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Volumn 1860, Issue 10, 2016, Pages 2285-2297

Galectin-related protein: An integral member of the network of chicken galectins 1. From strong sequence conservation of the gene confined to vertebrates to biochemical characteristics of the chicken protein and its crystal structure

Author keywords

Adhesion; Crystallography; Lectin; Phylogenesis; Proliferation

Indexed keywords

GALECTIN; GALECTIN 1; GALECTIN RELATED PROTEIN; LACTOSE; UNCLASSIFIED DRUG;

EID: 84978823970     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2016.06.001     Document Type: Article
Times cited : (31)

References (84)
  • 1
    • 84930821775 scopus 로고    scopus 로고
    • The magic of the sugar code
    • [1] Gabius, H.-J., The magic of the sugar code. Trends Biochem. Sci., 40, 2015, 341.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 341
    • Gabius, H.-J.1
  • 5
    • 84905368368 scopus 로고    scopus 로고
    • Convergent and divergent mechanisms of sugar recognition across kingdoms
    • [5] Taylor, M.E., Drickamer, K., Convergent and divergent mechanisms of sugar recognition across kingdoms. Curr. Opin. Struct. Biol. 28 (2014), 14–22.
    • (2014) Curr. Opin. Struct. Biol. , vol.28 , pp. 14-22
    • Taylor, M.E.1    Drickamer, K.2
  • 6
    • 84930820197 scopus 로고    scopus 로고
    • The glycobiology of the CD system: a dictionary for translating marker designations into glycan/lectin structure and function
    • [6] Gabius, H.-J., Kaltner, H., Kopitz, J., André, S., The glycobiology of the CD system: a dictionary for translating marker designations into glycan/lectin structure and function. Trends Biochem. Sci. 40 (2015), 360–376.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 360-376
    • Gabius, H.-J.1    Kaltner, H.2    Kopitz, J.3    André, S.4
  • 10
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • [10] Cooper, D.N.W., Galectinomics: finding themes in complexity. Biochim. Biophys. Acta 1572 (2002), 209–231.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 11
    • 84857738686 scopus 로고    scopus 로고
    • A toolbox of lectins for translating the sugar code: the galectin network in phylogenesis and tumors
    • [11] Kaltner, H., Gabius, H.-J., A toolbox of lectins for translating the sugar code: the galectin network in phylogenesis and tumors. Histol. Histopathol. 27 (2012), 397–416.
    • (2012) Histol. Histopathol. , vol.27 , pp. 397-416
    • Kaltner, H.1    Gabius, H.-J.2
  • 13
    • 0019152144 scopus 로고
    • Two lactose-binding lectins from chicken tissues. Purified lectin from intestine is different from those in liver and muscle
    • [13] Beyer, E.C., Zweig, S.E., Barondes, S.H., Two lactose-binding lectins from chicken tissues. Purified lectin from intestine is different from those in liver and muscle. J. Biol. Chem. 255 (1980), 4236–4239.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4236-4239
    • Beyer, E.C.1    Zweig, S.E.2    Barondes, S.H.3
  • 14
    • 0021113990 scopus 로고
    • Purification and characterization of β-galactoside-binding lectin from chick embryonic skin
    • [14] Oda, Y., Kasai, K.-i., Purification and characterization of β-galactoside-binding lectin from chick embryonic skin. Biochim. Biophys. Acta 761 (1983), 237–245.
    • (1983) Biochim. Biophys. Acta , vol.761 , pp. 237-245
    • Oda, Y.1    Kasai, K.-I.2
  • 15
    • 38749099077 scopus 로고    scopus 로고
    • Proto-type chicken galectins revisited: characterization of a third protein with distinctive hydrodynamic behaviour and expression pattern in organs of adult animals
    • [15] Kaltner, H., Solís, D., Kopitz, J., Lensch, M., Lohr, M., Manning, J.C., Mürnseer, M., Schnölzer, M., André, S., Sáiz, J.L., Gabius, H.-J., Proto-type chicken galectins revisited: characterization of a third protein with distinctive hydrodynamic behaviour and expression pattern in organs of adult animals. Biochem. J. 409 (2008), 591–599.
