메뉴 건너뛰기




Volumn 598, Issue , 2007, Pages 389-406

Biological roles of lectins in innate immunity: Molecular and structural basis for diversity in self/non-self recognition

Author keywords

[No Author keywords available]

Indexed keywords

C REACTIVE PROTEIN; LECTIN; PROTEIN DERIVATIVE;

EID: 84934436728     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-71767-8_27     Document Type: Conference Paper
Times cited : (59)

References (77)
  • 1
    • 0034708480 scopus 로고    scopus 로고
    • Adams, M.D, Celniker, S.E, Holt, R.A, Evans, C.A, Gocayne, J.D, Amanatides, P.G, Scherer, S.E, Li, P.W, Hoskins, R.A, Galle, R.F, George, R.A, Lewis, S.E, Richards, S, Ashburner, M, Henderson, S.N, Sutton, G.G, Wortman, J.R, Yandell, M.D, Zhang, Q, Chen, L.X, Brandon, R.C, Rogers, Y.H, Blazej, R.G, Champe, M, Pfeiffer, B.D, Wan, K.H, Doyle, C, Baxter, E.G, Helt, G, Nelson, C.R, Gabor, G.L, Abril, J.F, Agbayani, A, An, H.J, Andrews-Pfannkoch, C, Baldwin, D, Ballew, R.M, Basu, A, Baxendale, J, Bayraktaroglu, L, Beasley, E.M, Beeson, K.Y, Benos, P.V, Berman, B.P, Bhandari, D, Bolshakov, S, Borkova, D, Botchan, M.R, Bouck, J, Brokstein, P, Brottier, P, Burtis, K.C, Busam, D.A, Butler, H, Cadieu, E, Center, A, Chandra, I, Cherry, J.M, Cawley, S, Dahlke, C, Davenport, L.B, Davies, P, de Pablos, B, Delcher, A, Deng, Z, Mays, A.D, Dew, I, Dietz, S.M, Dodson, K, Doup, L.E, Downes, M, Dugan-Rocha, S, Dunkov, B.C, Dunn, P
    • Adams, M.D., Celniker, S.E., Holt, R.A., Evans, C.A., Gocayne, J.D., Amanatides, P.G., Scherer, S.E., Li, P.W., Hoskins, R.A., Galle, R.F., George, R.A., Lewis, S.E., Richards, S., Ashburner, M., Henderson, S.N., Sutton, G.G., Wortman, J.R., Yandell, M.D., Zhang, Q., Chen, L.X., Brandon, R.C., Rogers, Y.H., Blazej, R.G., Champe, M., Pfeiffer, B.D., Wan, K.H., Doyle, C., Baxter, E.G., Helt, G., Nelson, C.R., Gabor, G.L., Abril, J.F., Agbayani, A., An, H.J., Andrews-Pfannkoch, C., Baldwin, D., Ballew, R.M., Basu, A., Baxendale, J., Bayraktaroglu, L., Beasley, E.M., Beeson, K.Y., Benos, P.V., Berman, B.P., Bhandari, D., Bolshakov, S., Borkova, D., Botchan, M.R., Bouck, J., Brokstein, P., Brottier, P., Burtis, K.C., Busam, D.A., Butler, H., Cadieu, E., Center, A., Chandra, I., Cherry, J.M., Cawley, S., Dahlke, C., Davenport, L.B., .Davies, P., de Pablos, B., Delcher, A., Deng, Z., Mays, A.D., Dew, I., Dietz, S.M., Dodson, K., Doup, L.E., Downes, M., Dugan-Rocha, S., Dunkov, B.C., Dunn, P., Durbin, K.J., Evangelista, C.C., Ferraz, C., Ferriera, S., Fleischmann, W., Fosler, C., Gabrielian, A.E., Garg, N.S., Gelbart, W.M., Glasser, K., Glodek, A., Gong, F., Gorrell, J.H., Gu, Z., Guan, P., Harris, M., Harris, N.L., Harvey, D., Heiman, T.J., Hernandez, J.R., Houck, J., Hostin, D., Houston, K.A., Howland, T.J., Wei, M.H., Ibegwamm, C., Jalali, M., Kalush, F., Karpen, G.H., Ke, Z., Kennison, J.A., Ketchum, K.A., Kimmel, B.E., Kodira, C.D., Kraft, C., Kravitz, S., Kulp, D., Lai, Z., Lasko, P., Lei, Y., Levitsky, A.A., J., L., Z., L., Liang, Y., Lin, X., Liu, X., Mattei, B., McIntosh, T.C., McLeod, M.P., McPherson, D., G., M., V., M.N., C., M., J., M., Moshrefi, A., Mount, S.M., Moy, M., Murphy, B., Murphy, L., Muzny, D.M., Nelson, D.L., Nelson, D.R., Nelson, K.A., Nixon, K., Nusskern, D.R., Pacleb, J.M., Palazzolo, M., Pittman, G.S., Pan, S., Pollard, J., Puri, V., Reese, M.G., Reinert, K., Remington, K., Saunders, R.D., Scheeler, F., Shen, H., Shue, B.C., Siden-Kiamos, I., Simpson, M., Skupski, M.P., Smith, T., Spier, E., Spradling, A.C., Stapleton, M., Strong, R., Sun, E., Svirskas, R., Tector, C., Turner, R., Venter, E., Wang, A.H., Wang, X., Wang, Z.Y., Wassarman, D.A., Weinstock, G.M., Weissenbach, J., Williams, S.M., Woodage, T., Worley, K.C., Wu, D., Yang, S., Yao, Q.A., Ye, J., Yeh, R.F., Zaveri, J.S., Zhan, M., Zhang, G., Zhao, Q., Zheng, L., Zheng, X.H., Zhong, F.N., Zhong, W., Zhou, X., Zhu, S., Zhu, X., Smith, H.O., Gibbs, R.A., Myers, E.W., Rubin, G.M. and Venter, J.C. (2000) The genome sequence of Drosophila melanogaster. Science 287, 2185-2195.
  • 2
    • 0030831258 scopus 로고    scopus 로고
    • A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection
    • Adema, C.M., Hertel, L.A., Miller, R.D. and Loker, E.S. (1997) A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection. Proc. Natl. Acad. Sci. U S A 94, 8691-8696.
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 8691-8696
    • Adema, C.M.1    Hertel, L.A.2    Miller, R.D.3    Loker, E.S.4
  • 3
    • 1542285490 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of galectins from zebrafish (Danio rerio): Notochord-specific expression of a prototype galectin during early embryogenesis
    • Ahmed, H., Du, S.J., O'Leary, N. and Vasta, G.R. (2004) Biochemical and molecular characterization of galectins from zebrafish (Danio rerio): notochord-specific expression of a prototype galectin during early embryogenesis. Glycobiology 14, 219-232.
    • (2004) Glycobiology , vol.14 , pp. 219-232
    • Ahmed, H.1    Du, S.J.2    O'Leary, N.3    Vasta, G.R.4
  • 4
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: Critical proteins linking innate and acquired immunity
    • Akira, S., Takeda, K. and Kaisho, T. (2001) Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol. 2, 675-680.
    • (2001) Nat. Immunol , vol.2 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaisho, T.3
  • 6
    • 33845958124 scopus 로고    scopus 로고
    • A novel function for galectin-1 at the crossroad of innate and adaptive immunity: Galectin-1 regulates monocyte/macrophage physiology through a nonapoptotic ERK-dependent pathway
    • Barrionuevo, P., Beigier-Bompadre, M., Ilarregui, J.M., Toscano, M.A., Bianco, G.A., Isturiz, M.A. and Rabinovich, G.A. (2007) A novel function for galectin-1 at the crossroad of innate and adaptive immunity: galectin-1 regulates monocyte/macrophage physiology through a nonapoptotic ERK-dependent pathway. J. Immunol. 178, 436-445.
