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Volumn 469, Issue 1, 2015, Pages 1-16

Assembly, organization and regulation of cell-surface receptors by lectin-glycan complexes

Author keywords

CD45; Galectins; Glycan receptors; N and O glycosylation; Surface retention; VEGFR2

Indexed keywords

CELL SURFACE RECEPTOR; GALECTIN; GLYCAN; LECTIN; GALECTIN 3; GALECTIN 4; OLIGOSACCHARIDE;

EID: 84936774693     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150461     Document Type: Review
Times cited : (70)

References (140)
  • 2
    • 45449112374 scopus 로고    scopus 로고
    • Galectins: Structure, function and therapeutic potential
    • CrossRef PubMed
    • Yang, R.Y., Rabinovich, G.A. and Liu, F.T. (2008) Galectins: structure, function and therapeutic potential. Expert Rev. Mol. Med. 10, e17 CrossRef PubMed
    • (2008) Expert Rev. Mol. Med. , vol.10 , pp. e17
    • Yang, R.Y.1    Rabinovich, G.A.2    Liu, F.T.3
  • 3
    • 0036587663 scopus 로고    scopus 로고
    • Unlocking the secrets of galectins: A challenge at the frontier of glyco-immunology
    • PubMed
    • Rabinovich, G.A, Rubinstein, N. and Fainboim, L. (2002) Unlocking the secrets of galectins: a challenge at the frontier of glyco-immunology. J. Leukoc. Biol. 71, 741-752 PubMed
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 741-752
    • Rabinovich, G.A.1    Rubinstein, N.2    Fainboim, L.3
  • 4
    • 45549107987 scopus 로고    scopus 로고
    • Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways
    • CrossRef PubMed
    • Bi, S., Earl, L.A., Jacobs, L. and Baum, L.G. (2008) Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways. J. Biol. Chem. 283, 12248-12258 CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 12248-12258
    • Bi, S.1    Earl, L.A.2    Jacobs, L.3    Baum, L.G.4
  • 5
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein
    • CrossRef PubMed
    • Liao, D.I., Kapadia, G., Ahmed, H., Vasta, G.R. and Herzberg, O. (1994) Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein. Proc. Natl. Acad. Sci. U.S.A. 91, 1428-1432 CrossRef PubMed
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 6
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain
    • CrossRef PubMed
    • Stowell, S.R., Arthur, C.M., Slanina, K.A., Horton, J.R., Smith, D.F. and Cummings, R.D. (2008) Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain. J. Biol. Chem. 283, 20547-20559 CrossRef PubMed
    • (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
  • 7
    • 33947233260 scopus 로고    scopus 로고
    • Carbohydrate-recognition domains of galectin-9 are involved in intermolecular interaction with galectin-9 itself and other members of the galectin family
    • CrossRef PubMed
    • Miyanishi, N., Nishi, N., Abe, H., Kashio, Y., Shinonaga, R., Nakakita, S., Sumiyoshi, W., Yamauchi, A., Nakamura, T., Hirashima, M. et al. (2007) Carbohydrate-recognition domains of galectin-9 are involved in intermolecular interaction with galectin-9 itself and other members of the galectin family. Glycobiology 17, 423-432 CrossRef PubMed
    • (2007) Glycobiology , vol.17 , pp. 423-432
    • Miyanishi, N.1    Nishi, N.2    Abe, H.3    Kashio, Y.4    Shinonaga, R.5    Nakakita, S.6    Sumiyoshi, W.7    Yamauchi, A.8    Nakamura, T.9    Hirashima, M.10
  • 8
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • CrossRef PubMed
    • Hughes, R.C. (1999) Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim. Biophys. Acta 1473, 172-185 CrossRef PubMed
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 9
    • 1042289748 scopus 로고    scopus 로고
    • Presentation of galectin-1 by extracellular matrix triggers T cell death
    • CrossRef PubMed
    • He, J. and Baum, L.G. (2004) Presentation of galectin-1 by extracellular matrix triggers T cell death. J. Biol. Chem. 279, 4705-4712 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 4705-4712
    • He, J.1    Baum, L.G.2
  • 10
    • 0037844879 scopus 로고    scopus 로고
    • Microvillar membrane microdomains exist at physiological temperature: Role of galectin-4 as lipid raft stabilizer revealed by "superrafts"
    • CrossRef PubMed
    • Braccia, A., Villani, M., Immerdal, L., Niels-Christiansen, L.L., Nystrom, B.T., Hansen, G.H. and Danielsen, E.M. (2003) Microvillar membrane microdomains exist at physiological temperature: role of galectin-4 as lipid raft stabilizer revealed by "superrafts". J. Biol. Chem. 278, 15679-15684 CrossRef PubMed
    • (2003) J. Biol. Chem. , vol.278 , pp. 15679-15684
    • Braccia, A.1    Villani, M.2    Immerdal, L.3    Niels-Christiansen, L.L.4    Nystrom, B.T.5    Hansen, G.H.6    Danielsen, E.M.7
  • 11
    • 84895928786 scopus 로고    scopus 로고
    • Galectin-3 interactions with glycosphingolipids
    • CrossRef PubMed
    • Collins, P.M., Bum-Erdene, K., Yu, X. and Blanchard, H. (2014) Galectin-3 interactions with glycosphingolipids. J. Mol. Biol. 426, 1439-1451 CrossRef PubMed
    • (2014) J. Mol. Biol. , vol.426 , pp. 1439-1451
    • Collins, P.M.1    Bum-Erdene, K.2    Yu, X.3    Blanchard, H.4
  • 14
    • 59949094349 scopus 로고    scopus 로고
    • Endogenous galectin-3 is localized in membrane lipid rafts and regulates migration of dendritic cells
    • CrossRef PubMed
    • Hsu, D.K., Chernyavsky, A.I., Chen, H.Y., Yu, L., Grando, S.A. and Liu, F.T. (2009) Endogenous galectin-3 is localized in membrane lipid rafts and regulates migration of dendritic cells. J. Invest. Dermatol. 129, 573-583 CrossRef PubMed
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 573-583
    • Hsu, D.K.1    Chernyavsky, A.I.2    Chen, H.Y.3    Yu, L.4    Grando, S.A.5    Liu, F.T.6
  • 15
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • CrossRef PubMed
    • Ideo, H., Seko, A., Ishizuka, I. and Yamashita, K. (2003) The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 13, 713-723 CrossRef PubMed
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 16
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds: Domain regulation of receptor signaling at the plasma membrane
    • CrossRef PubMed
    • Lajoie, P., Goetz, J.G., Dennis, J.W. and Nabi, I.R. (2009) Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane. J. Cell Biol. 185, 381-385 CrossRef PubMed
    • (2009) J. Cell Biol. , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 17
    • 78049312395 scopus 로고    scopus 로고
    • Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells
    • CrossRef PubMed
    • Mishra, R., Grzybek, M., Niki, T., Hirashima, M. and Simons, K. (2010) Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells. Proc. Natl. Acad. Sci. U.S.A. 107, 17633-17638 CrossRef PubMed
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17633-17638
