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Volumn 75, Issue 5, 2017, Pages

Functions of galectins as 'self/non-self'-recognition and effector factors

Author keywords

Carbohydrate recognition domain; Chimera; Function; Galectins; Glycans; Pattern recognition receptors; Proto type; galactoside; Structure; Tandem repeat

Indexed keywords

GALECTIN; GLYCAN; PATTERN RECOGNITION RECEPTOR; REDOX EFFECTOR FACTOR 1; IMMUNOGLOBULIN RECEPTOR;

EID: 85028654168     PISSN: None     EISSN: 2049632X     Source Type: Journal    
DOI: 10.1093/femspd/ftx046     Document Type: Short Survey
Times cited : (49)

References (89)
  • 1
    • 79957467023 scopus 로고    scopus 로고
    • Promoter methylation in prostate cancer and its application for the early detection of prostate cancer using serum and urine samples
    • Ahmed H. Promoter methylation in prostate cancer and its application for the early detection of prostate cancer using serum and urine samples. Biomark Cancer 2010;2:17-33
    • (2010) Biomark Cancer , vol.2 , pp. 17-33
    • Ahmed, H.1
  • 2
    • 34248202726 scopus 로고    scopus 로고
    • Differential expression of galectins in normal, benign and malignant prostate epithelial cells: silencing of galectin-3 expression in prostate cancer by its promoter methylation
    • Ahmed H, Banerjee PP, Vasta GR. Differential expression of galectins in normal, benign and malignant prostate epithelial cells: silencing of galectin-3 expression in prostate cancer by its promoter methylation. Biochem Bioph Res Co 2007;358:241-6
    • (2007) Biochem Bioph Res Co , vol.358 , pp. 241-246
    • Ahmed, H.1    Banerjee, P.P.2    Vasta, G.R.3
  • 3
    • 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 MA, Amzel LM 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;12:451-61
    • (2002) Glycobiology , vol.12 , pp. 451-461
    • Ahmed, H.1    Bianchet, M.A.2    Amzel, L.M.3
  • 4
    • 77951939167 scopus 로고    scopus 로고
    • Evidence of heavy methylation in the galectin 3 promoter in early stages of prostate adenocarcinoma: development and validation of a methylated marker for early diagnosis of prostate cancer
    • Ahmed H, Cappello F, Rodolico V et al. Evidence of heavy methylation in the galectin 3 promoter in early stages of prostate adenocarcinoma: development and validation of a methylated marker for early diagnosis of prostate cancer. Transl Oncol 2009;2:146-56
    • (2009) Transl Oncol , vol.2 , pp. 146-156
    • Ahmed, H.1    Cappello, F.2    Rodolico, V.3
  • 5
    • 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 et al. Biochemical and molecular characterization of galectins from zebrafish (Danio rerio): notochord-specific expression of a prototype galectin during early embryogenesis. Glycobiology 2004;14:219-32
    • (2004) Glycobiology , vol.14 , pp. 219-232
    • Ahmed, H.1    Du, S.-J.2    O'Leary, N.3
  • 6
    • 85028672286 scopus 로고    scopus 로고
    • Animal models for assessing the biological roles of lectins
    • Vasta GR, Ahmed H (eds) Boca Raton, FL: CRC Press
    • Ahmed H, Rabinovich GA, Jackson SS et al. Animal models for assessing the biological roles of lectins. In: Vasta GR, Ahmed H (eds) Animals Lectins: A Functional View. Boca Raton, FL: CRC Press, 2008
    • Animals Lectins: A Functional View
    • Ahmed, H.1    Rabinovich, G.A.2    Jackson, S.S.3
  • 7
    • 43549108972 scopus 로고    scopus 로고
    • Unlike mammalian GRIFIN, the zebrafish homologue (DrGRIFIN) represents a functional carbohydratebinding galectin
    • Ahmed H, Vasta GR. Unlike mammalian GRIFIN, the zebrafish homologue (DrGRIFIN) represents a functional carbohydratebinding galectin. Biochem Bioph Res Co 2008;371:350-5
    • (2008) Biochem Bioph Res Co , vol.371 , pp. 350-355
    • Ahmed, H.1    Vasta, G.R.2
  • 8
    • 0242476502 scopus 로고    scopus 로고
    • Genomic analysis of immunity in a Urochordate and the emergence of the vertebrate immune system: "waiting for Godot"