    • (2008) Biochem. J. , vol.409 , pp. 591-599
    • Kaltner, H.1    Solís, D.2    Kopitz, J.3    Lensch, M.4    Lohr, M.5    Manning, J.C.6    Mürnseer, M.7    Schnölzer, M.8    André, S.9    Sáiz, J.L.10    Gabius, H.-J.11
  • 16
    • 66149166021 scopus 로고    scopus 로고
    • Unique chicken tandem-repeat-type galectin: implications of alternative splicing and a distinct expression profile compared to those of the three proto-type proteins
    • [16] Kaltner, H., Solís, D., André, S., Lensch, M., Manning, J.C., Mürnseer, M., Sáiz, J.L., Gabius, H.-J., Unique chicken tandem-repeat-type galectin: implications of alternative splicing and a distinct expression profile compared to those of the three proto-type proteins. Biochemistry 48 (2009), 4403–4416.
    • (2009) Biochemistry , vol.48 , pp. 4403-4416
    • Kaltner, H.1    Solís, D.2    André, S.3    Lensch, M.4    Manning, J.C.5    Mürnseer, M.6    Sáiz, J.L.7    Gabius, H.-J.8
  • 17
    • 79951748301 scopus 로고    scopus 로고
    • Toward comprehensive analysis of the galectin network in chicken: unique diversity of galectin-3 and comparison of its localization profile in organs of adult animals to the other four members of this lectin family
    • [17] Kaltner, H., Kübler, D., López-Merino, L., Lohr, M., Manning, J.C., Lensch, M., Seidler, J., Lehmann, W.D., André, S., Solís, D., Gabius, H.-J., Toward comprehensive analysis of the galectin network in chicken: unique diversity of galectin-3 and comparison of its localization profile in organs of adult animals to the other four members of this lectin family. Anat. Rec. 294 (2011), 427–444.
    • (2011) Anat. Rec. , vol.294 , pp. 427-444
    • Kaltner, H.1    Kübler, D.2    López-Merino, L.3    Lohr, M.4    Manning, J.C.5    Lensch, M.6    Seidler, J.7    Lehmann, W.D.8    André, S.9    Solís, D.10    Gabius, H.-J.11
  • 18
    • 84887890030 scopus 로고    scopus 로고
    • Copy-number variation of functional galectin genes: studying animal galectin-7 (p53-induced gene 1 in man) and tandem-repeat-type galectins-4 and -9
    • [18] Kaltner, H., Raschta, A.-S., Manning, J.C., Gabius, H.-J., Copy-number variation of functional galectin genes: studying animal galectin-7 (p53-induced gene 1 in man) and tandem-repeat-type galectins-4 and -9. Glycobiology 23 (2013), 1152–1163.
    • (2013) Glycobiology , vol.23 , pp. 1152-1163
    • Kaltner, H.1    Raschta, A.-S.2    Manning, J.C.3    Gabius, H.-J.4
  • 21
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: a multiple sequence alignment editor and analysis workbench
    • [21] Waterhouse, A.M., Procter, J.B., Martin, D.M., Clamp, M., Barton, G.J., Jalview Version 2: a multiple sequence alignment editor and analysis workbench. Bioinformatics 25 (2009), 1189–1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 22
  • 23
    • 84905463032 scopus 로고    scopus 로고
    • Human chimera-type galectin-3: defining the critical tail length for high-affinity glycoprotein/cell surface binding and functional competition with galectin-1 in neuroblastoma cell growth regulation
    • [23] Kopitz, J., Vértesy, S., André, S., Fiedler, S., Schnölzer, M., Gabius, H.-J., Human chimera-type galectin-3: defining the critical tail length for high-affinity glycoprotein/cell surface binding and functional competition with galectin-1 in neuroblastoma cell growth regulation. Biochimie 104 (2014), 90–99.
    • (2014) Biochimie , vol.104 , pp. 90-99
    • Kopitz, J.1    Vértesy, S.2    André, S.3    Fiedler, S.4    Schnölzer, M.5    Gabius, H.-J.6
  • 24
    • 84937422316 scopus 로고    scopus 로고
    • Structural significance of galectin design: impairment of homodimer stability by linker insertion and partial reversion by ligand presence
    • [24] Vértesy, S., Michalak, M., Miller, M.C., Schnölzer, M., André, S., Kopitz, J., Mayo, K.H., Gabius, H.-J., Structural significance of galectin design: impairment of homodimer stability by linker insertion and partial reversion by ligand presence. Protein Eng. Des. Sel. 28 (2015), 199–210.
