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Volumn 6, Issue MAR, 2016, Pages

Glycomic approaches for the discovery of targets in gastrointestinal cancer

Author keywords

Colorectal cancer; Gastric cancer; Glycan biomarkers; Glycomics; Imaging mass spectrometry; Microarray; Pancreatic cancer; Proximity ligation assay

Indexed keywords

HERMES ANTIGEN;

EID: 84964430153     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2016.00055     Document Type: Review
Times cited : (47)

References (220)
  • 1
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • Reis CA, Osorio H, Silva L, Gomes C, David L. Alterations in glycosylation as biomarkers for cancer detection. J Clin Pathol (2010) 63(4):322-9. doi:10.1136/jcp.2009.071035
    • (2010) J Clin Pathol , vol.63 , Issue.4 , pp. 322-329
    • Reis, C.A.1    Osorio, H.2    Silva, L.3    Gomes, C.4    David, L.5
  • 2
    • 84940449986 scopus 로고    scopus 로고
    • Glycosylation in cancer: mechanisms and clinical implications
    • Pinho SS, Reis CA. Glycosylation in cancer: mechanisms and clinical implications. Nat Rev Cancer (2015) 15(9):540-55. doi:10.1038/nrc3982
    • (2015) Nat Rev Cancer , vol.15 , Issue.9 , pp. 540-555
    • Pinho, S.S.1    Reis, C.A.2
  • 3
    • 84921930328 scopus 로고    scopus 로고
    • Protein glycosylation in cancer
    • Stowell SR, Ju T, Cummings RD. Protein glycosylation in cancer. Annu Rev Pathol (2015) 10:473-510. doi:10.1146/annurev-pathol-012414-040438
    • (2015) Annu Rev Pathol , vol.10 , pp. 473-510
    • Stowell, S.R.1    Ju, T.2    Cummings, R.D.3
  • 4
    • 84858766894 scopus 로고    scopus 로고
    • Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer
    • Rabinovich GA, Croci DO. Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer. Immunity (2012) 36(3):322-35. doi:10.1016/j.immuni.2012.03.004
    • (2012) Immunity , vol.36 , Issue.3 , pp. 322-335
    • Rabinovich, G.A.1    Croci, D.O.2
  • 5
    • 84930909270 scopus 로고    scopus 로고
    • Cancer intelligence acquired (CIA): tumor glycosylation and sialylation codes dismantling antitumor defense
    • Boligan KF, Mesa C, Fernandez LE, von Gunten S. Cancer intelligence acquired (CIA): tumor glycosylation and sialylation codes dismantling antitumor defense. Cell Mol Life Sci (2015) 72(7):1231-48. doi:10.1007/s00018-014-1799-5
    • (2015) Cell Mol Life Sci , vol.72 , Issue.7 , pp. 1231-1248
    • Boligan, K.F.1    Mesa, C.2    Fernandez, L.E.3    von Gunten, S.4
  • 6
    • 0027093480 scopus 로고
    • Quantitation and structures of oligosaccharide chains in human trachea mucin glycoproteins
    • Sangadala S, Bhat UR, Mendicino J. Quantitation and structures of oligosaccharide chains in human trachea mucin glycoproteins. Mol Cell Biochem (1992) 118(1):75-90. doi:10.1007/BF00249697
    • (1992) Mol Cell Biochem , vol.118 , Issue.1 , pp. 75-90
    • Sangadala, S.1    Bhat, U.R.2    Mendicino, J.3
  • 7
    • 84923305209 scopus 로고    scopus 로고
    • Simple sugars to complex disease-mucin-type O-glycans in cancer
    • Kudelka MR, Ju T, Heimburg-Molinaro J, Cummings RD. Simple sugars to complex disease-mucin-type O-glycans in cancer. Adv Cancer Res (2015) 126:53-135. doi:10.1016/bs.acr.2014.11.002
    • (2015) Adv Cancer Res , vol.126 , pp. 53-135
    • Kudelka, M.R.1    Ju, T.2    Heimburg-Molinaro, J.3    Cummings, R.D.4
  • 8
    • 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(6):599-604. doi:10.1038/sj.embor.7400705
    • (2006) EMBO Rep , vol.7 , Issue.6 , pp. 599-604
    • Brockhausen, I.1
  • 9
    • 84860365843 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family
    • Bennett EP, Mandel U, Clausen H, Gerken TA, Fritz TA, Tabak LA. Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology (2012) 22(6):736-56. doi:10.1093/glycob/cwr182
    • (2012) Glycobiology , vol.22 , Issue.6 , pp. 736-756
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 10
    • 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 EP. A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation. Glycobiology (1996) 6(6):635-46. doi:10.1093/glycob/6.6.635
    • (1996) Glycobiology , vol.6 , Issue.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 11
    • 58149199902 scopus 로고    scopus 로고
    • Expression of UDP-N-acetyl-d-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 in gastric mucosa, intestinal metaplasia, and gastric carcinoma
    • Gomes J, Marcos NT, Berois N, Osinaga E, Magalhaes A, Pinto-de-Sousa J, et al. Expression of UDP-N-acetyl-d-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 in gastric mucosa, intestinal metaplasia, and gastric carcinoma. J Histochem Cytochem (2009) 57(1):79-86. doi:10.1369/jhc.2008.952283
    • (2009) J Histochem Cytochem , vol.57 , Issue.1 , pp. 79-86
    • Gomes, J.1    Marcos, N.T.2    Berois, N.3    Osinaga, E.4    Magalhaes, A.5    Pinto-de-Sousa, J.6
  • 12
    • 0036534006 scopus 로고    scopus 로고
    • Expression of UDP-N-acetyl-alpha-d-galactosamine-polypeptide galNAc N-acetylgalactosaminyl transferase-3 in relation to differentiation and prognosis in patients with colorectal carcinoma
    • Shibao K, Izumi H, Nakayama Y, Ohta R, Nagata N, Nomoto M, et al. Expression of UDP-N-acetyl-alpha-d-galactosamine-polypeptide galNAc N-acetylgalactosaminyl transferase-3 in relation to differentiation and prognosis in patients with colorectal carcinoma. Cancer (2002) 94(7):1939-46. doi:10.1002/cncr.10423
    • (2002) Cancer , vol.94 , Issue.7 , pp. 1939-1946
    • Shibao, K.1    Izumi, H.2    Nakayama, Y.3    Ohta, R.4    Nagata, N.5    Nomoto, M.6
  • 13
    • 82955237343 scopus 로고    scopus 로고
    • Overexpression of GalNAc-transferase GalNAc-T3 promotes pancreatic cancer cell growth
    • Taniuchi K, Cerny RL, Tanouchi A, Kohno K, Kotani N, Honke K, et al. Overexpression of GalNAc-transferase GalNAc-T3 promotes pancreatic cancer cell growth. Oncogene (2011) 30(49):4843-54. doi:10.1038/onc.2011.194
    • (2011) Oncogene , vol.30 , Issue.49 , pp. 4843-4854
    • Taniuchi, K.1    Cerny, R.L.2    Tanouchi, A.3    Kohno, K.4    Kotani, N.5    Honke, K.6
  • 14
    • 79952106660 scopus 로고    scopus 로고
    • Location, location, location: new insights into O-GalNAc protein glycosylation
    • Gill DJ, Clausen H, Bard F. Location, location, location: new insights into O-GalNAc protein glycosylation. Trends Cell Biol (2011) 21(3):149-58. doi:10.1016/j.tcb.2010.11.004
    • (2011) Trends Cell Biol , vol.21 , Issue.3 , pp. 149-158
    • Gill, D.J.1    Clausen, H.2    Bard, F.3
  • 15
    • 84869460432 scopus 로고    scopus 로고
    • Polypeptide N-acetylgalactosaminyltransferase 2 regulates cellular metastasis-associated behavior in gastric cancer
    • Hua D, Shen L, Xu L, Jiang Z, Zhou Y, Yue A, et al. Polypeptide N-acetylgalactosaminyltransferase 2 regulates cellular metastasis-associated behavior in gastric cancer. Int J Mol Med (2012) 30(6):1267-74. doi:10.3892/ijmm.2012.1130
    • (2012) Int J Mol Med , vol.30 , Issue.6 , pp. 1267-1274
    • Hua, D.1    Shen, L.2    Xu, L.3    Jiang, Z.4    Zhou, Y.5    Yue, A.6
  • 16
    • 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, Whitehouse C, McFarlane I, Brockhausen I, Gschmeissner S, Schwientek T, 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(14):11007-15. doi:10.1074/jbc. M006523200
    • (2001) J Biol Chem , vol.276 , Issue.14 , pp. 11007-11015
    • Dalziel, M.1    Whitehouse, C.2    McFarlane, I.3    Brockhausen, I.4    Gschmeissner, S.5    Schwientek, T.6
  • 17
    • 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 NT, Pinho S, Grandela C, Cruz A, Samyn-Petit B, Harduin-Lepers A, 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(19):7050-7. doi:10.1158/0008-5472.CAN-04-1921
    • (2004) Cancer Res , vol.64 , Issue.19 , pp. 7050-7057
    • Marcos, N.T.1    Pinho, S.2    Grandela, C.3    Cruz, A.4    Samyn-Petit, B.5    Harduin-Lepers, A.6
  • 19
    • 0026489010 scopus 로고
    • Simple mucin-type carbohydrate antigens (Tn, sialosyl-Tn and T) in gastric mucosa, carcinomas and metastases
    • David L, Nesland JM, Clausen H, Carneiro F, Sobrinho-Simoes M. Simple mucin-type carbohydrate antigens (Tn, sialosyl-Tn and T) in gastric mucosa, carcinomas and metastases. APMIS Suppl (1992) 27:162-72
    • (1992) APMIS Suppl , vol.27 , pp. 162-172
    • David, L.1    Nesland, J.M.2    Clausen, H.3    Carneiro, F.4    Sobrinho-Simoes, M.5
  • 20
    • 33947423328 scopus 로고    scopus 로고
    • Biological significance of cancer-associated sialyl-Tn antigen: modulation of malignant phenotype in gastric carcinoma cells
    • Pinho S, Marcos NT, Ferreira B, Carvalho AS, Oliveira MJ, Santos-Silva F, et al. Biological significance of cancer-associated sialyl-Tn antigen: modulation of malignant phenotype in gastric carcinoma cells. Cancer Lett (2007) 249(2):157-70. doi:10.1016/j.canlet.2006.08.010
    • (2007) Cancer Lett , vol.249 , Issue.2 , pp. 157-170
    • Pinho, S.1    Marcos, N.T.2    Ferreira, B.3    Carvalho, A.S.4    Oliveira, M.J.5    Santos-Silva, F.6
  • 24
    • 84930503944 scopus 로고    scopus 로고
    • COSMC knockdown mediated aberrant O-glycosylation promotes oncogenic properties in pancreatic cancer
    • Hofmann BT, Schluter L, Lange P, Mercanoglu B, Ewald F, Folster A, et al. COSMC knockdown mediated aberrant O-glycosylation promotes oncogenic properties in pancreatic cancer. Mol Cancer (2015) 14:109. doi:10.1186/s12943-015-0386-1
    • (2015) Mol Cancer , vol.14 , pp. 109
    • Hofmann, B.T.1    Schluter, L.2    Lange, P.3    Mercanoglu, B.4    Ewald, F.5    Folster, A.6
  • 25
    • 0037168608 scopus 로고    scopus 로고
    • A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase
    • Ju T, Cummings RD. A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase. Proc Natl Acad Sci U S A (2002) 99(26):16613-8. doi:10.1073/pnas.262438199
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.26 , pp. 16613-16618
    • Ju, T.1    Cummings, R.D.2
  • 26
    • 84901976686 scopus 로고    scopus 로고
    • Comprehensive glycomics comparison between colon cancer cell cultures and tumours: implications for biomarker studies
    • Chik JH, Zhou J, Moh ES, Christopherson R, Clarke SJ, Molloy MP, et al. Comprehensive glycomics comparison between colon cancer cell cultures and tumours: implications for biomarker studies. J Proteomics (2014) 108:146-62. doi:10.1016/j.jprot.2014.05.002
    • (2014) J Proteomics , vol.108 , pp. 146-162
    • Chik, J.H.1    Zhou, J.2    Moh, E.S.3    Christopherson, R.4    Clarke, S.J.5    Molloy, M.P.6
  • 27
    • 84899505287 scopus 로고    scopus 로고
    • C1GALT1 overexpression promotes the invasive behavior of colon cancer cells through modifying O-glycosylation of FGFR2
    • Hung JS, Huang J, Lin YC, Huang MJ, Lee PH, Lai HS, et al. C1GALT1 overexpression promotes the invasive behavior of colon cancer cells through modifying O-glycosylation of FGFR2. Oncotarget (2014) 5(8):2096-106. doi:10.18632/oncotarget.1815
    • (2014) Oncotarget , vol.5 , Issue.8 , pp. 2096-2106
    • Hung, J.S.1    Huang, J.2    Lin, Y.C.3    Huang, M.J.4    Lee, P.H.5    Lai, H.S.6
  • 28
    • 0030658888 scopus 로고    scopus 로고
    • Carcinoma-associated expression of core 2 beta-1,6-N-acetylglucosaminyltransferase gene in human colorectal cancer: role of O-glycans in tumor progression
    • Shimodaira K, Nakayama J, Nakamura N, Hasebe O, Katsuyama T, Fukuda M. Carcinoma-associated expression of core 2 beta-1,6-N-acetylglucosaminyltransferase gene in human colorectal cancer: role of O-glycans in tumor progression. Cancer Res (1997) 57(23):5201-6
    • (1997) Cancer Res , vol.57 , Issue.23 , pp. 5201-5206
    • Shimodaira, K.1    Nakayama, J.2    Nakamura, N.3    Hasebe, O.4    Katsuyama, T.5    Fukuda, M.6
  • 29
    • 84877096549 scopus 로고    scopus 로고
    • Aberrant expression of mucin core proteins and o-linked glycans associated with progression of pancreatic cancer
    • Remmers N, Anderson JM, Linde EM, DiMaio DJ, Lazenby AJ, Wandall HH, et al. Aberrant expression of mucin core proteins and o-linked glycans associated with progression of pancreatic cancer. Clin Cancer Res (2013) 19(8):1981-93. doi:10.1158/1078-0432.CCR-12-2662
    • (2013) Clin Cancer Res , vol.19 , Issue.8 , pp. 1981-1993
    • Remmers, N.1    Anderson, J.M.2    Linde, E.M.3    DiMaio, D.J.4    Lazenby, A.J.5    Wandall, H.H.6
  • 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, Kudo T, Kawamoto R, Kubota T, Togayachi A, Hiruma 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(12):4572-7. doi:10.1073/pnas.0407983102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.12 , pp. 4572-4577
    • Iwai, T.1    Kudo, T.2    Kawamoto, R.3    Kubota, T.4    Togayachi, A.5    Hiruma, T.6
  • 31
    • 84864445615 scopus 로고    scopus 로고
    • Almost all human gastric mucin O-glycans harbor blood group A, B or H antigens and are potential binding sites for Helicobacter pylori
    • Rossez Y, Maes E, Lefebvre Darroman T, Gosset P, Ecobichon C, Joncquel Chevalier Curt M, et al. Almost all human gastric mucin O-glycans harbor blood group A, B or H antigens and are potential binding sites for Helicobacter pylori. Glycobiology (2012) 22(9):1193-206. doi:10.1093/glycob/cws072
    • (2012) Glycobiology , vol.22 , Issue.9 , pp. 1193-1206
    • Rossez, Y.1    Maes, E.2    Lefebvre Darroman, T.3    Gosset, P.4    Ecobichon, C.5    Joncquel Chevalier Curt, M.6
  • 32
    • 84863190461 scopus 로고    scopus 로고
    • Presence of terminal N-acetylgalactosaminebeta1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: involvement in Helicobacter pylori colonization?
