메뉴 건너뛰기




Volumn 8, Issue 2, 2009, Pages 232-244

Glycosylation specific for adhesion molecules in epidermis and its receptor revealed by glycoform-focused reverse genomics

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1,3 GALACTOSYLTRANSFERASE; BETA GALACTOSIDASE; CELL ADHESION MOLECULE; EPITOPE; GALECTIN 3; GLYCAN; OLIGOSACCHARIDE;

EID: 61649110718     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800145-MCP200     Document Type: Article
Times cited : (14)

References (53)
  • 1
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo, K., and Marth, J. D. (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126, 855-867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 2
    • 0042121374 scopus 로고    scopus 로고
    • Barrier function of the skin: "la raison d'être" of the epidermis
    • Madison, K. C. (2003) Barrier function of the skin: "la raison d'être" of the epidermis. J. Investig. Dermatol. 121, 231-241
    • (2003) J. Investig. Dermatol , vol.121 , pp. 231-241
    • Madison, K.C.1
  • 3
    • 0142025161 scopus 로고    scopus 로고
    • Carbohydrate expression and modification during keratinocyte differentiation in normal human and reconstructed epidermis
    • Mehul, B., Corre, C., Capon, C., Bernard, D., and Schmidt, R. (2003) Carbohydrate expression and modification during keratinocyte differentiation in normal human and reconstructed epidermis. Exp. Dermatol. 12, 537-545
    • (2003) Exp. Dermatol , vol.12 , pp. 537-545
    • Mehul, B.1    Corre, C.2    Capon, C.3    Bernard, D.4    Schmidt, R.5
  • 4
    • 0021331962 scopus 로고
    • Pattern of distribution of blood group antigens on human epidermal cells during maturation
    • Dabelsteen, E., Buschard, K., Hakomori, S.-i., and Young, W. W. (1984) Pattern of distribution of blood group antigens on human epidermal cells during maturation. J. Investig. Dermatol. 82, 13-17
    • (1984) J. Investig. Dermatol , vol.82 , pp. 13-17
    • Dabelsteen, E.1    Buschard, K.2    Hakomori, S.-I.3    Young, W.W.4
  • 7
    • 39449136167 scopus 로고    scopus 로고
    • A comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion
    • Furukawa, J.-i., Shinohara, Y., Kuramoto, H., Miura, Y., Shimaoka, H., Kurogochi, M., Nakano, M., and Nishimura, S.-I. (2008) A comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion. Anal. Chem., 80, 1094-1101
    • (2008) Anal. Chem , vol.80 , pp. 1094-1101
    • Furukawa, J.-I.1    Shinohara, Y.2    Kuramoto, H.3    Miura, Y.4    Shimaoka, H.5    Kurogochi, M.6    Nakano, M.7    Nishimura, S.-I.8
  • 9
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911-917
    • (1959) Can. J. Biochem. Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 11
    • 0028950435 scopus 로고
    • Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography
    • Nakagawa, H., Kawamura, Y., Kato, K., Shimada, I., Arata, Y., and Takahashi, N. (1995) Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography. Anal. Biochem. 226, 130-138
    • (1995) Anal. Biochem , vol.226 , pp. 130-138
    • Nakagawa, H.1    Kawamura, Y.2    Kato, K.3    Shimada, I.4    Arata, Y.5    Takahashi, N.6
  • 12
    • 0028957151 scopus 로고
    • Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides
    • Takahashi, N., Nakagawa, H., Fujikawa, K., Kawamura, Y., and Tomiya, N. (1995) Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides. Anal. Biochem. 226, 139-146
    • (1995) Anal. Biochem , vol.226 , pp. 139-146
    • Takahashi, N.1    Nakagawa, H.2    Fujikawa, K.3    Kawamura, Y.4    Tomiya, N.5
  • 13
    • 6044274617 scopus 로고    scopus 로고
    • Structural characterization of N-glycopeptides by matrix-dependent selective fragmentation of MALDI-TOF/TOF tandem mass spectrometry
    • Kurogochi, M., and Nishimura, S.-I. (2004) Structural characterization of N-glycopeptides by matrix-dependent selective fragmentation of MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 76, 6097-6101.