    • Mishra, R.1    Grzybek, M.2    Niki, T.3    Hirashima, M.4    Simons, K.5
  • 19
    • 38549106613 scopus 로고    scopus 로고
    • Interaction of galectin-9 with lipid rafts induces osteoblast proliferation through the c-Src/ERK signaling pathway
    • CrossRef PubMed
    • Tanikawa, R., Tanikawa, T., Okada, Y., Nakano, K., Hirashima, M., Yamauchi, A., Hosokawa, R. and Tanaka, Y. (2008) Interaction of galectin-9 with lipid rafts induces osteoblast proliferation through the c-Src/ERK signaling pathway. J. Bone Miner. Res. 23, 278-286 CrossRef PubMed
    • (2008) J. Bone Miner. Res. , vol.23 , pp. 278-286
    • Tanikawa, R.1    Tanikawa, T.2    Okada, Y.3    Nakano, K.4    Hirashima, M.5    Yamauchi, A.6    Hosokawa, R.7    Tanaka, Y.8
  • 20
    • 0027954503 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the soluble 14 kDa β-galactoside-binding lectin from bovine heart
    • CrossRef PubMed
    • Bourne, Y., Bolgiano, B., Nesa, M.P., Penfold, P., Johnson, D., Feizi, T. and Cambillau, C. (1994) Crystallization and preliminary X-ray diffraction studies of the soluble 14 kDa β-galactoside-binding lectin from bovine heart. J. Mol. Biol. 235, 787-789 CrossRef PubMed
    • (1994) J. Mol. Biol. , vol.235 , pp. 787-789
    • Bourne, Y.1    Bolgiano, B.2    Nesa, M.P.3    Penfold, P.4    Johnson, D.5    Feizi, T.6    Cambillau, C.7
  • 21
    • 14044272136 scopus 로고    scopus 로고
    • Dimeric galectin-1 binds with high affinity to α2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans
    • CrossRef PubMed
    • Leppanen, A., Stowell, S., Blixt, O. and Cummings, R.D. (2005) Dimeric galectin-1 binds with high affinity to α2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. J. Biol. Chem. 280, 5549-5562 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 5549-5562
    • Leppanen, A.1    Stowell, S.2    Blixt, O.3    Cummings, R.D.4
  • 22
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-Å resolution
    • PubMed
    • Lobsanov, Y.D., Gitt, M.A., Leffler, H., Barondes, S.H. and Rini, J.M. (1993) X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-Å resolution. J. Biol. Chem. 268, 27034-27038 PubMed
    • (1993) J. Biol. Chem. , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3    Barondes, S.H.4    Rini, J.M.5
  • 23
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • CrossRef PubMed
    • Ahmad, N., Gabius, H.J., Andre, S., Kaltner, H., Sabesan, S., Roy, R., Liu, B., Macaluso, F. and Brewer, C.F. (2004) Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J. Biol. Chem. 279, 10841-10847 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.J.2    Andre, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.7    Macaluso, F.8    Brewer, C.F.9
  • 25
    • 33847718338 scopus 로고    scopus 로고
    • Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer
    • CrossRef PubMed
    • Nieminen, J., Kuno, A., Hirabayashi, J. and Sato, S. (2007) Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer. J. Biol. Chem. 282, 1374-1383 CrossRef PubMed
    • (2007) J. Biol. Chem. , vol.282 , pp. 1374-1383
    • Nieminen, J.1    Kuno, A.2    Hirabayashi, J.3    Sato, S.4
  • 26
    • 79960720473 scopus 로고    scopus 로고
    • Glycosylation, galectins and cellular signaling
    • CrossRef PubMed
    • Boscher, C., Dennis, J.W. and Nabi, I.R. (2011) Glycosylation, galectins and cellular signaling. Curr. Opin. Cell Biol. 23, 383-392 CrossRef PubMed
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 383-392
    • Boscher, C.1    Dennis, J.W.2    Nabi, I.R.3
  • 27
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharide-mediated cellular interactions
    • CrossRef PubMed
    • Brewer, C.F., Miceli, M.C. and Baum, L.G. (2002) Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr. Opin. Struct. Biol. 12, 616-623 CrossRef PubMed
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 29
    • 0028359877 scopus 로고
    • Homogeneous aggregation of the 14-kDa β-galactoside specific vertebrate lectin complex with asialofetuin in mixed systems
    • CrossRef PubMed
    • Gupta, D. and Brewer, C.F. (1994) Homogeneous aggregation of the 14-kDa β-galactoside specific vertebrate lectin complex with asialofetuin in mixed systems. Biochemistry 33, 5526-5530 CrossRef PubMed
    • (1994) Biochemistry , vol.33 , pp. 5526-5530
    • Gupta, D.1    Brewer, C.F.2
  • 30
    • 0031528585 scopus 로고    scopus 로고
    • Cross-linking activities of galectins and other multivalent lectins
    • CrossRef
    • Brewer, C.F. (1997) Cross-linking activities of galectins and other multivalent lectins. Trends Glycosci. Glycotechnol. 9, 155-165 CrossRef
    • (1997) Trends Glycosci. Glycotechnol. , vol.9 , pp. 155-165
    • Brewer, C.F.1
  • 31
    • 84876004025 scopus 로고    scopus 로고
    • Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications
    • CrossRef PubMed
    • Dennis, J.W. and Brewer, C.F. (2013) Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications. Mol. Cell. Proteomics 12, 913-920 CrossRef PubMed
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 913-920
    • Dennis, J.W.1    Brewer, C.F.2
  • 32
    • 53049084874 scopus 로고    scopus 로고
    • N-Glycans in cancer progression
    • CrossRef PubMed
    • Lau, K.S. and Dennis, J.W. (2008) N-Glycans in cancer progression. Glycobiology 18, 750-760 CrossRef PubMed
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 33
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins; he made so many of them
    • CrossRef PubMed
    • Cooper, D.N. and Barondes, S.H. (1999) God must love galectins; he made so many of them. Glycobiology 9, 979-984 CrossRef PubMed
    • (1999) Glycobiology , vol.9 , pp. 979-984
    • Cooper, D.N.1    Barondes, S.H.2
  • 35
    • 84941137578 scopus 로고    scopus 로고
    • Golgi N-glycan branching N-acetylglucosaminyltransferases I, V and VI promote nutrient uptake and metabolism
    • CrossRef PubMed
    • Abdel Rahman, A.M., Ryczko, M., Nakano, M., Pawling, J., Rodrigues, T., Johswich, A., Taniguchi, N. and Dennis, J.W. (2015) Golgi N-glycan branching N-acetylglucosaminyltransferases I, V and VI promote nutrient uptake and metabolism. Glycobiology 25, 225-240 CrossRef PubMed
    • (2015) Glycobiology , vol.25 , pp. 225-240
    • Abdel Rahman, A.M.1    Ryczko, M.2    Nakano, M.3    Pawling, J.4    Rodrigues, T.5    Johswich, A.6    Taniguchi, N.7    Dennis, J.W.8
  • 36
    • 0036233290 scopus 로고    scopus 로고
    • UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: Regulation based on the kinetic properties of N-acetylglucosaminyltransferase V
    • CrossRef PubMed
    • Sasai, K., Ikeda, Y., Fujii, T., Tsuda, T. and Taniguchi, N. (2002) UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V. Glycobiology 12, 119-127 CrossRef PubMed