    • Kenny DT, Skoog EC, Linden SK, Struwe WB, Rudd PM, Karlsson NG. Presence of terminal N-acetylgalactosaminebeta1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: involvement in Helicobacter pylori colonization? Glycobiology (2012) 22(8):1077-85. doi:10.1093/glycob/cws076
    • (2012) Glycobiology , vol.22 , Issue.8 , pp. 1077-1085
    • Kenny, D.T.1    Skoog, E.C.2    Linden, S.K.3    Struwe, W.B.4    Rudd, P.M.5    Karlsson, N.G.6
  • 33
    • 0031875185 scopus 로고    scopus 로고
    • Expression of fully and under-glycosylated forms of MUC1 mucin in gastric carcinoma
    • Reis CA, David L, Seixas M, Burchell J, Sobrinho-Simoes M. Expression of fully and under-glycosylated forms of MUC1 mucin in gastric carcinoma. Int J Cancer (1998) 79(4):402-10. doi:10.1002/(SICI)1097-0215(19980821)79:4<402::AID-IJC16>3.0.CO;2-6
    • (1998) Int J Cancer , vol.79 , Issue.4 , pp. 402-410
    • Reis, C.A.1    David, L.2    Seixas, M.3    Burchell, J.4    Sobrinho-Simoes, M.5
  • 34
    • 54249093301 scopus 로고    scopus 로고
    • The implication of N-acetylglucosaminyltransferase V expression in gastric cancer
    • Tian H, Miyoshi E, Kawaguchi N, Shaker M, Ito Y, Taniguchi N, et al. The implication of N-acetylglucosaminyltransferase V expression in gastric cancer. Pathobiology (2008) 75(5):288-94. doi:10.1159/000151709
    • (2008) Pathobiology , vol.75 , Issue.5 , pp. 288-294
    • Tian, H.1    Miyoshi, E.2    Kawaguchi, N.3    Shaker, M.4    Ito, Y.5    Taniguchi, N.6
  • 35
    • 0034061923 scopus 로고    scopus 로고
    • Suppression of tumor growth and metastasis in Mgat5-deficient mice
    • Granovsky M, Fata J, Pawling J, Muller WJ, Khokha R, Dennis JW. Suppression of tumor growth and metastasis in Mgat5-deficient mice. Nat Med (2000) 6(3):306-12. doi:10.1038/73163
    • (2000) Nat Med , vol.6 , Issue.3 , pp. 306-312
    • Granovsky, M.1    Fata, J.2    Pawling, J.3    Muller, W.J.4    Khokha, R.5    Dennis, J.W.6
  • 36
    • 84857692860 scopus 로고    scopus 로고
    • Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics
    • Taniguchi N, Korekane H. Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics. BMB Rep (2011) 44(12):772-81. doi:10.5483/BMBRep.2011.44.12.772
    • (2011) BMB Rep , vol.44 , Issue.12 , pp. 772-781
    • Taniguchi, N.1    Korekane, H.2
  • 37
    • 84864378010 scopus 로고    scopus 로고
    • N-glycosylation of colorectal cancer tissues: a liquid chromatography and mass spectrometry-based investigation
    • Balog CI, Stavenhagen K, Fung WL, Koeleman CA, McDonnell LA, Verhoeven A, et al. N-glycosylation of colorectal cancer tissues: a liquid chromatography and mass spectrometry-based investigation. Mol Cell Proteomics (2012) 11(9):571-85. doi:10.1074/mcp. M111.011601
    • (2012) Mol Cell Proteomics , vol.11 , Issue.9 , pp. 571-585
    • Balog, C.I.1    Stavenhagen, K.2    Fung, W.L.3    Koeleman, C.A.4    McDonnell, L.A.5    Verhoeven, A.6
  • 38
    • 0032714567 scopus 로고    scopus 로고
    • Glycoprotein glycosylation and cancer progression
    • Dennis JW, Granovsky M, Warren CE. Glycoprotein glycosylation and cancer progression. Biochim Biophys Acta (1999) 1473(1):21-34. doi:10.1016/S0304-4165(99)00167-1
    • (1999) Biochim Biophys Acta , vol.1473 , Issue.1 , pp. 21-34
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 39
    • 0026014062 scopus 로고
    • Beta 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia
    • Fernandes B, Sagman U, Auger M, Demetrio M, Dennis JW. Beta 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia. Cancer Res (1991) 51(2):718-23
    • (1991) Cancer Res , vol.51 , Issue.2 , pp. 718-723
    • Fernandes, B.1    Sagman, U.2    Auger, M.3    Demetrio, M.4    Dennis, J.W.5
  • 40
    • 0032222421 scopus 로고    scopus 로고
    • Prognostic value of beta1,6-branched oligosaccharides in human colorectal carcinoma
    • Seelentag WK, Li WP, Schmitz SF, Metzger U, Aeberhard P, Heitz PU, et al. Prognostic value of beta1,6-branched oligosaccharides in human colorectal carcinoma. Cancer Res (1998) 58(23):5559-64
    • (1998) Cancer Res , vol.58 , Issue.23 , pp. 5559-5564
    • Seelentag, W.K.1    Li, W.P.2    Schmitz, S.F.3    Metzger, U.4    Aeberhard, P.5    Heitz, P.U.6
  • 41
    • 0034069025 scopus 로고    scopus 로고
    • Expression of N-acetylglucosaminyltransferase V in colorectal cancer correlates with metastasis and poor prognosis
    • Murata K, Miyoshi E, Kameyama M, Ishikawa O, Kabuto T, Sasaki Y, et al. Expression of N-acetylglucosaminyltransferase V in colorectal cancer correlates with metastasis and poor prognosis. Clin Cancer Res (2000) 6(5):1772-7
    • (2000) Clin Cancer Res , vol.6 , Issue.5 , pp. 1772-1777
    • Murata, K.1    Miyoshi, E.2    Kameyama, M.3    Ishikawa, O.4    Kabuto, T.5    Sasaki, Y.6
  • 42
    • 84909953198 scopus 로고    scopus 로고
    • Post-translational glycoprotein modifications regulate colon cancer stem cells and colon adenoma progression in Apc(min/+) mice through altered Wnt receptor signaling
    • Guo H, Nagy T, Pierce M. Post-translational glycoprotein modifications regulate colon cancer stem cells and colon adenoma progression in Apc(min/+) mice through altered Wnt receptor signaling. J Biol Chem (2014) 289(45):31534-49. doi:10.1074/jbc. M114.602680
    • (2014) J Biol Chem , vol.289 , Issue.45 , pp. 31534-31549
    • Guo, H.1    Nagy, T.2    Pierce, M.3
  • 43
    • 19944419437 scopus 로고    scopus 로고
    • A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer
    • Ishida H, Togayachi A, Sakai T, Iwai T, Hiruma T, Sato T, et al. A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer. FEBS Lett (2005) 579(1):71-8. doi:10.1016/j.febslet.2004.11.037
    • (2005) FEBS Lett , vol.579 , Issue.1 , pp. 71-78
    • Ishida, H.1    Togayachi, A.2    Sakai, T.3    Iwai, T.4    Hiruma, T.5    Sato, T.6
  • 44
    • 84937409236 scopus 로고    scopus 로고
    • Mass spectrometry-based N-linked glycomic profiling as a means for tracking pancreatic cancer metastasis
    • Park HM, Hwang MP, Kim YW, Kim KJ, Jin JM, Kim YH, et al. Mass spectrometry-based N-linked glycomic profiling as a means for tracking pancreatic cancer metastasis. Carbohydr Res (2015) 413:5-11. doi:10.1016/j.carres.2015.04.019
    • (2015) Carbohydr Res , vol.413 , pp. 5-11
    • Park, H.M.1    Hwang, M.P.2    Kim, Y.W.3    Kim, K.J.4    Jin, J.M.5    Kim, Y.H.6
  • 45
    • 33947581026 scopus 로고    scopus 로고
    • N-linked glycosylation profiling of pancreatic cancer serum using capillary liquid phase separation coupled with mass spectrometric analysis
    • Zhao J, Qiu W, Simeone DM, Lubman DM. N-linked glycosylation profiling of pancreatic cancer serum using capillary liquid phase separation coupled with mass spectrometric analysis. J Proteome Res (2007) 6(3):1126-38. doi:10.1021/pr0604458
    • (2007) J Proteome Res , vol.6 , Issue.3 , pp. 1126-1138
    • Zhao, J.1    Qiu, W.2    Simeone, D.M.3    Lubman, D.M.4
  • 46
    • 84867745007 scopus 로고    scopus 로고
    • Potential roles of N-glycosylation in cell adhesion
    • Gu J, Isaji T, Xu Q, Kariya Y, Gu W, Fukuda T, et al. Potential roles of N-glycosylation in cell adhesion. Glycoconj J (2012) 29(8-9):599-607. doi:10.1007/s10719-012-9386-1
    • (2012) Glycoconj J , vol.29 , Issue.8-9 , pp. 599-607
    • Gu, J.1    Isaji, T.2    Xu, Q.3    Kariya, Y.4    Gu, W.5    Fukuda, T.6
  • 47
    • 67649859659 scopus 로고    scopus 로고
    • The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin
    • Pinho SS, Reis CA, Paredes J, Magalhaes AM, Ferreira AC, Figueiredo J, et al. The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin. Hum Mol Genet (2009) 18(14):2599-608. doi:10.1093/hmg/ddp194
    • (2009) Hum Mol Genet , vol.18 , Issue.14 , pp. 2599-2608
    • Pinho, S.S.1    Reis, C.A.2    Paredes, J.3    Magalhaes, A.M.4    Ferreira, A.C.5    Figueiredo, J.6
  • 49
    • 61849083675 scopus 로고    scopus 로고
    • A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions
    • Gu J, Sato Y, Kariya Y, Isaji T, Taniguchi N, Fukuda T. A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions. J Proteome Res (2009) 8(2):431-5. doi:10.1021/pr800674g
    • (2009) J Proteome Res , vol.8 , Issue.2 , pp. 431-435
    • Gu, J.1    Sato, Y.2    Kariya, Y.3    Isaji, T.4    Taniguchi, N.5    Fukuda, T.6
  • 50
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • Yoshimura M, Ihara Y, Matsuzawa Y, Taniguchi N. Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J Biol Chem (1996) 271(23):13811-5. doi:10.1074/jbc.271.23.13811
    • (1996) J Biol Chem , vol.271 , Issue.23 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 51
    • 0035808365 scopus 로고    scopus 로고
    • The addition of bisecting N-acetylglucosamine residues to E-cadherin down-regulates the tyrosine phosphorylation of beta-catenin
    • Kitada T, Miyoshi E, Noda K, Higashiyama S, Ihara H, Matsuura N, et al. The addition of bisecting N-acetylglucosamine residues to E-cadherin down-regulates the tyrosine phosphorylation of beta-catenin. J Biol Chem (2001) 276(1):475-80. doi:10.1074/jbc. M006689200
    • (2001) J Biol Chem , vol.276 , Issue.1 , pp. 475-480
    • Kitada, T.1    Miyoshi, E.2    Noda, K.3    Higashiyama, S.4    Ihara, H.5    Matsuura, N.6
  • 52
    • 84873589547 scopus 로고    scopus 로고
    • E-cadherin and adherens-junctions stability in gastric carcinoma: functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V
    • Pinho SS, Figueiredo J, Cabral J, Carvalho S, Dourado J, Magalhaes A, et al. E-cadherin and adherens-junctions stability in gastric carcinoma: functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V. Biochim Biophys Acta (2013) 1830(3):2690-700. doi:10.1016/j.bbagen.2012.10.021
    • (2013) Biochim Biophys Acta , vol.1830 , Issue.3 , pp. 2690-2700
    • Pinho, S.S.1    Figueiredo, J.2    Cabral, J.3    Carvalho, S.4    Dourado, J.5    Magalhaes, A.6
  • 53
    • 84858138360 scopus 로고    scopus 로고
    • Loss and recovery of Mgat3 and GnT-III mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions
    • Pinho SS, Oliveira P, Cabral J, Carvalho S, Huntsman D, Gartner F, et al. Loss and recovery of Mgat3 and GnT-III mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions. PLoS One (2012) 7(3):e33191. doi:10.1371/journal.pone.0033191
    • (2012) PLoS One , vol.7 , Issue.3
    • Pinho, S.S.1    Oliveira, P.2    Cabral, J.3    Carvalho, S.4    Huntsman, D.5    Gartner, F.6
  • 54
    • 84860879220 scopus 로고    scopus 로고
    • Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1) in epithelial cell lines
    • Xu Q, Isaji T, Lu Y, Gu W, Kondo M, Fukuda T, et al. Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1) in epithelial cell lines. J Biol Chem (2012) 287(20):16563-74. doi:10.1074/jbc. M111.262154
    • (2012) J Biol Chem , vol.287 , Issue.20 , pp. 16563-16574
    • Xu, Q.1    Isaji, T.2    Lu, Y.3    Gu, W.4    Kondo, M.5    Fukuda, T.6
  • 55
    • 0037053318 scopus 로고    scopus 로고
    • Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching
    • Ihara S, Miyoshi E, Ko JH, Murata K, Nakahara S, Honke K, et al. Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching. J Biol Chem (2002) 277(19):16960-7. doi:10.1074/jbc. M200673200
    • (2002) J Biol Chem , vol.277 , Issue.19 , pp. 16960-16967
    • Ihara, S.1    Miyoshi, E.2    Ko, J.H.3    Murata, K.4    Nakahara, S.5    Honke, K.6
  • 56
    • 33845961737 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration
    • Zhao Y, Nakagawa T, Itoh S, Inamori K, Isaji T, Kariya Y, et al. N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration. J Biol Chem (2006) 281(43):32122-30. doi:10.1074/jbc. M607274200
    • (2006) J Biol Chem , vol.281 , Issue.43 , pp. 32122-32130
    • Zhao, Y.1    Nakagawa, T.2    Itoh, S.3    Inamori, K.4    Isaji, T.5    Kariya, Y.6
  • 57
    • 2442450486 scopus 로고    scopus 로고
    • Introduction of bisecting GlcNAc into integrin alpha5beta1 reduces ligand binding and down-regulates cell adhesion and cell migration
    • Isaji T, Gu J, Nishiuchi R, Zhao Y, Takahashi M, Miyoshi E, et al. Introduction of bisecting GlcNAc into integrin alpha5beta1 reduces ligand binding and down-regulates cell adhesion and cell migration. J Biol Chem (2004) 279(19):19747-54. doi:10.1074/jbc. M311627200
    • (2004) J Biol Chem , vol.279 , Issue.19 , pp. 19747-19754
    • Isaji, T.1    Gu, J.2    Nishiuchi, R.3    Zhao, Y.4    Takahashi, M.5    Miyoshi, E.6
  • 58