    • (2007) J. Immunol , vol.178 , pp. 436-445
    • Barrionuevo, P.1    Beigier-Bompadre, M.2    Ilarregui, J.M.3    Toscano, M.A.4    Bianco, G.A.5    Isturiz, M.A.6    Rabinovich, G.A.7
  • 8
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker, D.J. and Lowe, J.B. (2003) Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41R-53R.
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 9
    • 0036312626 scopus 로고    scopus 로고
    • A novel fucose recognition fold involved in innate immunity
    • Bianchet, M.A., Odom, E.W., Vasta, G.R. and Amzel, L.M. (2002) A novel fucose recognition fold involved in innate immunity. Nat. Struct. Biol. 9, 628-634.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 628-634
    • Bianchet, M.A.1    Odom, E.W.2    Vasta, G.R.3    Amzel, L.M.4
  • 11
    • 0030591452 scopus 로고    scopus 로고
    • The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily
    • Brissett, N.C. and Perkins, S.J. (1996) The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily. FEBS Lett. 388, 211-216.
    • (1996) FEBS Lett , vol.388 , pp. 211-216
    • Brissett, N.C.1    Perkins, S.J.2
  • 13
    • 0036915521 scopus 로고    scopus 로고
    • Identification of diversified genes that contain immunoglobulin-like variable regions in a protochordate
    • Cannon, J.P., Haire, R.N. and Litman, G.W. (2002) Identification of diversified genes that contain immunoglobulin-like variable regions in a protochordate. Nat. Immunol. 3, 1124-1125.
    • (2002) Nat. Immunol , vol.3 , pp. 1124-1125
    • Cannon, J.P.1    Haire, R.N.2    Litman, G.W.3
  • 14
    • 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
  • 15
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer, K. (1992) Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 360, 183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 16
    • 0033428909 scopus 로고    scopus 로고
    • C-Type lectin-like domains in Caenorhabditis elegans: Predictions from the complete genome sequence
    • Drickamer, K. and Dodd, R.B. (1999) C-Type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence. Glycobiology 9, 1357-1369.
    • (1999) Glycobiology , vol.9 , pp. 1357-1369
    • Drickamer, K.1    Dodd, R.B.2
  • 17
    • 0001044156 scopus 로고    scopus 로고
    • The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • Ewart, K.V., Li, Z., Yang, D.S., Fletcher, G.L. and Hew, C.L. (1998) The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochemistry 37, 4080-4085.
    • (1998) Biochemistry , vol.37 , pp. 4080-4085
    • Ewart, K.V.1    Li, Z.2    Yang, D.S.3    Fletcher, G.L.4    Hew, C.L.5
  • 18
    • 0037904914 scopus 로고    scopus 로고
    • Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2
    • Feinberg, H., Uitdehaag, J.C., Davies, J.M., Wallis, R., Drickamer, K. and Weis, W.I. (2003) Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2. EMBO J. 22, 2348-2359.
    • (2003) EMBO J , vol.22 , pp. 2348-2359
    • Feinberg, H.1    Uitdehaag, J.C.2    Davies, J.M.3    Wallis, R.4    Drickamer, K.5    Weis, W.I.6
  • 20
    • 0036584407 scopus 로고    scopus 로고
    • Evolution of the lectin-complement activation pathway and its role in innate immunity
    • Fujita, T. (2002) Evolution of the lectin-complement activation pathway and its role in innate immunity. Nat. Rev. Immunol. 2, 346-353.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 346-353
    • Fujita, T.1
  • 21
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway - its role in innate immunity and evolution
    • Fujita, T., Matsushita, M. and Endo, Y. (2004) The lectin-complement pathway - its role in innate immunity and evolution. Immunol. Rev. 198, 185-202.
    • (2004) Immunol. Rev , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 23
    • 0029645872 scopus 로고
    • The three domains of a bacterial sialidase: A beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll
    • Gaskell, A., Crennell, S. and Taylor, G. (1995) The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure 3, 1197-1205.
