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Volumn 421, Issue 2, 2009, Pages 211-221

The carbohydrate-binding domain on galectin-1 is more extensive for a complex glycan than for simple saccharides: Implications for galectin-glycan interactions at the cell surface

Author keywords

Carbohydrate binding domain; Cell surface; Galectin glycan interactions; Heteronuclear single quantum coherence nuclear magnetic resonance (HSQC NMR); NMR diffusion spectroscopy; Simple saccharide

Indexed keywords

CELL SURFACE; GALECTIN-GLYCAN INTERACTIONS; HETERONUCLEAR SINGLE QUANTUM COHERENCE NUCLEAR MAGNETIC RESONANCE (HSQC NMR); NMR DIFFUSION SPECTROSCOPY; SIMPLE SACCHARIDE;

EID: 67650866515     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090265     Document Type: Article
Times cited : (53)

References (52)
  • 2
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu, F. T. and Rabinovich, G. A. (2005) Galectins as modulators of tumour progression. Nat. Rev. Cancer 5, 29-41
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 3
    • 27744552971 scopus 로고    scopus 로고
    • Gal-1 interacts with the α5β1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27
    • Fischer, C., Sanchez-Ruderisch, H., Welzel, M., et al. (2005) Gal-1 interacts with the α5β1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27. J. Biol. Chem. 280, 37266-37277
    • (2005) J. Biol. Chem , vol.280 , pp. 37266-37277
    • Fischer, C.1    Sanchez-Ruderisch, H.2    Welzel, M.3
  • 4
    • 68749105767 scopus 로고    scopus 로고
    • Nesmelova, I. V., Dings, R. P. M. and Mayo, K. H. (2008) Understanding galectin structure-function relationship to design effective antagonists. In Galectins (Klyosov, A. A., Witczak, Z. J. and Platt, D., eds), pp. 33-69, John Wiley and Sons, New York
    • Nesmelova, I. V., Dings, R. P. M. and Mayo, K. H. (2008) Understanding galectin structure-function relationship to design effective antagonists. In Galectins (Klyosov, A. A., Witczak, Z. J. and Platt, D., eds), pp. 33-69, John Wiley and Sons, New York
  • 5
    • 84859510271 scopus 로고    scopus 로고
    • Klyosov, A. A. (2008) Galectins and their functions in plain language. In Galectins (Klyosov, A. A., Witczak, Z. J. and Platt, D., eds), pp. 9-31, John Wiley and Sons, New York
    • Klyosov, A. A. (2008) Galectins and their functions in plain language. In Galectins (Klyosov, A. A., Witczak, Z. J. and Platt, D., eds), pp. 9-31, John Wiley and Sons, New York
  • 6
    • 8844261143 scopus 로고    scopus 로고
    • Cell surface biology mediated by low affinity multivalent protein-glycan interactions
    • Collins, B. E. and Paulson, J. C. (2004) Cell surface biology mediated by low affinity multivalent protein-glycan interactions. Curr. Opin. Chem. Biol. 8, 617-625
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 617-625
    • Collins, B.E.1    Paulson, J.C.2
  • 7
    • 0035800186 scopus 로고    scopus 로고
    • Pectins: Structure, biosynthesis and oligogalacturonide-related signaling
    • Ridley, B. L., O'Neill, M. A. and Mohnen, D. (2001) Pectins: structure, biosynthesis and oligogalacturonide-related signaling. Phytochemistry 57, 929-967
    • (2001) Phytochemistry , vol.57 , pp. 929-967
    • Ridley, B.L.1    O'Neill, M.A.2    Mohnen, D.3
  • 8
    • 35548945407 scopus 로고    scopus 로고
    • Effect of polysaccharide structure on mechanical and thermal properties of galactomannan-based films
    • Mikkonen, K. S., Rita, H., Helen, H., Talja, R. A., Hyvoenen, L. and Tenkanen, M. (2007) Effect of polysaccharide structure on mechanical and thermal properties of galactomannan-based films. Biomacromolecules 8, 3198-3205
    • (2007) Biomacromolecules , vol.8 , pp. 3198-3205
    • Mikkonen, K.S.1    Rita, H.2    Helen, H.3    Talja, R.A.4    Hyvoenen, L.5    Tenkanen, M.6