    • 66449112293 scopus 로고    scopus 로고
    • An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III
    • Sato Y, Isaji T, Tajiri M, Yoshida-Yamamoto S, Yoshinaka T, Somehara T, et al. An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III. J Biol Chem (2009) 284(18):11873-81. doi:10.1074/jbc. M807660200
    • (2009) J Biol Chem , vol.284 , Issue.18 , pp. 11873-11881
    • Sato, Y.1    Isaji, T.2    Tajiri, M.3    Yoshida-Yamamoto, S.4    Yoshinaka, T.5    Somehara, T.6
  • 59
    • 0035526267 scopus 로고    scopus 로고
    • Sialyltransferases in cancer
    • Dall'Olio F, Chiricolo M. Sialyltransferases in cancer. Glycoconj J (2001) 18(11-12):841-50. doi:10.1023/A:1022288022969
    • (2001) Glycoconj J , vol.18 , Issue.11-12 , pp. 841-850
    • Dall'Olio, F.1    Chiricolo, M.2
  • 60
    • 84897566999 scopus 로고    scopus 로고
    • Interactions between Siglec-7/9 receptors and ligands influence NK cell-dependent tumor immunosurveillance
    • Jandus C, Boligan KF, Chijioke O, Liu H, Dahlhaus M, Demoulins T, et al. Interactions between Siglec-7/9 receptors and ligands influence NK cell-dependent tumor immunosurveillance. J Clin Invest (2014) 124(4):1810-20. doi:10.1172/JCI65899
    • (2014) J Clin Invest , vol.124 , Issue.4 , pp. 1810-1820
    • Jandus, C.1    Boligan, K.F.2    Chijioke, O.3    Liu, H.4    Dahlhaus, M.5    Demoulins, T.6
  • 61
    • 84907588573 scopus 로고    scopus 로고
    • Engagement of myelomonocytic Siglecs by tumor-associated ligands modulates the innate immune response to cancer
    • Laubli H, Pearce OM, Schwarz F, Siddiqui SS, Deng L, Stanczak MA, et al. Engagement of myelomonocytic Siglecs by tumor-associated ligands modulates the innate immune response to cancer. Proc Natl Acad Sci U S A (2014) 111(39):14211-6. doi:10.1073/pnas.1409580111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.39 , pp. 14211-14216
    • Laubli, H.1    Pearce, O.M.2    Schwarz, F.3    Siddiqui, S.S.4    Deng, L.5    Stanczak, M.A.6
  • 62
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • Kim YJ, Varki A. Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj J (1997) 14(5):569-76. doi:10.1023/A:1018580324971
    • (1997) Glycoconj J , vol.14 , Issue.5 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 63
    • 84903589790 scopus 로고    scopus 로고
    • Sialosignaling: sialyltransferases as engines of self-fueling loops in cancer progression
    • Dall'Olio F, Malagolini N, Trinchera M, Chiricolo M. Sialosignaling: sialyltransferases as engines of self-fueling loops in cancer progression. Biochim Biophys Acta (2014) 1840(9):2752-64. doi:10.1016/j.bbagen.2014.06.006
    • (2014) Biochim Biophys Acta , vol.1840 , Issue.9 , pp. 2752-2764
    • Dall'Olio, F.1    Malagolini, N.2    Trinchera, M.3    Chiricolo, M.4
  • 64
    • 0034242133 scopus 로고    scopus 로고
    • Clinical correlations of alpha2,6-sialyltransferase expression in colorectal cancer patients
    • Lise M, Belluco C, Perera SP, Patel R, Thomas P, Ganguly A. Clinical correlations of alpha2,6-sialyltransferase expression in colorectal cancer patients. Hybridoma (2000) 19(4):281-6. doi:10.1089/027245700429828
    • (2000) Hybridoma , vol.19 , Issue.4 , pp. 281-286
    • Lise, M.1    Belluco, C.2    Perera, S.P.3    Patel, R.4    Thomas, P.5    Ganguly, A.6
  • 65
    • 0037648070 scopus 로고    scopus 로고
    • Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer
    • Gretschel S, Haensch W, Schlag PM, Kemmner W. Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer. Oncology (2003) 65(2):139-45. doi:10.1159/000072339
    • (2003) Oncology , vol.65 , Issue.2 , pp. 139-145
    • Gretschel, S.1    Haensch, W.2    Schlag, P.M.3    Kemmner, W.4
  • 66
    • 0032791947 scopus 로고    scopus 로고
    • Altered mRNA expression of glycosyltransferases in human gastric carcinomas
    • Petretti T, Schulze B, Schlag PM, Kemmner W. Altered mRNA expression of glycosyltransferases in human gastric carcinomas. Biochim Biophys Acta (1999) 1428(2-3):209-18. doi:10.1016/S0304-4165(99)00080-X
    • (1999) Biochim Biophys Acta , vol.1428 , Issue.2-3 , pp. 209-218
    • Petretti, T.1    Schulze, B.2    Schlag, P.M.3    Kemmner, W.4
  • 67
    • 84879165131 scopus 로고    scopus 로고
    • Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells
    • Gomes C, Osorio H, Pinto MT, Campos D, Oliveira MJ, Reis CA. Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells. PLoS One (2013) 8(6):e66737. doi:10.1371/journal.pone.0066737
    • (2013) PLoS One , vol.8 , Issue.6
    • Gomes, C.1    Osorio, H.2    Pinto, M.T.3    Campos, D.4    Oliveira, M.J.5    Reis, C.A.6
  • 68
    • 84879200371 scopus 로고    scopus 로고
    • alpha2,3-sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues
    • Perez-Garay M, Arteta B, Llop E, Cobler L, Pages L, Ortiz R, et al. alpha2,3-sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues. Int J Biochem Cell Biol (2013) 45(8):1748-57. doi:10.1016/j.biocel.2013.05.015
    • (2013) Int J Biochem Cell Biol , vol.45 , Issue.8 , pp. 1748-1757
    • Perez-Garay, M.1    Arteta, B.2    Llop, E.3    Cobler, L.4    Pages, L.5    Ortiz, R.6
  • 69
    • 77958523756 scopus 로고    scopus 로고
    • alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo
    • Perez-Garay M, Arteta B, Pages L, de Llorens R, de Bolos C, Vidal-Vanaclocha F, et al. alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo. PLoS One (2010) 5(9):e12524. doi:10.1371/journal.pone.0012524
    • (2010) PLoS One , vol.5 , Issue.9
    • Perez-Garay, M.1    Arteta, B.2    Pages, L.3    de Llorens, R.4    de Bolos, C.5    Vidal-Vanaclocha, F.6
  • 70
    • 84891556529 scopus 로고    scopus 로고
    • Cell surface sialic acid modulates extracellular matrix adhesion and migration in pancreatic adenocarcinoma cells
    • Bassaganas S, Perez-Garay M, Peracaula R. Cell surface sialic acid modulates extracellular matrix adhesion and migration in pancreatic adenocarcinoma cells. Pancreas (2014) 43(1):109-17. doi:10.1097/MPA.0b013e31829d9090
    • (2014) Pancreas , vol.43 , Issue.1 , pp. 109-117
    • Bassaganas, S.1    Perez-Garay, M.2    Peracaula, R.3
  • 71
    • 0033653099 scopus 로고    scopus 로고
    • Expression of Lewis(a), sialyl Lewis(a), Lewis(x) and sialyl Lewis(x) antigens as prognostic factors in patients with colorectal cancer
    • Nakagoe T, Fukushima K, Nanashima A, Sawai T, Tsuji T, Jibiki M, et al. Expression of Lewis(a), sialyl Lewis(a), Lewis(x) and sialyl Lewis(x) antigens as prognostic factors in patients with colorectal cancer. Can J Gastroenterol (2000) 14(9):753-60
    • (2000) Can J Gastroenterol , vol.14 , Issue.9 , pp. 753-760
    • Nakagoe, T.1    Fukushima, K.2    Nanashima, A.3    Sawai, T.4    Tsuji, T.5    Jibiki, M.6
  • 72
    • 0025806980 scopus 로고
    • Expression of various sialylated carbohydrate antigens in malignant and nonmalignant pancreatic tissues
    • Satomura Y, Sawabu N, Takemori Y, Ohta H, Watanabe H, Okai T, et al. Expression of various sialylated carbohydrate antigens in malignant and nonmalignant pancreatic tissues. Pancreas (1991) 6(4):448-58. doi:10.1097/00006676-199107000-00012
    • (1991) Pancreas , vol.6 , Issue.4 , pp. 448-458
    • Satomura, Y.1    Sawabu, N.2    Takemori, Y.3    Ohta, H.4    Watanabe, H.5    Okai, T.6
  • 73
    • 23844538187 scopus 로고    scopus 로고
    • Role of sialyltransferases involved in the biosynthesis of Lewis antigens in human pancreatic tumour cells
    • Peracaula R, Tabares G, Lopez-Ferrer A, Brossmer R, de Bolos C, de Llorens R. Role of sialyltransferases involved in the biosynthesis of Lewis antigens in human pancreatic tumour cells. Glycoconj J (2005) 22(3):135-44. doi:10.1007/s10719-005-0734-2
    • (2005) Glycoconj J , vol.22 , Issue.3 , pp. 135-144
    • Peracaula, R.1    Tabares, G.2    Lopez-Ferrer, A.3    Brossmer, R.4    de Bolos, C.5    de Llorens, R.6
  • 74
    • 0036244496 scopus 로고    scopus 로고
    • Predictive factors for preoperative serum levels of sialy Lewis(x), sialyl Lewis(a) and sialyl Tn antigens in gastric cancer patients
    • Nakagoe T, Sawai T, Tsuji T, Jibiki MA, Nanashima A, Yamaguchi H, et al. Predictive factors for preoperative serum levels of sialy Lewis(x), sialyl Lewis(a) and sialyl Tn antigens in gastric cancer patients. Anticancer Res (2002) 22(1A):451-8
    • (2002) Anticancer Res , vol.22 , Issue.1 , pp. 451-458
    • Nakagoe, T.1    Sawai, T.2    Tsuji, T.3    Jibiki, M.A.4    Nanashima, A.5    Yamaguchi, H.6
  • 75
    • 0031937018 scopus 로고    scopus 로고
    • Dimeric sialyl-Le(x) expression in gastric carcinoma correlates with venous invasion and poor outcome
    • Amado M, Carneiro F, Seixas M, Clausen H, Sobrinho-Simoes M. Dimeric sialyl-Le(x) expression in gastric carcinoma correlates with venous invasion and poor outcome. Gastroenterology (1998) 114(3):462-70. doi:10.1016/S0016-5085(98)70529-3
    • (1998) Gastroenterology , vol.114 , Issue.3 , pp. 462-470
    • Amado, M.1    Carneiro, F.2    Seixas, M.3    Clausen, H.4    Sobrinho-Simoes, M.5
  • 76
    • 7844240122 scopus 로고    scopus 로고
    • Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: sialosyl-Lewis(a), sialosyl-Lewis(x) and sialosyl-Tn
    • Baldus SE, Zirbes TK, Monig SP, Engel S, Monaca E, Rafiqpoor K, et al. Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: sialosyl-Lewis(a), sialosyl-Lewis(x) and sialosyl-Tn. Tumour Biol (1998) 19(6):445-53. doi:10.1159/000030036
    • (1998) Tumour Biol , vol.19 , Issue.6 , pp. 445-453
    • Baldus, S.E.1    Zirbes, T.K.2    Monig, S.P.3    Engel, S.4    Monaca, E.5    Rafiqpoor, K.6
  • 77
    • 0027250266 scopus 로고
    • Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: clinicopathological and immunohistochemical study
    • Nakamori S, Kameyama M, Imaoka S, Furukawa H, Ishikawa O, Sasaki Y, et al. Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: clinicopathological and immunohistochemical study. Cancer Res (1993) 53(15):3632-7
    • (1993) Cancer Res , vol.53 , Issue.15 , pp. 3632-3637
    • Nakamori, S.1    Kameyama, M.2    Imaoka, S.3    Furukawa, H.4    Ishikawa, O.5    Sasaki, Y.6
  • 78
    • 0028048830 scopus 로고
    • The selectins and their ligands
    • Rosen SD, Bertozzi CR. The selectins and their ligands. Curr Opin Cell Biol (1994) 6(5):663-73. doi:10.1016/0955-0674(94)90092-2
    • (1994) Curr Opin Cell Biol , vol.6 , Issue.5 , pp. 663-673
    • Rosen, S.D.1    Bertozzi, C.R.2
  • 79
    • 84952685671 scopus 로고    scopus 로고
    • Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer
    • Mereiter S, Magalhaes A, Adamczyk B, Jin C, Almeida A, Drici L, et al. Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer. Biochim Biophys Acta (2015). doi:10.1016/j.bbagen.2015.12.016
    • (2015) Biochim Biophys Acta
    • Mereiter, S.1    Magalhaes, A.2    Adamczyk, B.3    Jin, C.4    Almeida, A.5    Drici, L.6
  • 80
    • 36749041486 scopus 로고    scopus 로고
    • Altered expression of the RON receptor tyrosine kinase in various epithelial cancers and its contribution to tumourigenic phenotypes in thyroid cancer cells
    • Wang MH, Lee W, Luo YL, Weis MT, Yao HP. Altered expression of the RON receptor tyrosine kinase in various epithelial cancers and its contribution to tumourigenic phenotypes in thyroid cancer cells. J Pathol (2007) 213(4):402-11. doi:10.1002/path.2245
    • (2007) J Pathol , vol.213 , Issue.4 , pp. 402-411
    • Wang, M.H.1    Lee, W.2    Luo, Y.L.3    Weis, M.T.4    Yao, H.P.5
  • 81
    • 74449090319 scopus 로고    scopus 로고
    • The Ron receptor tyrosine kinase positively regulates angiogenic chemokine production in prostate cancer cells
    • Thobe MN, Gurusamy D, Pathrose P, Waltz SE. The Ron receptor tyrosine kinase positively regulates angiogenic chemokine production in prostate cancer cells. Oncogene (2010) 29(2):214-26. doi:10.1038/onc.2009.331
    • (2010) Oncogene , vol.29 , Issue.2 , pp. 214-226
    • Thobe, M.N.1    Gurusamy, D.2    Pathrose, P.3    Waltz, S.E.4
  • 82
    • 76249113994 scopus 로고    scopus 로고
    • Silencing of RON receptor signaling promotes apoptosis and gemcitabine sensitivity in pancreatic cancers
    • Logan-Collins J, Thomas RM, Yu P, Jaquish D, Mose E, French R, et al. Silencing of RON receptor signaling promotes apoptosis and gemcitabine sensitivity in pancreatic cancers. Cancer Res (2010) 70(3):1130-40. doi:10.1158/0008-5472.CAN-09-0761
    • (2010) Cancer Res , vol.70 , Issue.3 , pp. 1130-1140
