메뉴 건너뛰기




Volumn 46, Issue 1, 2015, Pages 94-106

Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse

Author keywords

Galectin; Glycan ligands; Microbial recognition; Parasite; Phytoplankton

Indexed keywords

ALGAE; BACTERIA (MICROORGANISMS); CRASSOSTREA VIRGINICA; EQUIDAE; INVERTEBRATA; MAMMALIA; MOLLUSCA; OSTREIDAE; PERKINSUS MARINUS; PROTOZOA; VERTEBRATA;

EID: 84937163196     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2015.05.012     Document Type: Article
Times cited : (58)

References (107)
  • 1
    • 0001810168 scopus 로고    scopus 로고
    • The information-storing potential of the sugar code
    • Chapman & Hill, Weinheim, H.-J. Gabius, S. Gabius (Eds.)
    • Laine R.A. The information-storing potential of the sugar code. Glycosciences: Status and Perspectives 1997, 5-14. Chapman & Hill, Weinheim. H.-J. Gabius, S. Gabius (Eds.).
    • (1997) Glycosciences: Status and Perspectives , pp. 5-14
    • Laine, R.A.1
  • 3
    • 0002703227 scopus 로고    scopus 로고
    • Transgenic approaches to glycobiology
    • H.-J. Gabius, S. Gabius (Eds.)
    • Hathaway H.J., Shur B.D. Transgenic approaches to glycobiology. Glycosciences: Status and Perspectives 1997, 507-517. H.-J. Gabius, S. Gabius (Eds.).
    • (1997) Glycosciences: Status and Perspectives , pp. 507-517
    • Hathaway, H.J.1    Shur, B.D.2
  • 4
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • Cooper D.N.W. Galectinomics: finding themes in complexity. Biochimica Biophysica Acta 2002, 1572:209-231.
    • (2002) Biochimica Biophysica Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 5
    • 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., O'Leary N. C-type lectins and galectins mediate innate and adaptive immune functions: their roles in the complement activation pathway. Dev. Comp. Immunol. 1999, 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
  • 7
    • 33646150212 scopus 로고    scopus 로고
    • The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain
    • Stalz H., Roth U., Schleuder D., Macht M., Haebel S., Strupat K., et al. The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain. Glycobiology 2006, 16:402-414.
    • (2006) Glycobiology , vol.16 , pp. 402-414
    • Stalz, H.1    Roth, U.2    Schleuder, D.3    Macht, M.4    Haebel, S.5    Strupat, K.6
  • 8
    • 33644666110 scopus 로고    scopus 로고
    • Anovel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex
    • Saouros S., Edwards-Jones B., Reiss M., Sawmynaden K., Cota E., Simpson P., et al. Anovel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. J.Biological. Chem. 2005, 280:38583-38591.
    • (2005) J.Biological. Chem. , vol.280 , pp. 38583-38591
    • Saouros, S.1    Edwards-Jones, B.2    Reiss, M.3    Sawmynaden, K.4    Cota, E.5    Simpson, P.6
  • 9
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution
    • Hirabayashi J., Kasai K. The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 1993, 3:297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 10
    • 0024306543 scopus 로고
    • The Mac-2 antigen is a galactose-specific lectin that binds IgE
    • Cherayil B.J., Weiner S.J., Pillai S. The Mac-2 antigen is a galactose-specific lectin that binds IgE. JExp Med 1989, 170:1959-1972.
    • (1989) JExp Med , vol.170 , pp. 1959-1972
    • Cherayil, B.J.1    Weiner, S.J.2    Pillai, S.3
  • 11
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper D.N., Barondes S.H. Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J.Cell. Biol. 1990, 110:1681-1691.
    • (1990) J.Cell. Biol. , vol.110 , pp. 1681-1691
    • Cooper, D.N.1    Barondes, S.H.2
  • 12
    • 0028986607 scopus 로고
    • Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis
    • Cho M., Cummings R.D. Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis. J.Biological Chem. 1995, 270:5207-5212.
    • (1995) J.Biological Chem. , vol.270 , pp. 5207-5212
    • Cho, M.1    Cummings, R.D.2
  • 13
    • 0028074969 scopus 로고
    • Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages
    • Sato S., Hughes R.C. Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages. J.Biological Chem. 1994, 269:4424-4430.
    • (1994) J.Biological Chem. , vol.269 , pp. 4424-4430
    • Sato, S.1    Hughes, R.C.2
  • 14
    • 0030000860 scopus 로고    scopus 로고
    • Anew pathway for protein export in Saccharomyces cerevisiae
    • Cleves A.E., Cooper D.N., Barondes S.H., Kelly R.B. Anew pathway for protein export in Saccharomyces cerevisiae. J.Cell Biol. 1996, 133:1017-1026.
    • (1996) J.Cell Biol. , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, S.H.3    Kelly, R.B.4
  • 16
    • 0027158151 scopus 로고
    • Galaptin-mediated adhesion of human ovarian carcinoma A121 cells and detection of cellular galaptin-binding glycoproteins
    • Skrincosky D.M., Allen H.J., Bernacki R.J. Galaptin-mediated adhesion of human ovarian carcinoma A121 cells and detection of cellular galaptin-binding glycoproteins. Cancer Res. 1993, 53:2667-2675.
    • (1993) Cancer Res. , vol.53 , pp. 2667-2675
    • Skrincosky, D.M.1    Allen, H.J.2    Bernacki, R.J.3
  • 17
    • 0036333446 scopus 로고    scopus 로고
    • Zebrafish mutants identify an essential role for laminins in notochord formation
    • Parsons M.J., Pollard S.M., Saude L., Feldman B., Coutinho P., Hirst E.M.A., et al. Zebrafish mutants identify an essential role for laminins in notochord formation. Development 2002, 129:3137-3146.
