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Volumn 21, Issue 3, 2011, Pages 149-158

Location, location, location: New insights into O-GalNAc protein glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

FUCOSE; GALACTOSE; GLUCOSE; GLYCAN; MANNOSE; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE; PROTEIN; SIALIC ACID; SIALYLTRANSFERASE; URIDINE DIPHOSPHATE; XYLOSE;

EID: 79952106660     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2010.11.004     Document Type: Review
Times cited : (191)

References (102)
  • 1
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., et al. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473:4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1
  • 2
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • Lowe J.B., Marth J.D. A genetic approach to mammalian glycan function. Annu. Rev. Biochem. 2003, 72:643-691.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 3
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart G.W. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 1997, 66:315-335.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 4
    • 33645450506 scopus 로고    scopus 로고
    • Mechanisms in protein O-glycan biosynthesis and clinical and molecular aspects of protein O-glycan biosynthesis defects: a review
    • Wopereis S., et al. Mechanisms in protein O-glycan biosynthesis and clinical and molecular aspects of protein O-glycan biosynthesis defects: a review. Clin. Chem. 2006, 52:574-600.
    • (2006) Clin. Chem. , vol.52 , pp. 574-600
    • Wopereis, S.1
  • 5
    • 59649099685 scopus 로고    scopus 로고
    • Role of unusual O-glycans in intercellular signaling
    • Luther K.B., Haltiwanger R.S. Role of unusual O-glycans in intercellular signaling. Int. J. Biochem. Cell Biol. 2009, 41:1011-1024.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1011-1024
    • Luther, K.B.1    Haltiwanger, R.S.2
  • 6
    • 64949127643 scopus 로고    scopus 로고
    • Comprehensive analysis of glycosyltransferases in eukaryotic genomes for structural and functional characterization of glycans
    • Hashimoto K., et al. Comprehensive analysis of glycosyltransferases in eukaryotic genomes for structural and functional characterization of glycans. Carbohydr. Res. 2009, 344:881-887.
    • (2009) Carbohydr. Res. , vol.344 , pp. 881-887
    • Hashimoto, K.1
  • 7
    • 0035077832 scopus 로고    scopus 로고
    • O-Glycosylation of the mucin type
    • Hanisch F.G. O-Glycosylation of the mucin type. Biol. Chem. 2001, 382:143-149.
    • (2001) Biol. Chem. , vol.382 , pp. 143-149
    • Hanisch, F.G.1
  • 8
    • 22844433667 scopus 로고    scopus 로고
    • The chemistry and biology of mucin-type O-linked glycosylation
    • Hang H.C., Bertozzi C.R. The chemistry and biology of mucin-type O-linked glycosylation. Bioorg. Med. Chem. 2005, 13:5021-5034.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 5021-5034
    • Hang, H.C.1    Bertozzi, C.R.2
  • 9
    • 0035933704 scopus 로고    scopus 로고
    • Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance
    • Garner B., et al. Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance. J. Biol. Chem. 2001, 276:22200-22208.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22200-22208
    • Garner, B.1
  • 10
    • 36048942112 scopus 로고    scopus 로고
    • Gel-forming mucins appeared early in metazoan evolution
    • Lang T., et al. Gel-forming mucins appeared early in metazoan evolution. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:16209-16214.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 16209-16214
    • Lang, T.1
  • 11
    • 0032428668 scopus 로고    scopus 로고
    • Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation
    • Ellies L.G., et al. Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation. Immunity 1998, 9:881-890.
    • (1998) Immunity , vol.9 , pp. 881-890
    • Ellies, L.G.1
  • 12
    • 33744799438 scopus 로고    scopus 로고
    • Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions
    • Brockhausen I. Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions. EMBO Rep. 2006, 7:599-604.
    • (2006) EMBO Rep. , vol.7 , pp. 599-604
    • Brockhausen, I.1
  • 13
    • 40749160803 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation and its potential use in drug and vaccine development
    • Tarp M.A., Clausen H. Mucin-type O-glycosylation and its potential use in drug and vaccine development. Biochim. Biophys. Acta 2008, 1780:546-563.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 546-563
    • Tarp, M.A.1    Clausen, H.2
  • 14
    • 0029854393 scopus 로고    scopus 로고
    • A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation
    • Clausen H., Bennett E.P. A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation. Glycobiology 1996, 6:635-646.