    • Azumi K, De Santis R, De Tomaso A et al. Genomic analysis of immunity in a Urochordate and the emergence of the vertebrate immune system: "waiting for Godot". Immunogenetics 2003;55:570-81
    • (2003) Immunogenetics , vol.55 , pp. 570-581
    • Azumi, K.1    De Santis, R.2    De Tomaso, A.3
  • 9
    • 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 JM et al. 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 2007;178:436-45
    • (2007) J Immunol , vol.178 , pp. 436-445
    • Barrionuevo, P.1    Beigier-Bompadre, M.2    Ilarregui, J.M.3
  • 10
    • 79960601577 scopus 로고    scopus 로고
    • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry
    • Bi S, Hong PW, Lee B et al. Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. P Natl Acad Sci USA 2011;108:10650-5
    • (2011) P Natl Acad Sci USA , vol.108 , pp. 10650-10655
    • Bi, S.1    Hong, P.W.2    Lee, B.3
  • 11
    • 0034663733 scopus 로고    scopus 로고
    • Soluble beta-galactosylbinding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes
    • Bianchet MA, Ahmed H, Vasta GR et al. Soluble beta-galactosylbinding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes. Proteins 2000;40:378-88
    • (2000) Proteins , vol.40 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3
  • 12
    • 0036312626 scopus 로고    scopus 로고
    • A novel fucose recognition fold involved in innate immunity
    • Bianchet MA, Odom EW, Vasta GR et al. A novel fucose recognition fold involved in innate immunity. Nat Struct Biol 2002;9:628-34
    • (2002) Nat Struct Biol , vol.9 , pp. 628-634
    • Bianchet, M.A.1    Odom, E.W.2    Vasta, G.R.3
  • 13
    • 84946491906 scopus 로고    scopus 로고
    • Re-wiring regulatory cell networks in immunity by galectin-glycan interactions
    • Blidner AG, Mendez-Huergo SP, Cagnoni AJ et al. Re-wiring regulatory cell networks in immunity by galectin-glycan interactions. FEBS Lett 2015;589:3407-18
    • (2015) FEBS Lett , vol.589 , pp. 3407-3418
    • Blidner, A.G.1    Mendez-Huergo, S.P.2    Cagnoni, A.J.3
  • 14
    • 36849020587 scopus 로고    scopus 로고
    • A pivotal role for galectin-1 in fetomaternal tolerance
    • Blois SM, Ilarregui JM, Tometten M et al. A pivotal role for galectin-1 in fetomaternal tolerance. Nat Med 2007;13:1450-7
    • (2007) Nat Med , vol.13 , pp. 1450-1457
    • Blois, S.M.1    Ilarregui, J.M.2    Tometten, M.3
  • 15
  • 16
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer CF, Miceli MC, Baum LG. Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr Opin Struct Biol 2002;12:616-23
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 17
    • 84920996275 scopus 로고    scopus 로고
    • Galectins and neuroinflammation
    • Chen HL, Liao F, Lin TN et al. Galectins and neuroinflammation. Adv Neurobiol 2014;9:517-42
    • (2014) Adv Neurobiol , vol.9 , pp. 517-542
    • Chen, H.L.1    Liao, F.2    Lin, T.N.3
  • 18
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves AE, Cooper DN, Barondes SH et al. A new pathway for protein export in Saccharomyces cerevisiae. J Cell Biol 1996;133:1017-26
    • (1996) J Cell Biol , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, S.H.3
  • 20
    • 0035174596 scopus 로고    scopus 로고
    • Uncoupling of chondrocyte death and vascular invasion inmouse galectin 3 nullmutant bones
    • Colnot C, Sidhu SS, Balmain N et al. Uncoupling of chondrocyte death and vascular invasion inmouse galectin 3 nullmutant bones. Dev Biol 2001;229:203-14
    • (2001) Dev Biol , vol.229 , pp. 203-214
    • Colnot, C.1    Sidhu, S.S.2    Balmain, N.3
  • 21
    • 0025786162 scopus 로고
    • Endogenous muscle lectin inhibits myoblast adhesion to laminin
    • Cooper DN, Massa SM, Barondes SH. Endogenous muscle lectin inhibits myoblast adhesion to laminin. J Cell Biol 1991;115:1437-48
    • (1991) J Cell Biol , vol.115 , pp. 1437-1448
    • Cooper, D.N.1    Massa, S.M.2    Barondes, S.H.3
  • 22
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • Cooper DNW. Galectinomics: finding themes in complexity. Biochim Biophys Acta 2002;1572:209-31
