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Volumn 2, Issue 2, 2011, Pages 425-432

Evolutional and clinical implications of the epigenetic regulation of protein glycosylation

Author keywords

Epigenetics; Glycome; Glycosyltransferases; Protein glycosylation

Indexed keywords

BIOLOGICAL MARKER; GLYCAN; GLYCOSYLTRANSFERASE;

EID: 84856254596     PISSN: 18687075     EISSN: 18687083     Source Type: Journal    
DOI: 10.1007/s13148-011-0039-1     Document Type: Review
Times cited : (19)

References (74)
  • 2
    • 44849133511 scopus 로고    scopus 로고
    • Sweet and sour: The impact of sugars on disease
    • DOI 10.1093/rheumatology/ken081
    • Alavi A, Axford JS (2008) Sweet and sour: the impact of sugars on disease. Rheumatology (Oxford) 47:760-770 (Pubitemid 351796358)
    • (2008) Rheumatology , vol.47 , Issue.6 , pp. 760-770
    • Alavi, A.1    Axford, J.S.2
  • 3
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: The anti-inflammatory activity of sialylated IgG Fcs
    • Anthony RM, Ravetch JV (2010) A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J Clin Immunol 30(Suppl 1):S9-S14
    • (2010) J Clin Immunol , vol.30 , Issue.SUPPL. 1
    • Anthony, R.M.1    Ravetch, J.V.2
  • 4
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • DOI 10.1126/science.1154315
    • Anthony RM, Nimmerjahn F, Ashline DJ, Reinhold VN, Paulson JC, Ravetch JV (2008) Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320:373-376 (Pubitemid 351555659)
    • (2008) Science , vol.320 , Issue.5874 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3    Reinhold, V.N.4    Paulson, J.C.5    Ravetch, J.V.6
  • 5
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISSPROT database
    • Apweiler R, Hermjakob H, Sharon N (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISSPROT database. Biochim Biophys Acta 1473:4-8
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 6
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • DOI 10.1146/annurev.immunol.25.022106.141702
    • Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA (2007) The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol 25:21-50 (Pubitemid 46697901)
    • (2007) Annual Review of Immunology , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 8
    • 34447327844 scopus 로고    scopus 로고
    • Evolution of carbohydrate antigens - Microbial forces shaping host glycomes?
    • DOI 10.1093/glycob/cwm005
    • Bishop JR, Gagneux P (2007) Evolution of carbohydrate antigens- microbial forces shaping host glycomes? Glycobiology 17:23R-34R (Pubitemid 47053737)
    • (2007) Glycobiology , vol.17 , Issue.5
    • Bishop, J.R.1    Gagneux, P.2
  • 9
    • 0031723937 scopus 로고    scopus 로고
    • Glycoproteins and their relationship to human disease
    • Brockhausen I, Schutzbach J, Kuhns W (1998) Glycoproteins and their relationship to human disease. Acta Anat 161:36-78 (Pubitemid 28478160)
    • (1998) Acta Anatomica , vol.161 , Issue.1-4 , pp. 36-78
    • Brockhausen, I.1
  • 10
    • 68949176934 scopus 로고    scopus 로고
    • Autoimmune thyroid disease: Unlocking a complex puzzle
    • Brown RS (2009) Autoimmune thyroid disease: unlocking a complex puzzle. Curr Opin Pediatr 21:523-528
    • (2009) Curr Opin Pediatr , vol.21 , pp. 523-528
    • Brown, R.S.1
  • 11
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in Archaea: Sweet and extreme
    • Calo D, Kaminski L, Eichler J (2010) Protein glycosylation in Archaea: sweet and extreme. Glycobiology 20:1065-1076
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 12
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • DOI 10.1038/nri2056, PII NRI2056
    • Crocker PR, Paulson JC, Varki A (2007) Siglecs and their roles in the immune system. Nat Rev Immunol 7:255-266 (Pubitemid 46480955)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.4 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 13
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings RD (2009) The repertoire of glycan determinants in the human glycome. Mol Biosyst 5:1087-1104
    • (2009) Mol Biosyst , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 14