    • (1996) Glycobiology , vol.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 15
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases
    • Ten Hagen K.G., et al. All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 2003, 13:1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1
  • 16
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian E., Ten Hagen K.G. Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj. J. 2009, 26:325-334.
    • (2009) Glycoconj. J. , vol.26 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 17
    • 77955279149 scopus 로고    scopus 로고
    • The role of mucin-type O-glycans in eukaryotic development
    • Tabak L.A. The role of mucin-type O-glycans in eukaryotic development. Semin. Cell Dev. Biol. 2010, 21:616-621.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 616-621
    • Tabak, L.A.1
  • 18
    • 0021813383 scopus 로고
    • Mucin synthesis. UDP-GlcNAc:GalNAc-R beta 3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc beta 1-3GalNAc-R (GlcNAc to GalNAc) beta 6-N-acetylglucosaminyltransferase from pig and rat colon mucosa
    • Brockhausen I., et al. Mucin synthesis. UDP-GlcNAc:GalNAc-R beta 3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc beta 1-3GalNAc-R (GlcNAc to GalNAc) beta 6-N-acetylglucosaminyltransferase from pig and rat colon mucosa. Biochemistry 1985, 24:1866-1874.
    • (1985) Biochemistry , vol.24 , pp. 1866-1874
    • Brockhausen, I.1
  • 19
    • 53849139401 scopus 로고    scopus 로고
    • Glycan structures of ocular surface mucins in man, rabbit and dog display species differences
    • Royle L., et al. Glycan structures of ocular surface mucins in man, rabbit and dog display species differences. Glycoconj. J. 2008, 25:763-773.
    • (2008) Glycoconj. J. , vol.25 , pp. 763-773
    • Royle, L.1
  • 20
    • 69249122444 scopus 로고    scopus 로고
    • Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier
    • Argueso P., et al. Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier. J. Biol. Chem. 2009, 284:23037-23045.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23037-23045
    • Argueso, P.1
  • 21
    • 0035137134 scopus 로고    scopus 로고
    • Roles of O-linked oligosaccharides in immune responses
    • Tsuboi S., Fukuda M. Roles of O-linked oligosaccharides in immune responses. Bioessays 2001, 23:46-53.
    • (2001) Bioessays , vol.23 , pp. 46-53
    • Tsuboi, S.1    Fukuda, M.2
  • 22
    • 70349323001 scopus 로고    scopus 로고
    • Golgi linked protein glycosylation and associated diseases
    • Ungar D. Golgi linked protein glycosylation and associated diseases. Semin. Cell Dev. Biol. 2009, 20:762-769.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 762-769
    • Ungar, D.1
  • 23
    • 0021141716 scopus 로고
    • T and Tn, general carcinoma autoantigens
    • Springer G.F. T and Tn, general carcinoma autoantigens. Science 1984, 224:1198-1206.
    • (1984) Science , vol.224 , pp. 1198-1206
    • Springer, G.F.1
  • 24
    • 0033603316 scopus 로고    scopus 로고
    • High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells
    • Muller S., et al. High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells. J. Biol. Chem. 1999, 274:18165-18172.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18165-18172
    • Muller, S.1
  • 25
    • 0029809614 scopus 로고    scopus 로고
    • Mucin glycoproteins in neoplasia
    • Kim Y.S., et al. Mucin glycoproteins in neoplasia. Glycoconj. J. 1996, 13:693-707.
    • (1996) Glycoconj. J. , vol.13 , pp. 693-707
    • Kim, Y.S.1
  • 26
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: protection and control of the cell surface
    • Hollingsworth M.A., Swanson B.J. Mucins in cancer: protection and control of the cell surface. Nat. Rev. Cancer 2004, 4:45-60.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 27
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core 1 beta1,3-galactosyltransferase
    • Ju T., et al. Cloning and expression of human core 1 beta1,3-galactosyltransferase. J. Biol. Chem. 2002, 277:178-186.