    • (2015) Protein Eng. Des. Sel. , vol.28 , pp. 199-210
    • Vértesy, S.1    Michalak, M.2    Miller, M.C.3    Schnölzer, M.4    André, S.5    Kopitz, J.6    Mayo, K.H.7    Gabius, H.-J.8
  • 25
    • 0026244044 scopus 로고
    • Gnom: a program package for small-angle scattering data-processing
    • [25] Semenyuk, A.V., Svergun, D.I., Gnom: a program package for small-angle scattering data-processing. J. Appl. Crystallogr. 24 (1991), 537–540.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 26
  • 27
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • [27] Svergun, D.I., Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999), 2879–2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 28
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • [28] Volkov, V.V., Svergun, D.I., Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36 (2003), 860–864.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 29
    • 84978170733 scopus 로고    scopus 로고
    • Basic Principles of Analytical Ultracentrifugation
    • CRC Press Boca Raton, USA
    • [29] Schuck, P., Zhao, H., Bräutigam, C.A., Ghirlanda, R., Basic Principles of Analytical Ultracentrifugation. 2015, CRC Press, Boca Raton, USA.
    • (2015)
    • Schuck, P.1    Zhao, H.2    Bräutigam, C.A.3    Ghirlanda, R.4
  • 30
    • 84867580385 scopus 로고    scopus 로고
    • INK4a: anoikis-favouring decrease in N/O-glycan/cell surface sialylation by down-regulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model
    • INK4a: anoikis-favouring decrease in N/O-glycan/cell surface sialylation by down-regulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model. FEBS J. 279 (2012), 4062–4080.
    • (2012) FEBS J. , vol.279 , pp. 4062-4080
    • Amano, M.1    Eriksson, H.2    Manning, J.C.3    Detjen, K.M.4    André, S.5    Nishimura, S.-I.6    Lehtiö, J.7    Gabius, H.-J.8
  • 32
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • [32] Diederichs, K., Karplus, P.A., Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol. 4 (1997), 269–275.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 33
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • [33] Kabsch, W., Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D66 (2010), 133–144.
    • (2010) Acta Crystallogr. , vol.D66 , pp. 133-144
    • Kabsch, W.1
  • 34
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: space-group determination, scaling and intensity statistics
    • [34] Evans, P.R., An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D67 (2011), 282–292.
    • (2011) Acta Crystallogr. , vol.D67 , pp. 282-292
    • Evans, P.R.1
  • 35
    • 84879367781 scopus 로고    scopus 로고
    • How good are my data and what is the resolution?
    • [35] Evans, P.R., Murshudov, G.N., How good are my data and what is the resolution?. Acta Crystallogr. D69 (2013), 1204–1214.
    • (2013) Acta Crystallogr. , vol.D69 , pp. 1204-1214
    • Evans, P.R.1    Murshudov, G.N.2
  • 36
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • [36] Matthews, B.W., Solvent content of protein crystals. J. Mol. Biol. 33 (1968), 491–497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 38
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • [38] Murshudov, G.N., Vagin, A.A., Dodson, E.J., Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53 (1997), 240–255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 0035827555 scopus 로고    scopus 로고
    • Cell cycle regulation by galectin-12, a new member of the galectin superfamily
    • [43] Yang, R.Y., Hsu, D.K., Yu, L., Ni, J., Liu, F.T., Cell cycle regulation by galectin-12, a new member of the galectin superfamily. J. Biol. Chem. 276 (2001), 20252–20260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20252-20260
    • Yang, R.Y.1    Hsu, D.K.2    Yu, L.3    Ni, J.4    Liu, F.T.5
  • 44
    • 84917710465 scopus 로고    scopus 로고
    • Impact of sodium butyrate on the network of adhesion/growth-regulatory galectins in human colon cancer in vitro
    • [44] Katzenmaier, E.-M., André, S., Kopitz, J., Gabius, H.-J., Impact of sodium butyrate on the network of adhesion/growth-regulatory galectins in human colon cancer in vitro. Anticancer Res. 34 (2014), 5429–5438.
