin-4-binding protein is present in the biological fluids of mice, Proc Natl Acad Sci USA. 87:4202-4206.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4202-4206
    • Fernandez-Botran, R.1    Vitetta, E.S.2
  • 20
    • 0028233139 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K. and Simons, K., 1994, The role of N-glycans in the secretory pathway, Cell. 77:625-626.
    • (1994) Cell , vol.77 , pp. 625-626
    • Fiedler, K.1    Simons, K.2
  • 21
    • 0028274194 scopus 로고
    • Mutagenesis of the human interleukin-6 fourth predicted alpha-helix: Involvement of the Arg168 in the binding site
    • Fontaine, V., Ooms, J., and Content, J., 1994, Mutagenesis of the human interleukin-6 fourth predicted alpha-helix: involvement of the Arg168 in the binding site, Eur J Immunol. 24:1041-1045.
    • (1994) Eur J Immunol , vol.24 , pp. 1041-1045
    • Fontaine, V.1    Ooms, J.2    Content, J.3
  • 23
    • 0026763332 scopus 로고
    • The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide
    • Foxall, C., Watson, S.R., Dowbenko, D., Fennie, C., Lasky, L.A., Kiso, M., Hasegawa, A., Asa, A., and Brandley, B.K., 1992, The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide, J Cell Biol. 117:895-902.
    • (1992) J Cell Biol , vol.117 , pp. 895-902
    • Foxall, C.1    Watson, S.R.2    Dowbenko, D.3    Fennie, C.4    Lasky, L.A.5    Kiso, M.6    Hasegawa, A.7    Asa, A.8    Brandley, B.K.9
  • 25
    • 0035831534 scopus 로고    scopus 로고
    • Carbohydrate recognition site of interleukin-2 in relation to cell proliferation
    • Fukushima, K. and Yamashita K., 2001, Carbohydrate recognition site of interleukin-2 in relation to cell proliferation, J Biol Chem. 276:7351-7356.
    • (2001) J Biol Chem , vol.276 , pp. 7351-7356
    • Fukushima, K.1    Yamashita, K.2
  • 26
    • 0030891208 scopus 로고    scopus 로고
    • Lectin-like characteristics of recombinant human interleukin-1beta recognizing glycans of the glycosylphosphatidylinositol anchor
    • Fukushima, K., Hara-Kuge, S., Ohkura, T., Seko, A., Ideo, H., Inazu, T., and Yamashita, K., 1997, Lectin-like characteristics of recombinant human interleukin-1beta recognizing glycans of the glycosylphosphatidylinositol anchor, J Biol Chem. 272:10579-10584.
    • (1997) J Biol Chem , vol.272 , pp. 10579-10584
    • Fukushima, K.1    Hara-Kuge, S.2    Ohkura, T.3    Seko, A.4    Ideo, H.5    Inazu, T.6    Yamashita, K.7
  • 27
    • 0027181195 scopus 로고
    • N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: The functional role of carbohydrate as to its lectin-like character and clearance velocity
    • Fukushima, K., Watanabe, H., Takeo, K., Nomura, M., Asahi, T., and Yamashita, K., 1993, N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity, Arch Biochem Biophys. 304:144-153.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 144-153
    • Fukushima, K.1    Watanabe, H.2    Takeo, K.3    Nomura, M.4    Asahi, T.5    Yamashita, K.6
  • 28
    • 0025848163 scopus 로고
    • Interleukin-2 receptor beta chain gene: Generation of three receptor forms by cloned human alpha and beta chain cDNA's
    • Hatakeyama, M., Kono, T., Kobayashi, N., Kawahara, A., Levin, S.D., Perlmutter, R.M., and Taniguchi, T., 1991, Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's, Science. 252:1523-1528.
    • (1991) Science , vol.252 , pp. 1523-1528
    • Hatakeyama, M.1    Kono, T.2    Kobayashi, N.3    Kawahara, A.4    Levin, S.D.5    Perlmutter, R.M.6    Taniguchi, T.7
  • 30
    • 0031913593 scopus 로고    scopus 로고
    • Interleukin 6 and its receptor: Ten years later
    • Hirano, T., 1998, Interleukin 6 and its receptor: ten years later, Int Rev Immunol. 16:249-284.