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 23
    • 77953282863 scopus 로고    scopus 로고
    • The zebrafish galectin Drgal1-l2 is expressed by proliferating Muller glia and photoreceptor progenitors and regulates the regeneration of rod photoreceptors
    • Craig SEL, Thummel R, Ahmed H et al. The zebrafish galectin Drgal1-l2 is expressed by proliferating Muller glia and photoreceptor progenitors and regulates the regeneration of rod photoreceptors. Invest Ophth Vis Sci 2010;51:3244-52
    • (2010) Invest Ophth Vis Sci , vol.51 , pp. 3244-3252
    • Craig, S.E.L.1    Thummel, R.2    Ahmed, H.3
  • 24
    • 84894136530 scopus 로고    scopus 로고
    • Glycosylationdependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors
    • Croci DO, Cerliani JP, Dalotto-Moreno T et al. Glycosylationdependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors. Cell 2014;156:744-58
    • (2014) Cell , vol.156 , pp. 744-758
    • Croci, D.O.1    Cerliani, J.P.2    Dalotto-Moreno, T.3
  • 25
    • 49749153118 scopus 로고    scopus 로고
    • Effects of clustered epitopes in multivalent ligand-receptor interactions
    • Dam TK, Brewer CF. Effects of clustered epitopes in multivalent ligand-receptor interactions. Biochemistry 2008;47:8470-6
    • (2008) Biochemistry , vol.47 , pp. 8470-8476
    • Dam, T.K.1    Brewer, C.F.2
  • 26
    • 77955432935 scopus 로고    scopus 로고
    • Maintenance of cell surface glycan density by lectin-glycan interactions: a homeostatic and innate immune regulatory mechanism
    • Dam TK, Brewer CF. Maintenance of cell surface glycan density by lectin-glycan interactions: a homeostatic and innate immune regulatory mechanism. Glycobiology 2010;20: 1061-4
    • (2010) Glycobiology , vol.20 , pp. 1061-1064
    • Dam, T.K.1    Brewer, C.F.2
  • 27
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity
    • Dodd RB, Drickamer K. Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology 2001;11:71R-9R
    • (2001) Glycobiology , vol.11 , pp. 71R-79R
    • Dodd, R.B.1    Drickamer, K.2
  • 29
    • 34447136940 scopus 로고    scopus 로고
    • Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival
    • Elola MT,Wolfenstein-Todel C, Troncoso MF et al. Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival. Cell Mol Life Sci 2007;64:1679-700
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1679-1700
    • Elola, M.T.1    Wolfenstein-Todel, C.2    Troncoso, M.F.3
  • 30
    • 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 MN et al. The galectin CvGal1 from the eastern oyster (Crassostrea virginica) binds to blood group A oligosaccharides on the hemocyte surface. J Biol Chem 2013;288:24394-409
    • (2013) J Biol Chem , vol.288 , pp. 24394-24409
    • Feng, C.1    Ghosh, A.2    Amin, M.N.3
  • 31
    • 84938674943 scopus 로고    scopus 로고
    • Galectin CvGal2 from the Eastern Oyster (Crassostrea virginica) displays unique specificity for ABH blood group oligosaccharides and differentially recognizes sympatric Perkinsus species
    • Feng C, Ghosh A, Amin MN et al. Galectin CvGal2 from the Eastern Oyster (Crassostrea virginica) displays unique specificity for ABH blood group oligosaccharides and differentially recognizes sympatric Perkinsus species. Biochemistry 2015a;54:4711-30
    • (2015) Biochemistry , vol.54 , pp. 4711-4730
    • Feng, C.1    Ghosh, A.2    Amin, M.N.3
  • 32
    • 84921710832 scopus 로고    scopus 로고
    • Manipulating galectin expression in zebrafish (Danio rerio)
    • Feng C, Nita-Lazar M, Gonzalez-Montalban N et al. Manipulating galectin expression in zebrafish (Danio rerio). Methods Mol Biol 2015b;1207:327-41
    • (2015) Methods Mol Biol , vol.1207 , pp. 327-341
    • Feng, C.1    Nita-Lazar, M.2    Gonzalez-Montalban, N.3
  • 33
    • 84924252300 scopus 로고    scopus 로고
    • Galectin-3 and heart failure: prognosis, prediction & clinical utility
