메뉴 건너뛰기




Volumn 14, Issue 4-5, 2014, Pages 525-546

Cell surface protein glycosylation in cancer

Author keywords

Biomarkers; Cancer; Glycoproteomics; Glycosylation; Glycosyltransferases; Membrane proteins

Indexed keywords

CELL PROTEIN; CELL SURFACE PROTEIN; ENZYME; GLYCAN; GLYCOSYLTRANSFERASE; MANNOSE; FUCOSE; N ACETYLGLUCOSAMINE; SIALIC ACID DERIVATIVE;

EID: 84896774734     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300387     Document Type: Review
Times cited : (431)

References (214)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: all of the theories are correct
    • Varki, A., Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 2
    • 77949272116 scopus 로고    scopus 로고
    • Glycan gene expression signatures in normal and malignant breast tissue; possible role in diagnosis and progression
    • Potapenko, I. O., Haakensen, V. D., Luders, T., Helland, A. et al., Glycan gene expression signatures in normal and malignant breast tissue; possible role in diagnosis and progression. Mol. Oncol. 2010, 4, 98-118.
    • (2010) Mol. Oncol. , vol.4 , pp. 98-118
    • Potapenko, I.O.1    Haakensen, V.D.2    Luders, T.3    Helland, A.4
  • 3
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation [mdash] potential for therapeutics and diagnostics
    • Dube, D. H., Bertozzi, C. R., Glycans in cancer and inflammation [mdash] potential for therapeutics and diagnostics. Nat. Rev. Drug Discov. 2005, 4, 477-488.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 4
    • 84860690776 scopus 로고    scopus 로고
    • The role of N-acetylglucosaminyltransferases V in the malignancy of human hepatocellular carcinoma
    • Wei, T., Liu, Q., He, F., Zhu, W. et al., The role of N-acetylglucosaminyltransferases V in the malignancy of human hepatocellular carcinoma. Exp. Mol. Pathol. 2012, 93, 8-17.
    • (2012) Exp. Mol. Pathol. , vol.93 , pp. 8-17
    • Wei, T.1    Liu, Q.2    He, F.3    Zhu, W.4
  • 5
    • 84255199499 scopus 로고    scopus 로고
    • Selectin ligand Sialyl-Lewis x antigen drives metastasis of hormone-dependent breast cancers
    • Julien, S., Ivetic, A., Grigoriadis, A., QiZe, D. et al., Selectin ligand Sialyl-Lewis x antigen drives metastasis of hormone-dependent breast cancers. Cancer Res. 2011, 71, 7683-7693.
    • (2011) Cancer Res. , vol.71 , pp. 7683-7693
    • Julien, S.1    Ivetic, A.2    Grigoriadis, A.3    QiZe, D.4
  • 6
    • 84866551038 scopus 로고    scopus 로고
    • Overexpression and β-1,6-N-acetylglucosaminylation-initiated aberrant glycosylation of TIMP-1: a "double whammy" strategy in colon cancer progression
    • Kim, Y.-S., Ahn, Y. H., Song, K. J., Kang, J. G. et al., Overexpression and β-1, 6-N-acetylglucosaminylation-initiated aberrant glycosylation of TIMP-1: a "double whammy" strategy in colon cancer progression. J. Biol. Chem. 2012, 287, 32467-32478.
    • (2012) J. Biol. Chem , vol.287 , pp. 32467-32478
    • Kim, Y.-S.1    Ahn, Y.H.2    Song, K.J.3    Kang, J.G.4
  • 7
    • 77349093763 scopus 로고    scopus 로고
    • Lewis(y) antigen stimulates the growth of ovarian cancer cells via regulation of the epidermal growth factor receptor pathway
    • Liu, J. J., Lin, B., Hao, Y. Y., Li, F. F. et al., Lewis(y) antigen stimulates the growth of ovarian cancer cells via regulation of the epidermal growth factor receptor pathway. Oncol. Rep. 2010, 23, 833-841.
    • (2010) Oncol. Rep. , vol.23 , pp. 833-841
    • Liu, J.J.1    Lin, B.2    Hao, Y.Y.3    Li, F.F.4
  • 8
    • 84876487888 scopus 로고    scopus 로고