    • (1998) Int Rev Immunol , vol.16 , pp. 249-284
    • Hirano, T.1
  • 31
    • 0031429943 scopus 로고    scopus 로고
    • Signalling mechanisms through gp130: A model of the cytokine system
    • Hirano, T., Nakajima, K., and Hibi, M., 1997, Signalling mechanisms through gp130: a model of the cytokine system, Cytokine Growth Factor Rev. 8:241-252.
    • (1997) Cytokine Growth Factor Rev , vol.8 , pp. 241-252
    • Hirano, T.1    Nakajima, K.2    Hibi, M.3
  • 32
    • 0029087143 scopus 로고
    • Immunodeficiency in IL-2-knockout mice
    • Horak, I., 1995, Immunodeficiency in IL-2-knockout mice, Clin Immunol Immunopathol. 76:172-173.
    • (1995) Clin Immunol Immunopathol , vol.76 , pp. 172-173
    • Horak, I.1
  • 33
    • 0034142220 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase activity is required for IL-4 induction of IL-4 receptor alpha-chain
    • Huang, H. and Paul, W.E., 2000, Protein tyrosine phosphatase activity is required for IL-4 induction of IL-4 receptor alpha-chain, J Immunol. 164:1211-1215.
    • (2000) J Immunol , vol.164 , pp. 1211-1215
    • Huang, H.1    Paul, W.E.2
  • 34
    • 0030962582 scopus 로고    scopus 로고
    • Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells
    • Imani, F., Rager, K.J., Catipovic, B., and Marsh, D.G., 1997, Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells, J Biol Chem. 272:7927-7931.
    • (1997) J Biol Chem , vol.272 , pp. 7927-7931
    • Imani, F.1    Rager, K.J.2    Catipovic, B.3    Marsh, D.G.4
  • 35
    • 0023268531 scopus 로고
    • Structure-function analysis of human interleukin-2. Identification of amino acid residues required for biological activity
    • Ju, G., Collins, L., Kaffka, K.L., Tsien, W.H., Chizzonite, R., Crowl, R., Bhatt, R., and Kilian, P.L., 1987, Structure-function analysis of human interleukin-2. Identification of amino acid residues required for biological activity, J Biol Chem. 262:5723-5731.
    • (1987) J Biol Chem , vol.262 , pp. 5723-5731
    • Ju, G.1    Collins, L.2    Kaffka, K.L.3    Tsien, W.H.4    Chizzonite, R.5    Crowl, R.6    Bhatt, R.7    Kilian, P.L.8
  • 37
    • 0029121950 scopus 로고
    • Self-association of interleukin 2 bound to its receptor
    • Kaplan, D., Smith, D., Huang, R., and Yildirim, Z., 1995, Self-association of interleukin 2 bound to its receptor, FASEB J. 9:1096-1102.
    • (1995) FASEB J , vol.9 , pp. 1096-1102
    • Kaplan, D.1    Smith, D.2    Huang, R.3    Yildirim, Z.4
  • 38
    • 0032733301 scopus 로고    scopus 로고
    • Structure and biology of mannan-binding protein, MBP, an important component of innate immunity
    • Kawasaki T., 1999, Structure and biology of mannan-binding protein, MBP, an important component of innate immunity, Biochim Biophys Acta. 1473:186-195.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 186-195
    • Kawasaki, T.1
  • 39
    • 0028595625 scopus 로고
    • Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22
    • Kelm, S., Schauer, R., Manuguerra, J.C., Gross H.J., and Crocker, P.R., 1994, Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22, Glycoconjugate J. 11:576-585.
    • (1994) Glycoconjugate J , vol.11 , pp. 576-585
    • Kelm, S.1    Schauer, R.2    Manuguerra, J.C.3    Gross, H.J.4    Crocker, P.R.5
  • 40
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: A historical introduction and overview
    • Kilpatrick, D., 2002, Animal lectins: a historical introduction and overview, Biochim Biophys Acta. 1572:187-197.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.1
  • 41
    • 0037136413 scopus 로고    scopus 로고
    • Mannan-binding lectin: Clinical significance and applications
    • Kilpatrick, D.C., 2002, Mannan-binding lectin: clinical significance and applications, Biochim Biophys Acta. 1572,401-413.
