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Volumn 281, Issue 5, 2014, Pages 1446-1464

Natural single amino acid polymorphism (F19Y) in human galectin-8: Detection of structural alterations and increased growth-regulatory activity on tumor cells

Author keywords

agglutination; carcinoma; ganglioside; lectin; proliferation; sandwich

Indexed keywords

CARBOHYDRATE; GALECTIN 8; PROTEIN VARIANT;

EID: 84895420067     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12716     Document Type: Article
Times cited : (44)

References (86)
  • 3
    • 84860228899 scopus 로고    scopus 로고
    • Galectins in acute and chronic inflammation
    • Liu F-T, Yang R-Y, &, Hsu DK, (2012) Galectins in acute and chronic inflammation. Ann N Y Acad Sci 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
  • 4
    • 84857738686 scopus 로고    scopus 로고
    • A toolbox of lectins for translating the sugar code: The galectin network in phylogenesis and tumors
    • Kaltner H, &, Gabius H-J, (2012) A toolbox of lectins for translating the sugar code: the galectin network in phylogenesis and tumors. Histol Histopathol 27, 397-416.
    • (2012) Histol Histopathol , vol.27 , pp. 397-416
    • Kaltner, H.1    Gabius, H.-J.2
  • 5
    • 0026344814 scopus 로고
    • Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside- binding lectin
    • Hirabayashi J, &, Kasai K-I, (1991) Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside-binding lectin. J Biol Chem 266, 23648-23653.
    • (1991) J Biol Chem , vol.266 , pp. 23648-23653
    • Hirabayashi, J.1    Kasai, K.-I.2
  • 6
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • Lõpez-Lucendo MF, Solís D, André S, Hirabayashi J, Kasai K-I, Kaltner H, Gabius H-J, &, Romero A, (2004) Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol 343, 957-970.
    • (2004) J Mol Biol , vol.343 , pp. 957-970
    • Lõpez-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.-I.5    Kaltner, H.6    Gabius, H.-J.7    Romero, A.8
  • 7
    • 2342480580 scopus 로고    scopus 로고
    • Functional variation in LGALS2 confers risk of myocardial infarction and regulates lymphotoxin-α secretion in vitro
    • Ozaki K, Inoue K, Sato H, Iida A, Ohnishi Y, Sekine A, Sato H, Odashiro K, Nobuyoshi M, Hori M, et al,. (2004) Functional variation in LGALS2 confers risk of myocardial infarction and regulates lymphotoxin-α secretion in vitro. Nature 429, 72-75.
    • (2004) Nature , vol.429 , pp. 72-75
    • Ozaki, K.1    Inoue, K.2    Sato, H.3    Iida, A.4    Ohnishi, Y.5    Sekine, A.6    Sato, H.7    Odashiro, K.8    Nobuyoshi, M.9    Hori, M.10
  • 8
    • 13844269257 scopus 로고    scopus 로고
    • Fine-scale SNP map of an 11-kb genomic region at 22q13.1 containing the galectin-1 gene
    • Iida A, Ozaki K, Tanaka T, &, Nakamura Y, (2005) Fine-scale SNP map of an 11-kb genomic region at 22q13.1 containing the galectin-1 gene. J Hum Genet 50, 42-45.
    • (2005) J Hum Genet , vol.50 , pp. 42-45
    • Iida, A.1    Ozaki, K.2    Tanaka, T.3    Nakamura, Y.4
  • 9
    • 75049083845 scopus 로고    scopus 로고
    • Lack of association between lymphotoxin-α, galectin-2 polymorphisms and coronary artery disease: A meta-analysis
    • Li W, Xu J, Wang X, Chen J, Zhang C, Sun K, &, Hui R, (2010) Lack of association between lymphotoxin-α, galectin-2 polymorphisms and coronary artery disease: a meta-analysis. Atherosclerosis 208, 433-436.