    • Logan-Collins, J.1    Thomas, R.M.2    Yu, P.3    Jaquish, D.4    Mose, E.5    French, R.6
  • 83
    • 77956039906 scopus 로고    scopus 로고
    • Ron receptor tyrosine kinase activation confers resistance to tamoxifen in breast cancer cell lines
    • McClaine RJ, Marshall AM, Wagh PK, Waltz SE. Ron receptor tyrosine kinase activation confers resistance to tamoxifen in breast cancer cell lines. Neoplasia (2010) 12(8):650-8. doi:10.1593/neo.10476
    • (2010) Neoplasia , vol.12 , Issue.8 , pp. 650-658
    • McClaine, R.J.1    Marshall, A.M.2    Wagh, P.K.3    Waltz, S.E.4
  • 84
    • 79959897520 scopus 로고    scopus 로고
    • RON (MST1R) is a novel prognostic marker and therapeutic target for gastroesophageal adenocarcinoma
    • Catenacci DV, Cervantes G, Yala S, Nelson EA, El-Hashani E, Kanteti R, et al. RON (MST1R) is a novel prognostic marker and therapeutic target for gastroesophageal adenocarcinoma. Cancer Biol Ther (2011) 12(1):9-46. doi:10.4161/cbt.12.1.15747
    • (2011) Cancer Biol Ther , vol.12 , Issue.1 , pp. 9-46
    • Catenacci, D.V.1    Cervantes, G.2    Yala, S.3    Nelson, E.A.4    El-Hashani, E.5    Kanteti, R.6
  • 85
    • 84921524523 scopus 로고    scopus 로고
    • Identification of potential pancreatic cancer serum markers: increased sialyl-Lewis X on ceruloplasmin
    • Balmana M, Sarrats A, Llop E, Barrabes S, Saldova R, Ferri MJ, et al. Identification of potential pancreatic cancer serum markers: increased sialyl-Lewis X on ceruloplasmin. Clin Chim Acta (2015) 442:56-62. doi:10.1016/j.cca.2015.01.007
    • (2015) Clin Chim Acta , vol.442 , pp. 56-62
    • Balmana, M.1    Sarrats, A.2    Llop, E.3    Barrabes, S.4    Saldova, R.5    Ferri, M.J.6
  • 86
    • 84890331323 scopus 로고    scopus 로고
    • Discovery of sialyl Lewis A and Lewis X modified protein cancer biomarkers using high density antibody arrays
    • Rho JH, Mead JR, Wright WS, Brenner DE, Stave JW, Gildersleeve JC, et al. Discovery of sialyl Lewis A and Lewis X modified protein cancer biomarkers using high density antibody arrays. J Proteomics (2014) 96:291-9. doi:10.1016/j.jprot.2013.10.030
    • (2014) J Proteomics , vol.96 , pp. 291-299
    • Rho, J.H.1    Mead, J.R.2    Wright, W.S.3    Brenner, D.E.4    Stave, J.W.5    Gildersleeve, J.C.6
  • 87
    • 84888586398 scopus 로고    scopus 로고
    • Increasing the alpha 2, 6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer
    • Park JJ, Lee M. Increasing the alpha 2, 6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer. Gut Liver (2013) 7(6):629-41. doi:10.5009/gnl.2013.7.6.629
    • (2013) Gut Liver , vol.7 , Issue.6 , pp. 629-641
    • Park, J.J.1    Lee, M.2
  • 88
    • 85016384924 scopus 로고    scopus 로고
    • Fucosylation is a promising target for cancer diagnosis and therapy
    • Miyoshi E, Moriwaki K, Terao N, Tan CC, Terao M, Nakagawa T, et al. Fucosylation is a promising target for cancer diagnosis and therapy. Biomolecules (2012) 2(1):34-45. doi:10.3390/biom2010034
    • (2012) Biomolecules , vol.2 , Issue.1 , pp. 34-45
    • Miyoshi, E.1    Moriwaki, K.2    Terao, N.3    Tan, C.C.4    Terao, M.5    Nakagawa, T.6
  • 89
    • 46349088505 scopus 로고    scopus 로고
    • Biological function of fucosylation in cancer biology
    • Miyoshi E, Moriwaki K, Nakagawa T. Biological function of fucosylation in cancer biology. J Biochem (2008) 143(6):725-9. doi:10.1093/jb/mvn011
    • (2008) J Biochem , vol.143 , Issue.6 , pp. 725-729
    • Miyoshi, E.1    Moriwaki, K.2    Nakagawa, T.3
  • 90
    • 0019457715 scopus 로고
    • Microheterogeneity of alpha-fetoprotein in patient serum as demonstrated by lectin affino-electrophoresis
    • Breborowicz J, Mackiewicz A, Breborowicz D. Microheterogeneity of alpha-fetoprotein in patient serum as demonstrated by lectin affino-electrophoresis. Scand J Immunol (1981) 14(1):15-20. doi:10.1111/j.1365-3083.1981.tb00179.x
    • (1981) Scand J Immunol , vol.14 , Issue.1 , pp. 15-20
    • Breborowicz, J.1    Mackiewicz, A.2    Breborowicz, D.3
  • 91
    • 84928825138 scopus 로고    scopus 로고
    • Elevated alpha-fetoprotein: differential diagnosis-hepatocellular carcinoma and other disorders
    • Wong RJ, Ahmed A, Gish RG. Elevated alpha-fetoprotein: differential diagnosis-hepatocellular carcinoma and other disorders. Clin Liver Dis (2015) 19(2):309-23. doi:10.1016/j.cld.2015.01.005
    • (2015) Clin Liver Dis , vol.19 , Issue.2 , pp. 309-323
    • Wong, R.J.1    Ahmed, A.2    Gish, R.G.3
  • 92
    • 84951189176 scopus 로고    scopus 로고
    • Increased alpha1-3 fucosylation of alpha-1-acid glycoprotein (AGP) in pancreatic cancer
    • Balmana M, Gimenez E, Puerta A, Llop E, Figueras J, Fort E, et al. Increased alpha1-3 fucosylation of alpha-1-acid glycoprotein (AGP) in pancreatic cancer. J Proteomics (2015) 132:144-54. doi:10.1016/j.jprot.2015.11.006
    • (2015) J Proteomics , vol.132 , pp. 144-154
    • Balmana, M.1    Gimenez, E.2    Puerta, A.3    Llop, E.4    Figueras, J.5    Fort, E.6
  • 93
    • 78650241976 scopus 로고    scopus 로고
    • The biosynthesis of the selectin-ligand sialyl Lewis x in colorectal cancer tissues is regulated by fucosyltransferase VI and can be inhibited by an RNA interference-based approach
    • Trinchera M, Malagolini N, Chiricolo M, Santini D, Minni F, Caretti A, et al. The biosynthesis of the selectin-ligand sialyl Lewis x in colorectal cancer tissues is regulated by fucosyltransferase VI and can be inhibited by an RNA interference-based approach. Int J Biochem Cell Biol (2011) 43(1):130-9. doi:10.1016/j.biocel.2010.10.004
    • (2011) Int J Biochem Cell Biol , vol.43 , Issue.1 , pp. 130-139
    • Trinchera, M.1    Malagolini, N.2    Chiricolo, M.3    Santini, D.4    Minni, F.5    Caretti, A.6
  • 94
    • 45549091249 scopus 로고    scopus 로고
    • Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot
    • Qiu Y, Patwa TH, Xu L, Shedden K, Misek DE, Tuck M, et al. Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot. J Proteome Res (2008) 7(4):1693-703. doi:10.1021/pr700706s
    • (2008) J Proteome Res , vol.7 , Issue.4 , pp. 1693-1703
    • Qiu, Y.1    Patwa, T.H.2    Xu, L.3    Shedden, K.4    Misek, D.E.5    Tuck, M.6
  • 95
    • 77955721192 scopus 로고    scopus 로고
    • alpha(1,2)Fucosylation in human colorectal carcinoma
    • Muinelo-Romay L, Gil-Martin E, Fernandez-Briera A. alpha(1,2)Fucosylation in human colorectal carcinoma. Oncol Lett (2010) 1(2):361-6. doi:10.3892/ol_00000064
    • (2010) Oncol Lett , vol.1 , Issue.2 , pp. 361-366
    • Muinelo-Romay, L.1    Gil-Martin, E.2    Fernandez-Briera, A.3
  • 96
    • 0033862773 scopus 로고    scopus 로고
    • Role of fucosyltransferases in the association between apomucin and Lewis antigen expression in normal and malignant gastric epithelium
    • Lopez-Ferrer A, de Bolos C, Barranco C, Garrido M, Isern J, Carlstedt I, et al. Role of fucosyltransferases in the association between apomucin and Lewis antigen expression in normal and malignant gastric epithelium. Gut (2000) 47(3):349-56. doi:10.1136/gut.47.3.349
    • (2000) Gut , vol.47 , Issue.3 , pp. 349-356
    • Lopez-Ferrer, A.1    de Bolos, C.2    Barranco, C.3    Garrido, M.4    Isern, J.5    Carlstedt, I.6
  • 97
    • 84918818967 scopus 로고    scopus 로고
    • Variation at ABO histo-blood group and FUT loci and diffuse and intestinal gastric cancer risk in a European population
    • Duell EJ, Bonet C, Munoz X, Lujan-Barroso L, Weiderpass E, Boutron-Ruault MC, et al. Variation at ABO histo-blood group and FUT loci and diffuse and intestinal gastric cancer risk in a European population. Int J Cancer (2015) 136(4):880-93. doi:10.1002/ijc.29034
    • (2015) Int J Cancer , vol.136 , Issue.4 , pp. 880-893
    • Duell, E.J.1    Bonet, C.2    Munoz, X.3    Lujan-Barroso, L.4    Weiderpass, E.5    Boutron-Ruault, M.C.6
  • 98
    • 84940455366 scopus 로고    scopus 로고
    • Helicobacter pylori chronic infection and mucosal inflammation switches the human gastric glycosylation pathways
    • Magalhaes A, Marcos-Pinto R, Nairn AV, Dela Rosa M, Ferreira RM, Junqueira-Neto S, et al. Helicobacter pylori chronic infection and mucosal inflammation switches the human gastric glycosylation pathways. Biochim Biophys Acta (2015) 1852(9):1928-39. doi:10.1016/j.bbadis.2015.07.001
    • (2015) Biochim Biophys Acta , vol.1852 , Issue.9 , pp. 1928-1939
    • Magalhaes, A.1    Marcos-Pinto, R.2    Nairn, A.V.3    Dela Rosa, M.4    Ferreira, R.M.5    Junqueira-Neto, S.6
  • 100
    • 65349145229 scopus 로고    scopus 로고
    • Core fucosylation of E-cadherin enhances cell-cell adhesion in human colon carcinoma WiDr cells
    • Osumi D, Takahashi M, Miyoshi E, Yokoe S, Lee SH, Noda K, et al. Core fucosylation of E-cadherin enhances cell-cell adhesion in human colon carcinoma WiDr cells. Cancer Sci (2009) 100(5):888-95. doi:10.1111/j.1349-7006.2009.01125.x
    • (2009) Cancer Sci , vol.100 , Issue.5 , pp. 888-895
    • Osumi, D.1    Takahashi, M.2    Miyoshi, E.3    Yokoe, S.4    Lee, S.H.5    Noda, K.6
  • 101
    • 84899648864 scopus 로고    scopus 로고
    • Decreased core-fucosylation contributes to malignancy in gastric cancer
    • Zhao YP, Xu XY, Fang M, Wang H, You Q, Yi CH, et al. Decreased core-fucosylation contributes to malignancy in gastric cancer. PLoS One (2014) 9(4):e94536. doi:10.1371/journal.pone.0094536
    • (2014) PLoS One , vol.9 , Issue.4
    • Zhao, Y.P.1    Xu, X.Y.2    Fang, M.3    Wang, H.4    You, Q.5    Yi, C.H.6
  • 102
    • 84918523488 scopus 로고    scopus 로고
    • Cancer metabolism and elevated O-GlcNAc in oncogenic signaling
    • Ma Z, Vosseller K. Cancer metabolism and elevated O-GlcNAc in oncogenic signaling. J Biol Chem (2014) 289(50):34457-65. doi:10.1074/jbc. R114.577718
    • (2014) J Biol Chem , vol.289 , Issue.50 , pp. 34457-34465
    • Ma, Z.1    Vosseller, K.2
  • 104
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
    • Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem (2011) 80:825-58. doi:10.1146/annurev-biochem-060608-102511
    • (2011) Annu Rev Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 105
    • 0036834748 scopus 로고    scopus 로고
    • The role of O-linked protein glycosylation in beta-cell dysfunction
    • Konrad RJ, Kudlow JE. The role of O-linked protein glycosylation in beta-cell dysfunction. Int J Mol Med (2002) 10(5):535-9. doi:10.3892/ijmm.10.5.535
    • (2002) Int J Mol Med , vol.10 , Issue.5 , pp. 535-539
    • Konrad, R.J.1    Kudlow, J.E.2
  • 106
    • 84878225772 scopus 로고    scopus 로고
    • Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-kappaB activity in pancreatic cancer cells
    • Ma Z, Vocadlo DJ, Vosseller K. Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-kappaB activity in pancreatic cancer cells. J Biol Chem (2013) 288(21):15121-30. doi:10.1074/jbc. M113.470047
    • (2013) J Biol Chem , vol.288 , Issue.21 , pp. 15121-15130
    • Ma, Z.1    Vocadlo, D.J.2    Vosseller, K.3
  • 107
    • 84930012265 scopus 로고    scopus 로고
    • Elevated O-GlcNAcylation promotes colonic inflammation and tumorigenesis by modulating NF-kappaB signaling
    • Yang YR, Kim DH, Seo YK, Park D, Jang HJ, Choi SY, et al. Elevated O-GlcNAcylation promotes colonic inflammation and tumorigenesis by modulating NF-kappaB signaling. Oncotarget (2015) 6(14):12529-42. doi:10.18632/oncotarget.3725
    • (2015) Oncotarget , vol.6 , Issue.14 , pp. 12529-12542
    • Yang, Y.R.1    Kim, D.H.2    Seo, Y.K.3    Park, D.4    Jang, H.J.5    Choi, S.Y.6
  • 108
    • 84923437834 scopus 로고    scopus 로고
    • Syndecans: from peripheral coreceptors to mainstream regulators of cell behaviour
    • Couchman JR, Gopal S, Lim HC, Norgaard S, Multhaupt HA. Syndecans: from peripheral coreceptors to mainstream regulators of cell behaviour. Int J Exp Pathol (2015) 96(1):1-10. doi:10.1111/iep.12112
    • (2015) Int J Exp Pathol , vol.96 , Issue.1 , pp. 1-10
    • Couchman, J.R.1    Gopal, S.2    Lim, H.C.3    Norgaard, S.4    Multhaupt, H.A.5
  • 109
    • 67650763171 scopus 로고    scopus 로고
    • Helicobacter pylori cag pathogenicity island-positive strains induce syndecan-4 expression in gastric epithelial cells
    • Magalhaes A, Marcos NT, Carvalho AS, David L, Figueiredo C, Bastos J, et al. Helicobacter pylori cag pathogenicity island-positive strains induce syndecan-4 expression in gastric epithelial cells. FEMS Immunol Med Microbiol (2009) 56(3):223-32. doi:10.1111/j.1574-695X.2009.00569.x
