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Volumn 169, Issue 11, 2014, Pages 824-834

Molecular characterization of a novel proto-type antimicrobial protein galectin-1 from striped murrel

Author keywords

Bacterial agglutination; Erythrocytes agglutination; Galectin; Gene expression; Murrel

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; BACTERIA; BINS; BIOACTIVITY; BLOOD; CLONING; ESCHERICHIA COLI; GENE EXPRESSION; GENES; GENETIC ENGINEERING; PROTEINS;

EID: 84929941087     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2014.03.005     Document Type: Article
Times cited : (21)

References (67)
  • 1
    • 0026007210 scopus 로고
    • Soluble 14-kDa beta-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 beta-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 1991, 266:5552-5557.
    • (1991) J Biol Chem , vol.266 , pp. 5552-5557
    • Abbott, W.M.1    Feizi, T.2
  • 2
    • 84881113852 scopus 로고    scopus 로고
    • Fish lily type lectin-1 contains β-prism 2 architecture: immunological characterization
    • Abirami A., Venkatesh K., Akila S., Rajesh P., Nagaram P., Prasanth B., et al. Fish lily type lectin-1 contains β-prism 2 architecture: immunological characterization. Mol Immunol 2013, 56:497-506.
    • (2013) Mol Immunol , vol.56 , pp. 497-506
    • Abirami, A.1    Venkatesh, K.2    Akila, S.3    Rajesh, P.4    Nagaram, P.5    Prasanth, B.6
  • 3
    • 4444329794 scopus 로고    scopus 로고
    • Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3
    • Ahmad N., Gabius H.J., Sabesan S., Oscarson S., Brewer C.F. Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3. Glycobiol 2004, 14:817-825.
    • (2004) Glycobiol , vol.14 , pp. 817-825
    • Ahmad, N.1    Gabius, H.J.2    Sabesan, S.3    Oscarson, S.4    Brewer, C.F.5
  • 4
    • 84872600707 scopus 로고    scopus 로고
    • An upstream initiator caspase 10 of snakehead murrel Channa striatus, containing DED, p20 and p10 subunits: Molecular cloning, gene expression and proteolytic activity
    • Arockiaraj J., Annie J.G., Dhanaraj M., Mukesh P., Milton J., Arun S. An upstream initiator caspase 10 of snakehead murrel Channa striatus, containing DED, p20 and p10 subunits: Molecular cloning, gene expression and proteolytic activity. Fish Shellfish Immunol 2013, 34:505-513.
    • (2013) Fish Shellfish Immunol , vol.34 , pp. 505-513
    • Arockiaraj, J.1    Annie, J.G.2    Dhanaraj, M.3    Mukesh, P.4    Milton, J.5    Arun, S.6
  • 5
    • 84883157872 scopus 로고    scopus 로고
    • Macrobrachium rosenbergii Cathepsin L: molecular characterization and gene expression in response to viral and bacterial infections
    • Arockiaraj J., Annie J.G., Dhanaraj M., Thirumalai M.K., Mukesh P., James M., et al. Macrobrachium rosenbergii Cathepsin L: molecular characterization and gene expression in response to viral and bacterial infections. Microbiol Res 2013, 168:569-579.
    • (2013) Microbiol Res , vol.168 , pp. 569-579
    • Arockiaraj, J.1    Annie, J.G.2    Dhanaraj, M.3    Thirumalai, M.K.4    Mukesh, P.5    James, M.6
  • 6
    • 84878667076 scopus 로고    scopus 로고
    • A novel prophenoloxidase, hemocyanin encoded copper containing active enzyme from prawn: gene characterization
    • Arockiaraj J., Annie J.G., Gopi P., James M., Mukesh P., Prasanth B., et al. A novel prophenoloxidase, hemocyanin encoded copper containing active enzyme from prawn: gene characterization. Gene 2013, 524:139-151.