    • (2004) Anal. Chem , vol.76 , pp. 6097-6101
    • Kurogochi, M.1    Nishimura, S.-I.2
  • 14
    • 33751397971 scopus 로고    scopus 로고
    • Unusual N-glycan structures in alpha-mannosidase II/IIx double null embryos identified by a systematic glycomics approach based on two-dimensional LC mapping and matrix-dependent selective fragmentation method in MALDI-TOF/TOF mass spectrometry
    • Hato, M., Nakagawa, H., Kurogochi, M., Akama, T. O., Marth, J. D., Fukuda, M. N., and Nishimura, S. (2006) Unusual N-glycan structures in alpha-mannosidase II/IIx double null embryos identified by a systematic glycomics approach based on two-dimensional LC mapping and matrix-dependent selective fragmentation method in MALDI-TOF/TOF mass spectrometry. Mol. Cell. Proteomics 5, 2146-2157
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2146-2157
    • Hato, M.1    Nakagawa, H.2    Kurogochi, M.3    Akama, T.O.4    Marth, J.D.5    Fukuda, M.N.6    Nishimura, S.7
  • 15
    • 30744447493 scopus 로고    scopus 로고
    • Analysis of total N-glycans in cell membrane fractions of cancer cells using a combination of serotonin affinity chromatography and normal phase chromatography
    • Naka, R., Kamoda, S., Ishizuka, A., Kinoshita, M., and Kakehi, K. (2006) Analysis of total N-glycans in cell membrane fractions of cancer cells using a combination of serotonin affinity chromatography and normal phase chromatography. J. Proteome Res. 5, 88-97
    • (2006) J. Proteome Res , vol.5 , pp. 88-97
    • Naka, R.1    Kamoda, S.2    Ishizuka, A.3    Kinoshita, M.4    Kakehi, K.5
  • 16
    • 0030213338 scopus 로고    scopus 로고
    • Bifunctional labeling reagent for oligosaccharides to incorporate both chromophore and biotin groups
    • Shinohara, Y., Sota, H., Gotoh, M., Hasebe, M., Tosu, M., Nakao, J., Hasegawa, Y., and Shiga, M. (1996) Bifunctional labeling reagent for oligosaccharides to incorporate both chromophore and biotin groups. Anal. Chem. 68, 2573-2579
    • (1996) Anal. Chem , vol.68 , pp. 2573-2579
    • Shinohara, Y.1    Sota, H.2    Gotoh, M.3    Hasebe, M.4    Tosu, M.5    Nakao, J.6    Hasegawa, Y.7    Shiga, M.8
  • 17
    • 0033135747 scopus 로고    scopus 로고
    • Protein glycosylation in development and disease
    • Dennis, J. W., Granovsky, M., and Warren, C. E. (1999) Protein glycosylation in development and disease. BioEssays 21, 412-421
    • (1999) BioEssays , vol.21 , pp. 412-421
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 18
    • 0025809160 scopus 로고
    • Sugars protect desmosome and corneosome glycoproteins from proteolysis
    • Walsh, A., and Chapman, S. J. (1991) Sugars protect desmosome and corneosome glycoproteins from proteolysis". Arch. Dermatol. Res. 283, 174-179
    • (1991) Arch. Dermatol. Res , vol.283 , pp. 174-179
    • Walsh, A.1    Chapman, S.J.2
  • 19
    • 0020545948 scopus 로고
    • Alternations in membrane sugars during epidermal differentiation: Visualization with lectins and role of glycosidases
    • Nemanick, M. K., Whitehead, S. J., and Elias, P. M. (1983) Alternations in membrane sugars during epidermal differentiation: visualization with lectins and role of glycosidases. J. Histochem. Cytochem. 38, 887-897
    • (1983) J. Histochem. Cytochem , vol.38 , pp. 887-897
    • Nemanick, M.K.1    Whitehead, S.J.2    Elias, P.M.3
  • 20
    • 0016772320 scopus 로고
    • Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose
    • Ogata, S., Muramatsu, T., and Kobata, A. (1975) Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose. J. Biochem. 78, 687-696
    • (1975) J. Biochem , vol.78 , pp. 687-696
    • Ogata, S.1    Muramatsu, T.2    Kobata, A.3
  • 21
    • 33645215992 scopus 로고    scopus 로고
    • The desmosome: Cell science lessons from human diseases
    • Kottke, M. D., Delva, E., and Kowalczyk, A. P. (2006) The desmosome: cell science lessons from human diseases. J. Cell Sci. 119, 797-806
    • (2006) J. Cell Sci , vol.119 , pp. 797-806
    • Kottke, M.D.1    Delva, E.2    Kowalczyk, A.P.3
  • 22
    • 0028075997 scopus 로고
    • Junctional epidermolysis bullosis: Defects in expression of epiligrin/ nicein/kalinin and integrin β4 that inhibit hemidesmosome formation
    • Gil, S. G., Brown, T. A., Ryan, M. C., and Carter, W. G. (1994) Junctional epidermolysis bullosis: defects in expression of epiligrin/ nicein/kalinin and integrin β4 that inhibit hemidesmosome formation. J. Investig. Dermatol. 103, 31S-38S
    • (1994) J. Investig. Dermatol , vol.103
    • Gil, S.G.1    Brown, T.A.2    Ryan, M.C.3    Carter, W.G.4
  • 23
    • 0021184542 scopus 로고
    • Regulated expression of an introduced MHC H-2K bm1 gene in murine embryonal carcinoma cells
    • Rosenthal, A., Wright, S., Cedar, H., Flavell, R., and Grosveld, F. (1984) Regulated expression of an introduced MHC H-2K bm1 gene in murine embryonal carcinoma cells. Nature 310, 415-418
    • (1984) Nature , vol.310 , pp. 415-418
    • Rosenthal, A.1    Wright, S.2    Cedar, H.3    Flavell, R.4    Grosveld, F.5
  • 25
    • 0032520789 scopus 로고    scopus 로고
    • Direct binding of the MHC class I molecule H-2Ld to CD8: Interaction with the amino terminus of a mature cell surface protein
    • Jelonek, M. T., Classon, B. J., Hudson, P. J., and Margulies, D. H. (1998) Direct binding of the MHC class I molecule H-2Ld to CD8: interaction with the amino terminus of a mature cell surface protein. J. Immunol. 160, 2809-2814
    • (1998) J. Immunol , vol.160 , pp. 2809-2814
    • Jelonek, M.T.1    Classon, B.J.2    Hudson, P.J.3    Margulies, D.H.4
  • 26
    • 0023115557 scopus 로고
    • The relation between major histocompatibility complex (MHC) restriction and the capacity of la to bind immunogenic peptides
    • Buus, S., Sette, A., Colon, S. N., Miles, C., and Grey, H. M. (1987) The relation between major histocompatibility complex (MHC) restriction and the capacity of la to bind immunogenic peptides. Science 235, 1353-1358
    • (1987) Science , vol.235 , pp. 1353-1358
    • Buus, S.1    Sette, A.2    Colon, S.N.3    Miles, C.4    Grey, H.M.5
  • 27
    • 0036496075 scopus 로고    scopus 로고
    • AMOP, a protein module alternatively spliced in cancer cells
    • Ciccarelli, F. D., Doerks, T., and Bork, P. (2002) AMOP, a protein module alternatively spliced in cancer cells. Trends Biochem. Sci. 27, 113-115
    • (2002) Trends Biochem. Sci , vol.27 , pp. 113-115
    • Ciccarelli, F.D.1    Doerks, T.2    Bork, P.3
  • 29
    • 32044445822 scopus 로고    scopus 로고
    • The molecular basis for gala(1,3)gal expression in animals with a deletion of the α1,3 galactosyltransferase gene
    • Milland, J., Christiansen, D., Lazarus, B. D., Taylor, S. G., Xing, P. X., and Sandrin, M. S. (2006) The molecular basis for gala(1,3)gal expression in animals with a deletion of the α1,3 galactosyltransferase gene. J. Immunol. 176, 2448-2454