    • (2009) FEMS Immunol Med Microbiol , vol.56 , Issue.3 , pp. 223-232
    • Magalhaes, A.1    Marcos, N.T.2    Carvalho, A.S.3    David, L.4    Figueiredo, C.5    Bastos, J.6
  • 110
    • 45649085812 scopus 로고    scopus 로고
    • Helicobacter pylori induces beta3GnT5 in human gastric cell lines, modulating expression of the SabA ligand sialyl-Lewis x
    • Marcos NT, Magalhaes A, Ferreira B, Oliveira MJ, Carvalho AS, Mendes N, et al. Helicobacter pylori induces beta3GnT5 in human gastric cell lines, modulating expression of the SabA ligand sialyl-Lewis x. J Clin Invest (2008) 118(6):2325-36. doi:10.1172/JCI34324
    • (2008) J Clin Invest , vol.118 , Issue.6 , pp. 2325-2336
    • Marcos, N.T.1    Magalhaes, A.2    Ferreira, B.3    Oliveira, M.J.4    Carvalho, A.S.5    Mendes, N.6
  • 111
    • 0035915759 scopus 로고    scopus 로고
    • Epithelial and stromal syndecan-1 expression as predictor of outcome in patients with gastric cancer
    • Wiksten JP, Lundin J, Nordling S, Lundin M, Kokkola A, von Boguslawski K, et al. Epithelial and stromal syndecan-1 expression as predictor of outcome in patients with gastric cancer. Int J Cancer (2001) 95(1):1-6. doi:10.1002/1097-0215(20010120)95:1<1::AID-IJC1000>3.0.CO;2-5
    • (2001) Int J Cancer , vol.95 , Issue.1 , pp. 1-6
    • Wiksten, J.P.1    Lundin, J.2    Nordling, S.3    Lundin, M.4    Kokkola, A.5    von Boguslawski, K.6
  • 112
    • 84961289702 scopus 로고    scopus 로고
    • Syndecan-1 expression is associated with tumor size and EGFR expression in colorectal carcinoma: a clinicopathological study of 230 cases
    • Kim SY, Choi EJ, Yun JA, Jung ES, Oh ST, Kim JG, et al. Syndecan-1 expression is associated with tumor size and EGFR expression in colorectal carcinoma: a clinicopathological study of 230 cases. Int J Med Sci (2015) 12(2):92-9. doi:10.7150/ijms.10497
    • (2015) Int J Med Sci , vol.12 , Issue.2 , pp. 92-99
    • Kim, S.Y.1    Choi, E.J.2    Yun, J.A.3    Jung, E.S.4    Oh, S.T.5    Kim, J.G.6
  • 113
    • 0033856662 scopus 로고    scopus 로고
    • Syndecan-1 expression is up-regulated in pancreatic but not in other gastrointestinal cancers
    • Conejo JR, KleeffJ, Koliopanos A, Matsuda K, Zhu ZW, Goecke H, et al. Syndecan-1 expression is up-regulated in pancreatic but not in other gastrointestinal cancers. Int J Cancer (2000) 88(1):12-20. doi:10.1002/1097-0215(20001001)88:1<12::AID-IJC3>3.0.CO;2-T
    • (2000) Int J Cancer , vol.88 , Issue.1 , pp. 12-20
    • Conejo, J.R.1    Kleeff, J.2    Koliopanos, A.3    Matsuda, K.4    Zhu, Z.W.5    Goecke, H.6
  • 115
    • 0032213027 scopus 로고    scopus 로고
    • The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer
    • KleeffJ, Ishiwata T, Kumbasar A, Friess H, Buchler MW, Lander AD, et al. The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer. J Clin Invest (1998) 102(9):1662-73. doi:10.1172/JCI4105
    • (1998) J Clin Invest , vol.102 , Issue.9 , pp. 1662-1673
    • Kleeff, J.1    Ishiwata, T.2    Kumbasar, A.3    Friess, H.4    Buchler, M.W.5    Lander, A.D.6
  • 116
    • 84861373535 scopus 로고    scopus 로고
    • A KrasG12D-driven genetic mouse model of pancreatic cancer requires glypican-1 for efficient proliferation and angiogenesis
    • Whipple CA, Young AL, Korc M. A KrasG12D-driven genetic mouse model of pancreatic cancer requires glypican-1 for efficient proliferation and angiogenesis. Oncogene (2012) 31(20):2535-44. doi:10.1038/onc.2011.430
    • (2012) Oncogene , vol.31 , Issue.20 , pp. 2535-2544
    • Whipple, C.A.1    Young, A.L.2    Korc, M.3
  • 117
    • 38149063860 scopus 로고    scopus 로고
    • Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells
    • Aikawa T, Whipple CA, Lopez ME, Gunn J, Young A, Lander AD, et al. Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells. J Clin Invest (2008) 118(1):89-99. doi:10.1172/JCI32412
    • (2008) J Clin Invest , vol.118 , Issue.1 , pp. 89-99
    • Aikawa, T.1    Whipple, C.A.2    Lopez, M.E.3    Gunn, J.4    Young, A.5    Lander, A.D.6
  • 118
    • 84936980504 scopus 로고    scopus 로고
    • Glypican-1 identifies cancer exosomes and detects early pancreatic cancer
    • Melo SA, Luecke LB, Kahlert C, Fernandez AF, Gammon ST, Kaye J, et al. Glypican-1 identifies cancer exosomes and detects early pancreatic cancer. Nature (2015) 523(7559):177-82. doi:10.1038/nature14581
    • (2015) Nature , vol.523 , Issue.7559 , pp. 177-182
    • Melo, S.A.1    Luecke, L.B.2    Kahlert, C.3    Fernandez, A.F.4    Gammon, S.T.5    Kaye, J.6
  • 119
    • 78049336816 scopus 로고    scopus 로고
    • De novo expression of CD44 variants in sporadic and hereditary gastric cancer
    • da Cunha CB, Oliveira C, Wen X, Gomes B, Sousa S, Suriano G, et al. De novo expression of CD44 variants in sporadic and hereditary gastric cancer. Lab Invest (2010) 90(11):1604-14. doi:10.1038/labinvest.2010.155
    • (2010) Lab Invest , vol.90 , Issue.11 , pp. 1604-1614
    • da Cunha, C.B.1    Oliveira, C.2    Wen, X.3    Gomes, B.4    Sousa, S.5    Suriano, G.6
  • 120
    • 84930470850 scopus 로고    scopus 로고
    • Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery
    • Campos D, Freitas D, Gomes J, Magalhaes A, Steentoft C, Gomes C, et al. Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery. Mol Cell Proteomics (2015) 14(6):1616-29. doi:10.1074/mcp. M114.046862
    • (2015) Mol Cell Proteomics , vol.14 , Issue.6 , pp. 1616-1629
    • Campos, D.1    Freitas, D.2    Gomes, J.3    Magalhaes, A.4    Steentoft, C.5    Gomes, C.6
  • 121
    • 84925710321 scopus 로고    scopus 로고
    • Lysosomal degradation of CD44 mediates ceramide nanoliposome-induced anoikis and diminished extravasation in metastatic carcinoma cells
    • Haakenson JK, Khokhlatchev AV, Choi YJ, Linton SS, Zhang P, Zaki PM, et al. Lysosomal degradation of CD44 mediates ceramide nanoliposome-induced anoikis and diminished extravasation in metastatic carcinoma cells. J Biol Chem (2015) 290(13):8632-43. doi:10.1074/jbc. M114.609677
    • (2015) J Biol Chem , vol.290 , Issue.13 , pp. 8632-8643
    • Haakenson, J.K.1    Khokhlatchev, A.V.2    Choi, Y.J.3    Linton, S.S.4    Zhang, P.5    Zaki, P.M.6
  • 122
    • 40849088147 scopus 로고    scopus 로고
    • Roles of plasma membrane-associated sialidase NEU3 in human cancers
    • Miyagi T, Wada T, Yamaguchi K. Roles of plasma membrane-associated sialidase NEU3 in human cancers. Biochim Biophys Acta (2008) 1780(3):532-7. doi:10.1016/j.bbagen.2007.09.016
    • (2008) Biochim Biophys Acta , vol.1780 , Issue.3 , pp. 532-537
    • Miyagi, T.1    Wada, T.2    Yamaguchi, K.3
  • 123
    • 0036678137 scopus 로고    scopus 로고
    • Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
    • Kakugawa Y, Wada T, Yamaguchi K, Yamanami H, Ouchi K, Sato I, et al. Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Proc Natl Acad Sci U S A (2002) 99(16):10718-23. doi:10.1073/pnas.152597199
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.16 , pp. 10718-10723
    • Kakugawa, Y.1    Wada, T.2    Yamaguchi, K.3    Yamanami, H.4    Ouchi, K.5    Sato, I.6
  • 124
    • 84925957244 scopus 로고    scopus 로고
    • Sialidase NEU3 contributes neoplastic potential on colon cancer cells as a key modulator of gangliosides by regulating Wnt signaling
    • Takahashi K, Hosono M, Sato I, Hata K, Wada T, Yamaguchi K, et al. Sialidase NEU3 contributes neoplastic potential on colon cancer cells as a key modulator of gangliosides by regulating Wnt signaling. Int J Cancer (2015) 137(7):1560-73. doi:10.1002/ijc.29527
    • (2015) Int J Cancer , vol.137 , Issue.7 , pp. 1560-1573
    • Takahashi, K.1    Hosono, M.2    Sato, I.3    Hata, K.4    Wada, T.5    Yamaguchi, K.6
  • 125
    • 84887053047 scopus 로고    scopus 로고
    • Investigations on aberrant glycosylation of glycosphingolipids in colorectal cancer tissues using liquid chromatography and matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS)
    • Holst S, Stavenhagen K, Balog CI, Koeleman CA, McDonnell LM, Mayboroda OA, et al. Investigations on aberrant glycosylation of glycosphingolipids in colorectal cancer tissues using liquid chromatography and matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS). Mol Cell Proteomics (2013) 12(11):3081-93. doi:10.1074/mcp. M113.030387
    • (2013) Mol Cell Proteomics , vol.12 , Issue.11 , pp. 3081-3093
    • Holst, S.1    Stavenhagen, K.2    Balog, C.I.3    Koeleman, C.A.4    McDonnell, L.M.5    Mayboroda, O.A.6
  • 126
    • 0037156936 scopus 로고    scopus 로고
    • Serum CEA and CA 15-3 as prognostic factors in primary breast cancer
    • Ebeling FG, Stieber P, Untch M, Nagel D, Konecny GE, Schmitt UM, et al. Serum CEA and CA 15-3 as prognostic factors in primary breast cancer. Br J Cancer (2002) 86(8):1217-22. doi:10.1038/sj.bjc.6600248
    • (2002) Br J Cancer , vol.86 , Issue.8 , pp. 1217-1222
    • Ebeling, F.G.1    Stieber, P.2    Untch, M.3    Nagel, D.4    Konecny, G.E.5    Schmitt, U.M.6
  • 127
    • 36849069347 scopus 로고    scopus 로고
    • American Society of Clinical Oncology 2007 update of recommendations for the use of tumor markers in breast cancer
    • Harris L, Fritsche H, Mennel R, Norton L, Ravdin P, Taube S, et al. American Society of Clinical Oncology 2007 update of recommendations for the use of tumor markers in breast cancer. J Clin Oncol (2007) 25(33):5287-312. doi:10.1200/JCO.2007.14.2364
    • (2007) J Clin Oncol , vol.25 , Issue.33 , pp. 5287-5312
    • Harris, L.1    Fritsche, H.2    Mennel, R.3    Norton, L.4    Ravdin, P.5    Taube, S.6
  • 128
    • 0036828534 scopus 로고    scopus 로고
    • Serum tumor marker CA 15.3 and stage are the two most powerful predictors of survival in primary breast cancer
    • Kumpulainen EJ, Keskikuru RJ, Johansson RT. Serum tumor marker CA 15.3 and stage are the two most powerful predictors of survival in primary breast cancer. Breast Cancer Res Treat (2002) 76(2):95-102. doi:10.1023/A:1020514925143
    • (2002) Breast Cancer Res Treat , vol.76 , Issue.2 , pp. 95-102
    • Kumpulainen, E.J.1    Keskikuru, R.J.2    Johansson, R.T.3
  • 129
    • 54849429384 scopus 로고    scopus 로고
    • Long-term prognostic study of carcinoembryonic antigen (CEA) and carbohydrate antigen 15-3 (CA 15-3) in breast cancer
    • Uehara M, Kinoshita T, Hojo T, Akashi-Tanaka S, Iwamoto E, Fukutomi T. Long-term prognostic study of carcinoembryonic antigen (CEA) and carbohydrate antigen 15-3 (CA 15-3) in breast cancer. Int J Clin Oncol (2008) 13(5):447-51. doi:10.1007/s10147-008-0773-3
    • (2008) Int J Clin Oncol , vol.13 , Issue.5 , pp. 447-451
    • Uehara, M.1    Kinoshita, T.2    Hojo, T.3    Akashi-Tanaka, S.4    Iwamoto, E.5    Fukutomi, T.6
  • 130
    • 0033453299 scopus 로고    scopus 로고
    • Comparison of CEA, MCA, CA 15-3 and CA 27-29 in follow-up and monitoring therapeutic response in breast cancer patients
    • Lauro S, Trasatti L, Bordin F, Lanzetta G, Bria E, Gelibter A, et al. Comparison of CEA, MCA, CA 15-3 and CA 27-29 in follow-up and monitoring therapeutic response in breast cancer patients. Anticancer Res (1999) 19(4C):3511-5
    • (1999) Anticancer Res , vol.19 , Issue.4 , pp. 3511-3515
    • Lauro, S.1    Trasatti, L.2    Bordin, F.3    Lanzetta, G.4    Bria, E.5    Gelibter, A.6
  • 132
    • 33746836162 scopus 로고    scopus 로고
    • Guidelines for referral of the patient with an adnexal mass
    • Gostout BS, Brewer MA. Guidelines for referral of the patient with an adnexal mass. Clin Obstet Gynecol (2006) 49(3):448-58. doi:10.1097/00003081-200609000-00005
    • (2006) Clin Obstet Gynecol , vol.49 , Issue.3 , pp. 448-458
    • Gostout, B.S.1    Brewer, M.A.2
  • 133
    • 84873743426 scopus 로고    scopus 로고
    • Aberrant PSA glycosylation-a sweet predictor of prostate cancer
    • Gilgunn S, Conroy PJ, Saldova R, Rudd PM, O'Kennedy RJ. Aberrant PSA glycosylation-a sweet predictor of prostate cancer. Nat Rev Urol (2013) 10(2):99-107. doi:10.1038/nrurol.2012.258
    • (2013) Nat Rev Urol , vol.10 , Issue.2 , pp. 99-107
    • Gilgunn, S.1    Conroy, P.J.2    Saldova, R.3    Rudd, P.M.4    O'Kennedy, R.J.5
  • 134
    • 79951985619 scopus 로고    scopus 로고
    • Core fucosylation and alpha2-3 sialylation in serum N-glycome is significantly increased in prostate cancer comparing to benign prostate hyperplasia
    • Saldova R, Fan Y, Fitzpatrick JM, Watson RW, Rudd PM. Core fucosylation and alpha2-3 sialylation in serum N-glycome is significantly increased in prostate cancer comparing to benign prostate hyperplasia. Glycobiology (2011) 21(2):195-205. doi:10.1093/glycob/cwq147