    • Filipe MD, Meijers WC, Rogier van der Velde A et al. Galectin-3 and heart failure: prognosis, prediction & clinical utility. Clin Chim Acta 2015;443:48-56
    • (2015) Clin Chim Acta , vol.443 , pp. 48-56
    • Filipe, M.D.1    Meijers, W.C.2    Rogier van der Velde, A.3
  • 34
    • 0032959619 scopus 로고    scopus 로고
    • The tat protein of HIV-1 induces galectin-3 expression
    • Fogel S, Guittaut M, Legrand A et al. The tat protein of HIV-1 induces galectin-3 expression. Glycobiology 1999;9:383-7
    • (1999) Glycobiology , vol.9 , pp. 383-387
    • Fogel, S.1    Guittaut, M.2    Legrand, A.3
  • 35
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius HJ. Animal lectins. Eur J Biochem 1997;243:543-76
    • (1997) Eur J Biochem , vol.243 , pp. 543-576
    • Gabius, H.J.1
  • 36
    • 84923008549 scopus 로고    scopus 로고
    • Timing of galectin-1 exposure differentially modulates Nipah virus entry and syncytium formation in endothelial cells
    • Garner OB, Yun T, Pernet O et al. Timing of galectin-1 exposure differentially modulates Nipah virus entry and syncytium formation in endothelial cells. J Virol 2015;89:2520-9
    • (2015) J Virol , vol.89 , pp. 2520-2529
    • Garner, O.B.1    Yun, T.2    Pernet, O.3
  • 37
    • 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 et al. Cod glycopeptide with picomolar affinity to galectin-3 suppresses T-cell apoptosis and prostate cancer metastasis. P Natl Acad Sci USA 2013;110:5052-7
    • (2013) P Natl Acad Sci USA , vol.110 , pp. 5052-5057
    • Guha, P.1    Kaptan, E.2    Bandyopadhyaya, G.3
  • 38
    • 33645234690 scopus 로고    scopus 로고
    • Bioluminescence imaging of live infected salmonids reveals that the fin bases are the major portal of entry for Novirhabdovirus
    • Harmache A, LeBerre M, Droineau S et al. Bioluminescence imaging of live infected salmonids reveals that the fin bases are the major portal of entry for Novirhabdovirus. J Virol 2006;80:3655-9
    • (2006) J Virol , vol.80 , pp. 3655-3659
    • Harmache, A.1    LeBerre, M.2    Droineau, S.3
  • 39
    • 77952762068 scopus 로고    scopus 로고
    • A novel clinically relevant animal model for studying galectin-3 and its ligands during colon carcinogenesis
    • Hill M, Mazal D, Biron VA et al. A novel clinically relevant animal model for studying galectin-3 and its ligands during colon carcinogenesis. J Histochem Cytochem 2010;58:553-65
    • (2010) J Histochem Cytochem , vol.58 , pp. 553-565
    • Hill, M.1    Mazal, D.2    Biron, V.A.3
  • 40
    • 0027169990 scopus 로고
    • The family of metazoan metalindependent beta-galactoside-binding lectins: structure, function and molecular evolution
    • Hirabayashi J, Kasai K. The family of metazoan metalindependent 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
  • 41
    • 1542367461 scopus 로고    scopus 로고
    • Galectin-9 in physiological and pathological conditions
    • Hirashima M, Kashio Y, Nishi N et al. Galectin-9 in physiological and pathological conditions. Glycoconjugate J 2004;19:593-600
    • (2004) Glycoconjugate J , vol.19 , pp. 593-600
    • Hirashima, M.1    Kashio, Y.2    Nishi, N.3
  • 42
    • 85028661944 scopus 로고    scopus 로고
    • Regulation of immune responses by galectin-3
    • Vasta GR, Ahmed H (eds) Boca Raton, FL: CRC Press
    • Hsu DK, Liu F-T. Regulation of immune responses by galectin-3. In: Vasta GR, Ahmed H (eds) Animals Lectins: A Functional View. Boca Raton, FL: CRC Press, 2008
    • Animals Lectins: A Functional View
    • Hsu, D.K.1    Liu, F.-T.2
  • 43
    • 7044247771 scopus 로고    scopus 로고
    • A role for insect galectins in parasite survival
    • Kamhawi S, Ramalho-Ortigao M, Pham VM et al. A role for insect galectins in parasite survival. Cell 2004;119:329-41
    • (2004) Cell , vol.119 , pp. 329-341
    • Kamhawi, S.1    Ramalho-Ortigao, M.2    Pham, V.M.3
  • 44
    • 84926435515 scopus 로고    scopus 로고
    • The genomic and genetic toolbox of the teleost medaka (Oryzias latipes)