    • (2002) Glycobiology , vol.12 , pp. 119-127
    • Sasai, K.1    Ikeda, Y.2    Fujii, T.3    Tsuda, T.4    Taniguchi, N.5
  • 37
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • CrossRef PubMed
    • Schachter, H. (1986) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem. Cell Biol. 64, 163-181 CrossRef PubMed
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 163-181
    • Schachter, H.1
  • 38
    • 0020356007 scopus 로고
    • A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc:α-D-mannoside β1,6 N-acetylglucosaminyltransferase
    • PubMed
    • Cummings, R.D., Trowbridge, I.S. and Kornfeld, S. (1982) A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc:α-D-mannoside β1,6 N-acetylglucosaminyltransferase. J. Biol. Chem. 257, 13421-13427 PubMed
    • (1982) J. Biol. Chem. , vol.257 , pp. 13421-13427
    • Cummings, R.D.1    Trowbridge, I.S.2    Kornfeld, S.3
  • 39
    • 0021227742 scopus 로고
    • The distribution of repeating [Galβ1,4GlcNAcβ1,3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines BW5147 and PHAR 2.1
    • PubMed
    • Cummings, R.D. and Kornfeld, S. (1984) The distribution of repeating [Galβ1,4GlcNAcβ1,3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines BW5147 and PHAR 2.1. J. Biol. Chem. 259, 6253-6260 PubMed
    • (1984) J. Biol. Chem. , vol.259 , pp. 6253-6260
    • Cummings, R.D.1    Kornfeld, S.2
  • 40
    • 19944419437 scopus 로고    scopus 로고
    • A novel β1,3-N-acetylglucosaminyltransferase (β3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer
    • CrossRef PubMed
    • Ishida, H., Togayachi, A., Sakai, T., Iwai, T., Hiruma, T., Sato, T., Okubo, R., Inaba, N., Kudo, T., Gotoh, M. et al. (2005) A novel β1,3-N-acetylglucosaminyltransferase (β3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer. FEBS Lett. 579, 71-78 CrossRef PubMed
    • (2005) FEBS Lett. , vol.579 , pp. 71-78
    • Ishida, H.1    Togayachi, A.2    Sakai, T.3    Iwai, T.4    Hiruma, T.5    Sato, T.6    Okubo, R.7    Inaba, N.8    Kudo, T.9    Gotoh, M.10
  • 41
    • 33751006121 scopus 로고    scopus 로고
    • Comprehensive enzymatic characterization of glycosyltransferases with a β3GT or β4GT motif
    • CrossRef PubMed
    • Togayachi, A., Sato, T. and Narimatsu, H. (2006) Comprehensive enzymatic characterization of glycosyltransferases with a β3GT or β4GT motif. Methods Enzymol. 416, 91-102 CrossRef PubMed
    • (2006) Methods Enzymol. , vol.416 , pp. 91-102
    • Togayachi, A.1    Sato, T.2    Narimatsu, H.3
  • 42
    • 0023255440 scopus 로고
    • β1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • CrossRef PubMed
    • Dennis, J.W., Laferte, S., Waghorne, C., Breitman, M.L. and Kerbel, R.S. (1987) β1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science 236, 582-585 CrossRef PubMed
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.W.1    Laferte, S.2    Waghorne, C.3    Breitman, M.L.4    Kerbel, R.S.5
  • 43
    • 0034061923 scopus 로고    scopus 로고
    • Suppression of tumor growth and metastasis in Mgat5-deficient mice
    • CrossRef PubMed
    • Granovsky, M., Fata, J., Pawling, J., Muller, W.J., Khokha, R. and Dennis, J.W. (2000) Suppression of tumor growth and metastasis in Mgat5-deficient mice. Nat. Med. 6, 306-312 CrossRef PubMed
    • (2000) Nat. Med. , vol.6 , pp. 306-312
    • Granovsky, M.1    Fata, J.2    Pawling, J.3    Muller, W.J.4    Khokha, R.5    Dennis, J.W.6
  • 44
    • 0030754637 scopus 로고    scopus 로고
    • Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene
    • CrossRef PubMed
    • Buckhaults, P., Chen, L., Fregien, N. and Pierce, M. (1997) Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene. J. Biol. Chem. 272, 19575-19581 CrossRef PubMed
    • (1997) J. Biol. Chem. , vol.272 , pp. 19575-19581
    • Buckhaults, P.1    Chen, L.2    Fregien, N.3    Pierce, M.4
  • 45
    • 0033566771 scopus 로고    scopus 로고
    • Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: A possible enzymatic basis of the formation of abnormal biantennary sugar chain
    • PubMed
    • Takamatsu, S., Oguri, S., Minowa, M.T., Yoshida, A., Nakamura, K., Takeuchi, M. and Kobata, A. (1999) Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain. Cancer Res. 59, 3949-3953 PubMed
    • (1999) Cancer Res. , vol.59 , pp. 3949-3953
    • Takamatsu, S.1    Oguri, S.2    Minowa, M.T.3    Yoshida, A.4    Nakamura, K.5    Takeuchi, M.6    Kobata, A.7
  • 46
    • 0024815933 scopus 로고
    • The biosynthesis of branched O-glycans
    • PubMed
    • Schachter, H. and Brockhausen, I. (1989) The biosynthesis of branched O-glycans. Symp. Soc. Exp. Biol. 43, 1-26 PubMed
    • (1989) Symp. Soc. Exp. Biol. , vol.43 , pp. 1-26
    • Schachter, H.1    Brockhausen, I.2
  • 47
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core 1 β1,3-galactosyltransferase
    • CrossRef PubMed
    • Ju, T., Brewer, K., D'Souza, A., Cummings, R.D. and Canfield, W.M. (2002) Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277, 178-186 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 178-186
    • Ju, T.1    Brewer, K.2    D'Souza, A.3    Cummings, R.D.4    Canfield, W.M.5
  • 48
    • 0034646696 scopus 로고    scopus 로고
    • Control of O-glycan branch formation: Molecular cloning and characterization of a novel thymus-associated core 2 β1,6-N-acetylglucosaminyltransferase
    • CrossRef PubMed
    • Schwientek, T., Yeh, J.C., Levery, S.B., Keck, B., Merkx, G., van Kessel, A.G., Fukuda, M. and Clausen, H. (2000) Control of O-glycan branch formation: molecular cloning and characterization of a novel thymus-associated core 2 β1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 275, 11106-11113 CrossRef PubMed
    • (2000) J. Biol. Chem. , vol.275 , pp. 11106-11113
    • Schwientek, T.1    Yeh, J.C.2    Levery, S.B.3    Keck, B.4    Merkx, G.5    Van Kessel, A.G.6    Fukuda, M.7    Clausen, H.8
  • 49
    • 0033582478 scopus 로고    scopus 로고
    • Control of O-glycan branch formation: Molecular cloning of human cDNA encoding a novel β1,6-N-acetylglucosaminyltransferase forming core 2 and core 4
    • CrossRef PubMed
    • Schwientek, T., Nomoto, M., Levery, S.B., Merkx, G., van Kessel, A.G., Bennett, E.P., Hollingsworth, M.A. and Clausen, H. (1999) Control of O-glycan branch formation: molecular cloning of human cDNA encoding a novel β1,6-N-acetylglucosaminyltransferase forming core 2 and core 4. J. Biol. Chem. 274, 4504-4512 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 4504-4512
    • Schwientek, T.1    Nomoto, M.2    Levery, S.B.3    Merkx, G.4    Van Kessel, A.G.5    Bennett, E.P.6    Hollingsworth, M.A.7    Clausen, H.8
  • 50
    • 0038446674 scopus 로고    scopus 로고
    • A novel I-branching β-1,6-N-acetylglucosaminyltransferase involved in human blood group I antigen expression