    • (2010) Atherosclerosis , vol.208 , pp. 433-436
    • Li, W.1    Xu, J.2    Wang, X.3    Chen, J.4    Zhang, C.5    Sun, K.6    Hui, R.7
  • 11
    • 0027414461 scopus 로고
    • Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma
    • Lotz MM, Andrews CW Jr, Korzelius CA, Lee EC, Steele GD Jr, Clarke A, &, Mercurio AM, (1993) Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma. Proc Natl Acad Sci USA 90, 3466-3470.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3466-3470
    • Lotz, M.M.1    Andrews, Jr.C.W.2    Korzelius, C.A.3    Lee, E.C.4    Steele, Jr.G.D.5    Clarke, A.6    Mercurio, A.M.7
  • 13
    • 80052328867 scopus 로고    scopus 로고
    • A galectin-3 sequence polymorphism confers TRAIL sensitivity to human breast cancer cells
    • Mazurek N, Byrd JC, Sun Y, Ueno S, &, Bresalier RS, (2011) A galectin-3 sequence polymorphism confers TRAIL sensitivity to human breast cancer cells. Cancer 117, 4375-4380.
    • (2011) Cancer , vol.117 , pp. 4375-4380
    • Mazurek, N.1    Byrd, J.C.2    Sun, Y.3    Ueno, S.4    Bresalier, R.S.5
  • 15
    • 80052623499 scopus 로고    scopus 로고
    • Galectin-3 gene (LGALS3) +292C allele is a genetic predisposition factor for rheumatoid arthritis in Taiwan
    • Hu CY, Chang SK, Wu CS, Tsai WI, &, Hsu PN, (2011) Galectin-3 gene (LGALS3) +292C allele is a genetic predisposition factor for rheumatoid arthritis in Taiwan. Clin Rheumatol 30, 1227-1233.
    • (2011) Clin Rheumatol , vol.30 , pp. 1227-1233
    • Hu, C.Y.1    Chang, S.K.2    Wu, C.S.3    Tsai, W.I.4    Hsu, P.N.5
  • 16
    • 84861532568 scopus 로고    scopus 로고
    • The effect of galectin-3 genetic variants on the susceptibility and prognosis of gliomas in a Chinese population
    • Chen HJ, Zheng ZC, Yuan BQ, Liu Z, Jing J, &, Wang SS, (2012) The effect of galectin-3 genetic variants on the susceptibility and prognosis of gliomas in a Chinese population. Neurosci Lett 518, 1-4.
    • (2012) Neurosci Lett , vol.518 , pp. 1-4
    • Chen, H.J.1    Zheng, Z.C.2    Yuan, B.Q.3    Liu, Z.4    Jing, J.5    Wang, S.S.6
  • 17
    • 84870051940 scopus 로고    scopus 로고
    • Galectin-3 genetic variants are associated with platinum-based chemotherapy response and prognosis in patients with NSCLC
    • Wu F, Hu N, Li Y, Bian B, Xu G, &, Zheng Y, (2012) Galectin-3 genetic variants are associated with platinum-based chemotherapy response and prognosis in patients with NSCLC. Cell Oncol 35, 175-180.
    • (2012) Cell Oncol , vol.35 , pp. 175-180
    • Wu, F.1    Hu, N.2    Li, Y.3    Bian, B.4    Xu, G.5    Zheng, Y.6
  • 18
    • 84863438780 scopus 로고    scopus 로고
    • Non-synonymous single nucleotide polymorphisms in genes for immunoregulatory galectins: Association of galectin-8 (F19Y) occurrence with autoimmune diseases in a Caucasian population
    • Pál Z, Antal P, Srivastava SK, Hullám G, Semsei AF, Gál J, Svébis M, Soõs G, Szalai C, André S, et al,. (2012) Non-synonymous single nucleotide polymorphisms in genes for immunoregulatory galectins: association of galectin-8 (F19Y) occurrence with autoimmune diseases in a Caucasian population. Biochim Biophys Acta 1820, 1512-1518.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 1512-1518
    • Pál, Z.1    Antal, P.2    Srivastava, S.K.3    Hullám, G.4    Semsei, A.F.5    Gál, J.6    Svébis, M.7    Soõs, G.8    Szalai, C.9    André, S.10
  • 20
    • 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
    • Kaltner H, Solís D, André S, Lensch M, Manning JC, Mürnseer M, Sáiz JL, &, Gabius H-J, (2009) 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, 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
  • 21
    • 0034915081 scopus 로고    scopus 로고
    • Immunohistochemical profile of galectin-8 expression in benign and malignant tumors of epithelial, mesenchymatous and adipous origins, and of the nervous system
    • Danguy A, Rorive S, Decaestecker C, Bronckart Y, Kaltner H, Hadari YR, Goren R, Zick Y, Petein M, Salmon I, et al,. (2001) Immunohistochemical profile of galectin-8 expression in benign and malignant tumors of epithelial, mesenchymatous and adipous origins, and of the nervous system. Histol Histopathol 16, 861-868.