    • (2011) Glycobiology , vol.21 , Issue.2 , pp. 195-205
    • Saldova, R.1    Fan, Y.2    Fitzpatrick, J.M.3    Watson, R.W.4    Rudd, P.M.5
  • 135
    • 0346880272 scopus 로고    scopus 로고
    • Diagnostic value of CA 19-9 in patients with pancreatic cancer and nonspecific gastrointestinal symptoms
    • SafiF, Schlosser W, Kolb G, Beger HG. Diagnostic value of CA 19-9 in patients with pancreatic cancer and nonspecific gastrointestinal symptoms. J Gastrointest Surg (1997) 1(2):106-12. doi:10.1016/S1091-255X(97)80097-2
    • (1997) J Gastrointest Surg , vol.1 , Issue.2 , pp. 106-112
    • Safi, F.1    Schlosser, W.2    Kolb, G.3    Beger, H.G.4
  • 136
    • 33846595479 scopus 로고    scopus 로고
    • ASCO 2006 update of recommendations for the use of tumor markers in gastrointestinal cancer
    • Locker GY, Hamilton S, Harris J, Jessup JM, Kemeny N, Macdonald JS, et al. ASCO 2006 update of recommendations for the use of tumor markers in gastrointestinal cancer. J Clin Oncol (2006) 24(33):5313-27. doi:10.1200/JCO.2006.08.2644
    • (2006) J Clin Oncol , vol.24 , Issue.33 , pp. 5313-5327
    • Locker, G.Y.1    Hamilton, S.2    Harris, J.3    Jessup, J.M.4    Kemeny, N.5    Macdonald, J.S.6
  • 137
    • 0035042086 scopus 로고    scopus 로고
    • The prognostic significance of preoperative serum CA 19-9 in patients with resectable gastric carcinoma: comparison with CEA
    • Duraker N, Celik AN. The prognostic significance of preoperative serum CA 19-9 in patients with resectable gastric carcinoma: comparison with CEA. J Surg Oncol (2001) 76(4):266-71. doi:10.1002/jso.1044
    • (2001) J Surg Oncol , vol.76 , Issue.4 , pp. 266-271
    • Duraker, N.1    Celik, A.N.2
  • 138
    • 84969422791 scopus 로고    scopus 로고
    • Tumor markers in pancreatic cancer: 2013
    • Shah UA, Saif MW. Tumor markers in pancreatic cancer: 2013. JOP (2013) 14(4):318-21. doi:10.6092/1590-8577/1653
    • (2013) JOP , vol.14 , Issue.4 , pp. 318-321
    • Shah, U.A.1    Saif, M.W.2
  • 139
    • 24744451447 scopus 로고    scopus 로고
    • Carcinoembryonic antigen in the staging and follow-up of patients with colorectal cancer
    • Goldstein MJ, Mitchell EP. Carcinoembryonic antigen in the staging and follow-up of patients with colorectal cancer. Cancer Invest (2005) 23(4):338-51. doi:10.1081/CNV-58878
    • (2005) Cancer Invest , vol.23 , Issue.4 , pp. 338-351
    • Goldstein, M.J.1    Mitchell, E.P.2
  • 140
    • 84937676063 scopus 로고    scopus 로고
    • Practice guideline for the surveillance of patients after curative treatment of colon and rectal cancer
    • Steele SR, Chang GJ, Hendren S, Weiser M, Irani J, Buie WD, et al. Practice guideline for the surveillance of patients after curative treatment of colon and rectal cancer. Dis Colon Rectum (2015) 58(8):713-25. doi:10.1097/DCR.0000000000000410
    • (2015) Dis Colon Rectum , vol.58 , Issue.8 , pp. 713-725
    • Steele, S.R.1    Chang, G.J.2    Hendren, S.3    Weiser, M.4    Irani, J.5    Buie, W.D.6
  • 141
    • 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, Adriaenssens E, Ottenberg K, Furlan A, Courtand G, Vercoutter-Edouart AS, 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(1):54-64. doi:10.1093/glycob/cwj033
    • (2006) Glycobiology , vol.16 , Issue.1 , pp. 54-64
    • Julien, S.1    Adriaenssens, E.2    Ottenberg, K.3    Furlan, A.4    Courtand, G.5    Vercoutter-Edouart, A.S.6
  • 142
    • 16844364289 scopus 로고    scopus 로고
    • Stable expression of sialyl-Tn antigen in T47-D cells induces a decrease of cell adhesion and an increase of cell migration
    • Julien S, Lagadec C, Krzewinski-Recchi MA, Courtand G, Le Bourhis X, Delannoy P. Stable expression of sialyl-Tn antigen in T47-D cells induces a decrease of cell adhesion and an increase of cell migration. Breast Cancer Res Treat (2005) 90(1):77-84. doi:10.1007/s10549-004-3137-3
    • (2005) Breast Cancer Res Treat , vol.90 , Issue.1 , pp. 77-84
    • Julien, S.1    Lagadec, C.2    Krzewinski-Recchi, M.A.3    Courtand, G.4    Le Bourhis, X.5    Delannoy, P.6
  • 143
    • 84904111274 scopus 로고    scopus 로고
    • Effect of ST3GAL 4 and FUT 7 on sialyl Lewis X synthesis and multidrug resistance in human acute myeloid leukemia
    • Ma H, Zhou H, Li P, Song X, Miao X, Li Y, et al. Effect of ST3GAL 4 and FUT 7 on sialyl Lewis X synthesis and multidrug resistance in human acute myeloid leukemia. Biochim Biophys Acta (2014) 1842(9):1681-92. doi:10.1016/j.bbadis.2014.06.014
    • (2014) Biochim Biophys Acta , vol.1842 , Issue.9 , pp. 1681-1692
    • Ma, H.1    Zhou, H.2    Li, P.3    Song, X.4    Miao, X.5    Li, Y.6
  • 144
    • 77956547393 scopus 로고    scopus 로고
    • Overexpression of fucosyltransferase IV promotes A431 cell proliferation through activating MAPK and PI3K/Akt signaling pathways
    • Yang XS, Liu S, Liu YJ, Liu JW, Liu TJ, Wang XQ, et al. Overexpression of fucosyltransferase IV promotes A431 cell proliferation through activating MAPK and PI3K/Akt signaling pathways. J Cell Physiol (2010) 225(2):612-9. doi:10.1002/jcp.22250
    • (2010) J Cell Physiol , vol.225 , Issue.2 , pp. 612-619
    • Yang, X.S.1    Liu, S.2    Liu, Y.J.3    Liu, J.W.4    Liu, T.J.5    Wang, X.Q.6
  • 145
    • 0034698077 scopus 로고    scopus 로고
    • The Asn-420-linked sugar chain in human epidermal growth factor receptor suppresses ligand-independent spontaneous oligomerization. Possible role of a specific sugar chain in controllable receptor activation
    • Tsuda T, Ikeda Y, Taniguchi N. The Asn-420-linked sugar chain in human epidermal growth factor receptor suppresses ligand-independent spontaneous oligomerization. Possible role of a specific sugar chain in controllable receptor activation. J Biol Chem (2000) 275(29):21988-94. doi:10.1074/jbc. M003400200
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 21988-21994
    • Tsuda, T.1    Ikeda, Y.2    Taniguchi, N.3
  • 146
    • 57349114162 scopus 로고    scopus 로고
    • The cell-cell adhesion molecule E-cadherin
    • van Roy F, Berx G. The cell-cell adhesion molecule E-cadherin. Cell Mol Life Sci (2008) 65(23):3756-88. doi:10.1007/s00018-008-8281-1
    • (2008) Cell Mol Life Sci , vol.65 , Issue.23 , pp. 3756-3788
    • van Roy, F.1    Berx, G.2
  • 148
    • 32344433111 scopus 로고    scopus 로고
    • Genetics, pathology, and clinics of familial gastric cancer
    • Oliveira C, Seruca R, Carneiro F. Genetics, pathology, and clinics of familial gastric cancer. Int J Surg Pathol (2006) 14(1):21-33. doi:10.1177/106689690601400105
    • (2006) Int J Surg Pathol , vol.14 , Issue.1 , pp. 21-33
    • Oliveira, C.1    Seruca, R.2    Carneiro, F.3
  • 149
    • 84937605601 scopus 로고    scopus 로고
    • Preventing E-cadherin aberrant N-glycosylation at Asn-554 improves its critical function in gastric cancer
    • Carvalho S, Catarino TA, Dias AM, Kato M, Almeida A, Hessling B, et al. Preventing E-cadherin aberrant N-glycosylation at Asn-554 improves its critical function in gastric cancer. Oncogene (2015). doi:10.1038/onc.2015.225
    • (2015) Oncogene
    • Carvalho, S.1    Catarino, T.A.2    Dias, A.M.3    Kato, M.4    Almeida, A.5    Hessling, B.6
  • 150
    • 79953721653 scopus 로고    scopus 로고
    • Modulation of E-cadherin function and dysfunction by N-glycosylation
    • Pinho SS, Seruca R, Gartner F, Yamaguchi Y, Gu J, Taniguchi N, et al. Modulation of E-cadherin function and dysfunction by N-glycosylation. Cell Mol Life Sci (2011) 68(6):1011-20. doi:10.1007/s00018-010-0595-0
    • (2011) Cell Mol Life Sci , vol.68 , Issue.6 , pp. 1011-1020
    • Pinho, S.S.1    Seruca, R.2    Gartner, F.3    Yamaguchi, Y.4    Gu, J.5    Taniguchi, N.6
  • 152
  • 153
    • 84862563760 scopus 로고    scopus 로고
    • Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells
    • Schjoldager KT, Vakhrushev SY, Kong Y, Steentoft C, Nudelman AS, Pedersen NB, et al. Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells. Proc Natl Acad Sci U S A (2012) 109(25):9893-8. doi:10.1073/pnas.1203563109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.25 , pp. 9893-9898
    • Schjoldager, K.T.1    Vakhrushev, S.Y.2    Kong, Y.3    Steentoft, C.4    Nudelman, A.S.5    Pedersen, N.B.6
  • 155
    • 84867426941 scopus 로고    scopus 로고
    • Site-specific protein O-glycosylation modulates proprotein processing-deciphering specific functions of the large polypeptide GalNAc-transferase gene family
    • Schjoldager KT, Clausen H. Site-specific protein O-glycosylation modulates proprotein processing-deciphering specific functions of the large polypeptide GalNAc-transferase gene family. Biochim Biophys Acta (2012) 1820(12):2079-94. doi:10.1016/j.bbagen.2012.09.014
    • (2012) Biochim Biophys Acta , vol.1820 , Issue.12 , pp. 2079-2094
    • Schjoldager, K.T.1    Clausen, H.2
  • 157
    • 83755205437 scopus 로고    scopus 로고
    • Analysis of glycans derived from glycoconjugates by capillary electrophoresis-mass spectrometry
    • Mechref Y. Analysis of glycans derived from glycoconjugates by capillary electrophoresis-mass spectrometry. Electrophoresis (2011) 32(24):3467-81. doi:10.1002/elps.201100342
    • (2011) Electrophoresis , vol.32 , Issue.24 , pp. 3467-3481
    • Mechref, Y.1
  • 158
    • 84943593972 scopus 로고    scopus 로고
    • In-depth N-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage-and EGFR-specific protein N-glycosylation
    • Sethi MK, Kim H, Park CK, Baker MS, Paik YK, Packer NH, et al. In-depth N-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage-and EGFR-specific protein N-glycosylation. Glycobiology (2015) 25(10):1064-78. doi:10.1093/glycob/cwv042
    • (2015) Glycobiology , vol.25 , Issue.10 , pp. 1064-1078
    • Sethi, M.K.1    Kim, H.2    Park, C.K.3    Baker, M.S.4    Paik, Y.K.5    Packer, N.H.6
  • 159
    • 79952389488 scopus 로고    scopus 로고
    • Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms
    • Bones J, Byrne JC, O'Donoghue N, McManus C, Scaife C, Boissin H, et al. Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms. J Proteome Res (2011) 10(3):1246-65. doi:10.1021/pr101036b
    • (2011) J Proteome Res , vol.10 , Issue.3 , pp. 1246-1265
    • Bones, J.1    Byrne, J.C.2    O'Donoghue, N.3    McManus, C.4    Scaife, C.5    Boissin, H.6
  • 160
    • 78650351800 scopus 로고    scopus 로고
    • Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation
    • Bones J, Mittermayr S, O'Donoghue N, Guttman A, Rudd PM. Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation. Anal Chem (2010) 82(24):10208-15. doi:10.1021/ac102860w
    • (2010) Anal Chem , vol.82 , Issue.24 , pp. 10208-10215
    • Bones, J.1    Mittermayr, S.2    O'Donoghue, N.3    Guttman, A.4    Rudd, P.M.5
  • 162
    • 84885038677 scopus 로고    scopus 로고
    • Clinical utility of high-throughput glycome analysis in patients with pancreatic cancer
    • Nouso K, Amano M, Ito YM, Miyahara K, Morimoto Y, Kato H, et al. Clinical utility of high-throughput glycome analysis in patients with pancreatic cancer. J Gastroenterol (2013) 48(10):1171-9. doi:10.1007/s00535-012-0732-7
    • (2013) J Gastroenterol , vol.48 , Issue.10 , pp. 1171-1179
    • Nouso, K.1    Amano, M.2    Ito, Y.M.3    Miyahara, K.4    Morimoto, Y.5    Kato, H.6
  • 163
    • 84863794084 scopus 로고    scopus 로고
    • Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins
    • Mann BF, Goetz JA, House MG, Schmidt CM, Novotny MV. Glycomic and proteomic profiling of pancreatic cyst fluids identifies hyperfucosylated lactosamines on the N-linked glycans of overexpressed glycoproteins. Mol Cell Proteomics (2012) 11(7):M111015792. doi:10.1074/mcp. M111.015792
    • (2012) Mol Cell Proteomics , vol.11 , Issue.7
    • Mann, B.F.1    Goetz, J.A.2    House, M.G.3    Schmidt, C.M.4    Novotny, M.V.5
  • 164
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • Kaji H, Saito H, Yamauchi Y, Shinkawa T, Taoka M, Hirabayashi J, et al. Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins. Nat Biotechnol (2003) 21(6):667-72. doi:10.1038/nbt829
    • (2003) Nat Biotechnol , vol.21 , Issue.6 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3    Shinkawa, T.4    Taoka, M.5    Hirabayashi, J.6
  • 165
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • Yang Z, Hancock WS. Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J Chromatogr A (2004) 1053(1-2):79-88. doi:10.1016/S0021-9673(04)01433-5