    • Kirchmaier S, Naruse K, Wittbrodt J et al. The genomic and genetic toolbox of the teleost medaka (Oryzias latipes). Genetics 2015;199:905-18
    • (2015) Genetics , vol.199 , pp. 905-918
    • Kirchmaier, S.1    Naruse, K.2    Wittbrodt, J.3
  • 45
    • 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 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 Biol Chem 2013;288:24410-28
    • (2013) J Biol Chem , vol.288 , pp. 24410-24428
    • Kurz, S.1    Jin, C.2    Hykollari, A.3
  • 46
    • 21244502470 scopus 로고    scopus 로고
    • Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines
    • Levroney EL, Aguilar HC, Fulcher JA et al. Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines. J Immunol 2005;175:413-20
    • (2005) J Immunol , vol.175 , pp. 413-420
    • Levroney, E.L.1    Aguilar, H.C.2    Fulcher, J.A.3
  • 47
    • 2442519018 scopus 로고    scopus 로고
    • Selectins in T-cell recruitment to nonlymphoid tissues and sites of inflammation
    • Ley K, Kansas GS. Selectins in T-cell recruitment to nonlymphoid tissues and sites of inflammation. Nat Rev Immunol 2004;4:325-35
    • (2004) Nat Rev Immunol , vol.4 , pp. 325-335
    • Ley, K.1    Kansas, G.S.2
  • 48
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein
    • Liao DI, Kapadia G, Ahmed H et al. Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. P Natl Acad Sci USA 1994;91:1428-32
    • (1994) P Natl Acad Sci USA , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3
  • 49
    • 1542283662 scopus 로고    scopus 로고
    • Galectin 9 is the sugar-regulated urate transporter/channel UAT
    • Lipkowitz MS, Leal-Pinto E, Cohen BE et al. Galectin 9 is the sugar-regulated urate transporter/channel UAT. Glycoconjugate J 2004;19:491-8
    • (2004) Glycoconjugate J , vol.19 , pp. 491-498
    • Lipkowitz, M.S.1    Leal-Pinto, E.2    Cohen, B.E.3
  • 50
    • 84860228899 scopus 로고    scopus 로고
    • Galectins in acute and chronic inflammation
    • Liu FT, Yang RY, Hsu DK. Galectins in acute and chronic inflammation. Ann N Y Acad Sci 2012;1253:80-91
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 80-91
    • Liu, F.T.1    Yang, R.Y.2    Hsu, D.K.3
  • 51
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution
    • Lobsanov YD, Gitt MA, Leffler H et al. X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. J Biol Chem 1993;268:27034-8
    • (1993) J Biol Chem , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3
  • 52
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • Medzhitov R, Janeway CA, Jr. Decoding the patterns of self and nonself by the innate immune system. Science 2002;296:298-300
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway, C.A.2
  • 53
    • 84928755858 scopus 로고    scopus 로고
    • The bitter side of sweet: the role of Galectin-9 in immunopathogenesis of viral infections
    • Merani S, Chen W, Elahi S. The bitter side of sweet: the role of Galectin-9 in immunopathogenesis of viral infections. Rev Med Virol 2015;25:175-86
    • (2015) Rev Med Virol , vol.25 , pp. 175-186
    • Merani, S.1    Chen, W.2    Elahi, S.3
  • 54
    • 1542285489 scopus 로고    scopus 로고
    • Quaternary solution structures of galectins-1,-3, and-7
    • Morris S, Ahmad N, Andre S et al. Quaternary solution structures of galectins-1,-3, and-7. Glycobiology 2004;14:293-300
    • (2004) Glycobiology , vol.14 , pp. 293-300
    • Morris, S.1    Ahmad, N.2    Andre, S.3
  • 55
    • 84920952426 scopus 로고    scopus 로고
    • Desialylation of airway epithelial cells during influenza virus infection enhances pneumococcal adhesion via galectin binding
    • Nita-Lazar M, Banerjee A, Feng C et al. Desialylation of airway epithelial cells during influenza virus infection enhances pneumococcal adhesion via galectin binding. Mol Immunol 2015a;65:1-16
    • (2015) Mol Immunol , vol.65 , pp. 1-16
    • Nita-Lazar, M.1    Banerjee, A.2    Feng, C.3
  • 56
    • 84957433993 scopus 로고    scopus 로고