    • (2001) Histol Histopathol , vol.16 , pp. 861-868
    • Danguy, A.1    Rorive, S.2    Decaestecker, C.3    Bronckart, Y.4    Kaltner, H.5    Hadari, Y.R.6    Goren, R.7    Zick, Y.8    Petein, M.9    Salmon, I.10
  • 22
    • 0036175965 scopus 로고    scopus 로고
    • Galectin-8 expression decreases in cancer compared with normal and dysplastic human colon tissue and acts significantly on human colon cancer cell migration as a suppressor
    • Nagy N, Bronckart Y, Camby I, Legendre H, Lahm H, Kaltner H, Hadari Y, van Ham P, Yeaton P, Pector JC, et al,. (2002) Galectin-8 expression decreases in cancer compared with normal and dysplastic human colon tissue and acts significantly on human colon cancer cell migration as a suppressor. Gut 50, 392-401.
    • (2002) Gut , vol.50 , pp. 392-401
    • Nagy, N.1    Bronckart, Y.2    Camby, I.3    Legendre, H.4    Lahm, H.5    Kaltner, H.6    Hadari, Y.7    Van Ham, P.8    Yeaton, P.9    Pector, J.C.10
  • 23
    • 35348822484 scopus 로고    scopus 로고
    • Gene-expression signature of adhesion/growth-regulatory tissue lectins (galectins) in transitional cell cancer and its prognostic relevance
    • Langbein S, Brade J, Badawi JK, Hatzinger M, Kaltner H, Lensch M, Specht K, André S, Brinck U, Alken P, et al,. (2007) Gene-expression signature of adhesion/growth-regulatory tissue lectins (galectins) in transitional cell cancer and its prognostic relevance. Histopathology 51, 681-690.
    • (2007) Histopathology , vol.51 , pp. 681-690
    • Langbein, S.1    Brade, J.2    Badawi, J.K.3    Hatzinger, M.4    Kaltner, H.5    Lensch, M.6    Specht, K.7    André, S.8    Brinck, U.9    Alken, P.10
  • 26
    • 79952721100 scopus 로고    scopus 로고
    • Quantitative immunohistochemical fingerprinting of adhesion/growth- regulatory galectins in salivary gland tumours: Divergent profiles with diagnostic potential
    • Remmelink M, de Leval L, Decaestecker C, Duray A, Crompot E, Sirtaine N, André S, Kaltner H, Leroy X, Gabius H-J, et al,. (2011) Quantitative immunohistochemical fingerprinting of adhesion/growth-regulatory galectins in salivary gland tumours: divergent profiles with diagnostic potential. Histopathology 58, 543-556.
    • (2011) Histopathology , vol.58 , pp. 543-556
    • Remmelink, M.1    De Leval, L.2    Decaestecker, C.3    Duray, A.4    Crompot, E.5    Sirtaine, N.6    André, S.7    Kaltner, H.8    Leroy, X.9    Gabius, H.-J.10
  • 29
    • 21444438367 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors and JNK act as molecular switches, regulating the choice between growth arrest and apoptosis induced by galectin-8
    • Arbel-Goren R, Levy Y, Ronen D, &, Zick Y, (2005) Cyclin-dependent kinase inhibitors and JNK act as molecular switches, regulating the choice between growth arrest and apoptosis induced by galectin-8. J Biol Chem 280, 19105-19114.