    • CrossRef PubMed
    • Inaba, N., Hiruma, T., Togayachi, A., Iwasaki, H., Wang, X.H., Furukawa, Y., Sumi, R., Kudo, T., Fujimura, K., Iwai, T. et al. (2003) A novel I-branching β-1,6-N-acetylglucosaminyltransferase involved in human blood group I antigen expression. Blood 101, 2870-2876 CrossRef PubMed
    • (2003) Blood , vol.101 , pp. 2870-2876
    • Inaba, N.1    Hiruma, T.2    Togayachi, A.3    Iwasaki, H.4    Wang, X.H.5    Furukawa, Y.6    Sumi, R.7    Kudo, T.8    Fujimura, K.9    Iwai, T.10
  • 51
    • 0033515687 scopus 로고    scopus 로고
    • Regulation of I-branched poly-N-acetyllactosamine synthesis: Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I
    • CrossRef PubMed
    • Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O., Clausen, H., Fukuda, M.N. and Fukuda, M. (1999) Regulation of I-branched poly-N-acetyllactosamine synthesis: concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274, 9296-9304 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 9296-9304
    • Ujita, M.1    McAuliffe, J.2    Suzuki, M.3    Hindsgaul, O.4    Clausen, H.5    Fukuda, M.N.6    Fukuda, M.7
  • 53
    • 84858766894 scopus 로고    scopus 로고
    • Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer
    • CrossRef PubMed
    • Rabinovich, G.A. and Croci, D.O. (2012) Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer. Immunity 36, 322-335 CrossRef PubMed
    • (2012) Immunity , vol.36 , pp. 322-335
    • Rabinovich, G.A.1    Croci, D.O.2
  • 54
    • 84858790272 scopus 로고    scopus 로고
    • Galectin-1 triggers an immunoregulatory signature in Th cells functionally defined by IL-10 expression
    • CrossRef PubMed
    • Cedeno-Laurent, F., Opperman, M., Barthel, S.R., Kuchroo, V.K. and Dimitroff, C.J. (2012) Galectin-1 triggers an immunoregulatory signature in Th cells functionally defined by IL-10 expression. J. Immunol. 188, 3127-3137 CrossRef PubMed
    • (2012) J. Immunol. , vol.188 , pp. 3127-3137
    • Cedeno-Laurent, F.1    Opperman, M.2    Barthel, S.R.3    Kuchroo, V.K.4    Dimitroff, C.J.5
  • 55
    • 46949103440 scopus 로고    scopus 로고
    • Differential roles of galectin-1 and galectin-3 in regulating leukocyte viability and cytokine secretion
    • CrossRef PubMed
    • Stowell, S.R., Qian, Y., Karmakar, S., Koyama, N.S., Dias-Baruffi, M., Leffler, H., McEver, R.P. and Cummings, R.D. (2008) Differential roles of galectin-1 and galectin-3 in regulating leukocyte viability and cytokine secretion. J. Immunol. 180, 3091-3102 CrossRef PubMed
    • (2008) J. Immunol. , vol.180 , pp. 3091-3102
    • Stowell, S.R.1    Qian, Y.2    Karmakar, S.3    Koyama, N.S.4    Dias-Baruffi, M.5    Leffler, H.6    McEver, R.P.7    Cummings, R.D.8
  • 57
    • 40449120636 scopus 로고    scopus 로고
    • Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking
    • CrossRef PubMed
    • Norling, L.V., Sampaio, A.L., Cooper, D. and Perretti, M. (2008) Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. FASEB J. 22, 682-690 CrossRef PubMed
    • (2008) FASEB J. , vol.22 , pp. 682-690
    • Norling, L.V.1    Sampaio, A.L.2    Cooper, D.3    Perretti, M.4
  • 58
    • 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
    • CrossRef PubMed
    • Barrionuevo, P., Beigier-Bompadre, M., Ilarregui, J.M., Toscano, M.A., Bianco, G.A., Isturiz, M.A. and Rabinovich, G.A. (2007) 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. 178, 436-445 CrossRef PubMed
    • (2007) J. Immunol. , vol.178 , pp. 436-445
    • Barrionuevo, P.1    Beigier-Bompadre, M.2    Ilarregui, J.M.3    Toscano, M.A.4    Bianco, G.A.5    Isturiz, M.A.6    Rabinovich, G.A.7
  • 59
    • 0037320747 scopus 로고    scopus 로고
    • Opposite effects of galectin-1 on alternative metabolic pathways of L-arginine in resident, inflammatory, and activated macrophages
    • CrossRef PubMed
    • Correa, S.G., Sotomayor, C.E., Aoki, M.P., Maldonado, C.A. and Rabinovich, G.A. (2003) Opposite effects of galectin-1 on alternative metabolic pathways of L-arginine in resident, inflammatory, and activated macrophages. Glycobiology 13, 119-128 CrossRef PubMed
    • (2003) Glycobiology , vol.13 , pp. 119-128
    • Correa, S.G.1    Sotomayor, C.E.2    Aoki, M.P.3    Maldonado, C.A.4    Rabinovich, G.A.5
  • 60
    • 69049116053 scopus 로고    scopus 로고
    • Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1-driven immunoregulatory circuit involving interleukin 27 and interleukin 10
    • CrossRef PubMed
    • Ilarregui, J.M., Croci, D.O., Bianco, G.A., Toscano, M.A., Salatino, M., Vermeulen, M.E., Geffner, J.R. and Rabinovich, G.A. (2009) Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1-driven immunoregulatory circuit involving interleukin 27 and interleukin 10. Nat. Immunol. 10, 981-991 CrossRef PubMed
    • (2009) Nat. Immunol. , vol.10 , pp. 981-991
    • Ilarregui, J.M.1    Croci, D.O.2    Bianco, G.A.3    Toscano, M.A.4    Salatino, M.5    Vermeulen, M.E.6    Geffner, J.R.7    Rabinovich, G.A.8
  • 61
    • 33646491737 scopus 로고    scopus 로고
    • Galectin-1 suppresses autoimmune retinal disease by promoting concomitant Th2- and T regulatory-mediated anti-inflammatory responses
    • CrossRef PubMed
    • Toscano, M.A., Commodaro, A.G., Ilarregui, J.M., Bianco, G.A., Liberman, A., Serra, H.M., Hirabayashi, J., Rizzo, L.V. and Rabinovich, G.A. (2006) Galectin-1 suppresses autoimmune retinal disease by promoting concomitant Th2- and T regulatory-mediated anti-inflammatory responses. J. Immunol. 176, 6323-6332 CrossRef PubMed
    • (2006) J. Immunol. , vol.176 , pp. 6323-6332
    • Toscano, M.A.1    Commodaro, A.G.2    Ilarregui, J.M.3    Bianco, G.A.4    Liberman, A.5    Serra, H.M.6    Hirabayashi, J.7    Rizzo, L.V.8    Rabinovich, G.A.9
  • 62
    • 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
    • CrossRef PubMed
    • Andre, S., Kaltner, H., Lensch, M., Russwurm, R., Siebert, H.C., Fallsehr, C., Tajkhorshid, E., Heck, A.J., 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 CrossRef PubMed
    • (2005) Int. J. Cancer , vol.114 , pp. 46-57
    • Andre, S.1    Kaltner, H.2    Lensch, M.3    Russwurm, R.4    Siebert, H.C.5    Fallsehr, C.6    Tajkhorshid, E.7    Heck, A.J.8    Von Knebel Doeberitz, M.9    Gabius, H.J.10
  • 63
    • 0242412283 scopus 로고    scopus 로고
    • Modulation of O-glycans and N-glycans on murine CD8 T cells fails to alter annexin V ligand induction by galectin 1
    • CrossRef PubMed
    • Carlow, D.A., Williams, M.J. and Ziltener, H.J. (2003) Modulation of O-glycans and N-glycans on murine CD8 T cells fails to alter annexin V ligand induction by galectin 1. J. Immunol. 171, 5100-5106 CrossRef PubMed
    • (2003) J. Immunol. , vol.171 , pp. 5100-5106