    • (2013) Gene , vol.524 , pp. 139-151
    • Arockiaraj, J.1    Annie, J.G.2    Gopi, P.3    James, M.4    Mukesh, P.5    Prasanth, B.6
  • 8
    • 84884986921 scopus 로고    scopus 로고
    • An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: analysis of immune properties
    • Arockiaraj J., Gnanam A.J., Kumaresan V., Palanisamy R., Bhatt P., Thirumalai M.K., et al. An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: analysis of immune properties. Fish Shellfish Immunol 2013, 35:1511-1522.
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 1511-1522
    • Arockiaraj, J.1    Gnanam, A.J.2    Kumaresan, V.3    Palanisamy, R.4    Bhatt, P.5    Thirumalai, M.K.6
  • 9
    • 84872609450 scopus 로고    scopus 로고
    • An effective treatment to the spotted murrel Channa punctatus for epizootic ulcerative syndrome (EUS)
    • Arockiaraj J., Haniffa M.A., Perumalsamy P.R.R., Marimuthu K., Muruganandam M. An effective treatment to the spotted murrel Channa punctatus for epizootic ulcerative syndrome (EUS). Fishing Chimes 2003, 23:27-28.
    • (2003) Fishing Chimes , vol.23 , pp. 27-28
    • Arockiaraj, J.1    Haniffa, M.A.2    Perumalsamy, P.R.R.3    Marimuthu, K.4    Muruganandam, M.5
  • 10
    • 84864286886 scopus 로고    scopus 로고
    • Gene expression and functional studies of small heat shock protein 37 (MrHSP37) from Macrobrachium rosenbergii challenged with infectious hypodermal and hematopoietic necrosis virus (IHHNV)
    • Arockiaraj J., Puganeshwaran V., Sarasvathi E., Arunsingh A.V., Rofina Y.O., Subha B. Gene expression and functional studies of small heat shock protein 37 (MrHSP37) from Macrobrachium rosenbergii challenged with infectious hypodermal and hematopoietic necrosis virus (IHHNV). Mol Biol Rep 2012, 39:6671-6682.
    • (2012) Mol Biol Rep , vol.39 , pp. 6671-6682
    • Arockiaraj, J.1    Puganeshwaran, V.2    Sarasvathi, E.3    Arunsingh, A.V.4    Rofina, Y.O.5    Subha, B.6
  • 13
    • 0027965708 scopus 로고
    • Structure and function of a large family of animal lectins
    • Barondes S.H., Cooper D.N.W., Gitt M.A., Leffler H. Structure and function of a large family of animal lectins. J Biol Chem 1994, 269:20807-20810.
    • (1994) J Biol Chem , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.W.2    Gitt, M.A.3    Leffler, H.4
  • 14
    • 84887548583 scopus 로고    scopus 로고
    • Immunological role of C4 CC chemokine-1 from snakehead murrel Channa striatus
    • Bhatt P., Venkatesh K., Rajesh P., Mukesh K.C., Annie J.G., Mukesh P., et al. Immunological role of C4 CC chemokine-1 from snakehead murrel Channa striatus. Mol Immunol 2013, 57:292-301.
    • (2013) Mol Immunol , vol.57 , pp. 292-301
    • Bhatt, P.1    Venkatesh, K.2    Rajesh, P.3    Mukesh, K.C.4    Annie, J.G.5    Mukesh, P.6
  • 15
    • 0035824575 scopus 로고    scopus 로고
    • Distinct carbohydrate recognition domains of an invertebrate defense molecule recognize gram-negative and Grampositive bacteria
    • Bilej M., De Baetselier P., Van Dijck E., Stijlemans B., Colige A., Beschin A. Distinct carbohydrate recognition domains of an invertebrate defense molecule recognize gram-negative and Grampositive bacteria. J Biol Chem 2001, 276:45840-45847.
    • (2001) J Biol Chem , vol.276 , pp. 45840-45847
    • Bilej, M.1    De Baetselier, P.2    Van Dijck, E.3    Stijlemans, B.4    Colige, A.5    Beschin, A.6
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer C.F., Miceli M.C., Baum L.G. Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr Opin Struct Biol 2002, 12:616-623.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 19
    • 33749556658 scopus 로고    scopus 로고
    • Galectin-1: a small protein with major functions
    • Camby I., Le Mercier M., Lefranc F., Kiss R. Galectin-1: a small protein with major functions. Glycobiol 2006, 16:137R-57R.