    • (2002) Development , vol.129 , pp. 3137-3146
    • Parsons, M.J.1    Pollard, S.M.2    Saude, L.3    Feldman, B.4    Coutinho, P.5    Hirst, E.M.A.6
  • 18
    • 0027259106 scopus 로고
    • Characterization of quail intestinal mucin as a ligand for endogenous quail lectin
    • Fang R., Mantle M., Ceri H. Characterization of quail intestinal mucin as a ligand for endogenous quail lectin. Biochem J 1993, 293(Pt 3):867-872.
    • (1993) Biochem J , vol.293 , pp. 867-872
    • Fang, R.1    Mantle, M.2    Ceri, H.3
  • 20
    • 0030049078 scopus 로고    scopus 로고
    • The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites
    • Mey A., Leffler H., Hmama Z., Normier G., Revillard J.P. The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites. J.Immunol. 1996, 156:1572-1577.
    • (1996) J.Immunol. , vol.156 , pp. 1572-1577
    • Mey, A.1    Leffler, H.2    Hmama, Z.3    Normier, G.4    Revillard, J.P.5
  • 21
    • 0037083447 scopus 로고    scopus 로고
    • Role of galectin-3 as an adhesion molecule for neutrophil extravasation during streptococcal pneumonia
    • Sato S., Ouellet N., Pelletier I., Simard M., Rancourt A., Bergeron M.G. Role of galectin-3 as an adhesion molecule for neutrophil extravasation during streptococcal pneumonia. J.Immunol. 2002, 168:1813-1822.
    • (2002) J.Immunol. , vol.168 , pp. 1813-1822
    • Sato, S.1    Ouellet, N.2    Pelletier, I.3    Simard, M.4    Rancourt, A.5    Bergeron, M.G.6
  • 22
    • 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., et al. Galectin-3 binds lactosaminylated lipooligosaccharides from Neisseria gonorrhoeae and is selectively expressed by mucosal epithelial cells that are infected. Cell Microbiol. 2002, 4:649-662.
    • (2002) Cell Microbiol. , 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
  • 24
    • 0036207005 scopus 로고    scopus 로고
    • Association of a macrophage galactoside-binding protein with Mycobacterium-containing phagosomes
    • Beatty W.L., Rhoades E.R., Hsu D.K., Liu F.-T., Russell D.G. Association of a macrophage galactoside-binding protein with Mycobacterium-containing phagosomes. Cell Microbiol. 2002, 4:167-176.
    • (2002) Cell Microbiol. , vol.4 , pp. 167-176
    • Beatty, W.L.1    Rhoades, E.R.2    Hsu, D.K.3    Liu, F.-T.4    Russell, D.G.5
  • 25
    • 0030994616 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lipopolysaccharide binds galectin-3 and other human corneal epithelial proteins
    • Gupta S.K., Masinick S., Garrett M., Hazlett L.D. Pseudomonas aeruginosa lipopolysaccharide binds galectin-3 and other human corneal epithelial proteins. Infect Immun. 1997, 65:2747-2753.
    • (1997) Infect Immun. , vol.65 , pp. 2747-2753
    • Gupta, S.K.1    Masinick, S.2    Garrett, M.3    Hazlett, L.D.4
  • 26
    • 0038605468 scopus 로고    scopus 로고
    • Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells
    • Pelletier I., Hashidate T., Urashima T., Nishi N., Nakamura T., Futai M., et al. Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells. J.Biological Chem. 2003, 278:22223-22230.
    • (2003) J.Biological Chem. , vol.278 , pp. 22223-22230
    • Pelletier, I.1    Hashidate, T.2    Urashima, T.3    Nishi, N.4    Nakamura, T.5    Futai, M.6
  • 27
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta G.R. Roles of galectins in infection. Nat. Rev. Microbiol. 2009, 7:424-438.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 28
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • Barondes S.H., Cooper D.N., Gitt M.A., Leffler H. Galectins. Structure and function of a large family of animal lectins. J.Biological Chem. 1994, 269:20807-20810.
    • (1994) J.Biological Chem. , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 29
    • 0033777862 scopus 로고    scopus 로고
    • Galectins: a new family of regulators of inflammation
    • Liu F.T. Galectins: a new family of regulators of inflammation. Clin. Immunol. 2000, 97:79-88.
    • (2000) Clin. Immunol. , vol.97 , pp. 79-88
    • Liu, F.T.1
  • 30
    • 0030447353 scopus 로고    scopus 로고
    • The primary structure and carbohydrate specificity of a beta-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis
    • Ahmed H., Pohl J., Fink N.E., Strobel F., Vasta G.R. The primary structure and carbohydrate specificity of a beta-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis. J.Biological Chem. 1996, 271:33083-33094.
    • (1996) J.Biological Chem. , vol.271 , pp. 33083-33094
    • Ahmed, H.1    Pohl, J.2    Fink, N.E.3    Strobel, F.4    Vasta, G.R.5
  • 31
    • 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., Vasta G.R. Biochemical and molecular characterization of galectins from zebrafish (Danio rerio): notochord-specific expression of a prototype galectin during early embryogenesis. Glycobiology 2004, 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
  • 33
    • 0031476218 scopus 로고    scopus 로고
    • Galectins from amphibian species: carbohydrate specificity, molecular structure, and evolution
    • Vasta G.R., Ahmed H., Amzel L.M., Bianchet M.A. Galectins from amphibian species: carbohydrate specificity, molecular structure, and evolution. Trends Glycosci. Glycotechnol. 1997, 9:131-144.