    • (2002) J. Biol. Chem. , vol.277 , pp. 178-186
    • Ju, T.1
  • 28
    • 0029017524 scopus 로고
    • Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-R beta 3-N-acetyl-glucosaminyltransferase activity from colonic mucosal tissues and lack of the activity in human cancer cell lines
    • Vavasseur F., et al. Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-R beta 3-N-acetyl-glucosaminyltransferase activity from colonic mucosal tissues and lack of the activity in human cancer cell lines. Glycobiology 1995, 5:351-357.
    • (1995) Glycobiology , vol.5 , pp. 351-357
    • Vavasseur, F.1
  • 29
    • 0037066753 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans
    • Iwai T., et al. Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans. J. Biol. Chem. 2002, 277:12802-12809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12802-12809
    • Iwai, T.1
  • 30
    • 20144367969 scopus 로고    scopus 로고
    • Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells
    • Iwai T., et al. Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:4572-4577.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4572-4577
    • Iwai, T.1
  • 31
    • 1242337458 scopus 로고    scopus 로고
    • Mucins and mucin binding proteins in colorectal cancer
    • Byrd J.C., Bresalier R.S. Mucins and mucin binding proteins in colorectal cancer. Cancer Metastasis Rev. 2004, 23:77-99.
    • (2004) Cancer Metastasis Rev. , vol.23 , pp. 77-99
    • Byrd, J.C.1    Bresalier, R.S.2
  • 32
    • 0026662007 scopus 로고
    • Expression cloning of a cDNA encoding UDP-GlcNAc:Gal beta 1-3-GalNAc-R (GlcNAc to GalNAc) beta 1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen
    • Bierhuizen M.F., Fukuda M. Expression cloning of a cDNA encoding UDP-GlcNAc:Gal beta 1-3-GalNAc-R (GlcNAc to GalNAc) beta 1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:9326-9330.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9326-9330
    • Bierhuizen, M.F.1    Fukuda, M.2
  • 33
    • 0034646696 scopus 로고    scopus 로고
    • Control of O-glycan branch formation. Molecular cloning and characterization of a novel thymus-associated core 2 beta1, 6-n-acetylglucosaminyltransferase
    • Schwientek T., et al. Control of O-glycan branch formation. Molecular cloning and characterization of a novel thymus-associated core 2 beta1, 6-n-acetylglucosaminyltransferase. J. Biol. Chem. 2000, 275:11106-11113.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11106-11113
    • Schwientek, T.1
  • 34
    • 0033582478 scopus 로고    scopus 로고
    • Control of O-glycan branch formation. Molecular cloning of human cDNA encoding a novel beta1,6-N-acetylglucosaminyltransferase forming core 2 and core 4
    • Schwientek T., et al. Control of O-glycan branch formation. Molecular cloning of human cDNA encoding a novel beta1,6-N-acetylglucosaminyltransferase forming core 2 and core 4. J. Biol. Chem. 1999, 274:4504-4512.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4504-4512
    • Schwientek, T.1
  • 35
    • 0033613934 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel beta-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches
    • Yeh J.C., et al. Molecular cloning and expression of a novel beta-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 1999, 274:3215-3221.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3215-3221
    • Yeh, J.C.1
  • 36
    • 0025851570 scopus 로고
    • Biosynthesis of O-glycans in leukocytes from normal donors and from patients with leukemia: increase in O-glycan core 2 UDP-GlcNAc:Gal beta 3 GalNAc alpha-R (GlcNAc to GalNAc) beta(1-6)-N-acetylglucosaminyltransferase in leukemic cells
    • Brockhausen I., et al. Biosynthesis of O-glycans in leukocytes from normal donors and from patients with leukemia: increase in O-glycan core 2 UDP-GlcNAc:Gal beta 3 GalNAc alpha-R (GlcNAc to GalNAc) beta(1-6)-N-acetylglucosaminyltransferase in leukemic cells. Cancer Res. 1991, 51:1257-1263.
    • (1991) Cancer Res. , vol.51 , pp. 1257-1263
    • Brockhausen, I.1
  • 37
    • 0023803332 scopus 로고
    • Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis
    • Piller F., et al. Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis. J. Biol. Chem. 1988, 263:15146-15150.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15146-15150
    • Piller, F.1
  • 38
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin
    • Li F., et al. Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. J. Biol. Chem. 1996, 271:3255-3264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3255-3264
    • Li, F.1
  • 39
    • 0032970473 scopus 로고    scopus 로고
    • Core 2-containing O-glycans on CD43 are preferentially expressed in the memory subset of human CD4 T cells
    • Mukasa R., et al. Core 2-containing O-glycans on CD43 are preferentially expressed in the memory subset of human CD4 T cells. Int. Immunol. 1999, 11:259-268.