    • (2006) Glycobiol , vol.16 , pp. 137R-157R
    • Camby, I.1    Le Mercier, M.2    Lefranc, F.3    Kiss, R.4
  • 20
    • 0028986609 scopus 로고
    • Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization
    • Cho M., Cummings R.D. Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization. J Biol Chem 1995, 270:5198-5206.
    • (1995) J Biol Chem , vol.270 , pp. 5198-5206
    • Cho, M.1    Cummings, R.D.2
  • 21
    • 0001488264 scopus 로고
    • Self/non-self recognition in invertebrates
    • Coombe D.R., Ey P.L., Jenkin C.R. Self/non-self recognition in invertebrates. Q Rev Biol 1984, 59:231-255.
    • (1984) Q Rev Biol , vol.59 , pp. 231-255
    • Coombe, D.R.1    Ey, P.L.2    Jenkin, C.R.3
  • 22
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • Cooper D.N. Galectinomics: finding themes in complexity. Biochim Biophys Acta 2002, 1572:209-231.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.1
  • 23
    • 44449164359 scopus 로고    scopus 로고
    • Microbial flora from the Epizootic Ulcerative Syndrome (EUS) infected murrel Channa striatus (Bloch, 1797) in Tirunelveli region
    • Dhanaraj M., Haniffa M.A., Ramakrishnan C.M., Arunsingh S.V. Microbial flora from the Epizootic Ulcerative Syndrome (EUS) infected murrel Channa striatus (Bloch, 1797) in Tirunelveli region. Turk J Vet Anim Sci 2008, 32:221-224.
    • (2008) Turk J Vet Anim Sci , vol.32 , pp. 221-224
    • Dhanaraj, M.1    Haniffa, M.A.2    Ramakrishnan, C.M.3    Arunsingh, S.V.4
  • 24
    • 0347284261 scopus 로고    scopus 로고
    • A C-type lectin associated and translocated with cortical granules during oocyte maturation and egg fertilization in fish
    • Dong C.H., Yang T., Yan Z.A., Zhang L., Gui J.F. A C-type lectin associated and translocated with cortical granules during oocyte maturation and egg fertilization in fish. Dev Biol 2004, 265:341-354.
    • (2004) Dev Biol , vol.265 , pp. 341-354
    • Dong, C.H.1    Yang, T.2    Yan, Z.A.3    Zhang, L.4    Gui, J.F.5
  • 25
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • Drickamer K., Taylor M.E. Evolving views of protein glycosylation. Trends Biochem Sci 1998, 23:321-324.
    • (1998) Trends Biochem Sci , vol.23 , pp. 321-324
    • Drickamer, K.1    Taylor, M.E.2
  • 26
    • 21844453220 scopus 로고    scopus 로고
    • Characterization of a galactose binding serum lectin from the Indian catfish, Clarias batrachus: possible involvement of fish lectins in differential recognition of pathogens
    • Dutta S., Sinham B., Bhattacharya B., Chatterjee B., Mazumder S. Characterization of a galactose binding serum lectin from the Indian catfish, Clarias batrachus: possible involvement of fish lectins in differential recognition of pathogens. Comp Biochem Physiol C 2005, 14:76-84.
    • (2005) Comp Biochem Physiol C , vol.14 , pp. 76-84
    • Dutta, S.1    Sinham, B.2    Bhattacharya, B.3    Chatterjee, B.4    Mazumder, S.5
  • 27
    • 78649635168 scopus 로고    scopus 로고
    • A d-galactose-binding lectin purified from coronate moon turban, Turbo (Lunella) coreensis, with a unique amino acid sequence and the ability to recognize lacto-series glycosphingolipids
    • Fujii Y., Kawsar S.M.A., Matsumoto R., Yasumitsu H., Ishizaki N., Dogasaki C., et al. A d-galactose-binding lectin purified from coronate moon turban, Turbo (Lunella) coreensis, with a unique amino acid sequence and the ability to recognize lacto-series glycosphingolipids. Comp Biochem Physiol B 2011, 158:30-37.