    • (2014) Anticancer Res. , vol.34 , pp. 5429-5438
    • Katzenmaier, E.-M.1    André, S.2    Kopitz, J.3    Gabius, H.-J.4
  • 46
    • 19944431311 scopus 로고    scopus 로고
    • Determination of structural and functional overlap/divergence of five proto-type galectins by analysis of the growth-regulatory interaction with ganglioside GM1 in silico and in vitro on human neuroblastoma cells
    • [46] André, S., Kaltner, H., Lensch, M., Russwurm, R., Siebert, H.-C., Fallsehr, C., Tajkhorshid, E., Heck, A.J.R., von Knebel-Döberitz, M., Gabius, H.-J., Kopitz, J., Determination of structural and functional overlap/divergence of five proto-type galectins by analysis of the growth-regulatory interaction with ganglioside GM1 in silico and in vitro on human neuroblastoma cells. Int. J. Cancer 114 (2005), 46–57.
    • (2005) Int. J. Cancer , vol.114 , pp. 46-57
    • André, S.1    Kaltner, H.2    Lensch, M.3    Russwurm, R.4    Siebert, H.-C.5    Fallsehr, C.6    Tajkhorshid, E.7    Heck, A.J.R.8    von Knebel-Döberitz, M.9    Gabius, H.-J.10    Kopitz, J.11
  • 47
    • 0031048272 scopus 로고    scopus 로고
    • Identification and characterization of galectin-9, a novel β-galactoside-binding mammalian lectin
    • [47] Wada, J., Kanwar, Y.S., Identification and characterization of galectin-9, a novel β-galactoside-binding mammalian lectin. J. Biol. Chem. 272 (1997), 6078–6086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6078-6086
    • Wada, J.1    Kanwar, Y.S.2
  • 48
    • 77449102731 scopus 로고    scopus 로고
    • Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages
    • [48] Barrès, C., Blanc, L., Bette-Bobillo, P., André, S., Mamoun, R., Gabius, H.-J., Vidal, M., Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood 115 (2010), 696–705.
    • (2010) Blood , vol.115 , pp. 696-705
    • Barrès, C.1    Blanc, L.2    Bette-Bobillo, P.3    André, S.4    Mamoun, R.5    Gabius, H.-J.6    Vidal, M.7
  • 49
    • 33646863285 scopus 로고    scopus 로고
    • Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine-specificity and the effect of naturally clustered ligand presentation
    • [49] Wu, A.M., Singh, T., Wu, J.H., Lensch, M., André, S., Gabius, H.-J., Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine-specificity and the effect of naturally clustered ligand presentation. Glycobiology 16 (2006), 524–537.
    • (2006) Glycobiology , vol.16 , pp. 524-537
    • Wu, A.M.1    Singh, T.2    Wu, J.H.3    Lensch, M.4    André, S.5    Gabius, H.-J.6
  • 50
    • 84866096820 scopus 로고    scopus 로고
    • Allosteric regulation of the carbohydrate-binding ability of a novel conger eel galectin by D-mannoside
    • [50] Watanabe, M., Nakamura, O., Muramoto, K., Ogawa, T., Allosteric regulation of the carbohydrate-binding ability of a novel conger eel galectin by D-mannoside. J. Biol. Chem. 287 (2012), 31061–31072.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31061-31072
    • Watanabe, M.1    Nakamura, O.2    Muramoto, K.3    Ogawa, T.4
  • 51
    • 42749084551 scopus 로고    scopus 로고
    • Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea
    • [51] Wälti, M.A., Walser, P.J., Thore, S., Grunler, A., Bednar, M., Kunzler, M., Aebi, M., Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea. J. Mol. Biol. 379 (2008), 146–159.
    • (2008) J. Mol. Biol. , vol.379 , pp. 146-159
    • Wälti, M.A.1    Walser, P.J.2    Thore, S.3    Grunler, A.4    Bednar, M.5    Kunzler, M.6    Aebi, M.7
  • 53
    • 33751002037 scopus 로고    scopus 로고
    • Lectin-resistant CHO glycosylation mutants
    • [53] Patnaik, S.K., Stanley, P., Lectin-resistant CHO glycosylation mutants. Methods Enzymol. 416 (2006), 159–182.
    • (2006) Methods Enzymol. , vol.416 , pp. 159-182
    • Patnaik, S.K.1    Stanley, P.2
  • 54
    • 0022550421 scopus 로고
    • Drug targeting to the liver with lactosylated albumins: does the glycoprotein target the drug or is the drug targeting the glycoprotein?