    • (2006) J. Immunol , vol.176 , pp. 2448-2454
    • Milland, J.1    Christiansen, D.2    Lazarus, B.D.3    Taylor, S.G.4    Xing, P.X.5    Sandrin, M.S.6
  • 30
    • 0038394491 scopus 로고    scopus 로고
    • Characterization of the rat α(1,3)galactosyltransferase: Evidence for two independent genes encoding glycosyltransferases that synthesize Gala(1,3)Gal by two separate glycosylation pathways
    • Taylor, S. G., McKenzie, I. F., and Sandrin, M. S. (2003) Characterization of the rat α(1,3)galactosyltransferase: evidence for two independent genes encoding glycosyltransferases that synthesize Gala(1,3)Gal by two separate glycosylation pathways. Glycobiology 13, 327-337
    • (2003) Glycobiology , vol.13 , pp. 327-337
    • Taylor, S.G.1    McKenzie, I.F.2    Sandrin, M.S.3
  • 31
    • 37549030141 scopus 로고    scopus 로고
    • Production and characterization of transgenic mice systemically expressing endo-β-galactosidase C
    • Watanabe, S., Misawa, M., Matsuzaki, T., Sakurai, T., Muramatsu, T., Yokomine, T. A., and Sato, M. (2008) Production and characterization of transgenic mice systemically expressing endo-β-galactosidase C. Glycobiology 18, 9-19
    • (2008) Glycobiology , vol.18 , pp. 9-19
    • Watanabe, S.1    Misawa, M.2    Matsuzaki, T.3    Sakurai, T.4    Muramatsu, T.5    Yokomine, T.A.6    Sato, M.7
  • 32
    • 37549039442 scopus 로고    scopus 로고
    • Accelerated proliferation and abnormal differentiation of epidermal keratinocytes in endo-β-galactosidase C transgenic mice
    • Misawa, M., Watanabe, S., Ihara, S., Muramatsu, T., and Matsuzaki, T. (2008) Accelerated proliferation and abnormal differentiation of epidermal keratinocytes in endo-β-galactosidase C transgenic mice. Glycobiology 18, 20-27
    • (2008) Glycobiology , vol.18 , pp. 20-27
    • Misawa, M.1    Watanabe, S.2    Ihara, S.3    Muramatsu, T.4    Matsuzaki, T.5
  • 34
    • 0343435291 scopus 로고
    • Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity
    • Bleil, J. D., and Wassarman, P. M. (1988) Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity. Proc. Natl. Acad. Sci. U. S. A. 85, 6778-6782
    • (1988) Proc. Natl. Acad. Sci. U. S. A , vol.85 , pp. 6778-6782
    • Bleil, J.D.1    Wassarman, P.M.2
  • 35
    • 0028902581 scopus 로고
    • Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro
    • Litscher, E. S., Juntunen, K., Seppo, A., Penttila, L., Niemela, R., Renkonen, O., and Wassarman, P. M. (1995) Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry 34, 4662-4669
    • (1995) Biochemistry , vol.34 , pp. 4662-4669
    • Litscher, E.S.1    Juntunen, K.2    Seppo, A.3    Penttila, L.4    Niemela, R.5    Renkonen, O.6    Wassarman, P.M.7
  • 36
    • 0035823508 scopus 로고    scopus 로고
    • Occurrence of oligosialic acids on integrin α5 subunit and their involvement in cell adhesion to fibronectin
    • Nadanaka, S., Sato, C., Kitajima, K., Katagiri, K., Irie, S., and Yamagata, T. (2001) Occurrence of oligosialic acids on integrin α5 subunit and their involvement in cell adhesion to fibronectin. J. Biol. Chem. 276, 33657-33664
    • (2001) J. Biol. Chem , vol.276 , pp. 33657-33664
    • Nadanaka, S.1    Sato, C.2    Kitajima, K.3    Katagiri, K.4    Irie, S.5    Yamagata, T.6
  • 37
    • 0028239080 scopus 로고