    • (2011) Comp Biochem Physiol B , vol.158 , pp. 30-37
    • Fujii, Y.1    Kawsar, S.M.A.2    Matsumoto, R.3    Yasumitsu, H.4    Ishizaki, N.5    Dogasaki, C.6
  • 28
    • 0034851982 scopus 로고    scopus 로고
    • Galectins as modulators of cell adhesion
    • Hughes R.C. Galectins as modulators of cell adhesion. Biochimie 2001, 83:667-676.
    • (2001) Biochimie , vol.83 , pp. 667-676
    • Hughes, R.C.1
  • 29
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes R.C. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1999, 1473:172-185.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 30
    • 18044393424 scopus 로고    scopus 로고
    • Cloning and characterisation of tandem-repeat type galectin in rainbow trout (Oncorhynchus mykiss)
    • Inagawa H., Kuroda A., Nishizawa T., Honda T., Ototake M., Yokomizo Y., et al. Cloning and characterisation of tandem-repeat type galectin in rainbow trout (Oncorhynchus mykiss). Fish Shellfish Immunol 2001, 11:217-231.
    • (2001) Fish Shellfish Immunol , vol.11 , pp. 217-231
    • Inagawa, H.1    Kuroda, A.2    Nishizawa, T.3    Honda, T.4    Ototake, M.5    Yokomizo, Y.6
  • 33
    • 0023969635 scopus 로고
    • Purification and properties of agglutinins from conger eel, Conger myriaster (Brevoort), skin mucus
    • Kamiya H., Muramoto K., Goto R. Purification and properties of agglutinins from conger eel, Conger myriaster (Brevoort), skin mucus. Dev Comp Immunol 1988, 12:309-318.
    • (1988) Dev Comp Immunol , vol.12 , pp. 309-318
    • Kamiya, H.1    Muramoto, K.2    Goto, R.3
  • 34
    • 33846393242 scopus 로고    scopus 로고
    • A novel anti-inflammatory function of human galectin-1: inhibition of hematopoietic progenitor cell mobilization
    • Kiss J., Kunstar A., Fajka-Boja R., Dudics V., Tovarj J., Legradi A., et al. A novel anti-inflammatory function of human galectin-1: inhibition of hematopoietic progenitor cell mobilization. Exp Hematol 2007, 35:305-313.
    • (2007) Exp Hematol , vol.35 , pp. 305-313
    • Kiss, J.1    Kunstar, A.2    Fajka-Boja, R.3    Dudics, V.4    Tovarj, J.5    Legradi, A.6
  • 35
    • 0036198820 scopus 로고    scopus 로고
    • Activation of carp leukocytes by a galactose binding protein from Aphanomyces piscicida
    • Kurata O., Hatai K. Activation of carp leukocytes by a galactose binding protein from Aphanomyces piscicida. Dev Comp Immunol 2002, 26:161-169.
    • (2002) Dev Comp Immunol , vol.26 , pp. 161-169
    • Kurata, O.1    Hatai, K.2
  • 36
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • Lemaitre B., Reichhart J.M., Hoffmann J.A. Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc Natl Acad Sci USA 1997, 94:14614-14619.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichhart, J.M.2    Hoffmann, J.A.3
  • 37
    • 84877633464 scopus 로고    scopus 로고
    • Anti-viral activity of galectin-1 from flounder Paralichthys olivaceus
    • Liu S., Guobin H., Chen S., Shicui Z. Anti-viral activity of galectin-1 from flounder Paralichthys olivaceus. Fish Shellfish Immunol 2013, 34:1463-1469.
    • (2013) Fish Shellfish Immunol , vol.34 , pp. 1463-1469
    • Liu, S.1    Guobin, H.2    Chen, S.3    Shicui, Z.4
  • 38
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgenm T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgenm, T.D.2
  • 39
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • Lopez-Lucendo M.F., Solis D., Andre S., Hirabayashi J., Kasai K., Kaltner H., et al. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol 2004, 343:957-970.