    • Galectins regulate the inflammatory response in airway epithelial cells exposed to microbial neuraminidase by modulating the expression of SOCS1 and RIG1
    • Nita-Lazar M, Banerjee A, Feng C et al. Galectins regulate the inflammatory response in airway epithelial cells exposed to microbial neuraminidase by modulating the expression of SOCS1 and RIG1. Mol Immunol 2015b;68: 194-202
    • (2015) Mol Immunol , vol.68 , pp. 194-202
    • Nita-Lazar, M.1    Banerjee, A.2    Feng, C.3
  • 57
    • 84962076531 scopus 로고    scopus 로고
    • The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells
    • Nita-Lazar M, Mancini J, Feng C et al. The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells. Dev Comp Immunol 2016;55:241-52
    • (2016) Dev Comp Immunol , vol.55 , pp. 241-252
    • Nita-Lazar, M.1    Mancini, J.2    Feng, C.3
  • 58
    • 33644981902 scopus 로고    scopus 로고
    • Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis)
    • Odom EW, Vasta GR. Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis). J Biol Chem 2006;281:1698-713
    • (2006) J Biol Chem , vol.281 , pp. 1698-1713
    • Odom, E.W.1    Vasta, G.R.2
  • 59
    • 0032582653 scopus 로고    scopus 로고
    • GRIFIN, a novel lens-specific protein related to the galectin family
    • Ogden AT, Nunes I, Ko K et al. GRIFIN, a novel lens-specific protein related to the galectin family. J Biol Chem 1998;273:28889-96
    • (1998) J Biol Chem , vol.273 , pp. 28889-28896
    • Ogden, A.T.1    Nunes, I.2    Ko, K.3
  • 60
    • 51449101867 scopus 로고    scopus 로고
    • Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis
    • Okumura CY, Baum LG, Johnson PJ. Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis. Cell Microbiol 2008;10:2078-90
    • (2008) Cell Microbiol , vol.10 , pp. 2078-2090
    • Okumura, C.Y.1    Baum, L.G.2    Johnson, P.J.3
  • 61
    • 0037066780 scopus 로고    scopus 로고
    • Characterization of a novel Drosophila melanogaster galectin. Expression in developing immune, neural, and muscle tissues
    • Pace KE, Lebestky T, Hummel T et al. Characterization of a novel Drosophila melanogaster galectin. Expression in developing immune, neural, and muscle tissues. J Biol Chem 2002;277:13091-8
    • (2002) J Biol Chem , vol.277 , pp. 13091-13098
    • Pace, K.E.1    Lebestky, T.2    Hummel, T.3
  • 62
    • 84874329045 scopus 로고    scopus 로고
    • Increased adiposity, dysregulated glucose metabolism and systemic inflammation in Galectin-3 KOmice
    • Pang J, Rhodes DH, PiniMet al. Increased adiposity, dysregulated glucose metabolism and systemic inflammation in Galectin-3 KOmice. PLoS One 2013;8:e57915
    • (2013) PLoS One , vol.8
    • Pang, J.1    Rhodes, D.H.2    Pini, M.3
  • 63
    • 84938415944 scopus 로고    scopus 로고
    • Galectin-3 is a regulator of metaflammation in adipose tissue and pancreatic islets
    • Pejnovic NN, Pantic JM, Jovanovic IP et al. Galectin-3 is a regulator of metaflammation in adipose tissue and pancreatic islets. Adipocyte 2013;2:266-71
    • (2013) Adipocyte , vol.2 , pp. 266-271
    • Pejnovic, N.N.1    Pantic, J.M.2    Jovanovic, I.P.3
  • 66
    • 33745848466 scopus 로고    scopus 로고
    • Clustering of pre-B cell integrins induces galectin-1-dependent pre-B cell receptor relocalization and activation
    • Rossi B, Espeli M, Schiff C et al. Clustering of pre-B cell integrins induces galectin-1-dependent pre-B cell receptor relocalization and activation. J Immunol 2006;177:796-803
    • (2006) J Immunol , vol.177 , pp. 796-803
    • Rossi, B.1    Espeli, M.2    Schiff, C.3
  • 67
    • 33644666110 scopus 로고    scopus 로고
    • A novel 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 et al. A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. J Biol Chem 2005;280:38583-91
    • (2005) J Biol Chem , vol.280 , pp. 38583-38591
    • Saouros, S.1    Edwards-Jones, B.2    Reiss, M.3
  • 68
    • 0026673762 scopus 로고
    • Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin
    • Sato S, Hughes, RC Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. J Biol Chem 1992;267:6983-90