  • 9
    • 66249131691 scopus 로고    scopus 로고
    • Using pulse field gradient NMR diffusion measurements to define molecular weight distributions in glycan preparations
    • Miller, M., Klyosov, A., Platt, D. and Mayo, K. H. (2009) Using pulse field gradient NMR diffusion measurements to define molecular weight distributions in glycan preparations, Carbohydr. Res. 344, 1205-1212
    • (2009) Carbohydr. Res , vol.344 , pp. 1205-1212
    • Miller, M.1    Klyosov, A.2    Platt, D.3    Mayo, K.H.4
  • 10
    • 67650985359 scopus 로고    scopus 로고
    • Galactose-pronged polysaccharides in a formulation for antifibrotic therapies,
    • U.S. Pat. 20080107622 USPTO (United States Patent and Trademark Office) pending
    • Klyosov, A. and Platt, D. (2008) Galactose-pronged polysaccharides in a formulation for antifibrotic therapies, U.S. Pat. 20080107622 USPTO (United States Patent and Trademark Office) pending
    • (2008)
    • Klyosov, A.1    Platt, D.2
  • 11
    • 38649104444 scopus 로고    scopus 로고
    • Determination of galactose mannose residues in natural galactomannans using a fast and efficient high-performance liquid chromatography/UV detection
    • Tapie, N., Malhiac, C., Hucher, N. and Grisel, M. (2008) Determination of galactose mannose residues in natural galactomannans using a fast and efficient high-performance liquid chromatography/UV detection. J. Chromatogr. A 1181, 45-50
    • (2008) J. Chromatogr. A , vol.1181 , pp. 45-50
    • Tapie, N.1    Malhiac, C.2    Hucher, N.3    Grisel, M.4
  • 12
    • 0001900145 scopus 로고
    • Isolation and structural characterization of rhamnogalacturonan oligmers
    • Food Polysaccharides and their Applications Stephen, A.M, ed, pp, Marcel Dekker, New York
    • Voragen, A. G. J., Pilnik, W., Thibault, J. F., Axelos, M. A. and Renard, C. M. G. C. (1995) Isolation and structural characterization of rhamnogalacturonan oligmers. In Food Polysaccharides and their Applications (Stephen, A.M., ed), pp. 287-340, Food Science and Technology Series, Marcel Dekker, New York
    • (1995) Food Science and Technology Series , pp. 287-340
    • Voragen, A.G.J.1    Pilnik, W.2    Thibault, J.F.3    Axelos, M.A.4    Renard, C.M.G.C.5
  • 13
    • 34848848768 scopus 로고    scopus 로고
    • Inhibition of galectin-3 mediated cellular interactions by pectic polysaccharides from dietary sources
    • Sathisha, U. V., Jayaram, S., Nayaka, M. A. H. and Dharmesh, S. M. (2007) Inhibition of galectin-3 mediated cellular interactions by pectic polysaccharides from dietary sources. Glycoconj. J. 24, 497-507
    • (2007) Glycoconj. J , vol.24 , pp. 497-507
    • Sathisha, U.V.1    Jayaram, S.2    Nayaka, M.A.H.3    Dharmesh, S.M.4
  • 14
    • 0037132694 scopus 로고    scopus 로고
    • Inhibition of human cancer cell growth and metastasis in nude mice by oral intake of modified citrus pectin
    • Nangia-Makker, P., Hogan, V., Honjo, Y., Baccarini, S., Tait, L., Bresalier, R. and Raz, (2002) Inhibition of human cancer cell growth and metastasis in nude mice by oral intake of modified citrus pectin. J. Natl. Cancer Inst. 94, 1854-1862
    • (2002) J. Natl. Cancer Inst , vol.94 , pp. 1854-1862
    • Nangia-Makker, P.1    Hogan, V.2    Honjo, Y.3    Baccarini, S.4    Tait, L.5    Bresalier, R.6    Raz7
  • 16
    • 24944585018 scopus 로고    scopus 로고
    • A novel carbohydrate-based therapeutic GCS-100 overcomes bortezomib resistance and enhances dexamethasone-induced apoptosis in multiple myeloma cells
    • Chauhan, D., Li, G., Podar, K., Hideshima, T., Neri, P., He, D., Mitsiades, N., Richardson, P., Chang, Y., Schindler, J. et al. (2005) A novel carbohydrate-based therapeutic GCS-100 overcomes bortezomib resistance and enhances dexamethasone-induced apoptosis in multiple myeloma cells. Cancer Res. 65, 8350-8358