    • (2002) Biochim Biophys Acta , pp. 1572
    • Kilpatrick, D.C.1
  • 42
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto, T., Taga, T., and Akira S., 1992a, Cytokine signal transduction, Cell. 76:253-262.
    • (1992) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 43
    • 0026485304 scopus 로고
    • Interleukin-6 and its receptor: A paradigm for cytokines
    • Kishimoto, T., Akira, S., and Taga, T., 1992b, Interleukin-6 and its receptor: a paradigm for cytokines, Science. 258:593-597.
    • (1992) Science , vol.258 , pp. 593-597
    • Kishimoto, T.1    Akira, S.2    Taga, T.3
  • 44
    • 0027767628 scopus 로고
    • Inhibitors of protein tyrosine kinases and protein tyrosine phosphatases suppress IL-4-induced CD23 expression and release by human B lymphocytes
    • Kolb, J.P. and Abadie, A., 1993, Inhibitors of protein tyrosine kinases and protein tyrosine phosphatases suppress IL-4-induced CD23 expression and release by human B lymphocytes, Eur Cytokine Netw. 4:429-438.
    • (1993) Eur Cytokine Netw , vol.4 , pp. 429-438
    • Kolb, J.P.1    Abadie, A.2
  • 45
    • 0029096521 scopus 로고
    • Demonstration of interleukin-3 receptor-associated antigen in the central nervous system
    • Konishi, Y., Chui, D.H., Kunishita, T., Yamamura, T., Higashi, Y., and Tabira, T., 1995, Demonstration of interleukin-3 receptor-associated antigen in the central nervous system, J Neurosci Res. 41:572-582.
    • (1995) J Neurosci Res , vol.41 , pp. 572-582
    • Konishi, Y.1    Chui, D.H.2    Kunishita, T.3    Yamamura, T.4    Higashi, Y.5    Tabira, T.6
  • 46
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky, L.A., 1992, Selectins: interpreters of cell-specific carbohydrate information during inflammation, Science. 258:964-969.
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 47
    • 0026769413 scopus 로고
    • Identification of a receptor binding site in the carboxyl terminus of human interleukin-6
    • Leebeck, F.W., Kariya, K., Schwabe, M., and Fowlkes, D.M., 1992, Identification of a receptor binding site in the carboxyl terminus of human interleukin-6, J Biol Chem. 267:14832-14838.
    • (1992) J Biol Chem , vol.267 , pp. 14832-14838
    • Leebeck, F.W.1    Kariya, K.2    Schwabe, M.3    Fowlkes, D.M.4
  • 48
    • 0037155279 scopus 로고    scopus 로고
    • Isolectins I-A and I-B of Griffonia (Bandeiraea) simplicifolia. Crystal structure of metal-free GS I-B(4) and molecular basis for metal binding and monosaccharide specificity
    • Lescar, J., Loris, R., Mitchell, E., Gautier, C., Chazalet, V., Cox, V., Wyns, L., Perez, S., Breton, C., and Imberty, A., 2002, Isolectins I-A and I-B of Griffonia (Bandeiraea) simplicifolia. Crystal structure of metal-free GS I-B(4) and molecular basis for metal binding and monosaccharide specificity, J Biol Chem. 277:6608-6614.
    • (2002) J Biol Chem , vol.277 , pp. 6608-6614
    • Lescar, J.1    Loris, R.2    Mitchell, E.3    Gautier, C.4    Chazalet, V.5    Cox, V.6    Wyns, L.7    Perez, S.8    Breton, C.9    Imberty, A.10
  • 49
    • 0027500807 scopus 로고
    • Structure-function analysis of the C-terminal segment of human interleukin-6
    • Li, X., Rock, F., Chong, P., Cockle, S., Keating, A., Ziltener, H., and Klein, M., 1993, Structure-function analysis of the C-terminal segment of human interleukin-6, J Biol Chem. 268:22377-22384.