    • (1995) Structure , vol.3 , pp. 1197-1205
    • Gaskell, A.1    Crennell, S.2    Taylor, G.3
  • 24
    • 0034693055 scopus 로고    scopus 로고
    • Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins
    • Honda, S., Kashiwagi, M., Miyamoto, K., Takei, Y. and Hirose, S. (2000) Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins. J. Biol. Chem. 275, 33151-33157.
    • (2000) J. Biol. Chem , vol.275 , pp. 33151-33157
    • Honda, S.1    Kashiwagi, M.2    Miyamoto, K.3    Takei, Y.4    Hirose, S.5
  • 27
    • 0036800448 scopus 로고    scopus 로고
    • Galectin-3 binds lactosaminylated lipooligosaccharides from Neisseria gonorrhoeae and is selectively expressed by mucosal epithelial cells that are infected
    • John, C.M., Jarvis, G.A., Swanson, K.V., Leffler, H., Cooper, M.D., Huflejt, M.E. and Griffiss, J.M. (2002) Galectin-3 binds lactosaminylated lipooligosaccharides from Neisseria gonorrhoeae and is selectively expressed by mucosal epithelial cells that are infected. Cell Micorbiol. 4, 649-662.
    • (2002) Cell Micorbiol , vol.4 , pp. 649-662
    • John, C.M.1    Jarvis, G.A.2    Swanson, K.V.3    Leffler, H.4    Cooper, M.D.5    Huflejt, M.E.6    Griffiss, J.M.7
  • 29
    • 0032544089 scopus 로고    scopus 로고
    • A peptidoglycan recognition protein in innate immunity conserved from insects to humans
    • Kang, D., Liu, G., Lundstrom, A., Gelius, E. and Steiner, H. (1998) A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc. Natl. Acad. Sci. U S A 95, 10078-10082.
    • (1998) Proc. Natl. Acad. Sci. U S A , vol.95 , pp. 10078-10082
    • Kang, D.1    Liu, G.2    Lundstrom, A.3    Gelius, E.4    Steiner, H.5
  • 31
    • 5144234518 scopus 로고    scopus 로고
    • Recognition strategies in the innate immune system of ancestral chordates
    • Khalturin, K., Panzer, Z., Cooper, M.D. and Bosch, T.C. (2004) Recognition strategies in the innate immune system of ancestral chordates. Mol. Immunol. 41, 1077-1087.
    • (2004) Mol. Immunol , vol.41 , pp. 1077-1087
    • Khalturin, K.1    Panzer, Z.2    Cooper, M.D.3    Bosch, T.C.4
  • 32
    • 0142089668 scopus 로고    scopus 로고
    • L-selectin: An emerging player in chemokine function
    • Khan, A.I. and Kubes, P. (2003) L-selectin: an emerging player in chemokine function. Microcirculation 10, 351-358.
    • (2003) Microcirculation , vol.10 , pp. 351-358
    • Khan, A.I.1    Kubes, P.2
  • 33
    • 0042195829 scopus 로고    scopus 로고
    • Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster
    • Kim, M.S., Byun, M. and Oh, B.H. (2003) Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat. Immunol. 4, 787-793.
    • (2003) Nat. Immunol , vol.4 , pp. 787-793
    • Kim, M.S.1    Byun, M.2    Oh, B.H.3
  • 34
    • 17644409070 scopus 로고    scopus 로고
    • The X-lectins: A new family with homology to the Xenopus laevis oocyte lectin XL-35
    • Lee, J.K., Baum, L.G., Moremen, K. and Pierce, M. (2004) The X-lectins: a new family with homology to the Xenopus laevis oocyte lectin XL-35. Glycoconj.J. 21, 443-450.