    • L1CAM from human melanoma carries a novel type of N-glycan with Galbeta1-4Galbeta1- motif. Involvement of N-linked glycans in migratory and invasive behaviour of melanoma cells
    • Hoja-Lukowicz, D., Link-Lenczowski, P., Carpentieri, A., Amoresano, A. et al., L1CAM from human melanoma carries a novel type of N-glycan with Galbeta1-4Galbeta1- motif. Involvement of N-linked glycans in migratory and invasive behaviour of melanoma cells. Glycoconj. J. 2013, 30, 205-225.
    • (2013) Glycoconj. J. , vol.30 , pp. 205-225
    • Hoja-Lukowicz, D.1    Link-Lenczowski, P.2    Carpentieri, A.3    Amoresano, A.4
  • 11
    • 33747362656 scopus 로고    scopus 로고
    • Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems
    • Butler, M., Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems. Cytotechnology 2006, 50, 57-76.
    • (2006) Cytotechnology , vol.50 , pp. 57-76
    • Butler, M.1
  • 12
    • 67650252530 scopus 로고    scopus 로고
    • Molecular profiling of breast cancer cell lines defines relevant tumor models and provides a resource for cancer gene discovery
    • Kao, J., Salari, K., Bocanegra, M., Choi, Y.-L. et al., Molecular profiling of breast cancer cell lines defines relevant tumor models and provides a resource for cancer gene discovery. PLoS One 2009, 4, e6146.
    • (2009) PLoS One , vol.4
    • Kao, J.1    Salari, K.2    Bocanegra, M.3    Choi, Y.-L.4
  • 13
    • 33845209913 scopus 로고    scopus 로고
    • A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
    • Neve, R. M., Chin, K., Fridlyand, J., Yeh, J. et al., A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. Cancer Cell 2006, 10, 515-527.
    • (2006) Cancer Cell , vol.10 , pp. 515-527
    • Neve, R.M.1    Chin, K.2    Fridlyand, J.3    Yeh, J.4
  • 14
    • 1342326910 scopus 로고    scopus 로고
    • Relevance of breast cancer cell lines as models for breast tumours: an update
    • Lacroix, M., Leclercq, G., Relevance of breast cancer cell lines as models for breast tumours: an update. Breast Cancer Res. Treat 2004, 83, 249-289.
    • (2004) Breast Cancer Res. Treat , vol.83 , pp. 249-289
    • Lacroix, M.1    Leclercq, G.2
  • 15
    • 84856661228 scopus 로고    scopus 로고
    • Glycoprotein profiles of human breast cells demonstrate a clear clustering of normal/benign versus malignant cell lines and basal versus luminal cell lines
    • Yen, T.-Y., Macher, B. A., McDonald, C. A., Alleyne-Chin, C., Timpe, L. C., Glycoprotein profiles of human breast cells demonstrate a clear clustering of normal/benign versus malignant cell lines and basal versus luminal cell lines. J. Proteome Res. 2011, 11, 656-667.
    • (2011) J. Proteome Res. , vol.11 , pp. 656-667
    • Yen, T.-Y.1    Macher, B.A.2    McDonald, C.A.3    Alleyne-Chin, C.4    Timpe, L.C.5
  • 16
    • 53049096773 scopus 로고    scopus 로고
    • Lectin microarrays identify cell-specific and functionally significant cell surface glycan markers
    • Tao, S.-C., Li, Y., Zhou, J., Qian, J. et al., Lectin microarrays identify cell-specific and functionally significant cell surface glycan markers. Glycobiology 2008, 18, 761-769.
    • (2008) Glycobiology , vol.18 , pp. 761-769
    • Tao, S.-C.1    Li, Y.2    Zhou, J.3    Qian, J.4
  • 18
    • 77949574043 scopus 로고    scopus 로고
    • DNA methylation profiles of ovarian epithelial carcinoma tumors and cell lines
    • Houshdaran, S., Hawley, S., Palmer, C., Campan, M. et al., DNA methylation profiles of ovarian epithelial carcinoma tumors and cell lines. PLoS One 2010, 5, e9359.