    • (1993) J Biol Chem , vol.268 , pp. 22377-22384
    • Li, X.1    Rock, F.2    Chong, P.3    Cockle, S.4    Keating, A.5    Ziltener, H.6    Klein, M.7
  • 50
    • 0029826526 scopus 로고    scopus 로고
    • Interleukin 1 beta and fever
    • Licinio, J. and Wong, M.L., 1996, Interleukin 1 beta and fever, Nat Med. 2:1314-1315.
    • (1996) Nat Med , vol.2 , pp. 1314-1315
    • Licinio, J.1    Wong, M.L.2
  • 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., and Rini, J.M., 1993, 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. 268:27034-27038.
    • (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
  • 52
    • 0025866948 scopus 로고
    • Structure-activity relationship study of human interleukin-3. Identification of residues required for biological activity by site-directed mutagenesis
    • Lokker, N.A., Movva, N.R., Strittmatter, U., Fagg, B., and Zenke, G., 1991, Structure-activity relationship study of human interleukin-3. Identification of residues required for biological activity by site-directed mutagenesis, J Biol Chem. 266:10624-10631.
    • (1991) J Biol Chem , vol.266 , pp. 10624-10631
    • Lokker, N.A.1    Movva, N.R.2    Strittmatter, U.3    Fagg, B.4    Zenke, G.5
  • 53
    • 0031114123 scopus 로고    scopus 로고
    • Tyrosine and serine protein kinase activities associated with ligand-induced internalized TCR/CD3 complexes
    • Luton, F., Legendre, V., Gorvel, J.P., Schmitt-Verhulst, A.M., and Boyer, C., 1997, Tyrosine and serine protein kinase activities associated with ligand-induced internalized TCR/CD3 complexes, J Immunol. 158:3140-3147.
    • (1997) J Immunol , vol.158 , pp. 3140-3147
    • Luton, F.1    Legendre, V.2    Gorvel, J.P.3    Schmitt-Verhulst, A.M.4    Boyer, C.5
  • 54
    • 0026641183 scopus 로고
    • Glycosylation of the interleukin-1 receptor type I is required for optimal binding of interleukin-1
    • Mancilla, J., Ikejima, T., and Dinarello, C.A., 1992, Glycosylation of the interleukin-1 receptor type I is required for optimal binding of interleukin-1, Lymphokine Cytokine Res. 11:197-205.
    • (1992) Lymphokine Cytokine Res , vol.11 , pp. 197-205
    • Mancilla, J.1    Ikejima, T.2    Dinarello, C.A.3
  • 55
    • 0023803143 scopus 로고
    • Isolation and characterization of endogenous ligands for liver mannan-binding protein
    • Mori, K., Kawasaki, T., Yamashina, I., 1988, Isolation and characterization of endogenous ligands for liver mannan-binding protein, Arch Biochem Biophys. 264:647-656.
    • (1988) Arch Biochem Biophys , vol.264 , pp. 647-656
    • Mori, K.1    Kawasaki, T.2    Yamashina, I.3
  • 56
    • 0023024465 scopus 로고
    • Uromodulin. An immunosuppressive 85-kilodalton glycoprotein isolated from human pregnancy urine is a high affinity ligand for recombinant interleukin 1 alpha
    • Muchmore, A.V. and Decker, J.M., 1986, Uromodulin. An immunosuppressive 85-kilodalton glycoprotein isolated from human pregnancy urine is a high affinity ligand for recombinant interleukin 1 alpha, J Biol Chem. 261:13404-13407.
    • (1986) J Biol Chem , vol.261 , pp. 13404-13407
    • Muchmore, A.V.1    Decker, J.M.2
  • 57
    • 0023135180 scopus 로고
    • The lectin-like interaction between recombinant tumor necrosis factor and uromodulin
    • Muchmore, A.V. and Decker, J.M., 1987, The lectin-like interaction between recombinant tumor necrosis factor and uromodulin, J Immunol. 138:2541-2546.
    • (1987) J Immunol , vol.138 , pp. 2541-2546
    • Muchmore, A.V.1    Decker, J.M.2
  • 58
    • 0028817807 scopus 로고
    • The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22
    • Nath, D., van der Merwe, P.A., Kelm, S., Bradfield, P., and Crocker, P.R., 1995, The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22, J Biol Chem. 270:26184-26191.