    • Carlow, D.A.1    Williams, M.J.2    Ziltener, H.J.3
  • 64
    • 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
    • CrossRef PubMed
    • Kopitz, J., von Reitzenstein, C., Burchert, M., Cantz, M. and 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 CrossRef PubMed
    • (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
  • 65
    • 0035889895 scopus 로고    scopus 로고
    • CD45 modulates galectin-1-induced T cell death: Regulation by expression of core 2 O-glycans
    • CrossRef PubMed
    • Nguyen, J.T., Evans, D.P., Galvan, M., Pace, K.E., Leitenberg, D., Bui, T.N. and Baum, L.G. (2001) CD45 modulates galectin-1-induced T cell death: regulation by expression of core 2 O-glycans. J. Immunol. 167, 5697-5707 CrossRef PubMed
    • (2001) J. Immunol. , vol.167 , pp. 5697-5707
    • Nguyen, J.T.1    Evans, D.P.2    Galvan, M.3    Pace, K.E.4    Leitenberg, D.5    Bui, T.N.6    Baum, L.G.7
  • 66
    • 0033215424 scopus 로고    scopus 로고
    • Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1
    • PubMed
    • Pace, K.E., Lee, C., Stewart, P.L. and Baum, L.G. (1999) Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1. J. Immunol. 163, 3801-3811 PubMed
    • (1999) J. Immunol. , vol.163 , pp. 3801-3811
    • Pace, K.E.1    Lee, C.2    Stewart, P.L.3    Baum, L.G.4
  • 67
    • 0030940913 scopus 로고    scopus 로고
    • Galectin-1, an endogenous lectin produced by thymic epithelial cells, induces apoptosis of human thymocytes
    • CrossRef PubMed
    • Perillo, N.L., Uittenbogaart, C.H., Nguyen, J.T. and Baum, L.G. (1997) Galectin-1, an endogenous lectin produced by thymic epithelial cells, induces apoptosis of human thymocytes. J. Exp. Med. 185, 1851-1858 CrossRef PubMed
    • (1997) J. Exp. Med. , vol.185 , pp. 1851-1858
    • Perillo, N.L.1    Uittenbogaart, C.H.2    Nguyen, J.T.3    Baum, L.G.4
  • 68
    • 33751359796 scopus 로고    scopus 로고
    • Effects of N-glycan processing inhibitors on signaling events and induction of apoptosis in galectin-1-stimulated Jurkat T lymphocytes
    • CrossRef PubMed
    • Walzel, H., Fahmi, A.A., Eldesouky, M.A., Abou-Eladab, E.F., Waitz, G., Brock, J. and Tiedge, M. (2006) Effects of N-glycan processing inhibitors on signaling events and induction of apoptosis in galectin-1-stimulated Jurkat T lymphocytes. Glycobiology 16, 1262-1271 CrossRef PubMed
    • (2006) Glycobiology , vol.16 , pp. 1262-1271
    • Walzel, H.1    Fahmi, A.A.2    Eldesouky, M.A.3    Abou-Eladab, E.F.4    Waitz, G.5    Brock, J.6    Tiedge, M.7
  • 69
    • 0036798862 scopus 로고    scopus 로고
    • Ah, sweet mystery of death! Galectins and control of cell fate
    • CrossRef PubMed
    • Hernandez, J.D. and Baum, L.G. (2002) Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 12, 127R-136R CrossRef PubMed
    • (2002) Glycobiology , vol.12 , pp. 127R-136R
    • Hernandez, J.D.1    Baum, L.G.2
  • 71
    • 0034267915 scopus 로고    scopus 로고
    • CD7 delivers a pro-apoptotic signal during galectin-1-induced T cell death
    • CrossRef PubMed
    • Pace, K.E., Hahn, H.P., Pang, M., Nguyen, J.T. and Baum, L.G. (2000) CD7 delivers a pro-apoptotic signal during galectin-1-induced T cell death. J. Immunol. 165, 2331-2334 CrossRef PubMed
    • (2000) J. Immunol. , vol.165 , pp. 2331-2334
    • Pace, K.E.1    Hahn, H.P.2    Pang, M.3    Nguyen, J.T.4    Baum, L.G.5
  • 72
    • 33749514807 scopus 로고    scopus 로고
    • Galectin-1 binds different CD43 glycoforms to cluster CD43 and regulate T cell death
    • CrossRef PubMed
    • Hernandez, J.D., Nguyen, J.T., He, J., Wang, W., Ardman, B., Green, J.M., Fukuda, M. and Baum, L.G. (2006) Galectin-1 binds different CD43 glycoforms to cluster CD43 and regulate T cell death. J. Immunol. 177, 5328-5336 CrossRef PubMed
    • (2006) J. Immunol. , vol.177 , pp. 5328-5336
    • Hernandez, J.D.1    Nguyen, J.T.2    He, J.3    Wang, W.4    Ardman, B.5    Green, J.M.6    Fukuda, M.7    Baum, L.G.8
  • 73
    • 0029589620 scopus 로고
    • Apoptosis of T cells mediated by galectin-1
    • CrossRef PubMed
    • Perillo, N.L., Pace, K.E., Seilhamer, J.J. and Baum, L.G. (1995) Apoptosis of T cells mediated by galectin-1. Nature 378, 736-739 CrossRef PubMed
    • (1995) Nature , vol.378 , pp. 736-739
    • Perillo, N.L.1    Pace, K.E.2    Seilhamer, J.J.3    Baum, L.G.4
  • 74
    • 53249142239 scopus 로고    scopus 로고
    • CD45 glycosylation controls T-cell life and death
    • CrossRef PubMed
    • Earl, L.A. and Baum, L.G. (2008) CD45 glycosylation controls T-cell life and death. Immunol. Cell Biol. 86, 608-615 CrossRef PubMed
    • (2008) Immunol. Cell Biol. , vol.86 , pp. 608-615
    • Earl, L.A.1    Baum, L.G.2
  • 75
    • 0024327898 scopus 로고
    • The leukocyte common antigen family
    • CrossRef PubMed
    • Thomas, M.L. (1989) The leukocyte common antigen family. Annu. Rev. Immunol. 7, 339-369 CrossRef PubMed
    • (1989) Annu. Rev. Immunol. , vol.7 , pp. 339-369
    • Thomas, M.L.1
  • 77
    • 77449124815 scopus 로고    scopus 로고
    • N-andO-glycans modulate galectin-1 binding, CD45 signaling, and T cell death
    • CrossRef PubMed
    • Earl, L.A., Bi, S. and Baum, L.G. (2010) N-andO-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. J. Biol. Chem. 285, 2232-2244 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 2232-2244
    • Earl, L.A.1    Bi, S.2    Baum, L.G.3
  • 79
    • 33646857224 scopus 로고    scopus 로고
    • Endothelial cell expression of galectin-1 induced by prostate cancer cells inhibits T-cell transendothelial migration
    • PubMed
    • He, J. and Baum, L.G. (2006) Endothelial cell expression of galectin-1 induced by prostate cancer cells inhibits T-cell transendothelial migration. Lab. Invest. 86, 578-590 PubMed
    • (2006) Lab. Invest. , vol.86 , pp. 578-590
    • He, J.1    Baum, L.G.2
  • 80
    • 0030939803 scopus 로고    scopus 로고
    • ICAMs redistributed by chemokines to cellular uropods as a mechanism for recruitment of T lymphocytes
    • CrossRef PubMed
    • del Pozo, M.A., Cabanas, C., Montoya, M.C., Ager, A., Sanchez-Mateos, P. and Sanchez-Madrid, F. (1997) ICAMs redistributed by chemokines to cellular uropods as a mechanism for recruitment of T lymphocytes. J. Cell Biol. 137, 493-508 CrossRef PubMed
    • (1997) J. Cell Biol. , vol.137 , pp. 493-508
    • Del Pozo, M.A.1    Cabanas, C.2    Montoya, M.C.3    Ager, A.4    Sanchez-Mateos, P.5    Sanchez-Madrid, F.6
  • 83
    • 30744445427 scopus 로고    scopus 로고
    • Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death
    • CrossRef PubMed
    • Stillman, B.N., Hsu, D.K., Pang, M., Brewer, C.F., Johnson, P., Liu, F.T. and Baum, L.G. (2006) Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death. J. Immunol. 176, 778-789 CrossRef PubMed