    • (2004) Glycoconj.J , vol.21 , pp. 443-450
    • Lee, J.K.1    Baum, L.G.2    Moremen, K.3    Pierce, M.4
  • 35
    • 4744375297 scopus 로고    scopus 로고
    • Evolution of sialic acid-binding proteins: Molecular cloning and expression of fish siglec-4
    • Lehmann, F., Gathje, H., Kelm, S. and Dietz, F. (2004) Evolution of sialic acid-binding proteins: molecular cloning and expression of fish siglec-4. Glycobiology 14, 959-968.
    • (2004) Glycobiology , vol.14 , pp. 959-968
    • Lehmann, F.1    Gathje, H.2    Kelm, S.3    Dietz, F.4
  • 36
    • 0035897571 scopus 로고    scopus 로고
    • Structure of two FREP genes that combine IgSF and fibrinogen domains, with comments on diversity of the FREP gene family in the snail Biomphalaria glabrata
    • Leonard, P.M., Adema, C.M., Zhang, S.M. and Loker, E.S. (2001) Structure of two FREP genes that combine IgSF and fibrinogen domains, with comments on diversity of the FREP gene family in the snail Biomphalaria glabrata. Gene 269, 155-165.
    • (2001) Gene , vol.269 , pp. 155-165
    • Leonard, P.M.1    Adema, C.M.2    Zhang, S.M.3    Loker, E.S.4
  • 38
    • 2442519018 scopus 로고    scopus 로고
    • Selectins in T-cell recruitment to non-lymphoid tissues and sites of inflammation
    • Ley, K. and Kansas, G.S. (2004) Selectins in T-cell recruitment to non-lymphoid tissues and sites of inflammation. Nat. Rev. Immunol. 4, 325-335.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 325-335
    • Ley, K.1    Kansas, G.S.2
  • 39
    • 0029022485 scopus 로고
    • Structure and expression of Hemolin, an insect member of the immunoglobulin gene superfamily
    • Lindstrom-Dinnetz, I., Sun, S.C. and Faye, I. (1995) Structure and expression of Hemolin, an insect member of the immunoglobulin gene superfamily. Eur. J. Biochem. 230, 920-925.
    • (1995) Eur. J. Biochem , vol.230 , pp. 920-925
    • Lindstrom-Dinnetz, I.1    Sun, S.C.2    Faye, I.3
  • 40
    • 27644578820 scopus 로고    scopus 로고
    • Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta
    • Ling, E. and Yu, X.Q. (2006) Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta. Dev. Comp. Immunol. 30, 289-299.
    • (2006) Dev. Comp. Immunol , vol.30 , pp. 289-299
    • Ling, E.1    Yu, X.Q.2
  • 41
    • 11144241063 scopus 로고    scopus 로고
    • Liu, F.T. and Rabinovich, G.A. (2005) Galectins as modulators of tumour progression. Nat. Rex. Cancer 5, 29-41.
    • Liu, F.T. and Rabinovich, G.A. (2005) Galectins as modulators of tumour progression. Nat. Rex. Cancer 5, 29-41.
  • 42
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu, Y. and Eisenberg, D. (2002) 3D domain swapping: as domains continue to swap. Protein Sci. 11, 1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 47
    • 0344299170 scopus 로고    scopus 로고
    • Physiological aspects of the immunoglobulin superfamily in invertebrates
    • Mendoza, H.L. and Faye, I. (1999) Physiological aspects of the immunoglobulin superfamily in invertebrates. Dev. Comp. Immunol. 23, 359-374.
    • (1999) Dev. Comp. Immunol , vol.23 , pp. 359-374
    • Mendoza, H.L.1    Faye, I.2
  • 48
    • 33644981902 scopus 로고    scopus 로고
    • Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis)
    • Odom, E.W. and Vasta, G.R. (2006) Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis). J. Biol. Chem. 281, 1698-1713.
    • (2006) J. Biol. Chem , vol.281 , pp. 1698-1713
    • Odom, E.W.1    Vasta, G.R.2
  • 49
    • 32944477673 scopus 로고    scopus 로고
    • The evolution of adaptive immunity
    • Pancer, Z. and Cooper, M.D. (2006) The evolution of adaptive immunity. Annu. Rev. Immunol. 24, 497-518.