    • (1992) J Biol Chem , vol.267 , pp. 6983-6990
    • Sato, S.1    Hughes, R.C.2
  • 69
    • 84860233524 scopus 로고    scopus 로고
    • Glycans, galectins, and HIV-1 infection
    • Sato S, Ouellet M, St-Pierre C et al. Glycans, galectins, and HIV-1 infection. Ann N Y Acad Sci 2012;1253:133-48
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 133-148
    • Sato, S.1    Ouellet, M.2    St-Pierre, C.3
  • 70
    • 0032574694 scopus 로고    scopus 로고
    • Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature
    • Schwarz FP, Ahmed H, Bianchet MA et al. Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature. Biochemistry 1998;37:5867-77
    • (1998) Biochemistry , vol.37 , pp. 5867-5877
    • Schwarz, F.P.1    Ahmed, H.2    Bianchet, M.A.3
  • 71
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution
    • Seetharaman J, Kanigsberg A, Slaaby R et al. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution. J Biol Chem 1998;273:13047-52
    • (1998) J Biol Chem , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3
  • 72
    • 84897479520 scopus 로고    scopus 로고
    • A galectin from the kuruma shrimp (Marsupenaeus japonicus) functions as an opsonin and promotes bacterial clearance fromhemolymph
    • Shi X-Z, Wang L, Xu S et al. A galectin from the kuruma shrimp (Marsupenaeus japonicus) functions as an opsonin and promotes bacterial clearance fromhemolymph. PLoS One 2014;9:e91794
    • (2014) PLoS One , vol.9
    • Shi, X.-Z.1    Wang, L.2    Xu, S.3
  • 73
    • 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 et al. The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain. Glycobiology 2006;16:402-14
    • (2006) Glycobiology , vol.16 , pp. 402-414
    • Stalz, H.1    Roth, U.2    Schleuder, D.3
  • 74
    • 77749239686 scopus 로고    scopus 로고
    • Innate immune lectins kill bacteria expressing blood group antigen
    • Stowell SR, Arthur CM, Dias-Baruffi M et al. Innate immune lectins kill bacteria expressing blood group antigen. Nat Med 2010;16:295-301
    • (2010) Nat Med , vol.16 , pp. 295-301
    • Stowell, S.R.1    Arthur, C.M.2    Dias-Baruffi, M.3
  • 75
    • 46949103440 scopus 로고    scopus 로고
    • Differential roles of galectin-1 and galectin-3 in regulating leukocyte viability and cytokine secretion
    • Stowell SR, Qian Y, Karmakar S et al. Differential roles of galectin-1 and galectin-3 in regulating leukocyte viability and cytokine secretion. J Immunol 2008;180:3091-102
    • (2008) J Immunol , vol.180 , pp. 3091-3102
    • Stowell, S.R.1    Qian, Y.2    Karmakar, S.3
  • 76
    • 35548934271 scopus 로고    scopus 로고
    • A galectin of unique domain organization from hemocytes of the Eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus
    • Tasumi S, Vasta GR. A galectin of unique domain organization from hemocytes of the Eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus. J Immunol 2007;179:3086-98
    • (2007) J Immunol , vol.179 , pp. 3086-3098
    • Tasumi, S.1    Vasta, G.R.2
  • 77
    • 58849139114 scopus 로고    scopus 로고
    • Binding of oligosaccharide ligands to the selectins requires additional interactions with the carbohydrate-recognition domains
    • Taylor ME, Drickamer K (eds). Oxford, NY: Oxford University Press
    • Taylor ME, Drickamer K. Binding of oligosaccharide ligands to the selectins requires additional interactions with the carbohydrate-recognition domains. In: Taylor ME, Drickamer K (eds) Introduction of Glycobiology. Oxford, NY: Oxford University Press, 2003, 207
    • (2003) Introduction of Glycobiology , pp. 207
    • Taylor, M.E.1    Drickamer, K.2
  • 78
    • 84911926248 scopus 로고    scopus 로고
    • Galectin-1 exerts inhibitory effects during DENV-1 infection
    • Toledo KA, Fermino ML, Andrade Cdel C et al. Galectin-1 exerts inhibitory effects during DENV-1 infection. PLoS One 2014;9:e112474
    • (2014) PLoS One , vol.9
    • Toledo, K.A.1    Fermino, M.L.2    Andrade Cdel, C.3