    • 16644367146 scopus 로고    scopus 로고
    • ABO blood-group antigens in oral cancer
    • DOI 10.1177/154405910508400103
    • Dabelsteen E, Gao S (2005) ABO blood-group antigens in oral cancer. J Dent Res 84:21-28 (Pubitemid 43822056)
    • (2005) Journal of Dental Research , vol.84 , Issue.1 , pp. 21-28
    • Dabelsteen, E.1    Gao, S.2
  • 16
    • 0037137493 scopus 로고    scopus 로고
    • UDPN-acetylglucosamine:alpha-6-D-mannoside beta1, 6N- acetylglucosaminyltransferase v (Mgat5) deficient mice
    • Dennis JW, Pawling J, Cheung P, Partridge E, Demetriou M(2002) UDPN-acetylglucosamine:alpha-6-D-mannoside beta1, 6N- acetylglucosaminyltransferase V (Mgat5) deficient mice. Biochim Biophys Acta 1573:414-422
    • (2002) Biochim Biophys Acta , vol.1573 , pp. 414-422
    • Dennis, J.W.1    Pawling, J.2    Cheung, P.3    Partridge, E.4    Demetriou, M.5
  • 17
    • 70350685770 scopus 로고    scopus 로고
    • Adaptive regulation at the cell surface by N-glycosylation
    • Dennis JW, Lau KS, Demetriou M, Nabi IR (2009) Adaptive regulation at the cell surface by N-glycosylation. Traffic 10:1569-1578
    • (2009) Traffic , vol.10 , pp. 1569-1578
    • Dennis, J.W.1    Lau, K.S.2    Demetriou, M.3    Nabi, I.R.4
  • 19
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • DOI 10.1016/S0968-0004(98)01246-8, PII S0968000498012468
    • Drickamer K, TaylorME (1998) Evolving views of protein glycosylation. Trends Biochem Sci 23:321-324 (Pubitemid 28461861)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.9 , pp. 321-324
    • Drickamer, K.1    Taylor, M.E.2
  • 20
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation - Potential for therapeutics and diagnostics
    • DOI 10.1038/nrd1751
    • Dube DH, Bertozzi CR (2005) Glycans in cancer and inflammationpotential for therapeutics and diagnostics. Nat Rev Drug Discov 4:477-488 (Pubitemid 40861990)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.6 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 21
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • DOI 10.1146/annurev.biochem.71.110601.135458
    • Esko JD, Selleck SB (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 71:435-471 (Pubitemid 34800227)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 22
    • 0037137478 scopus 로고    scopus 로고
    • Human disorders in N-glycosylation and animal models
    • DOI 10.1016/S0304-4165(02)00408-7, PII S0304416502004087
    • Freeze HH (2002) Human disorders in N-glycosylation and animal models. Biochim Biophys Acta 1573:388-393 (Pubitemid 35335449)
    • (2002) Biochimica et Biophysica Acta - General Subjects , vol.1573 , Issue.3 , pp. 388-393
    • Freeze, H.H.1
  • 23
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • DOI 10.1038/nrg1894, PII N1894
    • Freeze HH (2006) Genetic defects in the human glycome. Nat Rev Genet 7:537-551 (Pubitemid 43943571)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.7 , pp. 537-551
    • Freeze, H.H.1
  • 24
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • DOI 10.1038/nrc1649
    • Fuster MM, Esko JD (2005) The sweet and sour of cancer: glycans as novel therapeutic targets. Nat Rev Cancer 5:526-542 (Pubitemid 40942829)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.7 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 25
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • DOI 10.1093/glycob/9.8.747
    • Gagneux P, Varki A (1999) Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9:747-755 (Pubitemid 29376001)
    • (1999) Glycobiology , vol.9 , Issue.8 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 26
    • 58149391280 scopus 로고    scopus 로고
    • Glycosylation of serum proteins in inflammatory diseases
    • Gornik O, Lauc G (2008) Glycosylation of serum proteins in inflammatory diseases. Dis Markers 25:267-278
    • (2008) Dis Markers , vol.25 , pp. 267-278
    • Gornik, O.1    Lauc, G.2
  • 28
    • 71749102704 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: An update on defects affecting the biosynthesis of dolichol-linked oligosaccharides
    • Haeuptle MA, Hennet T (2009) Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides. Hum Mutat 30:1628-1641