    • (2004) J Mol Biol , vol.343 , pp. 957-970
    • Lopez-Lucendo, M.F.1    Solis, D.2    Andre, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6
  • 40
    • 0026627818 scopus 로고
    • Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin
    • Marshal P., Herrmann J., Leffler H., Barondes S.H., Cooper D.N.W. Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin. J Biol Chem 1992, 267:12942-12949.
    • (1992) J Biol Chem , vol.267 , pp. 12942-12949
    • Marshal, P.1    Herrmann, J.2    Leffler, H.3    Barondes, S.H.4    Cooper, D.N.W.5
  • 41
    • 0035524488 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Medzhitov R. Toll-like receptors and innate immunity. Nat Rev Immunol 2001, 1:135-145.
    • (2001) Nat Rev Immunol , vol.1 , pp. 135-145
    • Medzhitov, R.1
  • 42
    • 0035890468 scopus 로고    scopus 로고
    • Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica)
    • Mistry A.C., Honda S., Hirose S. Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica). Biochem J 2001, 160:107-115.
    • (2001) Biochem J , vol.160 , pp. 107-115
    • Mistry, A.C.1    Honda, S.2    Hirose, S.3
  • 43
    • 0032973033 scopus 로고    scopus 로고
    • Functional and structural characterization of multiple galectins from the skin mucus of conger eel, Conger myriaster
    • Muramoto K., Kagawa D., Sato T., Ogawa T., Nishida Y., Kamiya H. Functional and structural characterization of multiple galectins from the skin mucus of conger eel, Conger myriaster. Comp Biochem Physiol B 1999, 123:33-45.
    • (1999) Comp Biochem Physiol B , vol.123 , pp. 33-45
    • Muramoto, K.1    Kagawa, D.2    Sato, T.3    Ogawa, T.4    Nishida, Y.5    Kamiya, H.6
  • 44
    • 0026504062 scopus 로고
    • The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus
    • Muramoto K., Kamiya H. The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus. Biochim Biophys Acta 1992, 1116:129-136.
    • (1992) Biochim Biophys Acta , vol.1116 , pp. 129-136
    • Muramoto, K.1    Kamiya, H.2
  • 45
    • 25844518483 scopus 로고    scopus 로고
    • Opsonic effect of congerin, a mucosal galectin of the Japanese conger, Conger myriaster (Brevoort)
    • Nakamura O., Matsuoka H., Ogawa T., Muramoto K., Kamiya H., Watanabe T. Opsonic effect of congerin, a mucosal galectin of the Japanese conger, Conger myriaster (Brevoort). Fish Shellfish Immunol 2006, 20:433-435.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 433-435
    • Nakamura, O.1    Matsuoka, H.2    Ogawa, T.3    Muramoto, K.4    Kamiya, H.5    Watanabe, T.6
  • 46
    • 4344643316 scopus 로고    scopus 로고
    • Opsonization with C1q and mannose-binding lectin targets apoptotic cells to dendritic cells
    • Nauta A.J., Castellano G., Xu W., Woltman A.M., Borrias M.C., Daha M.R., et al. Opsonization with C1q and mannose-binding lectin targets apoptotic cells to dendritic cells. J Immunol 2004, 173:3044-3050.
    • (2004) J Immunol , vol.173 , pp. 3044-3050
    • Nauta, A.J.1    Castellano, G.2    Xu, W.3    Woltman, A.M.4    Borrias, M.C.5    Daha, M.R.6
  • 47
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel W. The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur J Biochem 2003, 270:2109-2119.
    • (2003) Eur J Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 48
    • 0023973819 scopus 로고
    • Lectinophagocytosis: a molecular mechanism of recognition between cell surface sugars and lectins in the phagocytosis of bacteria
    • Ofek I., Sharon N. Lectinophagocytosis: a molecular mechanism of recognition between cell surface sugars and lectins in the phagocytosis of bacteria. Infect Immun 1988, 56:539-547.