    • (1999) Int. Immunol. , vol.11 , pp. 259-268
    • Mukasa, R.1
  • 40
    • 0035889895 scopus 로고    scopus 로고
    • CD45 modulates galectin-1-induced T cell death: regulation by expression of core 2 O-glycans
    • Nguyen J.T., et al. CD45 modulates galectin-1-induced T cell death: regulation by expression of core 2 O-glycans. J. Immunol. 2001, 167:5697-5707.
    • (2001) J. Immunol. , vol.167 , pp. 5697-5707
    • Nguyen, J.T.1
  • 41
    • 14844290268 scopus 로고    scopus 로고
    • Not core 2 beta 1,6-N-acetylglucosaminyltransferase-2 or -3 but -1 regulates sialyl-Lewis x expression in human precursor B cells
    • Kikuchi J., et al. Not core 2 beta 1,6-N-acetylglucosaminyltransferase-2 or -3 but -1 regulates sialyl-Lewis x expression in human precursor B cells. Glycobiology 2005, 15:271-280.
    • (2005) Glycobiology , vol.15 , pp. 271-280
    • Kikuchi, J.1
  • 42
    • 17644441326 scopus 로고    scopus 로고
    • Altered T cell surface glycosylation in HIV-1 infection results in increased susceptibility to galectin-1-induced cell death
    • Lanteri M., et al. Altered T cell surface glycosylation in HIV-1 infection results in increased susceptibility to galectin-1-induced cell death. Glycobiology 2003, 13:909-918.
    • (2003) Glycobiology , vol.13 , pp. 909-918
    • Lanteri, M.1
  • 43
    • 33744905018 scopus 로고    scopus 로고
    • C2GnT-M is downregulated in colorectal cancer and its re-expression causes growth inhibition of colon cancer cells
    • Huang M.C., et al. C2GnT-M is downregulated in colorectal cancer and its re-expression causes growth inhibition of colon cancer cells. Oncogene 2006, 25:3267-3276.
    • (2006) Oncogene , vol.25 , pp. 3267-3276
    • Huang, M.C.1
  • 44
    • 11844303459 scopus 로고    scopus 로고
    • Detection of glycosyltransferases in the golden hamster (Mesocricetus auratus) oviduct and evidence for the regulation of O-glycan biosynthesis during the estrous cycle
    • McBride D.S., et al. Detection of glycosyltransferases in the golden hamster (Mesocricetus auratus) oviduct and evidence for the regulation of O-glycan biosynthesis during the estrous cycle. Biochim. Biophys. Acta 2005, 1721:107-115.
    • (2005) Biochim. Biophys. Acta , vol.1721 , pp. 107-115
    • McBride, D.S.1
  • 45
    • 0037151059 scopus 로고    scopus 로고
    • Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila
    • Schwientek T., et al. Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila. J. Biol. Chem. 2002, 277:22623-22638.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22623-22638
    • Schwientek, T.1
  • 46
    • 0042317189 scopus 로고    scopus 로고
    • Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster
    • Ten Hagen K.G., et al. Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster. J. Biol. Chem. 2003, 278:35039-35048.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35039-35048
    • Ten Hagen, K.G.1
  • 47
    • 58149343579 scopus 로고    scopus 로고
    • Glycobiology on the fly: developmental and mechanistic insights from Drosophila
    • ten Hagen K.G., et al. Glycobiology on the fly: developmental and mechanistic insights from Drosophila. Glycobiology 2009, 19:102-111.
    • (2009) Glycobiology , vol.19 , pp. 102-111
    • ten Hagen, K.G.1
  • 48
    • 2642546399 scopus 로고    scopus 로고
    • Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis
    • Topaz O., et al. Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat. Genet. 2004, 36:579-581.