    • (2009) Hum Mutat , vol.30 , pp. 1628-1641
    • Haeuptle, M.A.1    Hennet, T.2
  • 29
    • 25144501600 scopus 로고    scopus 로고
    • The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach
    • DOI 10.1093/glycob/cwi063
    • Harduin-Lepers A, Mollicone R, Delannoy P, Oriol R (2005) The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach. Glycobiology 15:805-817 (Pubitemid 41417983)
    • (2005) Glycobiology , vol.15 , Issue.8 , pp. 805-817
    • Harduin-Lepers, A.1    Mollicone, R.2    Delannoy, P.3    Oriol, R.4
  • 30
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • DOI 10.1126/science.291.5512.2364
    • Helenius A, Aebi M (2001) Intracellular functions of N-linked glycans. Science 291:2364-2369 (Pubitemid 32231791)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 31
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth MA, Swanson BJ (2004) Mucins in cancer: protection and control of the cell surface. Nat Rev Cancer 4:45-60 (Pubitemid 38082153)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.1 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 32
    • 0035054508 scopus 로고    scopus 로고
    • Glycans as legislators of host-microbial interactions: Spanning the spectrum from symbiosis to pathogenicity
    • Hooper LV, Gordon JI (2001) Glycans as legislators of host-microbial interactions: spanning the spectrum from symbiosis to pathogenicity. Glycobiology 11:1R-10R (Pubitemid 32331669)
    • (2001) Glycobiology , vol.11 , Issue.2
    • Hooper, L.V.1    Gordon, J.I.2
  • 34
    • 33646740982 scopus 로고    scopus 로고
    • Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa
    • Iida S, Misaka H, Inoue M, Shibata M, Nakano R, Yamane-Ohnuki N, Wakitani M, Yano K, Shitara K, Satoh M (2006) Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa. Clin Cancer Res 12:2879-2887
    • (2006) Clin Cancer Res , vol.12 , pp. 2879-2887
    • Iida, S.1    Misaka, H.2    Inoue, M.3    Shibata, M.4    Nakano, R.5    Yamane-Ohnuki, N.6    Wakitani, M.7    Yano, K.8    Shitara, K.9    Satoh, M.10
  • 36
    • 0030811894 scopus 로고    scopus 로고
    • Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer
    • DOI 10.1023/A:1018532409041
    • Kannagi R (1997) Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer. Glycoconj J 14:577-584 (Pubitemid 27353201)
    • (1997) Glycoconjugate Journal , vol.14 , Issue.5 , pp. 577-584
    • Kannagi, R.1
  • 41
    • 0000656065 scopus 로고    scopus 로고
    • Regulation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines
    • Ko JH, Miyoshi E, Noda K, Ekuni A, Kang R, Ikeda Y, Taniguchi N (1999) Regulation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines. J Biol Chem 274:22941-22948
    • (1999) J Biol Chem , vol.274 , pp. 22941-22948
    • Ko, J.H.1    Miyoshi, E.2    Noda, K.3    Ekuni, A.4    Kang, R.5    Ikeda, Y.6    Taniguchi, N.7
  • 42
    • 78149457418 scopus 로고    scopus 로고
    • Protein glycosylation-an evolutionary crossroad between genes and environment
    • Lauc G, Zoldos V (2010) Protein glycosylation-an evolutionary crossroad between genes and environment. Mol Biosyst 6:2373-2379
    • (2010) Mol Biosyst , vol.6 , pp. 2373-2379
    • Lauc, G.1    Zoldos, V.2
  • 43
    • 75749136871 scopus 로고    scopus 로고
    • Complex genetic regulation of protein glycosylation
    • Lauc G, Rudan I, Campbell H, Rudd PM (2010) Complex genetic regulation of protein glycosylation. Mol Biosyst 6:329-335
    • (2010) Mol Biosyst , vol.6 , pp. 329-335
    • Lauc, G.1    Rudan, I.2    Campbell, H.3    Rudd, P.M.4
  • 44
    • 57449116570 scopus 로고    scopus 로고
    • The prospects of glycan biomarkers for the diagnosis of diseases
    • Lebrilla CB, An HJ (2009) The prospects of glycan biomarkers for the diagnosis of diseases. Mol Biosyst 5:17-20
    • (2009) Mol Biosyst , vol.5 , pp. 17-20
    • Lebrilla, C.B.1    An, H.J.2
  • 45
    • 27844500647 scopus 로고    scopus 로고
    • Glycoproteomics: Protein modifications for versatile functions
    • DOI 10.1038/sj.embor.7400556, PII 7400556
    • Lee RT, Lauc G, Lee YC (2005) Glycoproteomics: protein modifications for versatile functions. EMBO Rep 6:1018-1022 (Pubitemid 41637644)