    • (1988) Infect Immun , vol.56 , pp. 539-547
    • Ofek, I.1    Sharon, N.2
  • 49
    • 0033162445 scopus 로고    scopus 로고
    • Accelerated evolution in the protein-coding region of galectin cDNAs, congerin I and congerin II, from skin mucus of conger eel (Conger myriaster)
    • Ogawa T., Ishii C., Kagawa D., Muramoto K., Kamiya H. Accelerated evolution in the protein-coding region of galectin cDNAs, congerin I and congerin II, from skin mucus of conger eel (Conger myriaster). Biosci Biotechnol Biochem 1999, 63:1203-1208.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1203-1208
    • Ogawa, T.1    Ishii, C.2    Kagawa, D.3    Muramoto, K.4    Kamiya, H.5
  • 50
    • 0032966861 scopus 로고    scopus 로고
    • Enhancement of anti-Aeromonas salmonicida activity in Atlantic salmon (Salmo salar) macrophages by a mannose binding lectin
    • Ottinger C.A., Johnson S.C., Ewart K.V., Brown L.L., Ross N.W. Enhancement of anti-Aeromonas salmonicida activity in Atlantic salmon (Salmo salar) macrophages by a mannose binding lectin. Comp Biochem Physiol C 1999, 123:53-59.
    • (1999) Comp Biochem Physiol C , vol.123 , pp. 53-59
    • Ottinger, C.A.1    Johnson, S.C.2    Ewart, K.V.3    Brown, L.L.4    Ross, N.W.5
  • 52
    • 84877819382 scopus 로고    scopus 로고
    • Localization and functional properties of two galectin-1 proteins in Atlantic cod (Gadus morhua) mucosal tissues
    • Rajan B., Viswanath K., Jorge M.O., Fernandes M., Brinchmann F. Localization and functional properties of two galectin-1 proteins in Atlantic cod (Gadus morhua) mucosal tissues. Dev Comp Immunol 2013, 40:83-93.
    • (2013) Dev Comp Immunol , vol.40 , pp. 83-93
    • Rajan, B.1    Viswanath, K.2    Jorge, M.O.3    Fernandes, M.4    Brinchmann, F.5
  • 53
    • 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., Kawabata S. A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J Biol Chem 1997, 272:30703-30708.
    • (1997) J Biol Chem , vol.272 , pp. 30703-30708
    • Saito, T.1    Hatada, M.2    Iwanaga, S.3    Kawabata, S.4
  • 55
    • 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 1993, 18:221-226.
    • (1993) Trends Biochem Sci , vol.18 , pp. 221-226
    • Sharon, N.1
  • 56
    • 35648982951 scopus 로고    scopus 로고
    • Production of TNF-a, IL-1b, IL-12 and IFN-g in murine peritoneal macrophages on treatment with wheat germ agglutinin in vitro: involvement of tyrosine kinase pathways
    • Sodhi A., Kesherwani V. Production of TNF-a, IL-1b, IL-12 and IFN-g in murine peritoneal macrophages on treatment with wheat germ agglutinin in vitro: involvement of tyrosine kinase pathways. Glycoconj J 2007, 24:573-582.
    • (2007) Glycoconj J , vol.24 , pp. 573-582
    • Sodhi, A.1    Kesherwani, V.2
  • 57
    • 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., Aida K. Primary structure and characteristics of a lectin from skin mucus of the Japanese eel (Anguilla japonica). J Biol Chem 2002, 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
  • 58
    • 0346494354 scopus 로고    scopus 로고
    • Characteristics and primary structure of a galectin in the skin mucus of the Japanese eel (Anguilla japonica)
    • Tasumi S., Yang W.J., Usami T., Tsutsui S., Ohira T., Kawazoe I., et al. Characteristics and primary structure of a galectin in the skin mucus of the Japanese eel (Anguilla japonica). Dev Comp Immunol 2004, 28:325-335.