    • (1997) Trends Glycosci. Glycotechnol. , vol.9 , pp. 131-144
    • Vasta, G.R.1    Ahmed, H.2    Amzel, L.M.3    Bianchet, M.A.4
  • 34
    • 0032582653 scopus 로고    scopus 로고
    • GRIFIN, a novel lens-specific protein related to the galectin family
    • Ogden A.T., Nunes I., Ko K., Wu S., Hines C.S., Wang A.F., et al. GRIFIN, a novel lens-specific protein related to the galectin family. J.Biological Chem. 1998, 273:28889-28896.
    • (1998) J.Biological Chem. , vol.273 , pp. 28889-28896
    • Ogden, A.T.1    Nunes, I.2    Ko, K.3    Wu, S.4    Hines, C.S.5    Wang, A.F.6
  • 35
    • 43549108972 scopus 로고    scopus 로고
    • Unlike mammalian GRIFIN, the zebrafish homologue (DrGRIFIN) represents a functional carbohydrate-binding galectin
    • Ahmed H., Vasta G.R. Unlike mammalian GRIFIN, the zebrafish homologue (DrGRIFIN) represents a functional carbohydrate-binding galectin. Biochem. Biophysical Res. Commun. 2008, 371:350-355.
    • (2008) Biochem. Biophysical Res. Commun. , vol.371 , pp. 350-355
    • Ahmed, H.1    Vasta, G.R.2
  • 39
    • 0035174596 scopus 로고    scopus 로고
    • Uncoupling of chondrocyte death and vascular invasion in mouse galectin 3 null mutant bones
    • Colnot C., Sidhu S.S., Balmain N., Poirier F. Uncoupling of chondrocyte death and vascular invasion in mouse galectin 3 null mutant bones. Dev. Biol. 2001, 229:203-214.
    • (2001) Dev. Biol. , vol.229 , pp. 203-214
    • Colnot, C.1    Sidhu, S.S.2    Balmain, N.3    Poirier, F.4
  • 40
    • 34447106403 scopus 로고    scopus 로고
    • The role of galectin-3 in cancer drug resistance
    • Fukumori T., Kanayama H.-O., Raz A. The role of galectin-3 in cancer drug resistance. Drug Resist. Updat. 2007, 10:101-108.
    • (2007) Drug Resist. Updat. , vol.10 , pp. 101-108
    • Fukumori, T.1    Kanayama, H.-O.2    Raz, A.3
  • 41
    • 84875499442 scopus 로고    scopus 로고
    • Cod glycopeptide with picomolar affinity to galectin-3 suppresses T-cell apoptosis and prostate cancer metastasis
    • Guha P., Kaptan E., Bandyopadhyaya G., Kaczanowska S., Davila E., Thompson K., et al. Cod glycopeptide with picomolar affinity to galectin-3 suppresses T-cell apoptosis and prostate cancer metastasis. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:5052-5057.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 5052-5057
    • Guha, P.1    Kaptan, E.2    Bandyopadhyaya, G.3    Kaczanowska, S.4    Davila, E.5    Thompson, K.6
  • 42
  • 43
    • 84874201705 scopus 로고    scopus 로고
    • Galectins as self/non-self recognition receptors in innate and adaptive immunity: an unresolved paradox
    • Vasta G.R., Ahmed H., Nita-Lazar M., Banerjee A., Pasek M., Shridhar S., et al. Galectins as self/non-self recognition receptors in innate and adaptive immunity: an unresolved paradox. Front Immunol 2012, 3:199.
    • (2012) Front Immunol , vol.3 , pp. 199
    • Vasta, G.R.1    Ahmed, H.2    Nita-Lazar, M.3    Banerjee, A.4    Pasek, M.5    Shridhar, S.6
  • 45
    • 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., Henrikson D. Galectins in teleost fish: zebrafish (Danio rerio) as a model species to address their biological roles in development and innate immunity. Glycoconj. J. 2004, 21:503-521.
    • (2004) Glycoconj. J. , vol.21 , pp. 503-521
    • Vasta, G.R.1    Ahmed, H.2    Du, S.3    Henrikson, D.4
  • 47
    • 0036798862 scopus 로고    scopus 로고
    • Ah, sweet mystery of death! Galectins and control of cell fate
    • Hernandez J.D., Baum L.G. Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 2002, 12:127R-136R.
    • (2002) Glycobiology , vol.12 , pp. 127R-136R
    • Hernandez, J.D.1    Baum, L.G.2
  • 48
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu F.-T., Rabinovich G.A. Galectins as modulators of tumour progression. Nat. Rev. Cancer 2005, 5:29-41.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 29-41
    • Liu, F.-T.1    Rabinovich, G.A.2
  • 49
    • 0025201026 scopus 로고
    • Evidence for the role of 34-kDa galactoside-binding lectin in transformation and metastasis
    • Raz A., Zhu D.G., Hogan V., Shah N., Raz T., Karkash R., et al. Evidence for the role of 34-kDa galactoside-binding lectin in transformation and metastasis. Int. J. Cancer J. Int. du Cancer 1990, 46:871-877.
    • (1990) Int. J. Cancer J. Int. du Cancer , vol.46 , pp. 871-877
    • Raz, A.1    Zhu, D.G.2    Hogan, V.3    Shah, N.4    Raz, T.5    Karkash, R.6
  • 52
    • 0034444550 scopus 로고    scopus 로고
    • Host-pathogen interactions: basic concepts of microbial commensalism, colonization, infection, and disease
    • Casadevall A., Pirofski L.A. Host-pathogen interactions: basic concepts of microbial commensalism, colonization, infection, and disease. Infect. Immun. 2000, 68:6511-6518.