    • (2005) EMBO Reports , vol.6 , Issue.11 , pp. 1018-1022
    • Lee, R.T.1    Lauc, G.2    Lee, Y.C.3
  • 46
    • 0032743959 scopus 로고    scopus 로고
    • A recessive deletion in the GlcNAc-1-phosphotransferase gene results in peri-implantation embryonic lethality
    • Marek KW, Vijay IK, Marth JD (1999) A recessive deletion in the GlcNAc-1-phosphotransferase gene results in peri-implantation embryonic lethality. Glycobiology 9:1263-1271
    • (1999) Glycobiology , vol.9 , pp. 1263-1271
    • Marek, K.W.1    Vijay, I.K.2    Marth, J.D.3
  • 47
    • 54949106904 scopus 로고    scopus 로고
    • Mammalian glycosylation in immunity
    • Marth JD, Grewal PK (2008) Mammalian glycosylation in immunity. Nat Rev Immunol 8:874-887
    • (2008) Nat Rev Immunol , vol.8 , pp. 874-887
    • Marth, J.D.1    Grewal, P.K.2
  • 50
    • 78651238405 scopus 로고    scopus 로고
    • The effect of epigenetic regulation of fucosylation on TRAIL-induced apoptosis
    • Moriwaki K, Narisada M, Imai T, Shinzaki S and Miyoshi E (2010) The effect of epigenetic regulation of fucosylation on TRAIL-induced apoptosis. Glycoconj J 27(7-9):649-659
    • (2010) Glycoconj J , vol.27 , Issue.7-9 , pp. 649-659
    • Moriwaki, K.1    Narisada, M.2    Imai, T.3    Shinzaki, S.4    Miyoshi, E.5
  • 51
    • 47749097124 scopus 로고    scopus 로고
    • Regulation of glycan structures in animal tissues: Transcript profiling of glycan-related genes
    • Nairn AV, York WS, Harris K, Hall EM, Pierce JM, Moremen KW (2008) Regulation of glycan structures in animal tissues: transcript profiling of glycan-related genes. J Biol Chem 283:17298-17313
    • (2008) J Biol Chem , vol.283 , pp. 17298-17313
    • Nairn, A.V.1    York, W.S.2    Harris, K.3    Hall, E.M.4    Pierce, J.M.5    Moremen, K.W.6
  • 52
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • DOI 10.1146/annurev.immunol.26.021607.090232
    • Nimmerjahn F, Ravetch JV (2008) Anti-inflammatory actions of intravenous immunoglobulin. Annu Rev Immunol 26:513-533 (Pubitemid 351600384)
    • (2008) Annual Review of Immunology , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 53
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in Cellular Mechanisms of Health and Disease
    • DOI 10.1016/j.cell.2006.08.019, PII S0092867406010865
    • Ohtsubo K, Marth JD (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126:855-867 (Pubitemid 44310784)
    • (2006) Cell , vol.126 , Issue.5 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 57
    • 30344434022 scopus 로고    scopus 로고
    • High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G
    • DOI 10.1016/j.molimm.2005.07.010, PII S0161589005002865
    • Preithner S, Elm S, Lippold S, Locher M, Wolf A, da Silva AJ, Baeuerle PA, Prang NS (2006) High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G. Mol Immunol 43:1183-1193 (Pubitemid 43063171)
    • (2006) Molecular Immunology , vol.43 , Issue.8 , pp. 1183-1193
    • Preithner, S.1    Elm, S.2    Lippold, S.3    Locher, M.4    Wolf, A.5    Silva, A.J.D.6    Baeuerle, P.A.7    Prang, N.S.8
  • 59
    • 33750942982 scopus 로고    scopus 로고
    • Epigenetic variation and inheritance in mammals
    • DOI 10.1016/j.gde.2006.09.002, PII S0959437X0600195X, Genomes and Evolution
    • Rakyan VK, Beck S (2006) Epigenetic variation and inheritance in mammals. Curr Opin Genet Dev 16:573-577 (Pubitemid 44738519)
    • (2006) Current Opinion in Genetics and Development , vol.16 , Issue.6 , pp. 573-577
    • Rakyan, V.K.1    Beck, S.2
  • 60
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • Reis CA, Osorio H, Silva L, Gomes C, David L (2010) Alterations in glycosylation as biomarkers for cancer detection. J Clin Pathol 63:322-329
    • (2010) J Clin Pathol , Issue.63 , pp. 322-329
    • Reis, C.A.1    Osorio, H.2    Silva, L.3    Gomes, C.4    David, L.5
  • 61
    • 33646193822 scopus 로고    scopus 로고
    • Inherited epigenetic variation-revisiting soft inheritance
    • Richards EJ (2006) Inherited epigenetic variation-revisiting soft inheritance. Nat Rev Genet 7:395-401