    • (2005) Cancer Res , vol.65 , pp. 8350-8358
    • Chauhan, D.1    Li, G.2    Podar, K.3    Hideshima, T.4    Neri, P.5    He, D.6    Mitsiades, N.7    Richardson, P.8    Chang, Y.9    Schindler, J.10
  • 17
    • 67651000964 scopus 로고    scopus 로고
    • 15N backbone and side-chain chemical shift assignments for the 29 kDa human gal-1 protein dimer
    • 15N backbone and side-chain chemical shift assignments for the 29 kDa human gal-1 protein dimer. Biol. NMR Assign. 2, 203-205
    • (2008) Biol. NMR Assign , vol.2 , pp. 203-205
    • Nesmelova, I.V.1    Pang, M.2    Baum, L.G.3    Mayo, K.H.4
  • 18
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 19
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. and Blevins, R. A. (1994) NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 20
    • 0029927321 scopus 로고    scopus 로고
    • A recipe for designing water-soluble, β-sheet-forming peptides
    • Mayo, K. H., Ilyina, E. and Park, H. (1996) A recipe for designing water-soluble, β-sheet-forming peptides. Protein Sci. 5, 1301-1315
    • (1996) Protein Sci , vol.5 , pp. 1301-1315
    • Mayo, K.H.1    Ilyina, E.2    Park, H.3
  • 21
    • 0030893784 scopus 로고    scopus 로고
    • A pulsed-gradient NMR study of bovine pancreatic trypsin inhibitor self-association
    • Ilyina, E., Roongta, V., Pan, H., Woodward, C. and Mayo, K. H. (1997) A pulsed-gradient NMR study of bovine pancreatic trypsin inhibitor self-association. Biochemistry 36, 3383-3388
    • (1997) Biochemistry , vol.36 , pp. 3383-3388
    • Ilyina, E.1    Roongta, V.2    Pan, H.3    Woodward, C.4    Mayo, K.H.5
  • 23
    • 2642605367 scopus 로고    scopus 로고
    • Demonstration of protein-protein interaction specificity by NMR chemical shift mapping
    • Rajagopal, P., Waygood, E. B., Reizer, J., Saier, M. H. and Klevit, R. E. (1997) Demonstration of protein-protein interaction specificity by NMR chemical shift mapping. Protein Sci. 6, 2624-2627
    • (1997) Protein Sci , vol.6 , pp. 2624-2627
    • Rajagopal, P.1    Waygood, E.B.2    Reizer, J.3    Saier, M.H.4    Klevit, R.E.5
  • 24
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human gal-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • Lopez-Lucendo, M. F., Solis, D., Andre, S., Hirabayashi, J., Kasai, K., Kaltner, H., Gabius H.-J. and Romero, A. (2004) Growth-regulatory human gal-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
    • Lopez-Lucendo, M.F.1    Solis, D.2    Andre, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6    Gabius, H.-J.7    Romero, A.8
  • 25
    • 0032574694 scopus 로고    scopus 로고
    • Thermodynamics of bovine spleen gal-1 binding to disaccharides: Correlation with structure and its effect on oligomerization at the denaturation temperature
    • Schwarz, F. P., Ahmed, H., Bianchet, M. A., Amzel, L. M. and Vasta, G. R. (1998) Thermodynamics of bovine spleen gal-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature. Biochemistry 37, 5867-5877
    • (1998) Biochemistry , vol.37 , pp. 5867-5877
    • Schwarz, F.P.1    Ahmed, H.2    Bianchet, M.A.3    Amzel, L.M.4    Vasta, G.R.5
  • 26
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharide-mediated cellular interactions
    • 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
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 27
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • Dam, T. K., Gabius, H.-J., andre, S., Kaltner, H., Lensch, M. and Brewer, C. F. (2005) Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry 44, 12564-12571
    • (2005) Biochemistry , vol.44 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    andre, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 28
    • 0036793242 scopus 로고    scopus 로고
    • Sweet 'n' sour: The impact of differential glycosylation on T cell responses