    • [54] van der Sluijs, P., Bootsma, H.P., Postema, B., Moolenaar, F., Meijer, D.K.F., Drug targeting to the liver with lactosylated albumins: does the glycoprotein target the drug or is the drug targeting the glycoprotein?. Hepatology 6 (1986), 723–728.
    • (1986) Hepatology , vol.6 , pp. 723-728
    • van der Sluijs, P.1    Bootsma, H.P.2    Postema, B.3    Moolenaar, F.4    Meijer, D.K.F.5
  • 55
    • 84861492200 scopus 로고    scopus 로고
    • Down-regulation of the epidermal growth factor receptor by altering N-glycosylation: emerging role of β1,4-galactosyltransferases
    • [55] Gabius, H.-J., van de Wouwer, M., André, S., Villalobo, A., Down-regulation of the epidermal growth factor receptor by altering N-glycosylation: emerging role of β1,4-galactosyltransferases. Anticancer Res. 32 (2012), 1565–1572.
    • (2012) Anticancer Res. , vol.32 , pp. 1565-1572
    • Gabius, H.-J.1    van de Wouwer, M.2    André, S.3    Villalobo, A.4
  • 57
    • 42449105716 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins
    • [57] Zhou, D., Ge, H., Sun, J., Gao, Y., Teng, M., Niu, L., Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins. Proteins 71 (2008), 1582–1588.
    • (2008) Proteins , vol.71 , pp. 1582-1588
    • Zhou, D.1    Ge, H.2    Sun, J.3    Gao, Y.4    Teng, M.5    Niu, L.6
  • 58
    • 46449134897 scopus 로고    scopus 로고
    • Crystal structure of the putative carbohydrate recognition domain of human galectin-related protein
    • [58] Wälti, M.A., Thore, S., Aebi, M., Kunzler, M., Crystal structure of the putative carbohydrate recognition domain of human galectin-related protein. Proteins 72 (2008), 804–808.
    • (2008) Proteins , vol.72 , pp. 804-808
    • Wälti, M.A.1    Thore, S.2    Aebi, M.3    Kunzler, M.4
  • 59
    • 84922710893 scopus 로고    scopus 로고
    • Preliminary X-ray crystallographic analysis of an engineered variant of human chimera-type galectin-3 with a shortened N-terminal domain
    • [59] Flores-Ibarra, A., Ruiz, F.M., Vértesy, S., André, S., Gabius, H.-J., Romero, A., Preliminary X-ray crystallographic analysis of an engineered variant of human chimera-type galectin-3 with a shortened N-terminal domain. Acta Crystallogr. F71 (2015), 184–188.
    • (2015) Acta Crystallogr. , vol.F71 , pp. 184-188
    • Flores-Ibarra, A.1    Ruiz, F.M.2    Vértesy, S.3    André, S.4    Gabius, H.-J.5    Romero, A.6
  • 60
    • 33646854012 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray characterization of the GRP carbohydrate-recognition domain from Homo sapiens
    • [60] Zhou, D., Sun, J., Zhao, W., Zhang, X., Shi, Y., Teng, M., Niu, L., Dong, Y., Liu, P., Expression, purification, crystallization and preliminary X-ray characterization of the GRP carbohydrate-recognition domain from Homo sapiens. Acta Crystallogr. F62 (2006), 474–476.
    • (2006) Acta Crystallogr. , vol.F62 , pp. 474-476
    • Zhou, D.1    Sun, J.2    Zhao, W.3    Zhang, X.4    Shi, Y.5    Teng, M.6    Niu, L.7    Dong, Y.8    Liu, P.9
  • 61
    • 0037635976 scopus 로고    scopus 로고
    • Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and X-ray scattering
    • [61] He, L., André, S., Siebert, H.-C., Helmholz, H., Niemeyer, B., Gabius, H.-J., Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and X-ray scattering. Biophys. J. 85 (2003), 511–524.
    • (2003) Biophys. J. , vol.85 , pp. 511-524
    • He, L.1    André, S.2    Siebert, H.-C.3    Helmholz, H.4    Niemeyer, B.5    Gabius, H.-J.6
  • 62
    • 84941599865 scopus 로고    scopus 로고
    • Combining crystallography and hydrogen-deuterium exchange to study galectin-ligand complexes
    • [62] Ruiz, F.M., Gilles, U., Lindner, I., André, S., Romero, A., Reusch, D., Gabius, H.-J., Combining crystallography and hydrogen-deuterium exchange to study galectin-ligand complexes. Chem. Eur. J. 21 (2015), 13558–13568.