  • 79
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta GR. Roles of galectins in infection. Nat Rev Microbiol 2009;7:424-38
    • (2009) Nat Rev Microbiol , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 80
    • 80555149784 scopus 로고    scopus 로고
    • Galectins as pattern recognition receptors: structure, function, and evolution
    • Vasta GR. 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
  • 81
    • 85131977701 scopus 로고    scopus 로고
    • Animals lectins: a functional view
    • Vasta GR, Ahmed H (eds) Boca Raton, FL: CRC Press
    • Vasta GR, Ahmed H. Animals lectins: a functional view. In: Vasta GR, Ahmed H (eds) Animals Lectins: A Functional View. Boca Raton, FL: CRC Press, 2008
    • Animals Lectins: A Functional View
    • Vasta, G.R.1    Ahmed, H.2
  • 82
    • 84871686542 scopus 로고    scopus 로고
    • Diversity in recognition of glycans by F-type lectins and galectins: molecular, structural, and biophysical aspects
    • Vasta GR, Ahmed H, Bianchet MA et al. 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
  • 83
    • 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 GR, Ahmed H, Du S et al. Galectins in teleost fish: Zebrafish (Danio rerio) as a model species to address their biological roles in development and innate immunity. Glycoconjugate J 2004;21:503-21
    • (2004) Glycoconjugate J , vol.21 , pp. 503-521
    • Vasta, G.R.1    Ahmed, H.2    Du, S.3
  • 84
    • 84934436728 scopus 로고    scopus 로고
    • Biological roles of lectins in innate immunity: molecular and structural basis for diversity in self/non-self recognition
    • Vasta GR, Ahmed H, Tasumi S et al. Biological roles of lectins in innate immunity: molecular and structural basis for diversity in self/non-self recognition. Adv Exp Med Biol 2007;598:389-406
    • (2007) Adv Exp Med Biol , vol.598 , pp. 389-406
    • Vasta, G.R.1    Ahmed, H.2    Tasumi, S.3
  • 85
    • 84937163196 scopus 로고    scopus 로고
    • Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse
    • Vasta GR, Feng C, Bianchet MA et al. Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse. Fish Shellfish Immunol 2015;46:94-106
    • (2015) Fish Shellfish Immunol , vol.46 , pp. 94-106
    • Vasta, G.R.1    Feng, C.2    Bianchet, M.A.3
  • 86
    • 84942273628 scopus 로고    scopus 로고
    • F-type lectins: a new family of recognition factors
    • Vasta GR, Ahmed H (eds), Boca Raton, FL: CRC Press
    • Vasta GR, Odom EW, Bianchet MA et al. F-type lectins: a new family of recognition factors. In: Vasta GR, Ahmed H (eds), Animals Lectins: A Functional View. Boca Raton, FL: CRC Press, 2008
    • (2008) Animals Lectins: A Functional View
    • Vasta, G.R.1    Odom, E.W.2    Bianchet, M.A.3
  • 87
    • 14644417195 scopus 로고    scopus 로고
    • Ligand interactions of the Coprinopsis cinerea galectins
    • Walser PJ, Kues U, Aebi M et al. Ligand interactions of the Coprinopsis cinerea galectins. Fungal Genet Biol 2005;42: 293-305
    • (2005) Fungal Genet Biol , vol.42 , pp. 293-305
    • Walser, P.J.1    Kues, U.2    Aebi, M.3
  • 88
    • 80054002504 scopus 로고    scopus 로고
    • Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis
    • Yang ML, Chen YH,Wang SW et al. Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis. J Virol 2011a;85:10010-20
    • (2011) J Virol , vol.85 , pp. 10010-10020
    • Yang, M.L.1    Chen, Y.H.2    Wang, S.W.3
  • 89
    • 81755163611 scopus 로고    scopus 로고
    • Ablation of a galectin preferentially expressed in adipocytes increases lipolysis, reduces adiposity, and improves insulin sensitivity in mice
    • Yang RY, Yu L, Graham JL et al. Ablation of a galectin preferentially expressed in adipocytes increases lipolysis, reduces adiposity, and improves insulin sensitivity in mice. P Natl Acad Sci USA 2011b;108:18696-701
    • (2011) P Natl Acad Sci USA , vol.108 , pp. 18696-18701
    • Yang, R.Y.1    Yu, L.2    Graham, J.L.3


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