    • (2000) Infect. Immun. , vol.68 , pp. 6511-6518
    • Casadevall, A.1    Pirofski, L.A.2
  • 53
    • 0023886227 scopus 로고
    • Immune mechanisms in insects
    • Lackie A.M. Immune mechanisms in insects. Parasitol. Today 1988, 4:98-9105.
    • (1988) Parasitol. Today , vol.4 , pp. 98-9105
    • Lackie, A.M.1
  • 54
    • 84905647104 scopus 로고    scopus 로고
    • Microbe-host interactions are positively and negatively regulated by galectin-glycan interactions
    • Baum L.G., Garner O.B., Schaefer K., Lee B. Microbe-host interactions are positively and negatively regulated by galectin-glycan interactions. Front. Immunol. 2014, 5:284.
    • (2014) Front. Immunol. , vol.5 , pp. 284
    • Baum, L.G.1    Garner, O.B.2    Schaefer, K.3    Lee, B.4
  • 56
    • 0021739630 scopus 로고
    • Alectin on the hemocyte membrane of the oyster (Crassostrea virginica)
    • Vasta G.R., Cheng T.C., Marchalonis J.J. Alectin on the hemocyte membrane of the oyster (Crassostrea virginica). Cell Immunol. 1984, 88:475-488.
    • (1984) Cell Immunol. , vol.88 , pp. 475-488
    • Vasta, G.R.1    Cheng, T.C.2    Marchalonis, J.J.3
  • 57
    • 35548934271 scopus 로고    scopus 로고
    • Agalectin of unique domain organization from hemocytes of the eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus
    • Tasumi S., Vasta G.R. Agalectin of unique domain organization from hemocytes of the eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus. J.Immunol. 2007, 179:3086-3098.
    • (2007) J.Immunol. , vol.179 , pp. 3086-3098
    • Tasumi, S.1    Vasta, G.R.2
  • 58
    • 84883202399 scopus 로고    scopus 로고
    • The galectin CvGal1 from the eastern oyster (Crassostrea virginica) binds to blood group A oligosaccharides on the hemocyte surface
    • Feng C., Ghosh A., Amin M.N., Giomarelli B., Shridhar S., Banerjee A., et al. The galectin CvGal1 from the eastern oyster (Crassostrea virginica) binds to blood group A oligosaccharides on the hemocyte surface. J.Biological Chem. 2013, 288:24394-24409.
    • (2013) J.Biological Chem. , vol.288 , pp. 24394-24409
    • Feng, C.1    Ghosh, A.2    Amin, M.N.3    Giomarelli, B.4    Shridhar, S.5    Banerjee, A.6
  • 59
    • 84883164712 scopus 로고    scopus 로고
    • Hemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulfated and blood group A-modified N-glycans
    • Kurz S., Jin C., Hykollari A., Gregorich D., Giomarelli B., Vasta G.R., et al. Hemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulfated and blood group A-modified N-glycans. J.Biological Chem. 2013, 288:24410-24428.
    • (2013) J.Biological Chem. , vol.288 , pp. 24410-24428
    • Kurz, S.1    Jin, C.2    Hykollari, A.3    Gregorich, D.4    Giomarelli, B.5    Vasta, G.R.6
  • 60
    • 84937163642 scopus 로고    scopus 로고
    • The Galectin CvGal2 from the eastern oyster (Crassostrea virginica) displays unique specificity for ABH blood group oligosaccharides and differentially recognizes sympatric Perkinsus species
    • [Submitted]
    • C. Feng, A. Ghosh, M.N. Amin, T.R. Bachvaroff, S. Tasumi, M. Pasek, etal. The Galectin CvGal2 from the eastern oyster (Crassostrea virginica) displays unique specificity for ABH blood group oligosaccharides and differentially recognizes sympatric Perkinsus species. Biochemistry. [Submitted].
    • Biochemistry.
    • Feng, C.1    Ghosh, A.2    Amin, M.N.3    Bachvaroff, T.R.4    Tasumi, S.5    Pasek, M.6
  • 61
    • 36749079907 scopus 로고    scopus 로고
    • Identification and tissue expression analysis of C-type lectin and galectin in the Pacific oyster, Crassostrea gigas
    • Yamaura K., Takahashi K.G., Suzuki T. Identification and tissue expression analysis of C-type lectin and galectin in the Pacific oyster, Crassostrea gigas. Comp. Biochem. Physiol. Part B, Biochem. Mol. Biol. 2008, 149:168-175.
    • (2008) Comp. Biochem. Physiol. Part B, Biochem. Mol. Biol. , vol.149 , pp. 168-175
    • Yamaura, K.1    Takahashi, K.G.2    Suzuki, T.3
  • 62
    • 39749172949 scopus 로고    scopus 로고
    • Molecular and functional characterization of a tandem-repeat galectin from the freshwater snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni
    • Yoshino T.P., Dinguirard N., Kunert J., Hokke C.H. Molecular and functional characterization of a tandem-repeat galectin from the freshwater snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni. Gene 2008, 411:46-58.
    • (2008) Gene , vol.411 , pp. 46-58
    • Yoshino, T.P.1    Dinguirard, N.2    Kunert, J.3    Hokke, C.H.4
  • 63
    • 84863186338 scopus 로고    scopus 로고
    • Identification and transcriptional analysis of two types of lectins (SgCTL-1 and SgGal-1) from mollusk Solen grandis
    • Wei X., Yang J., Liu X., Yang D., Xu J., Fang J., et al. Identification and transcriptional analysis of two types of lectins (SgCTL-1 and SgGal-1) from mollusk Solen grandis. Fish Shellfish Immunol. 2012, 33:204-212.