    • (1995) J Biol Chem , vol.270 , pp. 26184-26191
    • Nath, D.1    Van Der Merwe, P.A.2    Kelm, S.3    Bradfield, P.4    Crocker, P.R.5
  • 59
    • 0033010373 scopus 로고    scopus 로고
    • The IL-4 receptor: Signalling mechanisms and biologic functions
    • Nelms, K., Keegan, A.D., Zamorano, J., Ryan, J.J., and Paul, W.E., 1999, The IL-4 receptor: signalling mechanisms and biologic functions, Annu Rev Immunol. 17:701-738.
    • (1999) Annu Rev Immunol , vol.17 , pp. 701-738
    • Nelms, K.1    Keegan, A.D.2    Zamorano, J.3    Ryan, J.J.4    Paul, W.E.5
  • 60
    • 0034210621 scopus 로고    scopus 로고
    • High-affinity binding to the GM-CSF receptor requires intact N-glycosylation sites in the extracellular domain of the beta subunit
    • Niu, L., Heaney, M.L., Vera, J.C., and Golde, D.W., 2000, High-affinity binding to the GM-CSF receptor requires intact N-glycosylation sites in the extracellular domain of the beta subunit, Blood. 95:3357-3362.
    • (2000) Blood , vol.95 , pp. 3357-3362
    • Niu, L.1    Heaney, M.L.2    Vera, J.C.3    Golde, D.W.4
  • 61
    • 0027751556 scopus 로고
    • Interleukin-2 receptor gamma chain: A functional component of the interleukin-7 receptor
    • Noguchi, N., Nakamura, Y., Russell, S.M., Ziegler, S.F., Tsang, M., Cao, X., and Leonard, W.J., 1993, Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor, Science. 262:1877-1880.
    • (1993) Science , vol.262 , pp. 1877-1880
    • Noguchi, N.1    Nakamura, Y.2    Russell, S.M.3    Ziegler, S.F.4    Tsang, M.5    Cao, X.6    Leonard, W.J.7
  • 62
    • 0023734986 scopus 로고
    • Isolation and immunohistochemical localization of a chondroitin sulfate proteoglycan from adult rat brain
    • Normand, G., Kuchler, S., Meyer, A., Vincendon, G., and Zanetta, J.P., 1988, Isolation and immunohistochemical localization of a chondroitin sulfate proteoglycan from adult rat brain, J Neurochem. 51:665-676.
    • (1988) J Neurochem , vol.51 , pp. 665-676
    • Normand, G.1    Kuchler, S.2    Meyer, A.3    Vincendon, G.4    Zanetta, J.P.5
  • 63
    • 0027177907 scopus 로고
    • Generation of a monoclonal antibody specific for ganglioside GM4: Evidence for GM4 expression on astrocytes in chicken cerebellum
    • Ozawa, H., Kotani, M., Kawashima, I., Numata, M., Ogawa, T., Terashima, T., and Tai, T., 1993, Generation of a monoclonal antibody specific for ganglioside GM4: evidence for GM4 expression on astrocytes in chicken cerebellum, J Biochem. 114:5-8.
    • (1993) J Biochem , vol.114 , pp. 5-8
    • Ozawa, H.1    Kotani, M.2    Kawashima, I.3    Numata, M.4    Ogawa, T.5    Terashima, T.6    Tai, T.7
  • 65
    • 0025764757 scopus 로고
    • Interleukin-4: A prototypic immunoregulatory lymphokine
    • Paul, W.E., 1991, Interleukin-4: a prototypic immunoregulatory lymphokine, Blood. 77:1859-1870.
    • (1991) Blood , vol.77 , pp. 1859-1870
    • Paul, W.E.1
  • 66
    • 0028206055 scopus 로고
    • CD22-mediated cell adhesion to cytokine-activated human endothelial cells. Positive and negative regulation by alpha 2-6-sialylation of cellular glycoproteins
    • Powell, L.D. and Varki, A., 1994, CD22-mediated cell adhesion to cytokine-activated human endothelial cells. Positive and negative regulation by alpha 2-6-sialylation of cellular glycoproteins, J Biol Chem. 269:10628-10636.