    • (2004) J Chromatogr A , vol.1053 , Issue.1-2 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 166
    • 33749537286 scopus 로고    scopus 로고
    • Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome
    • Durham M, Regnier FE. Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome. J Chromatogr A (2006) 1132(1-2):165-73. doi:10.1016/j.chroma.2006.07.070
    • (2006) J Chromatogr A , vol.1132 , Issue.1-2 , pp. 165-173
    • Durham, M.1    Regnier, F.E.2
  • 167
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H, Li XJ, Martin DB, Aebersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol (2003) 21(6):660-6. doi:10.1038/nbt827
    • (2003) Nat Biotechnol , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 168
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu T, Qian WJ, Gritsenko MA, Camp DG II, Monroe ME, Moore RJ, et al. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res (2005) 4(6):2070-80. doi:10.1021/pr0502065
    • (2005) J Proteome Res , vol.4 , Issue.6 , pp. 2070-2080
    • Liu, T.1    Qian, W.J.2    Gritsenko, M.A.3    Camp, D.G.4    Monroe, M.E.5    Moore, R.J.6
  • 169
    • 0016219421 scopus 로고
    • The binding of boronic acids to chymotrypsin
    • Rawn JD, Lienhard GE. The binding of boronic acids to chymotrypsin. Biochemistry (1974) 13(15):3124-30. doi:10.1021/bi00712a019
    • (1974) Biochemistry , vol.13 , Issue.15 , pp. 3124-3130
    • Rawn, J.D.1    Lienhard, G.E.2
  • 170
    • 33644841035 scopus 로고    scopus 로고
    • Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites
    • Alvarez-Manilla G, Atwood J III, Guo Y, Warren NL, Orlando R, Pierce M. Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites. J Proteome Res (2006) 5(3):701-8. doi:10.1021/pr050275j
    • (2006) J Proteome Res , vol.5 , Issue.3 , pp. 701-708
    • Alvarez-Manilla, G.1    Atwood, J.2    Guo, Y.3    Warren, N.L.4    Orlando, R.5    Pierce, M.6
  • 171
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund P, Bunkenborg J, Elortza F, Jensen ON, RoepstorffP. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J Proteome Res (2004) 3(3):556-66. doi:10.1021/pr034112b
    • (2004) J Proteome Res , vol.3 , Issue.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 172
    • 14944367556 scopus 로고    scopus 로고
    • Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry
    • Larsen MR, Hojrup P, RoepstorffP. Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry. Mol Cell Proteomics (2005) 4(2):107-19. doi:10.1074/mcp. M400068-MCP200
    • (2005) Mol Cell Proteomics , vol.4 , Issue.2 , pp. 107-119
    • Larsen, M.R.1    Hojrup, P.2    Roepstorff, P.3
  • 173
    • 33745827045 scopus 로고    scopus 로고
    • Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum
    • Zhao J, Simeone DM, Heidt D, Anderson MA, Lubman DM. Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum. J Proteome Res (2006) 5(7):1792-802. doi:10.1021/pr060034r
    • (2006) J Proteome Res , vol.5 , Issue.7 , pp. 1792-1802
    • Zhao, J.1    Simeone, D.M.2    Heidt, D.3    Anderson, M.A.4    Lubman, D.M.5
  • 174
    • 84964211695 scopus 로고    scopus 로고
    • Comprehensive protocol to simultaneously study protein phosphorylation, acetylation, and N-linked sialylated glycosylation
    • Melo-Braga MN, Ibanez-Vea M, Larsen MR, Kulej K. Comprehensive protocol to simultaneously study protein phosphorylation, acetylation, and N-linked sialylated glycosylation. Methods Mol Biol (2015) 1295:275-92. doi:10.1007/978-1-4939-2550-6_21
    • (2015) Methods Mol Biol , vol.1295 , pp. 275-292
    • Melo-Braga, M.N.1    Ibanez-Vea, M.2    Larsen, M.R.3    Kulej, K.4
  • 175
    • 0345598906 scopus 로고    scopus 로고
    • A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
    • Hang HC, Yu C, Kato DL, Bertozzi CR. A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc Natl Acad Sci U S A (2003) 100(25):14846-51. doi:10.1073/pnas.2335201100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.25 , pp. 14846-14851
    • Hang, H.C.1    Yu, C.2    Kato, D.L.3    Bertozzi, C.R.4
  • 176
    • 39149136217 scopus 로고    scopus 로고
    • Metabolic labeling of glycans with azido sugars and subsequent glycan-profiling and visualization via Staudinger ligation
    • Laughlin ST, Bertozzi CR. Metabolic labeling of glycans with azido sugars and subsequent glycan-profiling and visualization via Staudinger ligation. Nat Protoc (2007) 2(11):2930-44. doi:10.1038/nprot.2007.422
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2930-2944
    • Laughlin, S.T.1    Bertozzi, C.R.2
  • 177
    • 84942465452 scopus 로고    scopus 로고
    • Development of a novel method to evaluate sialylation of glycoproteins and analysis of gp96 sialylation in Hela, SW1990 and A549 cell lines
    • Liang Y, Hua Q, Pan P, Yang J, Zhang Q. Development of a novel method to evaluate sialylation of glycoproteins and analysis of gp96 sialylation in Hela, SW1990 and A549 cell lines. Biol Res (2015) 48:52. doi:10.1186/s40659-015-0041-8
    • (2015) Biol Res , vol.48 , pp. 52
    • Liang, Y.1    Hua, Q.2    Pan, P.3    Yang, J.4    Zhang, Q.5
  • 179
    • 70349113034 scopus 로고    scopus 로고
    • Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
    • An HJ, Froehlich JW, Lebrilla CB. Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. Curr Opin Chem Biol (2009) 13(4):421-6. doi:10.1016/j.cbpa.2009.07.022
    • (2009) Curr Opin Chem Biol , vol.13 , Issue.4 , pp. 421-426
    • An, H.J.1    Froehlich, J.W.2    Lebrilla, C.B.3
  • 180
    • 84958206500 scopus 로고    scopus 로고
    • The art of destruction: optimizing collision energies in quadrupole-time of flight (Q-TOF) instruments for glycopeptide-based glycoproteomics
    • Hinneburg H, Stavenhagen K, Schweiger-Hufnagel U, Pengelley S, Jabs W, Seeberger PH, et al. The art of destruction: optimizing collision energies in quadrupole-time of flight (Q-TOF) instruments for glycopeptide-based glycoproteomics. J Am Soc Mass Spectrom (2016) 27(3):507-19. doi:10.1007/s13361-015-1308-6
    • (2016) J Am Soc Mass Spectrom , vol.27 , Issue.3 , pp. 507-519
    • Hinneburg, H.1    Stavenhagen, K.2    Schweiger-Hufnagel, U.3    Pengelley, S.4    Jabs, W.5    Seeberger, P.H.6
  • 181
    • 84874635340 scopus 로고    scopus 로고
    • Glycoproteomic analysis of serum from patients with gastric precancerous lesions
    • Gomes C, Almeida A, Ferreira JA, Silva L, Santos-Sousa H, Pinto-de-Sousa J, et al. Glycoproteomic analysis of serum from patients with gastric precancerous lesions. J Proteome Res (2013) 12(3):1454-66. doi:10.1021/pr301112x
    • (2013) J Proteome Res , vol.12 , Issue.3 , pp. 1454-1466
    • Gomes, C.1    Almeida, A.2    Ferreira, J.A.3    Silva, L.4    Santos-Sousa, H.5    Pinto-de-Sousa, J.6
  • 182
    • 84875769040 scopus 로고    scopus 로고
    • In-depth research of multidrug resistance related cell surface glycoproteome in gastric cancer
    • Li K, Sun Z, Zheng J, Lu Y, Bian Y, Ye M, et al. In-depth research of multidrug resistance related cell surface glycoproteome in gastric cancer. J Proteomics (2013) 82:130-40. doi:10.1016/j.jprot.2013.02.021
    • (2013) J Proteomics , vol.82 , pp. 130-140
    • Li, K.1    Sun, Z.2    Zheng, J.3    Lu, Y.4    Bian, Y.5    Ye, M.6
  • 183
    • 0021049829 scopus 로고
    • Binding of cells to matrixes of distinct antibodies coated on solid surface
    • Chang TW. Binding of cells to matrixes of distinct antibodies coated on solid surface. J Immunol Methods (1983) 65(1-2):217-23. doi:10.1016/0022-1759(83)90318-6
    • (1983) J Immunol Methods , vol.65 , Issue.1-2 , pp. 217-223
    • Chang, T.W.1
  • 184
    • 79959503211 scopus 로고    scopus 로고
    • New technologies for glycomic analysis: toward a systematic understanding of the glycome
    • Rakus JF, Mahal LK. New technologies for glycomic analysis: toward a systematic understanding of the glycome. Annu Rev Anal Chem (Palo Alto Calif) (2011) 4:367-92. doi:10.1146/annurev-anchem-061010-113951
    • (2011) Annu Rev Anal Chem (Palo Alto Calif) , vol.4 , pp. 367-392
    • Rakus, J.F.1    Mahal, L.K.2
  • 185
    • 77957786881 scopus 로고    scopus 로고
    • Glycoprotein analysis using protein microarrays and mass spectrometry
    • Patwa T, Li C, Simeone DM, Lubman DM. Glycoprotein analysis using protein microarrays and mass spectrometry. Mass Spectrom Rev (2010) 29(5):830-44. doi:10.1002/mas.20269
    • (2010) Mass Spectrom Rev , vol.29 , Issue.5 , pp. 830-844
    • Patwa, T.1    Li, C.2    Simeone, D.M.3    Lubman, D.M.4
  • 186
    • 84902192402 scopus 로고    scopus 로고
    • Carbohydrate sequence of the prostate cancer-associated antigen F77 assigned by a mucin O-glycome designer array
    • Gao C, Liu Y, Zhang H, Zhang Y, Fukuda MN, Palma AS, et al. Carbohydrate sequence of the prostate cancer-associated antigen F77 assigned by a mucin O-glycome designer array. J Biol Chem (2014) 289(23):16462-77. doi:10.1074/jbc. M114.558932
    • (2014) J Biol Chem , vol.289 , Issue.23 , pp. 16462-16477
    • Gao, C.1    Liu, Y.2    Zhang, H.3    Zhang, Y.4    Fukuda, M.N.5    Palma, A.S.6
  • 187
    • 10344233222 scopus 로고    scopus 로고
    • Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
    • Blixt O, Head S, Mondala T, Scanlan C, Huflejt ME, Alvarez R, et al. Printed covalent glycan array for ligand profiling of diverse glycan binding proteins. Proc Natl Acad Sci U S A (2004) 101(49):17033-8. doi:10.1073/pnas.0407902101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.49 , pp. 17033-17038
    • Blixt, O.1    Head, S.2    Mondala, T.3    Scanlan, C.4    Huflejt, M.E.5    Alvarez, R.6
  • 188
    • 84920719200 scopus 로고    scopus 로고
    • The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites
    • Schneider C, Smith DF, Cummings RD, Boligan KF, Hamilton RG, Bochner BS, et al. The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites. Sci Transl Med (2015) 7(269):269ra1. doi:10.1126/scitranslmed.3010524
    • (2015) Sci Transl Med , vol.7 , Issue.269
    • Schneider, C.1    Smith, D.F.2    Cummings, R.D.3    Boligan, K.F.4    Hamilton, R.G.5    Bochner, B.S.6
  • 189
    • 45749142499 scopus 로고    scopus 로고
    • Carbohydrate arrays as tools for research and diagnostics
    • Horlacher T, Seeberger PH. Carbohydrate arrays as tools for research and diagnostics. Chem Soc Rev (2008) 37(7):1414-22. doi:10.1039/b708016f
    • (2008) Chem Soc Rev , vol.37 , Issue.7 , pp. 1414-1422
    • Horlacher, T.1    Seeberger, P.H.2
  • 190
    • 45049085821 scopus 로고    scopus 로고
    • Automated carbohydrate synthesis as platform to address fundamental aspects of glycobiology-current status and future challenges
    • Seeberger PH. Automated carbohydrate synthesis as platform to address fundamental aspects of glycobiology-current status and future challenges. Carbohydr Res (2008) 343(12):1889-96. doi:10.1016/j.carres.2008.05.023
    • (2008) Carbohydr Res , vol.343 , Issue.12 , pp. 1889-1896
    • Seeberger, P.H.1
  • 191
    • 0036193564 scopus 로고    scopus 로고
    • Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells
    • Wang D, Liu S, Trummer BJ, Deng C, Wang A. Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells. Nat Biotechnol (2002) 20(3):275-81. doi:10.1038/nbt0302-275
    • (2002) Nat Biotechnol , vol.20 , Issue.3 , pp. 275-281
    • Wang, D.1    Liu, S.2    Trummer, B.J.3    Deng, C.4    Wang, A.5
  • 192
    • 68149101314 scopus 로고    scopus 로고
    • Carbohydrate microarrays: key developments in glycobiology
    • Liu Y, Palma AS, Feizi T. Carbohydrate microarrays: key developments in glycobiology. Biol Chem (2009) 390(7):647-56. doi:10.1515/BC.2009.071
    • (2009) Biol Chem , vol.390 , Issue.7 , pp. 647-656
    • Liu, Y.1    Palma, A.S.2    Feizi, T.3
  • 193
    • 33750119810 scopus 로고    scopus 로고
    • Glycan microarray technologies: tools to survey host specificity of influenza viruses
    • Stevens J, Blixt O, Paulson JC, Wilson IA. Glycan microarray technologies: tools to survey host specificity of influenza viruses. Nat Rev Microbiol (2006) 4(11):857-64. doi:10.1038/nrmicro1530
    • (2006) Nat Rev Microbiol , vol.4 , Issue.11 , pp. 857-864
    • Stevens, J.1    Blixt, O.2    Paulson, J.C.3    Wilson, I.A.4
  • 194
    • 84863246476 scopus 로고    scopus 로고
    • A quantitative structure-activity relationship (QSAR) study on glycan array data to determine the specificities of glycan-binding proteins