    • (2004) Nat. Genet. , vol.36 , pp. 579-581
    • Topaz, O.1
  • 49
    • 33745828096 scopus 로고    scopus 로고
    • Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation
    • Kato K., et al. Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation. J. Biol. Chem. 2006, 281:18370-18377.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18370-18377
    • Kato, K.1
  • 50
    • 38649132270 scopus 로고    scopus 로고
    • Six new loci associated with blood low-density lipoprotein cholesterol, high-density lipoprotein cholesterol or triglycerides in humans
    • Kathiresan S., et al. Six new loci associated with blood low-density lipoprotein cholesterol, high-density lipoprotein cholesterol or triglycerides in humans. Nat. Genet. 2008, 40:189-197.
    • (2008) Nat. Genet. , vol.40 , pp. 189-197
    • Kathiresan, S.1
  • 51
    • 38649125868 scopus 로고    scopus 로고
    • Newly identified loci that influence lipid concentrations and risk of coronary artery disease
    • Willer C.J., et al. Newly identified loci that influence lipid concentrations and risk of coronary artery disease. Nat. Genet. 2008, 40:161-169.
    • (2008) Nat. Genet. , vol.40 , pp. 161-169
    • Willer, C.J.1
  • 52
    • 77955505564 scopus 로고    scopus 로고
    • Biological, clinical and population relevance of 95 loci for blood lipids
    • Teslovich T.M., et al. Biological, clinical and population relevance of 95 loci for blood lipids. Nature 2010, 466:707-713.
    • (2010) Nature , vol.466 , pp. 707-713
    • Teslovich, T.M.1
  • 53
    • 78449258533 scopus 로고    scopus 로고
    • O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3 - possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids
    • Gram Schjoldager K.T., et al. O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3 - possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids. J. Biol. Chem. 2010, 285:36293-36303.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36293-36303
    • Gram Schjoldager, K.T.1
  • 54
    • 74049090465 scopus 로고    scopus 로고
    • Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1
    • Miwa H.E., et al. Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1. J. Biol. Chem. 2010, 285:1208-1219.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1208-1219
    • Miwa, H.E.1
  • 55
    • 77953512867 scopus 로고    scopus 로고
    • An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand
    • Zhang L., et al. An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand. J. Biol. Chem. 2010, 285:19491-19501.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19491-19501
    • Zhang, L.1
  • 56
    • 0033520457 scopus 로고    scopus 로고
    • Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy
    • Bennett E.P., et al. Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J. Biol. Chem. 1999, 274:25362-25370.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25362-25370
    • Bennett, E.P.1
  • 57
    • 7444220526 scopus 로고    scopus 로고
    • The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
    • Fritz T.A., et al. The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:15307-15312.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15307-15312
    • Fritz, T.A.1
  • 58
    • 33646828699 scopus 로고    scopus 로고
    • Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2
    • Fritz T.A., et al. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2. J. Biol. Chem. 2006, 281:8613-8619.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8613-8619
    • Fritz, T.A.1
  • 59
    • 33646795021 scopus 로고    scopus 로고
    • Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)
    • Kubota T., et al. Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J. Mol. Biol. 2006, 359:708-727.
    • (2006) J. Mol. Biol. , vol.359 , pp. 708-727
    • Kubota, T.1
  • 60
    • 54549083447 scopus 로고    scopus 로고
    • Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs
    • Gerken T.A., et al. Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs. Glycobiology 2008, 18:861-870.
    • (2008) Glycobiology , vol.18 , pp. 861-870
    • Gerken, T.A.1
  • 61
    • 77955614342 scopus 로고    scopus 로고
    • Rescue of Drosophila melanogaster l(2)35Aa lethality is only mediated by polypeptide GalNAc-transferase pgant35A, but not by the evolutionary conserved human ortholog GalNAc-transferase-T11
    • Bennett E.P., et al. Rescue of Drosophila melanogaster l(2)35Aa lethality is only mediated by polypeptide GalNAc-transferase pgant35A, but not by the evolutionary conserved human ortholog GalNAc-transferase-T11. Glycoconj. J. 2010, 27:435-444.
    • (2010) Glycoconj. J. , vol.27 , pp. 435-444
    • Bennett, E.P.1
  • 62
    • 0032701175 scopus 로고    scopus 로고
    • A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates
    • Bennett E.P., et al. A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates. FEBS Lett. 1999, 460:226-230.