    • (2004) Dev Comp Immunol , vol.28 , pp. 325-335
    • Tasumi, S.1    Yang, W.J.2    Usami, T.3    Tsutsui, S.4    Ohira, T.5    Kawazoe, I.6
  • 59
    • 0036490246 scopus 로고    scopus 로고
    • Rhamnose-binding lectins from steelhead trout (Onchorhynchus mykiss) eggs recognize bacterial lipopolysaccharides and lipoteichoic acid
    • Tateno H., Ogawa T., Muramoto K., Kamiya H., Saneyoshi M. Rhamnose-binding lectins from steelhead trout (Onchorhynchus mykiss) eggs recognize bacterial lipopolysaccharides and lipoteichoic acid. Biosci Biotechnol Biochem 2002, 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
  • 60
    • 0036584407 scopus 로고    scopus 로고
    • Evolution of the lectin-complement pathway and its role in innate immunity
    • Teizo F. Evolution of the lectin-complement pathway and its role in innate immunity. Nat Rev Immunol 2002, 2:346-353.
    • (2002) Nat Rev Immunol , vol.2 , pp. 346-353
    • Teizo, F.1
  • 61
  • 62
    • 0032051601 scopus 로고    scopus 로고
    • Sialic acid binding lectin with antibacterial activity from the horse mussel: further characterization and immunolocalization
    • Tunkijjanukij S., Olafsen J.A. Sialic acid binding lectin with antibacterial activity from the horse mussel: further characterization and immunolocalization. Dev Comp Immunol 1998, 22:139-150.
    • (1998) Dev Comp Immunol , vol.22 , pp. 139-150
    • Tunkijjanukij, S.1    Olafsen, J.A.2
  • 63
    • 80555149784 scopus 로고    scopus 로고
    • Galectins as pattern recognition receptors: structure, function and evolution
    • Vasta G.R. Galectins as pattern recognition receptors: structure, function and evolution. Adv Exp Med Biol 2012, 946:21-36.
    • (2012) Adv Exp Med Biol , vol.946 , pp. 21-36
    • Vasta, G.R.1
  • 64
    • 73049088159 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of a C-type lectin (Ec-CTL) in orange-spotted grouper, Epinephelus coioides
    • Wei J., Xu D., Zhou J., Cui H., Yan Y., Ouyang Z., et al. Molecular cloning, characterization and expression analysis of a C-type lectin (Ec-CTL) in orange-spotted grouper, Epinephelus coioides. Fish Shellfish Immunol 2010, 28:178-186.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 178-186
    • Wei, J.1    Xu, D.2    Zhou, J.3    Cui, H.4    Yan, Y.5    Ouyang, Z.6
  • 65
    • 33750045193 scopus 로고    scopus 로고
    • Purification and characterization of a calcium-independent lectin (PjLec) from the haemolymph of the shrimp Penaeus japonicus
    • Yang H., Luo T., Li F., Li S., Xu X. Purification and characterization of a calcium-independent lectin (PjLec) from the haemolymph of the shrimp Penaeus japonicus. Fish Shellfish Immunol 2007, 22:88-97.
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 88-97
    • Yang, H.1    Luo, T.2    Li, F.3    Li, S.4    Xu, X.5
  • 66
    • 0028312214 scopus 로고
    • Purification and characterization of a galactose specific lectin from the egg of coho salmon Oncorhynchus kisutch, and its interaction with bacterial fish pathogens
    • Yousif A.N., Albright L.J., Evelyn T.P.T. Purification and characterization of a galactose specific lectin from the egg of coho salmon Oncorhynchus kisutch, and its interaction with bacterial fish pathogens. Dis Aquat Organ 1994, 20:127-136.
    • (1994) Dis Aquat Organ , vol.20 , pp. 127-136
    • Yousif, A.N.1    Albright, L.J.2    Evelyn, T.P.T.3
  • 67
    • 14844282115 scopus 로고    scopus 로고
    • A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes
    • Yu X.Q., Tracy M.E., Ling E., Scholz F.R., Trenczek T. A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes. Insect Biochem Mol Biol 2005, 35:285-295.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 285-295
    • Yu, X.Q.1    Tracy, M.E.2    Ling, E.3    Scholz, F.R.4    Trenczek, T.5


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