    • (2012) Fish Shellfish Immunol. , vol.33 , pp. 204-212
    • Wei, X.1    Yang, J.2    Liu, X.3    Yang, D.4    Xu, J.5    Fang, J.6
  • 64
    • 79952439186 scopus 로고    scopus 로고
    • Agalectin with quadruple-domain from bay scallop Argopecten irradians is involved in innate immune response
    • Song X., Zhang H., Wang L., Zhao J., Mu C., Song L., et al. Agalectin with quadruple-domain from bay scallop Argopecten irradians is involved in innate immune response. Dev. Comp. Immunol. 2011, 35:592-602.
    • (2011) Dev. Comp. Immunol. , vol.35 , pp. 592-602
    • Song, X.1    Zhang, H.2    Wang, L.3    Zhao, J.4    Mu, C.5    Song, L.6
  • 65
    • 74649085824 scopus 로고    scopus 로고
    • An immune responsive multidomain galectin from bay scallop Argopectens irradians
    • Song X., Zhang H., Zhao J., Wang L., Qiu L., Mu C., et al. An immune responsive multidomain galectin from bay scallop Argopectens irradians. Fish Shellfish Immunol. 2010, 28:326-332.
    • (2010) Fish Shellfish Immunol. , vol.28 , pp. 326-332
    • Song, X.1    Zhang, H.2    Zhao, J.3    Wang, L.4    Qiu, L.5    Mu, C.6
  • 66
    • 46549085873 scopus 로고    scopus 로고
    • Noble tandem-repeat galectin of Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni
    • Kim J.Y., Kim Y.M., Cho S.K., Choi K.S., Cho M. Noble tandem-repeat galectin of Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni. Dev. Comp. Immunol. 2008, 32:1131-1141.
    • (2008) Dev. Comp. Immunol. , vol.32 , pp. 1131-1141
    • Kim, J.Y.1    Kim, Y.M.2    Cho, S.K.3    Choi, K.S.4    Cho, M.5
  • 67
    • 80955166981 scopus 로고    scopus 로고
    • CDNA cloning and mRNA expression of a tandem-repeat galectin (PoGal2) from the pearl oyster, Pinctada fucata
    • Zhang D.C., Hu Y.T., Guo H.Y., Cui S.G., Su T.F., Jiang S.G. cDNA cloning and mRNA expression of a tandem-repeat galectin (PoGal2) from the pearl oyster, Pinctada fucata. Genet. Mol. Res.: GMR 2011, 10:1963-1974.
    • (2011) Genet. Mol. Res.: GMR , vol.10 , pp. 1963-1974
    • Zhang, D.C.1    Hu, Y.T.2    Guo, H.Y.3    Cui, S.G.4    Su, T.F.5    Jiang, S.G.6
  • 68
    • 77957877692 scopus 로고    scopus 로고
    • Amultidomain galectin involved in innate immune response of pearl oyster Pinctada fucata
    • Zhang D., Jiang S., Hu Y., Cui S., Guo H., Wu K., et al. Amultidomain galectin involved in innate immune response of pearl oyster Pinctada fucata. Dev. Comp. Immunol. 2011, 35:1-6.
    • (2011) Dev. Comp. Immunol. , vol.35 , pp. 1-6
    • Zhang, D.1    Jiang, S.2    Hu, Y.3    Cui, S.4    Guo, H.5    Wu, K.6
  • 69
    • 84903582963 scopus 로고    scopus 로고
    • Agalectin with quadruple-domain from red abalone Haliotis rufescens involved in the immune innate response against to Vibrio anguillarum
    • Maldonado-Aguayo W., Teneb J., Gallardo-Escarate C. Agalectin with quadruple-domain from red abalone Haliotis rufescens involved in the immune innate response against to Vibrio anguillarum. Fish Shellfish Immunol. 2014, 40:1-8.
    • (2014) Fish Shellfish Immunol. , vol.40 , pp. 1-8
    • Maldonado-Aguayo, W.1    Teneb, J.2    Gallardo-Escarate, C.3
  • 70
    • 84875921661 scopus 로고    scopus 로고
    • Differential expression of genes involved in immunity and biomineralization during Brown Ring Disease development and shell repair in the Manila clam, Ruditapes philippinarum
    • Jeffroy F., Brulle F., Paillard C. Differential expression of genes involved in immunity and biomineralization during Brown Ring Disease development and shell repair in the Manila clam, Ruditapes philippinarum. J.Invertebr Pathol. 2013, 113:129-136.
    • (2013) J.Invertebr Pathol. , vol.113 , pp. 129-136
    • Jeffroy, F.1    Brulle, F.2    Paillard, C.3
  • 71
    • 84890978065 scopus 로고    scopus 로고
    • Atandem-repeat galectin from blood clam Tegillarca granosa and its induced mRNA expression response against bacterial challenge
    • Bao Y., Shen H., Zhou H., Dong Y., Lin Z. Atandem-repeat galectin from blood clam Tegillarca granosa and its induced mRNA expression response against bacterial challenge. Genes Genom. 2013, 35:733-740.
    • (2013) Genes Genom. , vol.35 , pp. 733-740
    • Bao, Y.1    Shen, H.2    Zhou, H.3    Dong, Y.4    Lin, Z.5
  • 72
    • 84909606922 scopus 로고    scopus 로고
    • Afamily of variable immunoglobulin and lectin domain containing molecules in the snail Biomphalaria glabrata
    • Dheilly N.M., Duval D., Mouahid G., Emans R., Allienne J.F., Galinier R., et al. Afamily of variable immunoglobulin and lectin domain containing molecules in the snail Biomphalaria glabrata. Dev. Comp. Immunol. 2015, 48:234-243.