    • (2015) Chem. Eur. J. , vol.21 , pp. 13558-13568
    • Ruiz, F.M.1    Gilles, U.2    Lindner, I.3    André, S.4    Romero, A.5    Reusch, D.6    Gabius, H.-J.7
  • 64
    • 0033607322 scopus 로고    scopus 로고
    • The 2.15 Å crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin
    • [64] Varela, P.F., Solís, D., Díaz-Mauriño, T., Kaltner, H., Gabius, H.-J., Romero, A., The 2.15 Å crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin. J. Mol. Biol. 294 (1999), 537–549.
    • (1999) J. Mol. Biol. , vol.294 , pp. 537-549
    • Varela, P.F.1    Solís, D.2    Díaz-Mauriño, T.3    Kaltner, H.4    Gabius, H.-J.5    Romero, A.6
  • 65
    • 59149090057 scopus 로고    scopus 로고
    • Homodimeric chicken galectin CG-1B (C-14): crystal structure and detection of unique redox-dependent shape changes involving inter- and intrasubunit disulfide bridges by gel filtration, ultracentrifugation, site-directed mutagenesis, and peptide mass fingerprinting
    • [65] López-Lucendo, M.F., Solís, D., Sáiz, J.L., Kaltner, H., Russwurm, R., André, S., Gabius, H.-J., Romero, A., Homodimeric chicken galectin CG-1B (C-14): crystal structure and detection of unique redox-dependent shape changes involving inter- and intrasubunit disulfide bridges by gel filtration, ultracentrifugation, site-directed mutagenesis, and peptide mass fingerprinting. J. Mol. Biol. 386 (2009), 366–378.
    • (2009) J. Mol. Biol. , vol.386 , pp. 366-378
    • López-Lucendo, M.F.1    Solís, D.2    Sáiz, J.L.3    Kaltner, H.4    Russwurm, R.5    André, S.6    Gabius, H.-J.7    Romero, A.8
  • 66
    • 79960567167 scopus 로고    scopus 로고
    • Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor
    • [66] Peng, G., Sun, D., Rajashankar, K.R., Qian, Z., Holmes, K.V., Li, F., Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 10696–10701.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 10696-10701
    • Peng, G.1    Sun, D.2    Rajashankar, K.R.3    Qian, Z.4    Holmes, K.V.5    Li, F.6
  • 67
  • 68
    • 2342508517 scopus 로고    scopus 로고
    • Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP
    • [68] Rotblat, B., Niv, H., André, S., Kaltner, H., Gabius, H.-J., Kloog, Y., Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP. Cancer Res. 64 (2004), 3112–3118.
    • (2004) Cancer Res. , vol.64 , pp. 3112-3118
    • Rotblat, B.1    Niv, H.2    André, S.3    Kaltner, H.4    Gabius, H.-J.5    Kloog, Y.6
  • 72
    • 84930461770 scopus 로고    scopus 로고
    • Galectin-3 leads to attenuation of apoptosis through Bax heterodimerization in human thyroid carcinoma cells
    • [72] Harazono, Y., Kho, D.H., Balan, V., Nakajima, K., Zhang, T., Hogan, V., Raz, A., Galectin-3 leads to attenuation of apoptosis through Bax heterodimerization in human thyroid carcinoma cells. Oncotarget 5 (2014), 9992–10001.
    • (2014) Oncotarget , vol.5 , pp. 9992-10001
    • Harazono, Y.1    Kho, D.H.2    Balan, V.3    Nakajima, K.4    Zhang, T.5    Hogan, V.6    Raz, A.7
  • 74
    • 84922249793 scopus 로고    scopus 로고
    • Structural basis of Toxoplasma gondii MIC2-associated protein interaction with MIC2
    • [74] Huynh, M.H., Liu, B., Henry, M., Liew, L., Matthews, S.J., Carruthers, V.B., Structural basis of Toxoplasma gondii MIC2-associated protein interaction with MIC2. J. Biol. Chem. 290 (2015), 1432–1441.
    • (2015) J. Biol. Chem. , vol.290 , pp. 1432-1441
    • Huynh, M.H.1    Liu, B.2    Henry, M.3    Liew, L.4    Matthews, S.J.5    Carruthers, V.B.6
  • 75
    • 84875908545 scopus 로고    scopus 로고
    • Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8
    • [75] Kim, B.W., Hong, S.B., Kim, J.H., do Kwon, H., Song, H.K., Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8. Nat. Commun., 4, 2013, 1613.