    • (1999) FEBS Lett. , vol.460 , pp. 226-230
    • Bennett, E.P.1
  • 63
    • 0033600864 scopus 로고    scopus 로고
    • Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity
    • Ten Hagen K.G., et al. Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity. J. Biol. Chem. 1999, 274:27867-27874.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27867-27874
    • Ten Hagen, K.G.1
  • 64
    • 0034780414 scopus 로고    scopus 로고
    • Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides
    • Hanisch F.G., et al. Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides. Glycobiology 2001, 11:731-740.
    • (2001) Glycobiology , vol.11 , pp. 731-740
    • Hanisch, F.G.1
  • 65
    • 33845941133 scopus 로고    scopus 로고
    • Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates
    • Gerken T.A., et al. Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates. J. Biol. Chem. 2006, 281:32403-32416.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32403-32416
    • Gerken, T.A.1
  • 66
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • Pratt M.R., et al. Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem. Biol. 2004, 11:1009-1016.
    • (2004) Chem. Biol. , vol.11 , pp. 1009-1016
    • Pratt, M.R.1
  • 67
    • 67749133871 scopus 로고    scopus 로고
    • Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2
    • Perrine C.L., et al. Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J. Biol. Chem. 2009, 284:20387-20397.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20387-20397
    • Perrine, C.L.1
  • 68
    • 0034768392 scopus 로고    scopus 로고
    • N-acetylgalactosamine incorporation into a peptide containing consecutive threonine residues by UDP-N-acetyl-D-galactosaminide:polypeptide N-acetylgalactosaminyltransferases
    • Kato K., et al. N-acetylgalactosamine incorporation into a peptide containing consecutive threonine residues by UDP-N-acetyl-D-galactosaminide:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 2001, 11:821-829.
    • (2001) Glycobiology , vol.11 , pp. 821-829
    • Kato, K.1
  • 69
    • 0034624056 scopus 로고    scopus 로고
    • The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities
    • Hassan H., et al. The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. J. Biol. Chem. 2000, 275:38197-38205.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38197-38205
    • Hassan, H.1
  • 70
    • 53149142512 scopus 로고    scopus 로고
    • The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection
    • Raman J., et al. The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J. Biol. Chem. 2008, 283:22942-22951.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22942-22951
    • Raman, J.1
  • 71
    • 0345530978 scopus 로고    scopus 로고
    • Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core
    • Kinarsky L., et al. Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core. Glycobiology 2003, 13:929-939.
    • (2003) Glycobiology , vol.13 , pp. 929-939
    • Kinarsky, L.1
  • 72
    • 0036435680 scopus 로고    scopus 로고
    • Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1
    • Tenno M., et al. Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1. Biochem. Biophys. Res. Commun. 2002, 298:755-759.
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 755-759
    • Tenno, M.1
  • 73
    • 33947198189 scopus 로고    scopus 로고
    • The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation
    • Wandall H.H., et al. The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation. Glycobiology 2007, 17:374-387.
    • (2007) Glycobiology , vol.17 , pp. 374-387
    • Wandall, H.H.1
  • 74
    • 0035907293 scopus 로고    scopus 로고
    • Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9
    • Ten Hagen K.G., et al. Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9. J. Biol. Chem. 2001, 276:17395-17404.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17395-17404
    • Ten Hagen, K.G.1
  • 75
    • 0022343674 scopus 로고
    • Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation
    • Roth J., et al. Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 1985, 43:287-295.
    • (1985) Cell , vol.43 , pp. 287-295
    • Roth, J.1
  • 76
    • 0028587240 scopus 로고
    • Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland
    • Roth J., et al. Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:8935-8939.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8935-8939
    • Roth, J.1
  • 77
    • 0030931796 scopus 로고    scopus 로고
    • Altered Golgi localization of core 2 beta-1,6-N-acetylglucosaminyltransferase leads to decreased synthesis of branched O-glycans
    • Skrincosky D., et al. Altered Golgi localization of core 2 beta-1,6-N-acetylglucosaminyltransferase leads to decreased synthesis of branched O-glycans. J. Biol. Chem. 1997, 272:22695-22702.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22695-22702
    • Skrincosky, D.1
  • 78
    • 0039992226 scopus 로고    scopus 로고
    • Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus
    • Rottger S., et al. Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J. Cell Sci. 1998, 111(Pt 1):45-60.