    • (2006) Annu. Rev. Immunol , vol.24 , pp. 497-518
    • Pancer, Z.1    Cooper, M.D.2
  • 50
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • Rabinovich, G.A., Rubinstein, N. and Toscano, M.A. (2002) Role of galectins in inflammatory and immunomodulatory processes. Biochim. Biophys. Acta 1572, 274-284.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.A.3
  • 51
    • 1542283655 scopus 로고    scopus 로고
    • Shedding light on the immunomodulatory properties of galectins: Novel regulators of innate and adaptive immune responses
    • Rabinovich, G.A., Toscano, M.A., Ilarregui, J.M. and Rubinstein, N. (2004) Shedding light on the immunomodulatory properties of galectins: novel regulators of innate and adaptive immune responses. Glycoconj. J. 16, 565-573.
    • (2004) Glycoconj. J , vol.16 , pp. 565-573
    • Rabinovich, G.A.1    Toscano, M.A.2    Ilarregui, J.M.3    Rubinstein, N.4
  • 52
    • 0030662197 scopus 로고    scopus 로고
    • A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides
    • Saito, T., Hatada, M., Iwanaga, S. and Kawabata, S. (1997) A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J. Biol. Chem. 272, 30703-30708.
    • (1997) J. Biol. Chem , vol.272 , pp. 30703-30708
    • Saito, T.1    Hatada, M.2    Iwanaga, S.3    Kawabata, S.4
  • 53
    • 0025693237 scopus 로고
    • Hemolin: An insect-immune protein belonging to the immunoglobulin superfamily
    • Sun, S.C., Lindstrom, I., Boman, H.G., Faye, I. and Schmidt, O. (1990) Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science 250, 1729-1732.
    • (1990) Science , vol.250 , pp. 1729-1732
    • Sun, S.C.1    Lindstrom, I.2    Boman, H.G.3    Faye, I.4    Schmidt, O.5
  • 54
    • 0037178884 scopus 로고    scopus 로고
    • Primary structure and characteristics of a lectin from skin mucus of the Japanese eel Anguilla japonica
    • Tasumi, S., Ohira, T., Kawazoe, I., Suetake, H., Suzuki, Y. and Aida, K. (2002) Primary structure and characteristics of a lectin from skin mucus of the Japanese eel Anguilla japonica. J. Biol. Chem. 277, 27305-27311.
    • (2002) J. Biol. Chem , vol.277 , pp. 27305-27311
    • Tasumi, S.1    Ohira, T.2    Kawazoe, I.3    Suetake, H.4    Suzuki, Y.5    Aida, K.6
  • 55
    • 0036490246 scopus 로고    scopus 로고
    • Rhamnose-binding lectins from steelhead trout (Oncorhynchus mykiss) eggs recognize bacterial lipopolysaccharides and lipoteichoic acid
    • Tateno, H., Ogawa, T., Muramoto, K., Kamiya, H. and Saneyoshi, M. (2002) Rhamnose-binding lectins from steelhead trout (Oncorhynchus mykiss) eggs recognize bacterial lipopolysaccharides and lipoteichoic acid. Biosci. Biotechnol. Biochem. 66, 604-612.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 604-612
    • Tateno, H.1    Ogawa, T.2    Muramoto, K.3    Kamiya, H.4    Saneyoshi, M.5
  • 56
    • 58849139114 scopus 로고    scopus 로고
    • Binding of oligosaccharide ligands to the selectins requires additional interactions with the carbohydrate- recognition domains
    • M.E. Taylor and K. Drickamer Eds, Oxford University Press, Oxford; New York, p
    • Taylor, M.E. and Drickamer, K. (2003) Binding of oligosaccharide ligands to the selectins requires additional interactions with the carbohydrate- recognition domains. In: M.E. Taylor and K. Drickamer (Eds), Introduction of Glycobiology. Oxford University Press, Oxford; New York, p. 207.