    • Daniels, M. A., Hogquist, K. A. and Jameson, S. C. (2002) Sweet 'n' sour: the impact of differential glycosylation on T cell responses. Nat. Immunol. 3, 903-910
    • (2002) Nat. Immunol , vol.3 , pp. 903-910
    • Daniels, M.A.1    Hogquist, K.A.2    Jameson, S.C.3
  • 29
    • 0033520448 scopus 로고    scopus 로고
    • Heparin dodecasaccharide binding to platelet factor-4 and growth-related protein-α. Induction of a partially folded state and implications for heparin-induced thrombocytopenia
    • Mikhailov, D., Young, H. C., Linhardt, R. J. and Mayo, K. H. (1999) Heparin dodecasaccharide binding to platelet factor-4 and growth-related protein-α. Induction of a partially folded state and implications for heparin-induced thrombocytopenia. J. Biol. Chem. 274, 25317-25329
    • (1999) J. Biol. Chem , vol.274 , pp. 25317-25329
    • Mikhailov, D.1    Young, H.C.2    Linhardt, R.J.3    Mayo, K.H.4
  • 33
    • 35948955219 scopus 로고    scopus 로고
    • Exploring the structural diversity of mammalian carbohydrates ("glycospace") by statistical databank analysis
    • Werz, D. B., Ranzinger, R., Herget, S., Adibekian, A, von der Lieth, C.-W. and Seeberger, P. H. (2007) Exploring the structural diversity of mammalian carbohydrates ("glycospace") by statistical databank analysis. Chem. Biol. 2, 685-691
    • (2007) Chem. Biol , vol.2 , pp. 685-691
    • Werz, D.B.1    Ranzinger, R.2    Herget, S.3    Adibekian, A.4    von der Lieth, C.-W.5    Seeberger, P.H.6
  • 35
    • 0032491184 scopus 로고    scopus 로고
    • Leonidas, D. D.. Vatzaki, E. H., Vorum, H., Cells, J. E., Madsen, P. and Acharya, K. R. (1998) Structural basis for the recognition of carbohydrates by human galectin-7, Biochemistry 37, 13930-13940
    • Leonidas, D. D.. Vatzaki, E. H., Vorum, H., Cells, J. E., Madsen, P. and Acharya, K. R. (1998) Structural basis for the recognition of carbohydrates by human galectin-7, Biochemistry 37, 13930-13940
  • 36
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebr β-galactoside-binding protein
    • Liao, D. I., Kapadia, G., Ahmed, H., Vasta, G. R. and Herzberg, O. (1994) Structure of S-lectin, a developmentally regulated vertebr β-galactoside-binding protein Proc. Natl. Acad. Sci. U.S.A. 91, 1428-1432
    • (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
  • 37
    • 33845987092 scopus 로고    scopus 로고
    • Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohygrate recognition
    • Nagae, M., Nishi, N., Murata, T., Usui, T., Nakamura, T., Wakatsuki, S, and Kato, R. (2006) Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohygrate recognition. J. Biol. Chem. 281, 35884-35893
    • (2006) J. Biol. Chem , vol.281 , pp. 35884-35893
    • Nagae, M.1    Nishi, N.2    Murata, T.3    Usui, T.4    Nakamura, T.5    Wakatsuki, S.6    Kato, R.7
  • 39
    • 0034680688 scopus 로고    scopus 로고
    • (2,000) an the galactosyl distribution of commercial galactomannans
    • Daas, P. J. H., Schols, H, A. and de Jongh, H. H. J. (2,000) an the galactosyl distribution of commercial galactomannans. Carbohydr. Res. 329, 609-619
    • Carbohydr. Res , vol.329 , pp. 609-619
    • Daas, P.J.H.1    Schols, H.A.2    de Jongh, H.H.J.3
  • 40
    • 42949152852 scopus 로고    scopus 로고
    • Noncovalent cell surface engineering: Incorporation of bioactive synthetic glycopolymers into cellular membranes
    • Rabuka, D., Forstner. M. B., Groves. J. T. and Bertczzi, C. R. (2008) Noncovalent cell surface engineering: incorporation of bioactive synthetic glycopolymers into cellular membranes. J. Am. Chem, Soc. 130, 5947-5953
    • (2008) J. Am. Chem, Soc , vol.130 , pp. 5947-5953
    • Rabuka, D.1    Forstner, M.B.2    Groves, J.T.3    Bertczzi, C.R.4
  • 41
    • 34247863732 scopus 로고    scopus 로고