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 1 , pp. 45-60
    • Rottger, S.1
  • 79
    • 0030905585 scopus 로고    scopus 로고
    • A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans
    • Whitehouse C., et al. A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans. J. Cell Biol. 1997, 137:1229-1241.
    • (1997) J. Cell Biol. , vol.137 , pp. 1229-1241
    • Whitehouse, C.1
  • 80
    • 0027237510 scopus 로고
    • The biosynthesis of oligosaccharides in intact Golgi preparations from rat liver. Analysis of N-linked and O-linked glycans labeled by UDP-[6-3H]N-acetylgalactosamine
    • Hayes B.K., Varki A. The biosynthesis of oligosaccharides in intact Golgi preparations from rat liver. Analysis of N-linked and O-linked glycans labeled by UDP-[6-3H]N-acetylgalactosamine. J. Biol. Chem. 1993, 268:16170-16178.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16170-16178
    • Hayes, B.K.1    Varki, A.2
  • 81
    • 6544282655 scopus 로고    scopus 로고
    • Cloning and expression of a human gene encoding an N-acetylgalactosamine-alpha2,6-sialyltransferase (ST6GalNAc I): a candidate for synthesis of cancer-associated sialyl-Tn antigens
    • Ikehara Y., et al. Cloning and expression of a human gene encoding an N-acetylgalactosamine-alpha2,6-sialyltransferase (ST6GalNAc I): a candidate for synthesis of cancer-associated sialyl-Tn antigens. Glycobiology 1999, 9:1213-1224.
    • (1999) Glycobiology , vol.9 , pp. 1213-1224
    • Ikehara, Y.1
  • 82
    • 4944265751 scopus 로고    scopus 로고
    • Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen
    • Marcos N.T., et al. Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen. Cancer Res. 2004, 64:7050-7057.
    • (2004) Cancer Res. , vol.64 , pp. 7050-7057
    • Marcos, N.T.1
  • 83
    • 33645641216 scopus 로고    scopus 로고
    • The ST6GalNAc-I sialyltransferase localizes throughout the Golgi and is responsible for the synthesis of the tumor-associated sialyl-Tn O-glycan in human breast cancer
    • Sewell R., et al. The ST6GalNAc-I sialyltransferase localizes throughout the Golgi and is responsible for the synthesis of the tumor-associated sialyl-Tn O-glycan in human breast cancer. J. Biol. Chem. 2006, 281:3586-3594.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3586-3594
    • Sewell, R.1
  • 84
    • 29444454759 scopus 로고    scopus 로고
    • ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their O-glycosylation pattern and enhances their tumourigenicity
    • Julien S., et al. ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their O-glycosylation pattern and enhances their tumourigenicity. Glycobiology 2006, 16:54-64.
    • (2006) Glycobiology , vol.16 , pp. 54-64
    • Julien, S.1
  • 85
    • 0344012542 scopus 로고    scopus 로고
    • Src regulates Golgi structure and KDEL receptor-dependent retrograde transport to the endoplasmic reticulum
    • Bard F., et al. Src regulates Golgi structure and KDEL receptor-dependent retrograde transport to the endoplasmic reticulum. J. Biol. Chem. 2003, 278:46601-46606.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46601-46606
    • Bard, F.1
  • 86
    • 77953161781 scopus 로고    scopus 로고
    • Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
    • Gill D.J., et al. Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. J. Cell Biol. 2010, 189:843-858.
    • (2010) J. Cell Biol. , vol.189 , pp. 843-858
    • Gill, D.J.1
  • 87
    • 0026340756 scopus 로고
    • Presence of terminal N-acetylgalactosamine residues in subregions of the endoplasmic reticulum is influenced by cell differentiation in culture
    • Perez-Vilar J., et al. Presence of terminal N-acetylgalactosamine residues in subregions of the endoplasmic reticulum is influenced by cell differentiation in culture. J. Biol. Chem. 1991, 266:23967-23976.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23967-23976
    • Perez-Vilar, J.1
  • 88
    • 0032939863 scopus 로고    scopus 로고
    • Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family
    • Mandel U., et al. Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. Glycobiology 1999, 9:43-52.