    • (2006) J. Immunol. , vol.176 , pp. 778-789
    • Stillman, B.N.1    Hsu, D.K.2    Pang, M.3    Brewer, C.F.4    Johnson, P.5    Liu, F.T.6    Baum, L.G.7
  • 84
    • 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
    • CrossRef PubMed
    • Bi, S., Hong, P.W., Lee, B. and Baum, L.G. (2011) Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc. Natl. Acad. Sci. U.S.A. 108, 10650-10655 CrossRef PubMed
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10650-10655
    • Bi, S.1    Hong, P.W.2    Lee, B.3    Baum, L.G.4
  • 85
    • 77956919583 scopus 로고    scopus 로고
    • Ero1α is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of αIIbβ3
    • CrossRef PubMed
    • Swiatkowska, M., Padula, G., Michalec, L., Stasiak, M., Skurzynski, S. and Cierniewski, C.S. (2010) Ero1α is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of αIIbβ3. J. Biol. Chem. 285, 29874-29883 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 29874-29883
    • Swiatkowska, M.1    Padula, G.2    Michalec, L.3    Stasiak, M.4    Skurzynski, S.5    Cierniewski, C.S.6
  • 86
    • 0022537869 scopus 로고
    • Glycosylation of the T-cell antigen-specific receptor and its potential role in lectin-mediated cytotoxicity
    • CrossRef PubMed
    • Hubbard, S.C., Kranz, D.M., Longmore, G.D., Sitkovsky, M.V. and Eisen, H.N. (1986) Glycosylation of the T-cell antigen-specific receptor and its potential role in lectin-mediated cytotoxicity. Proc. Natl. Acad. Sci. U.S.A. 83, 1852-1856 CrossRef PubMed
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 1852-1856
    • Hubbard, S.C.1    Kranz, D.M.2    Longmore, G.D.3    Sitkovsky, M.V.4    Eisen, H.N.5
  • 87
    • 0032472057 scopus 로고    scopus 로고
    • Atomic structure of an αβ T cell receptor (TCR) heterodimer in complex with an anti-TCR Fab fragment derived from a mitogenic antibody
    • CrossRef PubMed
    • Wang, J., Lim, K., Smolyar, A., Teng, M., Liu, J., Tse, A.G., Liu, J., Hussey, R.E., Chishti, Y., Thomson, C.T. et al. (1998) Atomic structure of an αβ T cell receptor (TCR) heterodimer in complex with an anti-TCR Fab fragment derived from a mitogenic antibody. EMBO J. 17, 10-26 CrossRef PubMed
    • (1998) EMBO J. , vol.17 , pp. 10-26
    • Wang, J.1    Lim, K.2    Smolyar, A.3    Teng, M.4    Liu, J.5    Tse, A.G.6    Liu, J.7    Hussey, R.E.8    Chishti, Y.9    Thomson, C.T.10
  • 88
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • CrossRef PubMed
    • Demetriou, M., Granovsky, M., Quaggin, S. and Dennis, J.W. (2001) Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature 409, 733-739 CrossRef PubMed
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 89
    • 36849040950 scopus 로고    scopus 로고
    • Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling
    • CrossRef PubMed
    • Chen, I.J., Chen, H.L. and Demetriou, M. (2007) Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling. J. Biol. Chem. 282, 35361-35372 CrossRef PubMed
    • (2007) J. Biol. Chem. , vol.282 , pp. 35361-35372
    • Chen, I.J.1    Chen, H.L.2    Demetriou, M.3
  • 90
    • 0027136155 scopus 로고
    • Structural study of the sugar chains of human leukocyte common antigen CD45
    • CrossRef PubMed
    • Sato, T., Furukawa, K., Autero, M., Gahmberg, C.G. and Kobata, A. (1993) Structural study of the sugar chains of human leukocyte common antigen CD45. Biochemistry 32, 12694-12704 CrossRef PubMed
    • (1993) Biochemistry , vol.32 , pp. 12694-12704
    • Sato, T.1    Furukawa, K.2    Autero, M.3    Gahmberg, C.G.4    Kobata, A.5
  • 91
    • 84892165063 scopus 로고    scopus 로고
    • T cell antigen receptor activation and actin cytoskeleton remodeling
    • CrossRef PubMed
    • Kumari, S., Curado, S., Mayya, V. and Dustin, M.L. (2013) T cell antigen receptor activation and actin cytoskeleton remodeling. Biochim. Biophys. Acta 1838, 546-556 CrossRef PubMed
    • (2013) Biochim. Biophys. Acta , vol.1838 , pp. 546-556
    • Kumari, S.1    Curado, S.2    Mayya, V.3    Dustin, M.L.4
  • 92
    • 0036754181 scopus 로고    scopus 로고
    • The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production
    • CrossRef PubMed
    • Pradhan, D. and Morrow, J. (2002) The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production. Immunity 17, 303-315 CrossRef PubMed
    • (2002) Immunity , vol.17 , pp. 303-315
    • Pradhan, D.1    Morrow, J.2
  • 93
    • 84885339434 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein: Dynamic regulation of actin homeostasis: From activation through function and signal termination in T lymphocytes
    • CrossRef PubMed
    • Matalon, O., Reicher, B. and Barda-Saad, M. (2013) Wiskott-Aldrich syndrome protein: dynamic regulation of actin homeostasis: from activation through function and signal termination in T lymphocytes. Immunol. Rev. 256, 10-29 CrossRef PubMed
    • (2013) Immunol. Rev. , vol.256 , pp. 10-29
    • Matalon, O.1    Reicher, B.2    Barda-Saad, M.3
  • 94
    • 84877990371 scopus 로고    scopus 로고
    • Nck adapter proteins: Functional versatility in T cells
    • CrossRef PubMed
    • Lettau, M., Pieper, J. and Janssen, O. (2009) Nck adapter proteins: functional versatility in T cells. Cell Commun. Signal. 7, 1CrossRef PubMed
    • (2009) Cell Commun. Signal. , vol.7 , pp. 1
    • Lettau, M.1    Pieper, J.2    Janssen, O.3
  • 95
    • 33846224785 scopus 로고    scopus 로고
    • Full activation of the T cell receptor requires both clustering and conformational changes at CD3
    • CrossRef PubMed
    • Minguet, S., Swamy, M., Alarcon, B., Luescher, I.F. and Schamel, W.W. (2007) Full activation of the T cell receptor requires both clustering and conformational changes at CD3. Immunity 26, 43-54 CrossRef PubMed
    • (2007) Immunity , vol.26 , pp. 43-54
    • Minguet, S.1    Swamy, M.2    Alarcon, B.3    Luescher, I.F.4    Schamel, W.W.5
  • 96
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • CrossRef PubMed
    • Lau, K.S., Partridge, E.A., Grigorian, A., Silvescu, C.I., Reinhold, V.N., Demetriou, M. and Dennis, J.W. (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123-134 CrossRef PubMed
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 98
    • 0036790940 scopus 로고    scopus 로고
    • Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering
    • CrossRef PubMed
    • Gauthier, L., Rossi, B., Roux, F., Termine, E. and Schiff, C. (2002) Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering. Proc. Natl. Acad. Sci. U.S.A. 99, 13014-13019 CrossRef PubMed
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13014-13019
    • Gauthier, L.1    Rossi, B.2    Roux, F.3    Termine, E.4    Schiff, C.5
  • 99
    • 21844445331 scopus 로고    scopus 로고