    • (2005) J Biol Chem , vol.280 , pp. 19105-19114
    • Arbel-Goren, R.1    Levy, Y.2    Ronen, D.3    Zick, Y.4
  • 32
  • 33
    • 79251546715 scopus 로고    scopus 로고
    • Galectin-8 tandem-repeat structure is essential for T-cell proliferation but not for co-stimulation
    • Cattaneo V, Tribulatti MV, &, Campetella O, (2011) Galectin-8 tandem-repeat structure is essential for T-cell proliferation but not for co-stimulation. Biochem J 434, 153-160.
    • (2011) Biochem J , vol.434 , pp. 153-160
    • Cattaneo, V.1    Tribulatti, M.V.2    Campetella, O.3
  • 35
    • 65549122918 scopus 로고    scopus 로고
    • Autoantibodies against galectin-8: Their specificity, association with lymphopenia in systemic lupus erythematosus and detection in rheumatoid arthritis and acute inflammation
    • Massardo L, Metz C, Pardo E, Mezzano V, Babul M, Jarpa E, Guzmán AM, André S, Kaltner H, Gabius H-J, et al,. (2009) Autoantibodies against galectin-8: their specificity, association with lymphopenia in systemic lupus erythematosus and detection in rheumatoid arthritis and acute inflammation. Lupus 18, 539-546.
    • (2009) Lupus , vol.18 , pp. 539-546
    • Massardo, L.1    Metz, C.2    Pardo, E.3    Mezzano, V.4    Babul, M.5    Jarpa, E.6    Guzmán, A.M.7    André, S.8    Kaltner, H.9    Gabius, H.-J.10
  • 38
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • Ideo H, Seko A, Ishizuka I, &, Yamashita K, (2003) The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 13, 713-723.
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 40
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain
    • Stowell SR, Arthur CM, Slanina KA, Horton JR, Smith DF, &, Cummings RD, (2008) Dimeric galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain. J Biol Chem 283, 20547-20559.
    • (2008) J Biol Chem , vol.283 , pp. 20547-20559
    • Stowell, S.R.1    Arthur, C.M.2    Slanina, K.A.3    Horton, J.R.4    Smith, D.F.5    Cummings, R.D.6
  • 43
    • 79953197242 scopus 로고    scopus 로고
    • Galectin-8 N-domain recognition mechanism for sialylated and sulfated glycans
    • Ideo H, Matsuzaka T, Nonaka T, Seko A, &, Yamashita K, (2011) Galectin-8 N-domain recognition mechanism for sialylated and sulfated glycans. J Biol Chem 286, 11346-11355.
    • (2011) J Biol Chem , vol.286 , pp. 11346-11355
    • Ideo, H.1    Matsuzaka, T.2    Nonaka, T.3    Seko, A.4    Yamashita, K.5
  • 44
    • 84867096793 scopus 로고    scopus 로고
    • X-ray structure of a protease-resistant mutant form of human galectin-8 with two carbohydrate recognition domains
    • Yoshida H, Yamashita S, Teraoka M, Itoh A, Nakakita S, Nishi N, &, Kamitori S, (2012) X-ray structure of a protease-resistant mutant form of human galectin-8 with two carbohydrate recognition domains. FEBS J 279, 3937-3951.