    • (1994) J Biol Chem , vol.269 , pp. 10628-10636
    • Powell, L.D.1    Varki, A.2
  • 69
    • 0027252635 scopus 로고
    • Saturation mutagenesis of the human interleukin 6 receptor-binding site: Implications for its three-dimensional structure
    • Savino, R., Lahm, A., Giorgio, A., Cabiddo, A., Tramontano, A., and Ciliberto, G., 1993, Saturation mutagenesis of the human interleukin 6 receptor-binding site: implications for its three-dimensional structure, Proc Natl Acad Sci USA. 9:4067-4071.
    • (1993) Proc Natl Acad Sci USA , vol.9 , pp. 4067-4071
    • Savino, R.1    Lahm, A.2    Giorgio, A.3    Cabiddo, A.4    Tramontano, A.5    Ciliberto, G.6
  • 70
    • 0022359216 scopus 로고
    • Membrane carbohydrates of lymphoid cells: The receptor for interleukin 2
    • Schaaf-Lafontaine, N., Balthazart, C., and Hooghe, R.J., 1985, Membrane carbohydrates of lymphoid cells: the receptor for interleukin 2, Immunobiology. 170:249-255.
    • (1985) Immunobiology , vol.170 , pp. 249-255
    • Schaaf-Lafontaine, N.1    Balthazart, C.2    Hooghe, R.J.3
  • 71
    • 0023895601 scopus 로고
    • The lectin-like interaction between recombinant tumor necrosis factor and uromodulin
    • Sherblom, A.P., Decker, J.M., and Muchmore, A.V., 1988, The lectin-like interaction between recombinant tumor necrosis factor and uromodulin, J Biol Chem. 263:5418-5424.
    • (1988) J Biol Chem , vol.263 , pp. 5418-5424
    • Sherblom, A.P.1    Decker, J.M.2    Muchmore, A.V.3
  • 72
    • 0024401182 scopus 로고
    • IL-2, a lectin with specificity for high mannose glycopeptides
    • Sherblom, A.P., Sathyamoorthy, N., Decker, J.M., and Muchmore, A.V., 1989, IL-2, a lectin with specificity for high mannose glycopeptides, J Immunol. 143:939-944.
    • (1989) J Immunol , vol.143 , pp. 939-944
    • Sherblom, A.P.1    Sathyamoorthy, N.2    Decker, J.M.3    Muchmore, A.V.4
  • 73
    • 0028168799 scopus 로고
    • Functional dissection of p561ck, a protein tyrosine kinase which mediates interleukin-2-induced activation of the c-fos gene
    • Shibuya, H., Kohu, K., Yamada, K., Barsoumian, E.L., Perlmutter, R.M., and Taniguchi, T., 1994, Functional dissection of p561ck, a protein tyrosine kinase which mediates interleukin-2-induced activation of the c-fos gene, Mol Cell Biol. 14:5812-5819.
    • (1994) Mol Cell Biol , vol.14 , pp. 5812-5819
    • Shibuya, H.1    Kohu, K.2    Yamada, K.3    Barsoumian, E.L.4    Perlmutter, R.M.5    Taniguchi, T.6
  • 74
    • 0025730332 scopus 로고
    • Structural and functional analyses of glycosylation on the distinct molecules of human GM-CSF receptors
    • Shibuya, K., Chiba, S., Miyagawa, K., Kitamura, T., Miyazono, K., and Takaku, F., 1991, Structural and functional analyses of glycosylation on the distinct molecules of human GM-CSF receptors, Eur J Biochem. 198:659-666.
    • (1991) Eur J Biochem , vol.198 , pp. 659-666
    • Shibuya, K.1    Chiba, S.2    Miyagawa, K.3    Kitamura, T.4    Miyazono, K.5    Takaku, F.6
  • 76
    • 0031041014 scopus 로고    scopus 로고
    • 1.9 A crystal structure of interleukin 6: Implications for a novel mode of receptor dimerization and signalling
    • Somers, W., Stahl, M., and Seehra, J.S., 1997, 1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signalling, EMBO J. 16:989-997.