    • The pre-B-cell receptor: Selector of fitting immunoglobulin heavy chains for the B-cell repertoire
    • CrossRef PubMed
    • Melchers, F. (2005) The pre-B-cell receptor: selector of fitting immunoglobulin heavy chains for the B-cell repertoire. Nat. Rev. Immunol. 5, 578-584 CrossRef PubMed
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 578-584
    • Melchers, F.1
  • 100
    • 34247354176 scopus 로고    scopus 로고
    • Structural insight into pre-B cell receptor function
    • CrossRef PubMed
    • Bankovich, A.J., Raunser, S., Juo, Z.S., Walz, T., Davis, M.M. and Garcia, K.C. (2007) Structural insight into pre-B cell receptor function. Science 316, 291-294 CrossRef PubMed
    • (2007) Science , vol.316 , pp. 291-294
    • Bankovich, A.J.1    Raunser, S.2    Juo, Z.S.3    Walz, T.4    Davis, M.M.5    Garcia, K.C.6
  • 102
    • 84923863050 scopus 로고    scopus 로고
    • Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions
    • CrossRef PubMed
    • Bonzi, J., Bornet, O., Betzi, S., Kasper, B.T., Mahal, L.K., Mancini, S.J., Schiff, C., Sebban-Kreuzer, C., Guerlesquin, F. and Elantak, L. (2015) Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions. Nat. Commun. 6, 6194 CrossRef PubMed
    • (2015) Nat. Commun. , vol.6 , pp. 6194
    • Bonzi, J.1    Bornet, O.2    Betzi, S.3    Kasper, B.T.4    Mahal, L.K.5    Mancini, S.J.6    Schiff, C.7    Sebban-Kreuzer, C.8    Guerlesquin, F.9    Elantak, L.10
  • 103
    • 33745848466 scopus 로고    scopus 로고
    • Clustering of pre-B cell integrins induces galectin-1-dependent pre-B cell receptor relocalization and activation
    • CrossRef PubMed
    • Rossi, B., Espeli, M., Schiff, C. and Gauthier, L. (2006) Clustering of pre-B cell integrins induces galectin-1-dependent pre-B cell receptor relocalization and activation. J. Immunol. 177, 796-803 CrossRef PubMed
    • (2006) J. Immunol. , vol.177 , pp. 796-803
    • Rossi, B.1    Espeli, M.2    Schiff, C.3    Gauthier, L.4
  • 104
    • 70350371721 scopus 로고    scopus 로고
    • Galectin-1 co-clusters CD43/CD45 on dendritic cells and induces cell activation and migration through Syk and protein kinase C signaling
    • CrossRef PubMed
    • Fulcher, J.A., Chang, M.H., Wang, S., Almazan, T., Hashimi, S.T., Eriksson, A.U., Wen, X., Pang, M., Baum, L.G., Singh, R.R. et al. (2009) Galectin-1 co-clusters CD43/CD45 on dendritic cells and induces cell activation and migration through Syk and protein kinase C signaling. J. Biol. Chem. 284, 26860-26870 CrossRef PubMed
    • (2009) J. Biol. Chem. , vol.284 , pp. 26860-26870
    • Fulcher, J.A.1    Chang, M.H.2    Wang, S.3    Almazan, T.4    Hashimi, S.T.5    Eriksson, A.U.6    Wen, X.7    Pang, M.8    Baum, L.G.9    Singh, R.R.10
  • 105
    • 27644480032 scopus 로고    scopus 로고
    • Galectin-3 interacts with naive and primed neutrophils, inducing innate immune responses
    • PubMed
    • Nieminen, J., St-Pierre, C. and Sato, S. (2005) Galectin-3 interacts with naive and primed neutrophils, inducing innate immune responses. J. Leukoc. Biol. 78, 1127-1135 PubMed
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 1127-1135
    • Nieminen, J.1    St-Pierre, C.2    Sato, S.3
  • 108
    • 78651081983 scopus 로고    scopus 로고
    • Flipping the switches: CD40 and CD45 modulation of microglial activation states in HIV associated dementia (HAD)
    • CrossRef PubMed
    • Salemi, J., Obregon, D.F., Cobb, A., Reed, S., Sadic, E., Jin, J., Fernandez, F., Tan, J. and Giunta, B. (2011) Flipping the switches: CD40 and CD45 modulation of microglial activation states in HIV associated dementia (HAD). Mol. Neurodegener. 6, 3 CrossRef PubMed
    • (2011) Mol. Neurodegener. , vol.6 , pp. 3
    • Salemi, J.1    Obregon, D.F.2    Cobb, A.3    Reed, S.4    Sadic, E.5    Jin, J.6    Fernandez, F.7    Tan, J.8    Giunta, B.9
  • 109
    • 0033840101 scopus 로고    scopus 로고
    • Characterization of the carbohydrate chains of the secreted form of the human epidermal growth factor receptor
    • CrossRef PubMed
    • Stroop, C.J., Weber, W., Gerwig, G.J., Nimtz, M., Kamerling, J.P. and Vliegenthart, J.F. (2000) Characterization of the carbohydrate chains of the secreted form of the human epidermal growth factor receptor. Glycobiology 10, 901-917 CrossRef PubMed
    • (2000) Glycobiology , vol.10 , pp. 901-917
    • Stroop, C.J.1    Weber, W.2    Gerwig, G.J.3    Nimtz, M.4    Kamerling, J.P.5    Vliegenthart, J.F.6
  • 110
    • 84864345961 scopus 로고    scopus 로고
    • TGF-β sensitivity is determined by N-linked glycosylation of the type II TGF-β receptor
    • CrossRef PubMed
    • Kim, Y.W., Park, J., Lee, H.J., Lee, S.Y. and Kim, S.J. (2012) TGF-β sensitivity is determined by N-linked glycosylation of the type II TGF-β receptor. Biochem. J. 445, 403-411 CrossRef PubMed
    • (2012) Biochem. J. , vol.445 , pp. 403-411
    • Kim, Y.W.1    Park, J.2    Lee, H.J.3    Lee, S.Y.4    Kim, S.J.5
  • 111
    • 33645822097 scopus 로고    scopus 로고
    • Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells
    • CrossRef PubMed
    • Lagana, A., Goetz, J.G., Cheung, P., Raz, A., Dennis, J.W. and Nabi, I.R. (2006) Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Mol. Cell. Biol. 26, 3181-3193 CrossRef PubMed
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3181-3193
    • Lagana, A.1    Goetz, J.G.2    Cheung, P.3    Raz, A.4    Dennis, J.W.5    Nabi, I.R.6
  • 113
    • 84866551704 scopus 로고    scopus 로고
    • Galectin-3 protein regulates mobility of N-cadherin and GM1 ganglioside at cell-cell junctions of mammary carcinoma cells
    • CrossRef PubMed
    • Boscher, C., Zheng, Y.Z., Lakshminarayan, R., Johannes, L., Dennis, J.W., Foster, L.J. and Nabi, I.R. (2012) Galectin-3 protein regulates mobility of N-cadherin and GM1 ganglioside at cell-cell junctions of mammary carcinoma cells. J. Biol. Chem. 287, 32940-32952 CrossRef PubMed
    • (2012) J. Biol. Chem. , vol.287 , pp. 32940-32952
    • Boscher, C.1    Zheng, Y.Z.2    Lakshminarayan, R.3    Johannes, L.4    Dennis, J.W.5    Foster, L.J.6    Nabi, I.R.7
  • 114
    • 71749112448 scopus 로고    scopus 로고
    • Regulation of homotypic cell-cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains
    • CrossRef PubMed
    • Guo, H.B., Johnson, H., Randolph, M. and Pierce, M. (2009) Regulation of homotypic cell-cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains. J. Biol. Chem. 284, 34986-34997 CrossRef PubMed
    • (2009) J. Biol. Chem. , vol.284 , pp. 34986-34997
    • Guo, H.B.1    Johnson, H.2    Randolph, M.3    Pierce, M.4
  • 115
    • 0347993082 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways
    • CrossRef PubMed
    • Guo, H.B., Lee, I., Kamar, M. and Pierce, M. (2003) N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways. J. Biol. Chem. 278, 52412-52424 CrossRef PubMed