    • (2015) Dev. Comp. Immunol. , vol.48 , pp. 234-243
    • Dheilly, N.M.1    Duval, D.2    Mouahid, G.3    Emans, R.4    Allienne, J.F.5    Galinier, R.6
  • 73
    • 0030705195 scopus 로고    scopus 로고
    • Structure of the 32-kDa galectin gene of the nematode Caenorhabditis elegans
    • Arata Y., Hirabayashi J., Ki Kasai Structure of the 32-kDa galectin gene of the nematode Caenorhabditis elegans. J.Biological Chem. 1997, 272:26669-26677.
    • (1997) J.Biological Chem. , vol.272 , pp. 26669-26677
    • Arata, Y.1    Hirabayashi, J.2    Ki, K.3
  • 74
    • 0036668095 scopus 로고    scopus 로고
    • Novel carbohydrate specificity of the 16-kDa galectin from Caenorhabditis elegans: binding to blood group precursor oligosaccharides (type 1, type 2, Talpha, and Tbeta) and gangliosides
    • Ahmed H., Bianchet M.A., Amzel L.M., Hirabayashi J., Kasai K.-I., Giga-Hama Y., et al. Novel carbohydrate specificity of the 16-kDa galectin from Caenorhabditis elegans: binding to blood group precursor oligosaccharides (type 1, type 2, Talpha, and Tbeta) and gangliosides. Glycobiology 2002, 12:451-461.
    • (2002) Glycobiology , vol.12 , pp. 451-461
    • Ahmed, H.1    Bianchet, M.A.2    Amzel, L.M.3    Hirabayashi, J.4    Kasai, K.-I.5    Giga-Hama, Y.6
  • 75
    • 0025752947 scopus 로고
    • Structure and expression of the negative growth factor mouse beta-galactoside binding protein gene
    • Chiariotti L., Wells V., Bruni C.B., Mallucci L. Structure and expression of the negative growth factor mouse beta-galactoside binding protein gene. Biochimica Biophysica Acta 1991, 1089:54-60.
    • (1991) Biochimica Biophysica Acta , vol.1089 , pp. 54-60
    • Chiariotti, L.1    Wells, V.2    Bruni, C.B.3    Mallucci, L.4
  • 76
    • 0026089105 scopus 로고
    • Genomic sequence and organization of two members of a human lectin gene family
    • Gitt M.A., Barondes S.H. Genomic sequence and organization of two members of a human lectin gene family. Biochemistry 1991, 30:82-89.
    • (1991) Biochemistry , vol.30 , pp. 82-89
    • Gitt, M.A.1    Barondes, S.H.2
  • 77
    • 0034663733 scopus 로고    scopus 로고
    • Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes
    • Bianchet M.A., Ahmed H., Vasta G.R., Amzel L.M. Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes. Proteins 2000, 40:378-388.
    • (2000) Proteins , vol.40 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3    Amzel, L.M.4
  • 78
    • 84866159245 scopus 로고    scopus 로고
    • Evolution of vertebrate immunity
    • Boehm T. Evolution of vertebrate immunity. Current Biology: CB 2012, 22:R722-R732.
    • (2012) Current Biology: CB , vol.22 , pp. R722-R732
    • Boehm, T.1
  • 79
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas
    • Bachere E., Gueguen Y., Gonzalez M., de Lorgeril J., Garnier J., Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol Rev 2004, 198:149-168.
    • (2004) Immunol Rev , vol.198 , pp. 149-168
    • Bachere, E.1    Gueguen, Y.2    Gonzalez, M.3    de Lorgeril, J.4    Garnier, J.5    Romestand, B.6
  • 80
    • 0036858931 scopus 로고    scopus 로고
    • Identification of genes expressed in the gill tissue of the Pacific oyster (Crassostrea gigas) using expressed-sequence tags
    • Rafferty G.P., Powell R. Identification of genes expressed in the gill tissue of the Pacific oyster (Crassostrea gigas) using expressed-sequence tags. J.Molluscan Stud. 2002, 68:397.
    • (2002) J.Molluscan Stud. , vol.68 , pp. 397
    • Rafferty, G.P.1    Powell, R.2
  • 81
    • 0037448603 scopus 로고    scopus 로고
    • Immune gene discovery by expressed sequence tags generated from hemocytes of the bacteria-challenged oyster, Crassostrea gigas
    • Gueguen Y., Cadoret J.P., Flament D., Barreau-Roumiguiere C., Girardot A.L., Garnier J., et al. Immune gene discovery by expressed sequence tags generated from hemocytes of the bacteria-challenged oyster, Crassostrea gigas. Gene 2003, 303:139-145.
    • (2003) Gene , vol.303 , pp. 139-145
    • Gueguen, Y.1    Cadoret, J.P.2    Flament, D.3    Barreau-Roumiguiere, C.4    Girardot, A.L.5    Garnier, J.6
  • 82
    • 0026516931 scopus 로고
    • Function of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin
    • Jomori T., Natori S. Function of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin. FEBS Lett. 1992, 296:283-286.
    • (1992) FEBS Lett. , vol.296 , pp. 283-286
    • Jomori, T.1    Natori, S.2
  • 83
    • 0035831034 scopus 로고    scopus 로고
    • Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae
    • Levashina E.A., Moita L.F., Blandin S., Vriend G., Lagueux M., Kafatos F.C. Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell 2001, 104:709-718.