    • Hierarchical assembly of model cell surfaces: Synthesis of mucin mimetic polymers and their display on supported bilayers
    • Rabuka, D., Parthasarathy, R., Lee, G. S., Chen, X., Groves, J. T. and Bertozzi, C. R. (2007) Hierarchical assembly of model cell surfaces: synthesis of mucin mimetic polymers and their display on supported bilayers. J. Am. Chem. Soc. 129, 5462-5471
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5462-5471
    • Rabuka, D.1    Parthasarathy, R.2    Lee, G.S.3    Chen, X.4    Groves, J.T.5    Bertozzi, C.R.6
  • 43
    • 0033215424 scopus 로고    scopus 로고
    • Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by gal-1
    • Pace, K. E., Lee, C., Stewart, L. G. and Baum, L. G. (1999) Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by gal-1. J. Immunol. 153, 3801-3811
    • (1999) J. Immunol , vol.153 , pp. 3801-3811
    • Pace, K.E.1    Lee, C.2    Stewart, L.G.3    Baum, L.G.4
  • 44
    • 33344475311 scopus 로고    scopus 로고
    • Carbohydrate-induced modulation of cell membrane. VIII. Agglutination with mammalian lectin gal-1 increases osmofragility and membrane fluidity of trypsinized erythrocytes
    • Gupta, R. K., Pande, A. H., Gulla, K. C., Gabius, H.-J. and Hajela, K. (2006) Carbohydrate-induced modulation of cell membrane. VIII. Agglutination with mammalian lectin gal-1 increases osmofragility and membrane fluidity of trypsinized erythrocytes. FEBS Lett. 580, 1691-1695
    • (2006) FEBS Lett , vol.580 , pp. 1691-1695
    • Gupta, R.K.1    Pande, A.H.2    Gulla, K.C.3    Gabius, H.-J.4    Hajela, K.5
  • 45
    • 35548974811 scopus 로고    scopus 로고
    • Paradigms for glycan-binding receptors in cell adhesion
    • Taylor, M. E. and Drickamer, K. (2007) Paradigms for glycan-binding receptors in cell adhesion. Curr. Opin. Cell Biol. 19, 572-577
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 572-577
    • Taylor, M.E.1    Drickamer, K.2
  • 46
    • 33847718338 scopus 로고    scopus 로고
    • Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer
    • 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
    • (2007) J. Biol. Chem , vol.282 , pp. 1374-1383
    • Nieminen, J.1    Kuno, A.2    Hirabayashi, J.3    Sato, S.4
  • 47
    • 0034292424 scopus 로고    scopus 로고
    • Gal-1 induces partial TCR ζ-chain phosphoryation and antagonizes processive TCR signal transduction
    • Chung, C. D., Patel, V. P., Moran, M., Lewis, L. A. and Miceli, M. C. (2000) Gal-1 induces partial TCR ζ-chain phosphoryation and antagonizes processive TCR signal transduction. J. Immunol. 165, 3722-3729
    • (2000) J. Immunol , vol.165 , pp. 3722-3729
    • Chung, C.D.1    Patel, V.P.2    Moran, M.3    Lewis, L.A.4    Miceli, M.C.5
  • 48
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • 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
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 50
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • 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
    • (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
  • 51
    • 0037844879 scopus 로고    scopus 로고
    • Microvillar membrane microdomains exist at physiological temperature. Role of galectin-4 as lipid raft stabilizer revealed by "superrafts
    • Braccia, A., Villani, M., Immerdal, L., Niels-Christiansen, L. L., Nystrøm, 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
    • (2003) J. Biol. Chem , vol.278 , pp. 15679-15684
    • Braccia, A.1    Villani, M.2    Immerdal, L.3    Niels-Christiansen, L.L.4    Nystrøm, B.T.5    Hansen, G.H.6    Danielsen, E.M.7
  • 52
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • 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
    • (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


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