    • (2003) J. Biol. Chem. , vol.278 , pp. 52412-52424
    • Guo, H.B.1    Lee, I.2    Kamar, M.3    Pierce, M.4
  • 116
    • 41549127550 scopus 로고    scopus 로고
    • Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1
    • PubMed
    • Goetz, J.G., Joshi, B., Lajoie, P., Strugnell, S.S., Scudamore, T., Kojic, L.D. and Nabi, I.R. (2008) Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1. J. Cell Biol. 180, 1261-1275 PubMed
    • (2008) J. Cell Biol. , vol.180 , pp. 1261-1275
    • Goetz, J.G.1    Joshi, B.2    Lajoie, P.3    Strugnell, S.S.4    Scudamore, T.5    Kojic, L.D.6    Nabi, I.R.7
  • 117
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • CrossRef PubMed
    • Mitra, S.K. and Schlaepfer, D.D. (2006) Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18, 516-523 CrossRef PubMed
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 118
    • 66449123068 scopus 로고    scopus 로고
    • The Notch ligands Dll4 and Jagged1 have opposing effects on angiogenesis
    • CrossRef PubMed
    • Benedito, R., Roca, C., Sorensen, I., Adams, S., Gossler, A., Fruttiger, M. and Adams, R.H. (2009) The Notch ligands Dll4 and Jagged1 have opposing effects on angiogenesis. Cell 137, 1124-1135 CrossRef PubMed
    • (2009) Cell , vol.137 , pp. 1124-1135
    • Benedito, R.1    Roca, C.2    Sorensen, I.3    Adams, S.4    Gossler, A.5    Fruttiger, M.6    Adams, R.H.7
  • 119
    • 77949902267 scopus 로고    scopus 로고
    • α2,6-Sialic acid on platelet endothelial cell adhesion molecule (PECAM) regulates its homophilic interactions and downstream antiapoptotic signaling
    • CrossRef PubMed
    • Kitazume, S., Imamaki, R., Ogawa, K., Komi, Y., Futakawa, S., Kojima, S., Hashimoto, Y., Marth, J.D., Paulson, J.C. and Taniguchi, N. (2010) α2,6-Sialic acid on platelet endothelial cell adhesion molecule (PECAM) regulates its homophilic interactions and downstream antiapoptotic signaling. J. Biol. Chem. 285, 6515-6521 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 6515-6521
    • Kitazume, S.1    Imamaki, R.2    Ogawa, K.3    Komi, Y.4    Futakawa, S.5    Kojima, S.6    Hashimoto, Y.7    Marth, J.D.8    Paulson, J.C.9    Taniguchi, N.10
  • 121
    • 55849149808 scopus 로고    scopus 로고
    • Endothelial cell O-glycan deficiency causes blood/lymphatic misconnections and consequent fatty liver disease in mice
    • CrossRef PubMed
    • Fu, J., Gerhardt, H., McDaniel, J.M., Xia, B., Liu, X., Ivanciu, L., Ny, A., Hermans, K., Silasi-Mansat, R., McGee, S. et al. (2008) Endothelial cell O-glycan deficiency causes blood/lymphatic misconnections and consequent fatty liver disease in mice. J. Clin. Invest. 118, 3725-3737 CrossRef PubMed
    • (2008) J. Clin. Invest. , vol.118 , pp. 3725-3737
    • Fu, J.1    Gerhardt, H.2    McDaniel, J.M.3    Xia, B.4    Liu, X.5    Ivanciu, L.6    Ny, A.7    Hermans, K.8    Silasi-Mansat, R.9    McGee, S.10
  • 124
    • 45949085841 scopus 로고    scopus 로고
    • Galectin-1, a novel ligand of neuropilin-1, activates VEGFR-2 signaling and modulates the migration of vascular endothelial cells
    • CrossRef PubMed
    • Hsieh, S.H., Ying, N.W., Wu, M.H., Chiang, W.F., Hsu, C.L., Wong, T.Y., Jin, Y.T., Hong, T.M. and Chen, Y.L. (2008) Galectin-1, a novel ligand of neuropilin-1, activates VEGFR-2 signaling and modulates the migration of vascular endothelial cells. Oncogene 27, 3746-3753 CrossRef PubMed
    • (2008) Oncogene , vol.27 , pp. 3746-3753
    • Hsieh, S.H.1    Ying, N.W.2    Wu, M.H.3    Chiang, W.F.4    Hsu, C.L.5    Wong, T.Y.6    Jin, Y.T.7    Hong, T.M.8    Chen, Y.L.9
  • 125
    • 84879174123 scopus 로고    scopus 로고
    • VEGFR1 and VEGFR2 involvement in extracellular galectin-1- and galectin-3-induced angiogenesis
    • CrossRef PubMed
    • D'Haene, N., Sauvage, S., Maris, C., Adanja, I., Le Mercier, M., Decaestecker, C., Baum, L. and Salmon, I. (2013) VEGFR1 and VEGFR2 involvement in extracellular galectin-1- and galectin-3-induced angiogenesis. PLoS ONE 8, e67029 CrossRef PubMed
    • (2013) PLoS ONE , vol.8
    • D'Haene, N.1    Sauvage, S.2    Maris, C.3    Adanja, I.4    Le Mercier, M.5    Decaestecker, C.6    Baum, L.7    Salmon, I.8
  • 129
    • 84871983882 scopus 로고    scopus 로고
    • A unique galectin signature in human prostate cancer progression suggests galectin-1 as a key target for treatment of advanced disease
    • CrossRef PubMed
    • Laderach, D.J., Gentilini, L.D., Giribaldi, L., Delgado, V.C., Nugnes, L., Croci, D.O., Al Nakouzi, N., Sacca, P., Casas, G., Mazza, O. et al. (2013) A unique galectin signature in human prostate cancer progression suggests galectin-1 as a key target for treatment of advanced disease. Cancer Res. 73, 86-96 CrossRef PubMed
    • (2013) Cancer Res. , vol.73 , pp. 86-96
    • Laderach, D.J.1    Gentilini, L.D.2    Giribaldi, L.3    Delgado, V.C.4    Nugnes, L.5    Croci, D.O.6    Al Nakouzi, N.7    Sacca, P.8    Casas, G.9    Mazza, O.10
  • 131
    • 80051930613 scopus 로고    scopus 로고
    • Galectin-3 protein modulates cell surface expression and activation of vascular endothelial growth factor receptor 2 in human endothelial cells
    • CrossRef PubMed
    • Markowska, A.I., Jefferies, K.C. and Panjwani, N. (2011) Galectin-3 protein modulates cell surface expression and activation of vascular endothelial growth factor receptor 2 in human endothelial cells. J. Biol. Chem. 286, 29913-29921 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 29913-29921
    • Markowska, A.I.1    Jefferies, K.C.2    Panjwani, N.3
  • 132
    • 77956233662 scopus 로고    scopus 로고
    • Galectin-3 is an important mediator of VEGF- and bFGF-mediated angiogenic response
    • CrossRef PubMed
    • Markowska, A.I., Liu, F.T. and Panjwani, N. (2010) Galectin-3 is an important mediator of VEGF- and bFGF-mediated angiogenic response. J. Exp. Med. 207, 1981-1993 CrossRef PubMed
    • (2010) J. Exp. Med. , vol.207 , pp. 1981-1993
    • Markowska, A.I.1    Liu, F.T.2    Panjwani, N.3
  • 134
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • CrossRef PubMed
    • Ohtsubo, K., Takamatsu, S., Minowa, M.T., Yoshida, A., Takeuchi, M. and Marth, J.D. (2005) Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes. Cell 123, 1307-1321 CrossRef PubMed
    • (2005) Cell , vol.123 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6
  • 137
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • CrossRef PubMed
    • Sabharanjak, S., Sharma, P., Parton, R.G. and Mayor, S. (2002) GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. Dev. Cell 2, 411-423 CrossRef PubMed
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4


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