    • (2001) Cell , vol.104 , pp. 709-718
    • Levashina, E.A.1    Moita, L.F.2    Blandin, S.3    Vriend, G.4    Lagueux, M.5    Kafatos, F.C.6
  • 84
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet M., Manfruelli P., Pearson A., Mathey-Prevot B., Ezekowitz R.A. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 2002, 416:644-648.
    • (2002) Nature , vol.416 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 85
    • 33645884134 scopus 로고    scopus 로고
    • Differences in integrin-dependent phagocytosis among three hemocyte subpopulations of the Pacific oyster "Crassostrea gigas"
    • Terahara K., Takahashi K.G., Nakamura A., Osada M., Yoda M., Hiroi T., et al. Differences in integrin-dependent phagocytosis among three hemocyte subpopulations of the Pacific oyster "Crassostrea gigas". Dev. Comp. Immunol. 2006, 30:667-683.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 667-683
    • Terahara, K.1    Takahashi, K.G.2    Nakamura, A.3    Osada, M.4    Yoda, M.5    Hiroi, T.6
  • 86
    • 0034535375 scopus 로고    scopus 로고
    • Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to gram-negative bacteria
    • Yu X.Q., Kanost M.R. Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to gram-negative bacteria. J.Biological Chem. 2000, 275:37373-37381.
    • (2000) J.Biological Chem. , vol.275 , pp. 37373-37381
    • Yu, X.Q.1    Kanost, M.R.2
  • 87
    • 2942718954 scopus 로고    scopus 로고
    • Anovel lectin with a fibrinogen-like domain and its potential involvement in the innate immune response of Armigeres subalbatus against bacteria
    • Wang X., Rocheleau T.A., Fuchs J.F., Hillyer J.F., Chen C.C., Christensen B.M. Anovel lectin with a fibrinogen-like domain and its potential involvement in the innate immune response of Armigeres subalbatus against bacteria. Insect. Mol. Biol. 2004, 13:273-282.
    • (2004) Insect. Mol. Biol. , vol.13 , pp. 273-282
    • Wang, X.1    Rocheleau, T.A.2    Fuchs, J.F.3    Hillyer, J.F.4    Chen, C.C.5    Christensen, B.M.6
  • 88
    • 80052735652 scopus 로고    scopus 로고
    • Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
    • Davicino R.C., Elicabe R.J., Di Genaro M.S., Rabinovich G.A. Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms. Int. Immunopharmacol. 2011, 11:1457-1463.
    • (2011) Int. Immunopharmacol. , vol.11 , pp. 1457-1463
    • Davicino, R.C.1    Elicabe, R.J.2    Di Genaro, M.S.3    Rabinovich, G.A.4
  • 89
    • 0041534400 scopus 로고    scopus 로고
    • Collections and ficolins: humoral lectins of the innate immune defense
    • Holmskov U., Thiel S., Jensenius J.C. Collections and ficolins: humoral lectins of the innate immune defense. Annu. Rev. Immunol. 2003, 21:547-578.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 547-578
    • Holmskov, U.1    Thiel, S.2    Jensenius, J.C.3
  • 90
    • 84871686542 scopus 로고    scopus 로고
    • Diversity in recognition of glycans by F-type lectins and galectins: molecular, structural, and biophysical aspects
    • Vasta G.R., Ahmed H., Bianchet M.A., Fernandez-Robledo J.A., Amzel L.M. Diversity in recognition of glycans by F-type lectins and galectins: molecular, structural, and biophysical aspects. Ann. N. Y Acad. Sci. 2012, 1253:14-26.
    • (2012) Ann. N. Y Acad. Sci. , vol.1253 , pp. 14-26
    • Vasta, G.R.1    Ahmed, H.2    Bianchet, M.A.3    Fernandez-Robledo, J.A.4    Amzel, L.M.5
  • 93
    • 80054002504 scopus 로고    scopus 로고
    • Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis
    • Yang M.-L., Chen Y.-H., Wang S.-W., Huang Y.-J., Leu C.-H., Yeh N.-C., et al. Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis. J.Virology 2011, 85:10010-10020.
    • (2011) J.Virology , vol.85 , pp. 10010-10020
    • Yang, M.-L.1    Chen, Y.-H.2    Wang, S.-W.3    Huang, Y.-J.4    Leu, C.-H.5    Yeh, N.-C.6
  • 94
    • 79952188597 scopus 로고    scopus 로고
    • Identification, molecular characterization and expression analysis of a mucosal C-type lectin in the eastern oyster, Crassostrea virginica
    • Jing X., Espinosa E.P., Perrigault M., Allam B. Identification, molecular characterization and expression analysis of a mucosal C-type lectin in the eastern oyster, Crassostrea virginica. Fish shellfish Immunol. 2011, 30:851-858.
    • (2011) Fish shellfish Immunol. , vol.30 , pp. 851-858
    • Jing, X.1    Espinosa, E.P.2    Perrigault, M.3    Allam, B.4
  • 95
    • 0037036622 scopus 로고    scopus 로고
    • CDNA cloning and characterization of two iron superoxide dismutases from the oyster parasite Perkinsus marinus
    • Wright A.C., Ahmed H., Gauthier J.D., Silva A.M., Vasta G.R. cDNA cloning and characterization of two iron superoxide dismutases from the oyster parasite Perkinsus marinus. Mol. Biochem. Parasitol. 2002, 123:73-77.