    • (2003) Introduction of Glycobiology , pp. 207
    • Taylor, M.E.1    Drickamer, K.2
  • 57
    • 33644899372 scopus 로고    scopus 로고
    • Tsutsui, S., Tasumi, S., Suetake, H., Kikuchi, K. and Suzuki, Y. (2006) Carbohydrate-binding site of a novel mannose-specific lectin from fugu (Takifugu rubripes) skin mucus. Comp. Biochem. Physio. B Biochem. Mol. Biol. 143, 514-519.
    • Tsutsui, S., Tasumi, S., Suetake, H., Kikuchi, K. and Suzuki, Y. (2006) Carbohydrate-binding site of a novel mannose-specific lectin from fugu (Takifugu rubripes) skin mucus. Comp. Biochem. Physio. B Biochem. Mol. Biol. 143, 514-519.
  • 58
    • 0346961787 scopus 로고    scopus 로고
    • On the origins of adaptive immunity: Innate immune receptors join the tale
    • van den Berg, T.K., Yoder, J.A. and Litman, G.W. (2004) On the origins of adaptive immunity: innate immune receptors join the tale. Trends Immunol. 25, 11-16.
    • (2004) Trends Immunol , vol.25 , pp. 11-16
    • van den Berg, T.K.1    Yoder, J.A.2    Litman, G.W.3
  • 60
    • 4744351376 scopus 로고    scopus 로고
    • Galectins in teleost fish: Zebrafish (Danio rerio) as a model species to address their biological roles in development and innate immunity
    • Vasta, G.R., Ahmed, H., Du, S.-J. and Henrikson, D. (2004a) Galectins in teleost fish: Zebrafish (Danio rerio) as a model species to address their biological roles in development and innate immunity. Glycoconj. J. 21, 503-521.
    • (2004) Glycoconj. J , vol.21 , pp. 503-521
    • Vasta, G.R.1    Ahmed, H.2    Du, S.-J.3    Henrikson, D.4
  • 61
    • 4744359093 scopus 로고    scopus 로고
    • Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates
    • Vasta, G.R., Ahmed, H. and Odom, E.W. (2004b) Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates. Curr. Opin. Struct. Biol. 14, 617-630.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 617-630
    • Vasta, G.R.1    Ahmed, H.2    Odom, E.W.3
  • 62
    • 0033052588 scopus 로고    scopus 로고
    • C-type lectins and galectins mediate innate and adaptive immune functions: Their roles in the complement activation pathway
    • Vasta, G.R., Quesenberry, M., Ahmed, H. and O'Leary, N. (1999) C-type lectins and galectins mediate innate and adaptive immune functions: their roles in the complement activation pathway. Dev. Comp. Immunol. 23, 401-420.
    • (1999) Dev. Comp. Immunol , vol.23 , pp. 401-420
    • Vasta, G.R.1    Quesenberry, M.2    Ahmed, H.3    O'Leary, N.4
  • 63
    • 0035062580 scopus 로고    scopus 로고
    • Lectins from tunicates: Structure-function relationships in innate immunity
    • Vasta, G.R., Quesenberry, M.S., Ahmed, H. and O'Leary, N. (2001) Lectins from tunicates: structure-function relationships in innate immunity. Adv. Exp. Med. Biol. 484, 275-287.
    • (2001) Adv. Exp. Med. Biol , vol.484 , pp. 275-287
    • Vasta, G.R.1    Quesenberry, M.S.2    Ahmed, H.3    O'Leary, N.4
  • 64
    • 0036215134 scopus 로고    scopus 로고
    • Vilches, C. and Parham, P. (2002) KIR: diverse, rapidly evolving receptors of innate and adaptive immunity. Annu. Rev. Immunol. 20, 217-251.
    • Vilches, C. and Parham, P. (2002) KIR: diverse, rapidly evolving receptors of innate and adaptive immunity. Annu. Rev. Immunol. 20, 217-251.