    • Xuan P, Zhang Y, Tzeng TR, Wan XF, Luo F. A quantitative structure-activity relationship (QSAR) study on glycan array data to determine the specificities of glycan-binding proteins. Glycobiology (2012) 22(4):552-60. doi:10.1093/glycob/cwr163
    • (2012) Glycobiology , vol.22 , Issue.4 , pp. 552-560
    • Xuan, P.1    Zhang, Y.2    Tzeng, T.R.3    Wan, X.F.4    Luo, F.5
  • 195
    • 84875978675 scopus 로고    scopus 로고
    • Global comparisons of lectin-glycan interactions using a database of analyzed glycan array data
    • Kletter D, Singh S, Bern M, Haab BB. Global comparisons of lectin-glycan interactions using a database of analyzed glycan array data. Mol Cell Proteomics (2013) 12(4):1026-35. doi:10.1074/mcp. M112.026641
    • (2013) Mol Cell Proteomics , vol.12 , Issue.4 , pp. 1026-1035
    • Kletter, D.1    Singh, S.2    Bern, M.3    Haab, B.B.4
  • 197
    • 84925813800 scopus 로고    scopus 로고
    • Combination of automated solid-phase and enzymatic oligosaccharide synthesis provides access to alpha(2,3)-sialylated glycans
    • Fair RJ, Hahm HS, Seeberger PH. Combination of automated solid-phase and enzymatic oligosaccharide synthesis provides access to alpha(2,3)-sialylated glycans. Chem Commun (Camb) (2015) 51(28):6183-5. doi:10.1039/c5cc01368b
    • (2015) Chem Commun (Camb) , vol.51 , Issue.28 , pp. 6183-6185
    • Fair, R.J.1    Hahm, H.S.2    Seeberger, P.H.3
  • 198
    • 84929598644 scopus 로고    scopus 로고
    • Automated solid-phase synthesis of oligosaccharides containing sialic acids
    • Lai CH, Hahm HS, Liang CF, Seeberger PH. Automated solid-phase synthesis of oligosaccharides containing sialic acids. Beilstein J Org Chem (2015) 11:617-21. doi:10.3762/bjoc.11.69
    • (2015) Beilstein J Org Chem , vol.11 , pp. 617-621
    • Lai, C.H.1    Hahm, H.S.2    Liang, C.F.3    Seeberger, P.H.4
  • 199
    • 84921714540 scopus 로고    scopus 로고
    • Automated synthesis of chondroitin sulfate oligosaccharides
    • Liang CF, Hahm HS, Seeberger PH. Automated synthesis of chondroitin sulfate oligosaccharides. Methods Mol Biol (2015) 1229:3-10. doi:10.1007/978-1-4939-1714-3_1
    • (2015) Methods Mol Biol , vol.1229 , pp. 3-10
    • Liang, C.F.1    Hahm, H.S.2    Seeberger, P.H.3
  • 200
    • 84937064640 scopus 로고    scopus 로고
    • A self-assembling peptide scaffold for the multivalent presentation of antigens
    • Zacco E, Anish C, Martin CE, V Berlepsch H, Brandenburg E, Seeberger PH, et al. A self-assembling peptide scaffold for the multivalent presentation of antigens. Biomacromolecules (2015) 16(7):2188-97. doi:10.1021/acs.biomac.5b00572
    • (2015) Biomacromolecules , vol.16 , Issue.7 , pp. 2188-2197
    • Zacco, E.1    Anish, C.2    Martin, C.E.3    Berlepsch, H.V.4    Brandenburg, E.5    Seeberger, P.H.6
  • 201
    • 34249341648 scopus 로고    scopus 로고
    • Glycoprotein microarrays with multi-lectin detection: unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera
    • Zhao J, Patwa TH, Qiu W, Shedden K, Hinderer R, Misek DE, et al. Glycoprotein microarrays with multi-lectin detection: unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera. J Proteome Res (2007) 6(5):1864-74. doi:10.1021/pr070062p
    • (2007) J Proteome Res , vol.6 , Issue.5 , pp. 1864-1874
    • Zhao, J.1    Patwa, T.H.2    Qiu, W.3    Shedden, K.4    Hinderer, R.5    Misek, D.E.6
  • 202
    • 79951974583 scopus 로고    scopus 로고
    • Seromic profiling of colorectal cancer patients with novel glycopeptide microarray
    • Pedersen JW, Blixt O, Bennett EP, Tarp MA, Dar I, Mandel U, et al. Seromic profiling of colorectal cancer patients with novel glycopeptide microarray. Int J Cancer (2011) 128(8):1860-71. doi:10.1002/ijc.25778
    • (2011) Int J Cancer , vol.128 , Issue.8 , pp. 1860-1871
    • Pedersen, J.W.1    Blixt, O.2    Bennett, E.P.3    Tarp, M.A.4    Dar, I.5    Mandel, U.6
  • 203
    • 84878554709 scopus 로고    scopus 로고
    • Autoantibodies to MUC1 glycopeptides cannot be used as a screening assay for early detection of breast, ovarian, lung or pancreatic cancer
    • Burford B, Gentry-Maharaj A, Graham R, Allen D, Pedersen JW, Nudelman AS, et al. Autoantibodies to MUC1 glycopeptides cannot be used as a screening assay for early detection of breast, ovarian, lung or pancreatic cancer. Br J Cancer (2013) 108(10):2045-55. doi:10.1038/bjc.2013.214
    • (2013) Br J Cancer , vol.108 , Issue.10 , pp. 2045-2055
    • Burford, B.1    Gentry-Maharaj, A.2    Graham, R.3    Allen, D.4    Pedersen, J.W.5    Nudelman, A.S.6
  • 204
    • 84876896284 scopus 로고    scopus 로고
    • Lectin microarrays: concept, principle and applications
    • Hirabayashi J, Yamada M, Kuno A, Tateno H. Lectin microarrays: concept, principle and applications. Chem Soc Rev (2013) 42(10):4443-58. doi:10.1039/c3cs35419a
    • (2013) Chem Soc Rev , vol.42 , Issue.10 , pp. 4443-4458
    • Hirabayashi, J.1    Yamada, M.2    Kuno, A.3    Tateno, H.4
  • 205
    • 84923273061 scopus 로고    scopus 로고
    • The detection and discovery of glycan motifs in biological samples using lectins and antibodies: new methods and opportunities
    • Tang H, Hsueh P, Kletter D, Bern M, Haab B. The detection and discovery of glycan motifs in biological samples using lectins and antibodies: new methods and opportunities. Adv Cancer Res (2015) 126:167-202. doi:10.1016/bs.acr.2014.11.003
    • (2015) Adv Cancer Res , vol.126 , pp. 167-202
    • Tang, H.1    Hsueh, P.2    Kletter, D.3    Bern, M.4    Haab, B.5
  • 206
    • 64649101157 scopus 로고    scopus 로고
    • Microarrays in glycoproteomics research
    • Yue T, Haab BB. Microarrays in glycoproteomics research. Clin Lab Med (2009) 29(1):15-29. doi:10.1016/j.cll.2009.01.001
    • (2009) Clin Lab Med , vol.29 , Issue.1 , pp. 15-29
    • Yue, T.1    Haab, B.B.2
  • 207
    • 84900461743 scopus 로고    scopus 로고
    • Use of lectin microarray to differentiate gastric cancer from gastric ulcer
    • Huang WL, Li YG, Lv YC, Guan XH, Ji HF, Chi BR. Use of lectin microarray to differentiate gastric cancer from gastric ulcer. World J Gastroenterol (2014) 20(18):5474-82. doi:10.3748/wjg.v20.i18.5474
    • (2014) World J Gastroenterol , vol.20 , Issue.18 , pp. 5474-5482
    • Huang, W.L.1    Li, Y.G.2    Lv, Y.C.3    Guan, X.H.4    Ji, H.F.5    Chi, B.R.6
  • 208
    • 84983354484 scopus 로고    scopus 로고
    • Lectin-based protein microarray analysis of differences in serum alpha-2-macroglobulin glycosylation between patients with colorectal cancer and persons without cancer
    • Sunderic M, Sediva A, Robajac D, Miljus G, Gemeiner P, Nedic O, et al. Lectin-based protein microarray analysis of differences in serum alpha-2-macroglobulin glycosylation between patients with colorectal cancer and persons without cancer. Biotechnol Appl Biochem (2015). doi:10.1002/bab.1407
    • (2015) Biotechnol Appl Biochem
    • Sunderic, M.1    Sediva, A.2    Robajac, D.3    Miljus, G.4    Gemeiner, P.5    Nedic, O.6
  • 209
    • 84885160723 scopus 로고    scopus 로고
    • Specific glycoforms of MUC5AC and endorepellin accurately distinguish mucinous from nonmucinous pancreatic cysts
    • Cao Z, Maupin K, Curnutte B, Fallon B, Feasley CL, Brouhard E, et al. Specific glycoforms of MUC5AC and endorepellin accurately distinguish mucinous from nonmucinous pancreatic cysts. Mol Cell Proteomics (2013) 12(10):2724-34. doi:10.1074/mcp. M113.030700
    • (2013) Mol Cell Proteomics , vol.12 , Issue.10 , pp. 2724-2734
    • Cao, Z.1    Maupin, K.2    Curnutte, B.3    Fallon, B.4    Feasley, C.L.5    Brouhard, E.6
  • 210
    • 34250217743 scopus 로고    scopus 로고
    • Multiplexed analysis of glycan variation on native proteins captured by antibody microarrays
    • Chen S, LaRoche T, Hamelinck D, Bergsma D, Brenner D, Simeone D, et al. Multiplexed analysis of glycan variation on native proteins captured by antibody microarrays. Nat Methods (2007) 4(5):437-44. doi:10.1038/nmeth1035
    • (2007) Nat Methods , vol.4 , Issue.5 , pp. 437-444
    • Chen, S.1    LaRoche, T.2    Hamelinck, D.3    Bergsma, D.4    Brenner, D.5    Simeone, D.6
  • 211
    • 84866487628 scopus 로고    scopus 로고
    • Improved lectin ELISA for glycosylation analysis of biomarkers using PS-tag-fused single-chain Fv
    • Kumada Y, Ohigashi Y, Emori Y, Imamura K, Omura Y, Kishimoto M. Improved lectin ELISA for glycosylation analysis of biomarkers using PS-tag-fused single-chain Fv. J Immunol Methods (2012) 385(1-2):15-22. doi:10.1016/j.jim.2012.07.021
    • (2012) J Immunol Methods , vol.385 , Issue.1-2 , pp. 15-22
    • Kumada, Y.1    Ohigashi, Y.2    Emori, Y.3    Imamura, K.4    Omura, Y.5    Kishimoto, M.6
  • 213
    • 33751252292 scopus 로고    scopus 로고
    • Direct observation of individual endogenous protein complexes in situ by proximity ligation
    • Soderberg O, Gullberg M, Jarvius M, Ridderstrale K, Leuchowius KJ, Jarvius J, et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat Methods (2006) 3(12):995-1000. doi:10.1038/nmeth947
    • (2006) Nat Methods , vol.3 , Issue.12 , pp. 995-1000
    • Soderberg, O.1    Gullberg, M.2    Jarvius, M.3    Ridderstrale, K.4    Leuchowius, K.J.5    Jarvius, J.6
  • 214
    • 77649216263 scopus 로고    scopus 로고
    • MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in intestinal metaplasia and gastric carcinomas
    • Conze T, Carvalho AS, Landegren U, Almeida R, Reis CA, David L, et al. MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in intestinal metaplasia and gastric carcinomas. Glycobiology (2010) 20(2):199-206. doi:10.1093/glycob/cwp161
    • (2010) Glycobiology , vol.20 , Issue.2 , pp. 199-206
    • Conze, T.1    Carvalho, A.S.2    Landegren, U.3    Almeida, R.4    Reis, C.A.5    David, L.6
  • 215
    • 84863091545 scopus 로고    scopus 로고
    • Identification of new cancer biomarkers based on aberrant mucin glycoforms by in situ proximity ligation
    • Pinto R, Carvalho AS, Conze T, Magalhaes A, Picco G, Burchell JM, et al. Identification of new cancer biomarkers based on aberrant mucin glycoforms by in situ proximity ligation. J Cell Mol Med (2012) 16(7):1474-84. doi:10.1111/j.1582-4934.2011.01436.x
    • (2012) J Cell Mol Med , vol.16 , Issue.7 , pp. 1474-1484
    • Pinto, R.1    Carvalho, A.S.2    Conze, T.3    Magalhaes, A.4    Picco, G.5    Burchell, J.M.6
  • 217
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS
    • Caprioli RM, Farmer TB, Gile J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal Chem (1997) 69(23):4751-60. doi:10.1021/ac970888i
    • (1997) Anal Chem , vol.69 , Issue.23 , pp. 4751-4760
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 218
    • 84886893246 scopus 로고    scopus 로고
    • Matrix assisted laser desorption ionization imaging mass spectrometry workflow for spatial profiling analysis of N-linked glycan expression in tissues
    • Powers TW, Jones EE, Betesh LR, Romano PR, Gao P, Copland JA, et al. Matrix assisted laser desorption ionization imaging mass spectrometry workflow for spatial profiling analysis of N-linked glycan expression in tissues. Anal Chem (2013) 85(20):9799-806. doi:10.1021/ac402108x
    • (2013) Anal Chem , vol.85 , Issue.20 , pp. 9799-9806
    • Powers, T.W.1    Jones, E.E.2    Betesh, L.R.3    Romano, P.R.4    Gao, P.5    Copland, J.A.6
  • 219
    • 84906965809 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry profiling of N-glycans in formalin-fixed paraffin embedded clinical tissue blocks and tissue microarrays
    • Powers TW, Neely BA, Shao Y, Tang H, Troyer DA, Mehta AS, et al. MALDI imaging mass spectrometry profiling of N-glycans in formalin-fixed paraffin embedded clinical tissue blocks and tissue microarrays. PLoS One (2014) 9(9):e106255. doi:10.1371/journal.pone.0106255
    • (2014) PLoS One , vol.9 , Issue.9
    • Powers, T.W.1    Neely, B.A.2    Shao, Y.3    Tang, H.4    Troyer, D.A.5    Mehta, A.S.6
  • 220
    • 85012098029 scopus 로고    scopus 로고
    • Two-dimensional N-glycan distribution mapping of hepatocellular carcinoma tissues by MALDI-imaging mass spectrometry
    • Powers TW, Holst S, Wuhrer M, Mehta AS, Drake RR. Two-dimensional N-glycan distribution mapping of hepatocellular carcinoma tissues by MALDI-imaging mass spectrometry. Biomolecules (2015) 5(4):2554-72. doi:10.3390/biom5042554
    • (2015) Biomolecules , vol.5 , Issue.4 , pp. 2554-2572
    • Powers, T.W.1    Holst, S.2    Wuhrer, M.3    Mehta, A.S.4    Drake, R.R.5


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