    • (2012) FEBS J , vol.279 , pp. 3937-3951
    • Yoshida, H.1    Yamashita, S.2    Teraoka, M.3    Itoh, A.4    Nakakita, S.5    Nishi, N.6    Kamitori, S.7
  • 45
    • 77953741266 scopus 로고    scopus 로고
    • N-domain of human adhesion/growth-regulatory galectin-9: Preference for distinct conformers and non-sialylated N-glycans and detection of ligand-induced structural changes in crystal and solution
    • Solís D, Maté MJ, Lohr M, Ribeiro JP, Lõpez-Merino L, André S, Buzamet E, Cañada FJ, Kaltner H, Lensch M, et al,. (2010) N-domain of human adhesion/growth-regulatory galectin-9: preference for distinct conformers and non-sialylated N-glycans and detection of ligand-induced structural changes in crystal and solution. Int J Biochem Cell Biol 42, 1019-1029.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 1019-1029
    • Solís, D.1    Maté, M.J.2    Lohr, M.3    Ribeiro, J.P.4    Lõpez-Merino, L.5    André, S.6    Buzamet, E.7    Cañada, F.J.8    Kaltner, H.9    Lensch, M.10
  • 46
    • 84875908545 scopus 로고    scopus 로고
    • Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8
    • Kim B-W, Hong SB, Kim JH, Kwon DH, &, Song HK, (2013) Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8. Nat Commun 4, 1613.
    • (2013) Nat Commun , vol.4 , pp. 1613
    • Kim, B.-W.1    Hong, S.B.2    Kim, J.H.3    Kwon, D.H.4    Song, H.K.5
  • 47
    • 84874274351 scopus 로고    scopus 로고
    • Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy
    • Li S, Wandel MP, Li F, Liu Z, He C, Wu J, Shi Y, &, Randow F, (2013) Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy. Sci Signal 6, ra9.
    • (2013) Sci Signal , vol.6
    • Li, S.1    Wandel, M.P.2    Li, F.3    Liu, Z.4    He, C.5    Wu, J.6    Shi, Y.7    Randow, F.8
  • 48
    • 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
    • He L, André S, Siebert H-C, Helmholz H, Niemeyer B, &, Gabius H-J, (2003) 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, 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
  • 49
    • 77953572271 scopus 로고    scopus 로고
    • Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy
    • Göhler A, André S, Kaltner H, Sauer M, Gabius H-J, &, Doose S, (2010) Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy. Biophys J 98, 3044-3053.
    • (2010) Biophys J , vol.98 , pp. 3044-3053
    • Göhler, A.1    André, S.2    Kaltner, H.3    Sauer, M.4    Gabius, H.-J.5    Doose, S.6
  • 50
    • 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
    • Kaltner H, Solís D, Kopitz J, Lensch M, Lohr M, Manning JC, Mürnseer M, Schnölzer M, Siebert H-C, André S, et al,. (2008) 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, 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    Siebert, H.-C.9    André, S.10
  • 51
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, &, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 53
    • 28444497752 scopus 로고    scopus 로고
    • Monomer/dimer equilibrium of the AB-type lectin from mistletoe enables combination of toxin/agglutinin activities in one protein: Analysis of native and citraconylated proteins by ultracentrifugation/gel filtration and cell biological consequences of dimer destabilization
    • Jiménez M, Sáiz JL, André S, Gabius H-J, &, Solís D, (2005) Monomer/dimer equilibrium of the AB-type lectin from mistletoe enables combination of toxin/agglutinin activities in one protein: analysis of native and citraconylated proteins by ultracentrifugation/gel filtration and cell biological consequences of dimer destabilization. Glycobiology 15, 1386-1395.
    • (2005) Glycobiology , vol.15 , pp. 1386-1395
    • Jiménez, M.1    Sáiz, J.L.2    André, S.3    Gabius, H.-J.4    Solís, D.5
  • 54
    • 84877298793 scopus 로고    scopus 로고
    • Single-site mutational engineering and following monoPEGylation of the human lectin galectin-2: Effects on ligand binding, functional aspects, and clearance from serum
    • Kopitz J, Fik Z, André S, Smetana K Jr, &, Gabius H-J, (2013) Single-site mutational engineering and following monoPEGylation of the human lectin galectin-2: effects on ligand binding, functional aspects, and clearance from serum. Mol Pharmaceut 10, 2054-2061.