    • (2013) Nat. Commun. , vol.4 , pp. 1613
    • Kim, B.W.1    Hong, S.B.2    Kim, J.H.3    do Kwon, H.4    Song, H.K.5
  • 76
    • 84874274351 scopus 로고    scopus 로고
    • Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy
    • [76] Li, S., Wandel, M.P., Li, F.D., Liu, Z.H., He, C., Wu, J.H., Shi, Y.Y., Randow, F., Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy. Sci. Signal., 6, 2013.
    • (2013) Sci. Signal. , vol.6
    • Li, S.1    Wandel, M.P.2    Li, F.D.3    Liu, Z.H.4    He, C.5    Wu, J.H.6    Shi, Y.Y.7    Randow, F.8
  • 78
    • 84895420067 scopus 로고    scopus 로고
    • Natural single amino acid polymorphism (F19Y) in human galectin-8: detection of structural alterations and increased growth-regulatory activity on tumor cells
    • [78] Ruiz, F.M., Scholz, B.A., Buzamet, E., Kopitz, J., André, S., Menéndez, M., Romero, A., Solís, D., Gabius, H.-J., Natural single amino acid polymorphism (F19Y) in human galectin-8: detection of structural alterations and increased growth-regulatory activity on tumor cells. FEBS J. 281 (2014), 1446–1464.
    • (2014) FEBS J. , vol.281 , pp. 1446-1464
    • Ruiz, F.M.1    Scholz, B.A.2    Buzamet, E.3    Kopitz, J.4    André, S.5    Menéndez, M.6    Romero, A.7    Solís, D.8    Gabius, H.-J.9
  • 79
    • 84928975425 scopus 로고    scopus 로고
    • Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface
    • [79] Zhang, S., Moussodia, R.-O., Vértesy, S., André, S., Klein, M.L., Gabius, H.-J., Percec, V., Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), 5585–5590.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 5585-5590
    • Zhang, S.1    Moussodia, R.-O.2    Vértesy, S.3    André, S.4    Klein, M.L.5    Gabius, H.-J.6    Percec, V.7
  • 80
    • 84883302212 scopus 로고    scopus 로고
    • The growing galectin network in colon cancer and clinical relevance of cytoplasmic galectin-3 reactivity
    • [80] Dawson, H., André, S., Karamitopoulou, E., Zlobec, I., Gabius, H.-J., The growing galectin network in colon cancer and clinical relevance of cytoplasmic galectin-3 reactivity. Anticancer Res. 33 (2013), 3053–3059.
    • (2013) Anticancer Res. , vol.33 , pp. 3053-3059
    • Dawson, H.1    André, S.2    Karamitopoulou, E.3    Zlobec, I.4    Gabius, H.-J.5
  • 81
    • 84922161299 scopus 로고    scopus 로고
    • Human osteoarthritic knee cartilage: fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration
    • [81] Toegel, S., Bieder, D., André, S., Kayser, K., Walzer, S.M., Hobusch, G., Windhager, R., Gabius, H.-J., Human osteoarthritic knee cartilage: fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration. Histochem. Cell Biol. 142 (2014), 373–388.
    • (2014) Histochem. Cell Biol. , vol.142 , pp. 373-388
    • Toegel, S.1    Bieder, D.2    André, S.3    Kayser, K.4    Walzer, S.M.5    Hobusch, G.6    Windhager, R.7    Gabius, H.-J.8
  • 82
    • 79955915952 scopus 로고    scopus 로고
    • Routes in lectin evolution: case study on the C-type lectin-like domains
    • H.-J. Gabius Wiley-VCH Weinheim, Germany
    • [82] Gready, J.N., Zelensky, A.N., Routes in lectin evolution: case study on the C-type lectin-like domains. Gabius, H.-J., (eds.) The Sugar Code. Fundamentals of glycosciences, 2009, Wiley-VCH, Weinheim, Germany, 329–346.
    • (2009) The Sugar Code. Fundamentals of glycosciences , pp. 329-346
    • Gready, J.N.1    Zelensky, A.N.2
  • 84
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • [84] Karplus, P.A., Diederichs, K., Linking crystallographic model and data quality. Science 336 (2012), 1030–1033.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


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