  • 65
    • 0033816605 scopus 로고    scopus 로고
    • The homologue of mannose-binding lectin in the carp family cyprinidae is expressed at high level in spleen, and the deduced primary structure predicts affinity for galactose
    • Vitved, L., Holmskov, U., Koch, C., Teisner, B., Hansen, S., Salomonsen, J. and Skjodt, K. (2000) The homologue of mannose-binding lectin in the carp family cyprinidae is expressed at high level in spleen, and the deduced primary structure predicts affinity for galactose. Immunogenetics 51, 955-964.
    • (2000) Immunogenetics , vol.51 , pp. 955-964
    • Vitved, L.1    Holmskov, U.2    Koch, C.3    Teisner, B.4    Hansen, S.5    Salomonsen, J.6    Skjodt, K.7
  • 66
    • 0036748175 scopus 로고    scopus 로고
    • Structural and functional aspects of complement activation by mannose-binding protein
    • Wallis, R. (2002) Structural and functional aspects of complement activation by mannose-binding protein. Immunibiology 205, 433-445.
    • (2002) Immunibiology , vol.205 , pp. 433-445
    • Wallis, R.1
  • 67
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis, W.I. and Drickamer, K. (1994) Trimeric structure of a C-type mannose-binding protein. Structure 2, 1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 68
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis, W.I., Drickamer, K. and Hendrickson, W.A. (1992) Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 69
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis, W.I., Taylor, M.E. and Drickamer, K. (1998) The C-type lectin superfamily in the immune system. Immunol. Rev. 163, 19-34.
    • (1998) Immunol. Rev , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 73
    • 9444231673 scopus 로고    scopus 로고
    • C-type lectin-like domains in Fugu rubripes
    • Zelensky, A.N. and Gready, J.E. (2004) C-type lectin-like domains in Fugu rubripes. BMC Genomics 5, 51.
    • (2004) BMC Genomics , vol.5 , pp. 51
    • Zelensky, A.N.1    Gready, J.E.2
  • 74
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky, A.N. and Gready, J.E. (2005) The C-type lectin-like domain superfamily. FEBS Lett. 272, 6179-6217.
    • (2005) FEBS Lett , vol.272 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 75
    • 0034670154 scopus 로고    scopus 로고
    • Cloning, mapping and genomic organization of a fish C-type lectin gene from homozygous clones of rainbow trout (Oncorhynchus mykiss)
    • Zhang, H., Robison, B., Thorgaard, G.H. and Ristow, S.S. (2000) Cloning, mapping and genomic organization of a fish C-type lectin gene from homozygous clones of rainbow trout (Oncorhynchus mykiss). Biochim. Biophys. Acta 1494, 14-22.
    • (2000) Biochim. Biophys. Acta , vol.1494 , pp. 14-22
    • Zhang, H.1    Robison, B.2    Thorgaard, G.H.3    Ristow, S.S.4
  • 76
    • 3042802389 scopus 로고    scopus 로고
    • Diversification of Ig superfamily genes in an invertebrate
    • Zhang, S.-M., Ademam, C.M., Kepler, T.B. and Locker, E.S. (2004) Diversification of Ig superfamily genes in an invertebrate. Science 305, 251-254.
    • (2004) Science , vol.305 , pp. 251-254
    • Zhang, S.-M.1    Ademam, C.M.2    Kepler, T.B.3    Locker, E.S.4
  • 77
    • 0037362058 scopus 로고    scopus 로고
    • The FREP gene family in the snail Biomphalaria glabrata: Additional members, and evidence consistent with alternative splicing and FREP retrosequences. Fibrinogen-related proteins
    • Zhang, S.M. and Loker, E.S. (2003) The FREP gene family in the snail Biomphalaria glabrata: additional members, and evidence consistent with alternative splicing and FREP retrosequences. Fibrinogen-related proteins. Dev. Comp. Immunol. 27, 175-187.
    • (2003) Dev. Comp. Immunol , vol.27 , pp. 175-187
    • Zhang, S.M.1    Loker, E.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.