    • (1997) EMBO J , vol.16 , pp. 989-997
    • Somers, W.1    Stahl, M.2    Seehra, J.S.3
  • 79
    • 0027394657 scopus 로고
    • The IL-2/1L-2 receptor system: A current overview
    • Taniguchi, T. and Minami, Y., 1993, The IL-2/1L-2 receptor system: a current overview, Cell. 73:5-8.
    • (1993) Cell , vol.73 , pp. 5-8
    • Taniguchi, T.1    Minami, Y.2
  • 80
    • 0025778240 scopus 로고
    • The interleukin-2 receptor
    • Waldmann, T.A., 1991, The interleukin-2 receptor, J Biol Chem. 266:2681-2684.
    • (1991) J Biol Chem , vol.266 , pp. 2681-2684
    • Waldmann, T.A.1
  • 81
    • 0343115153 scopus 로고    scopus 로고
    • Inhibitors of glycoprotein processing alter T-cell proliferative responses to antigen and to interleukin 2
    • Wall, K.A., Pierce, J.D., and Elbein, A.D. Inhibitors of glycoprotein processing alter T-cell proliferative responses to antigen and to interleukin 2, Proc Natl Acad Sci USA. 85:5644-5648.
    • Proc Natl Acad Sci USA , vol.85 , pp. 5644-5648
    • Wall, K.A.1    Pierce, J.D.2    Elbein, A.D.3
  • 82
    • 0028302230 scopus 로고
    • The three-dimensional structure of human interleukin-5 at 2.4-angstroms resolution: Implication for the structures of other cytokines
    • Wells, T.N.C., Graber, P., Proudfoot, A.E.I., Arod, C.Y., Jordan, S.R., Lambert, M.H., Hassel, A.M., and Milburn, M.V., 1994, The three-dimensional structure of human interleukin-5 at 2.4-angstroms resolution: implication for the structures of other cytokines, Ann N Y Acad Sci. 725:118-127.
    • (1994) Ann N Y Acad Sci , vol.725 , pp. 118-127
    • Wells, T.N.C.1    Graber, P.2    Proudfoot, A.E.I.3    Arod, C.Y.4    Jordan, S.R.5    Lambert, M.H.6    Hassel, A.M.7    Milburn, M.V.8
  • 83
    • 0025242364 scopus 로고
    • Uromodulin: A specific inhibitor of IL-1-initiated human T cell colony formation
    • Winkelstein, A., Muchmore, A.V., Decker, J.M., and Blaese, R.M., 1990, Uromodulin: a specific inhibitor of IL-1-initiated human T cell colony formation, Immunopharmacol. 20:201-205.
    • (1990) Immunopharmacol , vol.20 , pp. 201-205
    • Winkelstein, A.1    Muchmore, A.V.2    Decker, J.M.3    Blaese, R.M.4
  • 84
    • 0026730827 scopus 로고
    • Effect of semi-random mutagenesis at the C-terminal 4 amino acids of human interleukin-6 on its biological activity
    • Yasueda, H., Miyasaka, Y., Shimamura, T., and Matsui, H., 1992, Effect of semi-random mutagenesis at the C-terminal 4 amino acids of human interleukin-6 on its biological activity, Biochem Biophys Res Commun. 187:18-25.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 18-25
    • Yasueda, H.1    Miyasaka, Y.2    Shimamura, T.3    Matsui, H.4
  • 85
    • 0029814157 scopus 로고    scopus 로고
    • Interleukin 2 is a lectin that associates its receptor with the T-cell receptor complex
    • Zanetta, J.P., Alonso, C., and Michalski, J.C., 1996, Interleukin 2 is a lectin that associates its receptor with the T-cell receptor complex, Biochem J. 318:49-53.
    • (1996) Biochem J , vol.318 , pp. 49-53
    • Zanetta, J.P.1    Alonso, C.2    Michalski, J.C.3
  • 86
    • 0037064069 scopus 로고    scopus 로고
    • Evidence for a lectin activity for human interleukin-3 and modelling of its carbohydrate-recognition domain
    • Zanetta, J.P., Bindeus, R., Normand, G., Durier, V., Lagant, P., Maes, E., and Vergoten, G., 2002, Evidence for a lectin activity for human interleukin-3 and modelling of its carbohydrate-recognition domain, J Biol Chem. 277:38764-38771.