    • Functional role of N-gly-cosylation in α5β1 integrin receptor. De-N-glycosylation induces dissociation or altered association of α5 and β1 subunits and concomitant loss of fibronectin binding activity
    • Zheng, M., Fang, H., and Hakomori, S.-i. (1994) Functional role of N-gly-cosylation in α5β1 integrin receptor. De-N-glycosylation induces dissociation or altered association of α5 and β1 subunits and concomitant loss of fibronectin binding activity. J. Biol. Chem. 209, 12325-12331
    • (1994) J. Biol. Chem , vol.209 , pp. 12325-12331
    • Zheng, M.1    Fang, H.2    Hakomori, S.-I.3
  • 38
    • 0030994616 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lipopolysaccharide binds galectin-3 and other human corneal epithelial proteins
    • Gupta, S. K., Masinick, S., Garrett, M., and Hazlett, L. D. (1997) Pseudomonas aeruginosa lipopolysaccharide binds galectin-3 and other human corneal epithelial proteins. Infect. Immun. 65, 2747-2753
    • (1997) Infect. Immun , vol.65 , pp. 2747-2753
    • Gupta, S.K.1    Masinick, S.2    Garrett, M.3    Hazlett, L.D.4
  • 39
    • 0032534494 scopus 로고    scopus 로고
    • Galectin-3 stimulates cell proliferation
    • Inohara, H., Akahani, S., and Raz. A. (1998) Galectin-3 stimulates cell proliferation. Exp. Cell. Res. 245, 294-302
    • (1998) Exp. Cell. Res , vol.245 , pp. 294-302
    • Inohara, H.1    Akahani, S.2    Raz, A.3
  • 40
    • 0029900083 scopus 로고    scopus 로고
    • Expression of galectin-3 modulates T-cell growth and apoptosis
    • Yang, R. Y., Hsu, D. K., and Liu, F. T. (1996) Expression of galectin-3 modulates T-cell growth and apoptosis. Proc. Natl. Acad. Sci. U. S. A. 93, 6737-6742
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 6737-6742
    • Yang, R.Y.1    Hsu, D.K.2    Liu, F.T.3
  • 41
    • 0031903188 scopus 로고    scopus 로고
    • Galectin-7, a marker of all types of stratified epithelia
    • Magnaldo, T., Fowlis, D., and Darmon, M. (1998) Galectin-7, a marker of all types of stratified epithelia. Differentiation 63, 159-168
    • (1998) Differentiation , vol.63 , pp. 159-168
    • Magnaldo, T.1    Fowlis, D.2    Darmon, M.3
  • 42
    • 0033613211 scopus 로고    scopus 로고
    • Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes
    • Bernerd, F., Sarasin, A., and Magnaldo, T. (1999) Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes. Proc. Natl. Acad. Sci. U. S. A. 96, 11329-11334
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 11329-11334
    • Bernerd, F.1    Sarasin, A.2    Magnaldo, T.3
  • 44
    • 0030064740 scopus 로고    scopus 로고
    • Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide
    • Stubbs, H. J., Lih, J. J., Gustafson, T. L., and Rice, K. G. (1996) Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide. Biochemistry 35, 937-947
    • (1996) Biochemistry , vol.35 , pp. 937-947
    • Stubbs, H.J.1    Lih, J.J.2    Gustafson, T.L.3    Rice, K.G.4
  • 46
    • 0014318282 scopus 로고
    • Chemistry of lipid of the posthemyolytic residue or stroma of erythrocytes. XVI. Occurrence of ceramide pentasaccharide in the membrane of erythrocytes and reticulocytes of rabbit
    • Eto, T., Iichikawa, Y., Nishimura, K., Ando, S., and Yamakawa, T. (1968) Chemistry of lipid of the posthemyolytic residue or stroma of erythrocytes. XVI. Occurrence of ceramide pentasaccharide in the membrane of erythrocytes and reticulocytes of rabbit. J. Biochem. 64, 205-213