    • (2013) Mol Pharmaceut , vol.10 , pp. 2054-2061
    • Kopitz, J.1    Fik, Z.2    André, S.3    Smetana, Jr.K.4    Gabius, H.-J.5
  • 55
    • 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
    • André S, Kaltner H, Lensch M, Russwurm R, Siebert H-C, Fallsehr C, Tajkhorshid E, Heck AJR, von Knebel Doeberitz M, Gabius H-J, et al,. (2005) 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, 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 Doeberitz, M.9    Gabius, H.-J.10
  • 56
    • 77955873679 scopus 로고    scopus 로고
    • How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity: Case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane
    • Kopitz J, Bergmann M, &, Gabius H-J, (2010) How adhesion/growth- regulatory galectins-1 and -3 attain cell specificity: case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane. IUBMB Life 62, 624-628.
    • (2010) IUBMB Life , vol.62 , pp. 624-628
    • Kopitz, J.1    Bergmann, M.2    Gabius, H.-J.3
  • 57
    • 0032080122 scopus 로고    scopus 로고
    • Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • Kopitz J, von Reitzenstein C, Burchert M, Cantz M, &, Gabius H-J, (1998) Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture. J Biol Chem 273, 11205-11211.
    • (1998) J Biol Chem , vol.273 , pp. 11205-11211
    • Kopitz, J.1    Von Reitzenstein, C.2    Burchert, M.3    Cantz, M.4    Gabius, H.-J.5
  • 58
    • 84862876828 scopus 로고    scopus 로고
    • Ganglioside GM1/galectin-dependent growth regulation in human neuroblastoma cells: Special properties of bivalent galectin-4 and significance of linker length for ligand selection
    • Kopitz J, Ballikaya S, André S, &, Gabius H-J, (2012) Ganglioside GM1/galectin-dependent growth regulation in human neuroblastoma cells: special properties of bivalent galectin-4 and significance of linker length for ligand selection. Neurochem Res 37, 1267-1276.
    • (2012) Neurochem Res , vol.37 , pp. 1267-1276
    • Kopitz, J.1    Ballikaya, S.2    André, S.3    Gabius, H.-J.4
  • 59
    • 64249146003 scopus 로고    scopus 로고
    • Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: Possible role in suppressing experimental autoimmune encephalomyelitis
    • Wang J, Lu ZH, Gabius H-J, Rohowsky-Kochan C, Ledeen RW, &, Wu G, (2009) Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: possible role in suppressing experimental autoimmune encephalomyelitis. J Immunol 182, 4036-4045.
    • (2009) J Immunol , vol.182 , pp. 4036-4045
    • Wang, J.1    Lu, Z.H.2    Gabius, H.-J.3    Rohowsky-Kochan, C.4    Ledeen, R.W.5    Wu, G.6
  • 60
    • 80052906797 scopus 로고    scopus 로고
    • Ganglioside GM1 deficiency in effector T cells from NOD mice induces resistance to regulatory T-cell suppression
    • Wu G, Lu ZH, Gabius H-J, Ledeen RW, &, Bleich D, (2011) Ganglioside GM1 deficiency in effector T cells from NOD mice induces resistance to regulatory T-cell suppression. Diabetes 60, 2341-2349.
    • (2011) Diabetes , vol.60 , pp. 2341-2349
    • Wu, G.1    Lu, Z.H.2    Gabius, H.-J.3    Ledeen, R.W.4    Bleich, D.5
  • 61
    • 84875124030 scopus 로고    scopus 로고
    • Context-dependent multifunctionality of galectin-1: A challenge for defining the lectin as therapeutic target
    • Smetana K Jr, André S, Kaltner H, Kopitz J, &, Gabius H-J, (2013) Context-dependent multifunctionality of galectin-1: a challenge for defining the lectin as therapeutic target. Expert Opin Ther Targets 17, 379-392.
    • (2013) Expert Opin Ther Targets , vol.17 , pp. 379-392
    • Smetana, Jr.K.1    André, S.2    Kaltner, H.3    Kopitz, J.4    Gabius, H.-J.5
  • 62
    • 84857071710 scopus 로고    scopus 로고
    • Galectin-8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston TLM, Wandel MP, von Muhlinen N, Foeglein A, &, Randow F, (2012) Galectin-8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature 482, 414-418.