    • (2002) J Biol Chem , vol.277 , pp. 38764-38771
    • Zanetta, J.P.1    Bindeus, R.2    Normand, G.3    Durier, V.4    Lagant, P.5    Maes, E.6    Vergoten, G.7
  • 87
    • 0031931055 scopus 로고
    • Differential binding of lectins IL-2 and CSL to Candida albicans and cancer cells
    • Zanetta, J.P., Bonaly, R., Maschke, S., Strecker, G., and Michalski, J.C., 1988, Differential binding of lectins IL-2 and CSL to Candida albicans and cancer cells, Glycobiology. 8:221-225.
    • (1988) Glycobiology , vol.8 , pp. 221-225
    • Zanetta, J.P.1    Bonaly, R.2    Maschke, S.3    Strecker, G.4    Michalski, J.C.5
  • 88
    • 0242618431 scopus 로고
    • Hypothesis: Immunodeficiencies in α-mannosidosis, mycosis, aids and cancer: A common mechanism of inhibition of the function of interleukin 2 by oligomannosides
    • Zanetta, J.P., Bonaly, R., Maschke, S., Strecker, G., and Michalski, J.C., 1988, Hypothesis: Immunodeficiencies in α-mannosidosis, mycosis, aids and cancer: a common mechanism of inhibition of the function of interleukin 2 by oligomannosides, Glycobiology. 8:v-xi.
    • (1988) Glycobiology , vol.8
    • Zanetta, J.P.1    Bonaly, R.2    Maschke, S.3    Strecker, G.4    Michalski, J.C.5
  • 89
    • 0023196481 scopus 로고
    • Isolation and immunochemical study of a soluble cerebellar lectin delineating its structure and function
    • Zanetta, J.P., Meyer, A., Kuchler, S., and Vincendon, G., 1987, Isolation and immunochemical study of a soluble cerebellar lectin delineating its structure and function, J Neurochem. 49:1250-1257.
    • (1987) J Neurochem , vol.49 , pp. 1250-1257
    • Zanetta, J.P.1    Meyer, A.2    Kuchler, S.3    Vincendon, G.4
  • 90
    • 0034866154 scopus 로고    scopus 로고
    • Diversity of sialic acids revealed using gas chromatography/mass spectrometry of heptafluorobutyrate derivatives
    • Zanetta, J.P., Pons, A., Iwersen, M., Mariller, C., Leroy, Y., Timmerman, P., and Schauer, R., 2001, Diversity of sialic acids revealed using gas chromatography/mass spectrometry of heptafluorobutyrate derivatives, Glycobiology. 11:663-676.
    • (2001) Glycobiology , vol.11 , pp. 663-676
    • Zanetta, J.P.1    Pons, A.2    Iwersen, M.3    Mariller, C.4    Leroy, Y.5    Timmerman, P.6    Schauer, R.7
  • 91
    • 0028834718 scopus 로고
    • Human lymphocyte activation is associated with the early and high-level expression of the endogenous lectin CSL at the cell surface
    • Zanetta, J.P., Wantyghem, J., Kuchler-Bopp, S., Badache, A., and Aubery, M., 1995, Human lymphocyte activation is associated with the early and high-level expression of the endogenous lectin CSL at the cell surface, Biochem J. 311:629-636.
    • (1995) Biochem J , vol.311 , pp. 629-636
    • Zanetta, J.P.1    Wantyghem, J.2    Kuchler-Bopp, S.3    Badache, A.4    Aubery, M.5
  • 92
    • 0025872622 scopus 로고
    • Expression of IL-2 receptor p55 and p75 chains by human B lymphocytes: Effects of activation and differentiation
    • Zola, H., Weedon, H., Thompson, G.R., Fung, M.C., Ingley, E., and Hapel, A.J., 1991, Expression of IL-2 receptor p55 and p75 chains by human B lymphocytes: effects of activation and differentiation, Immunology. 72:167-173.
    • (1991) Immunology , vol.72 , pp. 167-173
    • Zola, H.1    Weedon, H.2    Thompson, G.R.3    Fung, M.C.4    Ingley, E.5    Hapel, A.J.6


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