    • (1968) J. Biochem , vol.64 , pp. 205-213
    • Eto, T.1    Iichikawa, Y.2    Nishimura, K.3    Ando, S.4    Yamakawa, T.5
  • 47
    • 0015611944 scopus 로고
    • Determination of aminosugar linkages in glycolipids by methylation. Aminosugar linkages of ceramide pentasaccharides of rabbit erythrocytes and of Forssman antigen
    • Stellner, K., Saito, H., and Hakomori, S.-i. (1973) Determination of aminosugar linkages in glycolipids by methylation. Aminosugar linkages of ceramide pentasaccharides of rabbit erythrocytes and of Forssman antigen. Arch. Biochem, Biophys. 155, 464-472
    • (1973) Arch. Biochem, Biophys , vol.155 , pp. 464-472
    • Stellner, K.1    Saito, H.2    Hakomori, S.-I.3
  • 48
    • 0242690879 scopus 로고    scopus 로고
    • Significance of α-Gal (Galα1-3Galβ1-4GlcNAc-R) Epitopes and α1, 3 Galactosyltransferase in xeno-transplantation
    • Uri, G., and Tanemura, M. (1999) Significance of α-Gal (Galα1-3Galβ1-4GlcNAc-R) Epitopes and α1, 3 Galactosyltransferase in xeno-transplantation. Trends Glycosci. Glycotechnol. 11, 317-327
    • (1999) Trends Glycosci. Glycotechnol , vol.11 , pp. 317-327
    • Uri, G.1    Tanemura, M.2
  • 50
    • 0023930204 scopus 로고
    • Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. II. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones
    • Green, E. D., and Baenziger, J. U. (1988) Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. II. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones. J. Biol. Chem. 263, 36-44
    • (1988) J. Biol. Chem , vol.263 , pp. 36-44
    • Green, E.D.1    Baenziger, J.U.2
  • 51
    • 0029003930 scopus 로고
    • Purification and characterization of the GalNAc-4-sulfotransferase responsible for sulfation of GalNAc β 1,4GlcNAc-bearing oligosaccharides
    • Hooper, L. V., Hindsgaul, O., and Baenziger, J. U. (1995) Purification and characterization of the GalNAc-4-sulfotransferase responsible for sulfation of GalNAc β 1,4GlcNAc-bearing oligosaccharides. J. Biol. Chem. 270, 16327-16332
    • (1995) J. Biol. Chem , vol.270 , pp. 16327-16332
    • Hooper, L.V.1    Hindsgaul, O.2    Baenziger, J.U.3
  • 52
    • 0034751625 scopus 로고    scopus 로고
    • Detection of galectin-3 in tear fluid at disease states and immunohistochemical and lectin histochemical analysis in human corneal and conjunctival epithelium
    • Hrdlicková-Cela, E., Plzák, J., Smetana, K. Jr., Mělková, Z., Kaltner, H., Filipec, M., Liu, F. T., and Gabius, H. J. (2001) Detection of galectin-3 in tear fluid at disease states and immunohistochemical and lectin histochemical analysis in human corneal and conjunctival epithelium. Br. J. Ophthalmol. 85, 1336-1340
    • (2001) Br. J. Ophthalmol , vol.85 , pp. 1336-1340
    • Hrdlicková-Cela, E.1    Plzák, J.2    Smetana Jr., K.3    Mělková, Z.4    Kaltner, H.5    Filipec, M.6    Liu, F.T.7    Gabius, H.J.8
  • 53
    • 34247126011 scopus 로고    scopus 로고
    • Godovac-Zimmermann, J., Mulvey, C., Konstantoulaki, M., Sainsbury, R., and Brown, L. R. (2007) Promise of multiphoton detection in discovery and diagnostic proteomics. Expert Rev. Proteomics 4, 161-173
    • Godovac-Zimmermann, J., Mulvey, C., Konstantoulaki, M., Sainsbury, R., and Brown, L. R. (2007) Promise of multiphoton detection in discovery and diagnostic proteomics. Expert Rev. Proteomics 4, 161-173


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.