    • (2006) Nat Rev Genet , vol.7 , pp. 395-401
    • Richards, E.J.1
  • 62
    • 33749246714 scopus 로고    scopus 로고
    • a in gastric cancer cell lines depends on FUT3 expression regulated by promoter methylation
    • DOI 10.1016/j.canlet.2005.11.009, PII S0304383505009882
    • Serpa J, Mesquita P, Mendes N, Oliveira C, Almeida R, Santos-Silva F, Reis CA, LePendu J, David L (2006) Expression of Lea in gastric cancer cell lines depends on FUT3 expression regulated by promoter methylation. Cancer Lett 242:191-197 (Pubitemid 44485309)
    • (2006) Cancer Letters , vol.242 , Issue.2 , pp. 191-197
    • Serpa, J.1    Mesquita, P.2    Mendes, N.3    Oliveira, C.4    Almeida, R.5    Santos-Silva, F.6    Reis, C.A.7    LePendu, J.8    David, L.9
  • 63
  • 64
    • 63149160691 scopus 로고    scopus 로고
    • The effect of individual N-glycans on enzyme activity
    • Skropeta D (2009) The effect of individual N-glycans on enzyme activity. Bioorg Med Chem 17:2645-2653
    • (2009) Bioorg Med Chem , vol.17 , pp. 2645-2653
    • Skropeta, D.1
  • 65
    • 8644250670 scopus 로고    scopus 로고
    • + T cells: Evidence for epigenetic regulation of involved glycosyltransferase genes
    • DOI 10.1182/blood-2003-09-3047
    • Syrbe U, Jennrich S, Schottelius A, Richter A, Radbruch A, Hamann A (2004) Differential regulation of P-selectin ligand expression in naive versus memory CD4+ T cells: evidence for epigenetic regulation of involved glycosyltransferase genes. Blood 104:3243-3248 (Pubitemid 39507142)
    • (2004) Blood , vol.104 , Issue.10 , pp. 3243-3248
    • Syrbe, U.1    Jennrich, S.2    Schottelius, A.3    Richter, A.4    Radbruch, A.5    Hamann, A.6
  • 66
    • 0032869011 scopus 로고    scopus 로고
    • Implication of N-acetylglucosaminyltransferases III and V in cancer: Gene regulation and signaling mechanism
    • DOI 10.1016/S0925-4439(99)00066-6, PII S0925443999000666
    • Taniguchi N, Miyoshi E, Ko JH, Ikeda Y, Ihara Y (1999) Implication of N-acetylglucosaminyltransferases III and V in cancer: gene regulation and signaling mechanism. Biochim Biophys Acta 1455:287-300 (Pubitemid 29435995)
    • (1999) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1455 , Issue.2-3 , pp. 287-300
    • Taniguchi, N.1    Miyoshi, E.2    Ko, J.H.3    Ikeda, Y.4    Ihara, Y.5
  • 68
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases
    • DOI 10.1093/glycob/cwg007
    • Ten Hagen KG, Fritz TA, Tabak LA (2003) All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13:1R-16R (Pubitemid 36372510)
    • (2003) Glycobiology , vol.13 , Issue.1
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 69
  • 70
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3:97-130 (Pubitemid 23132602)
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 71
    • 33748191656 scopus 로고    scopus 로고
    • Nothing in Glycobiology Makes Sense, except in the Light of Evolution
    • DOI 10.1016/j.cell.2006.08.022, PII S0092867406010890
    • Varki A (2006) Nothing in glycobiology makes sense, except in the light of evolution. Cell 126:841-845 (Pubitemid 44310787)
    • (2006) Cell , vol.126 , Issue.5 , pp. 841-845
    • Varki, A.1
  • 72
    • 29444437433 scopus 로고    scopus 로고
    • Siglecs - The major subfamily of I-type lectins
    • DOI 10.1093/glycob/cwj008
    • Varki A, Angata T (2006) Siglecs-the major subfamily of I-type lectins. Glycobiology 16:1R-27R (Pubitemid 43009801)
    • (2006) Glycobiology , vol.16 , Issue.1
    • Varki, A.1    Angata, T.2
  • 73
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • DOI 10.1093/glycob/cwj099
    • Weerapana E, Imperiali B (2006) Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 16:91R-101R (Pubitemid 43779042)
    • (2006) Glycobiology , vol.16 , Issue.6
    • Weerapana, E.1    Imperiali, B.2
  • 74
    • 84856274815 scopus 로고    scopus 로고
    • Epigenetic regulation of protein glycosylation
    • Zoldoš V, Grgurević S, Lauc G (2010) Epigenetic regulation of protein glycosylation. Biomol Concepts 1:253-261
    • (2010) Biomol Concepts , vol.1 , pp. 253-261
    • Zoldoš, V.1    Grgurević, S.2    Lauc, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.