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.M.1    Wandel, M.P.2    Von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 67
    • 68249085064 scopus 로고    scopus 로고
    • MBL2, FCN1, FCN2 and FCN3: The genes behind the initiation of the lectin pathway of complement
    • Garred P, Honoré C, Ma YJ, Munthe-Fog L, &, Hummelshøj T, (2009) MBL2, FCN1, FCN2 and FCN3: the genes behind the initiation of the lectin pathway of complement. Mol Immunol 46, 2737-2744.
    • (2009) Mol Immunol , vol.46 , pp. 2737-2744
    • Garred, P.1    Honoré, C.2    Ma, Y.J.3    Munthe-Fog, L.4    Hummelshøj, T.5
  • 68
    • 0036147972 scopus 로고    scopus 로고
    • The S128R polymorphism of E-selectin mediates neuraminidase-resistant tethering of myeloid cells under shear flow
    • Rao RM, Clarke JL, Ortlepp S, Robinson MK, Landis RC, &, Haskard DO, (2002) The S128R polymorphism of E-selectin mediates neuraminidase-resistant tethering of myeloid cells under shear flow. Eur J Immunol 32, 251-260.
    • (2002) Eur J Immunol , vol.32 , pp. 251-260
    • Rao, R.M.1    Clarke, J.L.2    Ortlepp, S.3    Robinson, M.K.4    Landis, R.C.5    Haskard, D.O.6
  • 71
    • 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, 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
  • 73
    • 84979964089 scopus 로고    scopus 로고
    • T cells modulate glycans on CD43 and CD45 during development and activation, signal regulation, and survival
    • Clark MC, &, Baum LG, (2012) T cells modulate glycans on CD43 and CD45 during development and activation, signal regulation, and survival. Ann N Y Acad Sci 1253, 58-67.
    • (2012) Ann N y Acad Sci , vol.1253 , pp. 58-67
    • Clark, M.C.1    Baum, L.G.2
  • 74
    • 33749363387 scopus 로고    scopus 로고
    • Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death
    • Cabrera PV, Amano M, Mitoma J, Chan J, Said J, Fukuda M, &, Baum LG, (2006) Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death. Blood 108, 2399-2406.
    • (2006) Blood , vol.108 , pp. 2399-2406
    • Cabrera, P.V.1    Amano, M.2    Mitoma, J.3    Chan, J.4    Said, J.5    Fukuda, M.6    Baum, L.G.7
  • 76
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • In (Harding S.E. Rowe A.J. & Horton J.C. eds), Royal Society of Chemistry, Cambridge, UK.
    • Laue TM, Shah BD, Ridgeway TM, &, Pelletier SL, (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science (, Harding SE, Rowe AJ, &, Horton JC, eds), pp. 90-125. Royal Society of Chemistry, Cambridge, UK.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 77
    • 33745854191 scopus 로고    scopus 로고
    • Zinc ions induce the unfolding and self-association of boar spermadhesin PSP-I, a protein with a single CUB domain architecture, and promote its binding to heparin
    • Campanero-Rhodes MA, Menéndez M, Sáiz JL, Sanz L, Calvete JJ, &, Solís D, (2006) Zinc ions induce the unfolding and self-association of boar spermadhesin PSP-I, a protein with a single CUB domain architecture, and promote its binding to heparin. Biochemistry 45, 8227-8235.
    • (2006) Biochemistry , vol.45 , pp. 8227-8235
    • Campanero-Rhodes, M.A.1    Menéndez, M.2    Sáiz, J.L.3    Sanz, L.4    Calvete, J.J.5    Solís, D.6
  • 79
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4.
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D50, 760-763.
    • (1994) Acta Crystallogr , vol.50 D , pp. 760-763
  • 80
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • Kantardjieff KA, &, Rupp B, (2003) Matthews coefficient probabilities: improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals. Protein Sci 12, 1865-1871.
    • (2003) Protein Sci , vol.12 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 82
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, &, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D62, 439-450.
    • (2006) Acta Crystallogr , vol.62 D , pp. 439-450
    • Painter, J.1    Merritt, E.A.2


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