    • (1999) Glycobiology , vol.9 , pp. 43-52
    • Mandel, U.1
  • 89
    • 0001307877 scopus 로고    scopus 로고
    • Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor
    • Kim J.H., et al. Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor. J. Cell Biol. 1996, 134:1387-1399.
    • (1996) J. Cell Biol. , vol.134 , pp. 1387-1399
    • Kim, J.H.1
  • 90
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • Demaurex N., et al. Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J. Biol. Chem. 1998, 273:2044-2051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2044-2051
    • Demaurex, N.1
  • 91
    • 75749103348 scopus 로고    scopus 로고
    • Src signaling in cancer invasion
    • Guarino M. Src signaling in cancer invasion. J. Cell Physiol. 2010, 223:14-26.
    • (2010) J. Cell Physiol. , vol.223 , pp. 14-26
    • Guarino, M.1
  • 92
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman T.J. A renaissance for SRC. Nat. Rev. Cancer 2004, 4:470-480.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 93
    • 1842584776 scopus 로고    scopus 로고
    • Newest findings on the oldest oncogene; how activated src does it
    • Frame M.C. Newest findings on the oldest oncogene; how activated src does it. J. Cell Sci. 2004, 117:989-998.
    • (2004) J. Cell Sci. , vol.117 , pp. 989-998
    • Frame, M.C.1
  • 94
    • 0032500663 scopus 로고    scopus 로고
    • Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence
    • Gerken T.A., et al. Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence. J. Biol. Chem. 1998, 273:26580-26588.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26580-26588
    • Gerken, T.A.1
  • 95
    • 69949105150 scopus 로고    scopus 로고
    • Site directed processing: Role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2
    • Brockhausen I., et al. Site directed processing: Role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2. Biochim. Biophys. Acta 2009, 1790:1244-1257.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1244-1257
    • Brockhausen, I.1
  • 96
    • 0035815609 scopus 로고    scopus 로고
    • The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1
    • Dalziel M., et al. The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. J. Biol. Chem. 2001, 276:11007-11015.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11007-11015
    • Dalziel, M.1
  • 97
    • 33846964873 scopus 로고    scopus 로고
    • Galectin-3 interaction with Thomsen-Friedenreich disaccharide on cancer-associated MUC1 causes increased cancer cell endothelial adhesion
    • Yu L.G., et al. Galectin-3 interaction with Thomsen-Friedenreich disaccharide on cancer-associated MUC1 causes increased cancer cell endothelial adhesion. J. Biol. Chem. 2007, 282:773-781.
    • (2007) J. Biol. Chem. , vol.282 , pp. 773-781
    • Yu, L.G.1
  • 98
    • 27644442375 scopus 로고    scopus 로고
    • Protein glycosylation: chaperone mutation in Tn syndrome
    • Ju T., Cummings R.D. Protein glycosylation: chaperone mutation in Tn syndrome. Nature 2005, 437:1252.
    • (2005) Nature , vol.437 , pp. 1252
    • Ju, T.1    Cummings, R.D.2
  • 99
    • 33947423328 scopus 로고    scopus 로고
    • Biological significance of cancer-associated sialyl-Tn antigen: modulation of malignant phenotype in gastric carcinoma cells
    • Pinho S., et al. Biological significance of cancer-associated sialyl-Tn antigen: modulation of malignant phenotype in gastric carcinoma cells. Cancer Lett. 2007, 249:157-170.
    • (2007) Cancer Lett. , vol.249 , pp. 157-170
    • Pinho, S.1
  • 100
    • 70349758510 scopus 로고    scopus 로고
    • Src kinases as therapeutic targets for cancer
    • Kim L.C., et al. Src kinases as therapeutic targets for cancer. Nat. Rev. Clin. Oncol. 2009, 6:587-595.
    • (2009) Nat. Rev. Clin. Oncol. , vol.6 , pp. 587-595
    • Kim, L.C.1
  • 101
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H., et al. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 2010, 38(Suppl.):W529-W533.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.SUPPL.
    • Ashkenazy, H.1
  • 102
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures
    • Landau M., et al. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 2005, 33:W299-W302.
    • (2005) Nucleic Acids Res. , vol.33
    • Landau, M.1


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