    • (2002) Mol. Biochem. Parasitol. , vol.123 , pp. 73-77
    • Wright, A.C.1    Ahmed, H.2    Gauthier, J.D.3    Silva, A.M.4    Vasta, G.R.5
  • 96
    • 0037237750 scopus 로고    scopus 로고
    • The PmSOD1 gene of the protistan parasite Perkinsus marinus complements the sod2δ mutant of Saccharomyces cerevisiae, and directs an iron superoxide dismutase to mitochondria
    • Schott E.J., Vasta G.R. The PmSOD1 gene of the protistan parasite Perkinsus marinus complements the sod2δ mutant of Saccharomyces cerevisiae, and directs an iron superoxide dismutase to mitochondria. Mol. Biochem. Parasitol. 2003, 126:81-92.
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 81-92
    • Schott, E.J.1    Vasta, G.R.2
  • 97
    • 0037464553 scopus 로고    scopus 로고
    • Gene organization and homology modeling of two iron superoxide dismutases of the early branching protist Perkinsus marinus
    • Schott E.J., Robledo J.A.F., Wright A.C., Silva A.M., Vasta G.R. Gene organization and homology modeling of two iron superoxide dismutases of the early branching protist Perkinsus marinus. Gene 2003, 309:1-9.
    • (2003) Gene , vol.309 , pp. 1-9
    • Schott, E.J.1    Robledo, J.A.F.2    Wright, A.C.3    Silva, A.M.4    Vasta, G.R.5
  • 98
    • 0038362437 scopus 로고    scopus 로고
    • Superoxide dismutases from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity
    • Ahmed H., Schott E.J., Gauthier J.D., Vasta G.R. Superoxide dismutases from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity. Anal. Biochem. 2003, 318:132-141.
    • (2003) Anal. Biochem. , vol.318 , pp. 132-141
    • Ahmed, H.1    Schott, E.J.2    Gauthier, J.D.3    Vasta, G.R.4
  • 99
    • 1342265409 scopus 로고    scopus 로고
    • The protistan parasite Perkinsus marinus is resistant to selected reactive oxygen species
    • Schott E.J., Pecher W.T., Okafor F., Vasta G.R. The protistan parasite Perkinsus marinus is resistant to selected reactive oxygen species. Exp. Parasitol. 2003, 105:232-240.
    • (2003) Exp. Parasitol. , vol.105 , pp. 232-240
    • Schott, E.J.1    Pecher, W.T.2    Okafor, F.3    Vasta, G.R.4
  • 101
    • 73949097627 scopus 로고    scopus 로고
    • Development of an invitro assay to examine intracellular survival of Perkinsus marinus trophozoites upon phagocytosis by oyster (Crassostrea virginica and Crassostrea ariakensis) hemocytes
    • Alavi M.R., Fernandez-Robledo J.A., Vasta G.R. Development of an invitro assay to examine intracellular survival of Perkinsus marinus trophozoites upon phagocytosis by oyster (Crassostrea virginica and Crassostrea ariakensis) hemocytes. J.Parasitol. 2009, 95:900-907.
    • (2009) J.Parasitol. , vol.95 , pp. 900-907
    • Alavi, M.R.1    Fernandez-Robledo, J.A.2    Vasta, G.R.3
  • 103
    • 15444380346 scopus 로고    scopus 로고
    • Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells
    • Ouellet M., Mercier S., Pelletier I., Bounou S., Roy J., Hirabayashi J., et al. Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells. J.Immunol. 2005, 174:4120-4126.
    • (2005) J.Immunol. , vol.174 , pp. 4120-4126
    • Ouellet, M.1    Mercier, S.2    Pelletier, I.3    Bounou, S.4    Roy, J.5    Hirabayashi, J.6
  • 104
    • 51449101867 scopus 로고    scopus 로고
    • Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis
    • Okumura C.Y., Baum L.G., Johnson P.J. Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis. Cell Microbiol. 2008, 10:2078-2090.
    • (2008) Cell Microbiol. , vol.10 , pp. 2078-2090
    • Okumura, C.Y.1    Baum, L.G.2    Johnson, P.J.3
  • 105
    • 27744522582 scopus 로고    scopus 로고
    • Trichomonas vaginalis lipophosphoglycan mutants have reduced adherence and cytotoxicity to human ectocervical cells
    • Bastida-Corcuera F.D., Okumura C.Y., Colocoussi A., Johnson P.J. Trichomonas vaginalis lipophosphoglycan mutants have reduced adherence and cytotoxicity to human ectocervical cells. Eukaryot Cell 2005, 4:1951-1958.
    • (2005) Eukaryot Cell , vol.4 , pp. 1951-1958
    • Bastida-Corcuera, F.D.1    Okumura, C.Y.2    Colocoussi, A.3    Johnson, P.J.4
  • 106
    • 84909954111 scopus 로고    scopus 로고
    • Lectin-like molecules in transcriptome of Littorina littorea hemocytes
    • Gorbushin A.M., Borisova E.A. Lectin-like molecules in transcriptome of Littorina littorea hemocytes. Dev. Comp. Immunol. 2015, 48:210-220.
    • (2015) Dev. Comp. Immunol. , vol.48 , pp. 210-220
    • Gorbushin, A.M.1    Borisova, E.A.2
  • 107
    • 84937162137 scopus 로고    scopus 로고
    • De novo assembly of transcriptome from RNA-seq data as a tool to reveal the complexity of the snail Biomphalaria glabrata immune system
    • Dheilly NM, Duval D, Mouahid G, Emans R, Allienne JF, Genthon C, etal. De novo assembly of transcriptome from RNA-seq data as a tool to reveal the complexity of the snail Biomphalaria glabrata immune system. Release date: 2013 (). http://2ei.univ-perp.fr/?page_id=89.
    • (2013) Release date
    • Dheilly, N.M.1    Duval, D.2    Mouahid, G.3    Emans, R.4    Allienne, J.F.5    Genthon, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.