    • (2010) PLoS One , vol.5
    • Houshdaran, S.1    Hawley, S.2    Palmer, C.3    Campan, M.4
  • 19
    • 0028302147 scopus 로고
    • Immunohistochemical study of mucin carbohydrates and core proteins in human ovarian tumors
    • Tashiro, Y., Yonezawa, S., Kim, Y. S., Sato, E., Immunohistochemical study of mucin carbohydrates and core proteins in human ovarian tumors. Hum. Pathol. 1994, 25, 364-372.
    • (1994) Hum. Pathol. , vol.25 , pp. 364-372
    • Tashiro, Y.1    Yonezawa, S.2    Kim, Y.S.3    Sato, E.4
  • 20
    • 0027263949 scopus 로고
    • Immunohistochemical evaluation of sialosyl-Tn antigens in various ovarian carcinomas
    • Ryuko, K., Iwanari, O., Kitao, M., Moriwaki, S., Immunohistochemical evaluation of sialosyl-Tn antigens in various ovarian carcinomas. Gynecol. Oncol. 1993, 49, 215-224.
    • (1993) Gynecol. Oncol. , vol.49 , pp. 215-224
    • Ryuko, K.1    Iwanari, O.2    Kitao, M.3    Moriwaki, S.4
  • 21
    • 0020657454 scopus 로고
    • Discrimination between benign, borderline, and malignant epithelial ovarian tumors using tumor markers: an immunohistochemical study
    • Dietel, M., Discrimination between benign, borderline, and malignant epithelial ovarian tumors using tumor markers: an immunohistochemical study. Cancer Detect. Prev. 1983, 6, 255-262.
    • (1983) Cancer Detect. Prev. , vol.6 , pp. 255-262
    • Dietel, M.1
  • 22
    • 0026483419 scopus 로고
    • Sialyl Tn as a prognostic marker in epithelial ovarian cancer
    • Kobayashi, H., Terao, T., Kawashima, Y., Sialyl Tn as a prognostic marker in epithelial ovarian cancer. Br. J. Cancer 1992, 66, 984-985.
    • (1992) Br. J. Cancer , vol.66 , pp. 984-985
    • Kobayashi, H.1    Terao, T.2    Kawashima, Y.3
  • 23
    • 0033798902 scopus 로고    scopus 로고
    • Carbohydrate antigen expression in primary tumors, metastatic lesions, and serous effusions from patients diagnosed with epithelial ovarian carcinoma: evidence of up-regulated Tn and Sialyl Tn antigen expression in effusions
    • Davidson, B., Berner, A., Nesland, J. M., Risberg, B. et al., Carbohydrate antigen expression in primary tumors, metastatic lesions, and serous effusions from patients diagnosed with epithelial ovarian carcinoma: evidence of up-regulated Tn and Sialyl Tn antigen expression in effusions. Hum. Pathol. 2000, 31, 1081-1087.
    • (2000) Hum. Pathol. , vol.31 , pp. 1081-1087
    • Davidson, B.1    Berner, A.2    Nesland, J.M.3    Risberg, B.4
  • 24
    • 0034101785 scopus 로고    scopus 로고
    • Expression of carbohydrate antigens in advanced-stage ovarian carcinomas and their metastases-A clinicopathologic study
    • Davidson, B., Gotlieb, W. H., Ben-Baruch, G., Kopolovic, J. et al., Expression of carbohydrate antigens in advanced-stage ovarian carcinomas and their metastases-A clinicopathologic study. Gynecol. Oncol. 2000, 77, 35-43.
    • (2000) Gynecol. Oncol. , vol.77 , pp. 35-43
    • Davidson, B.1    Gotlieb, W.H.2    Ben-Baruch, G.3    Kopolovic, J.4
  • 25
    • 77956045259 scopus 로고    scopus 로고
    • Mass spectrometry and glycomics
    • Zaia, J., Mass spectrometry and glycomics. OMICS 2010, 14, 401-418.
    • (2010) OMICS , vol.14 , pp. 401-418
    • Zaia, J.1
  • 26
    • 70349467181 scopus 로고    scopus 로고
    • Lectins as tools in glycoconjugate research
    • Wu, A. M., Lisowska, E., Duk, M., Yang, Z., Lectins as tools in glycoconjugate research. Glycoconj. J. 2009, 26, 899-913.
    • (2009) Glycoconj. J. , vol.26 , pp. 899-913
    • Wu, A.M.1    Lisowska, E.2    Duk, M.3    Yang, Z.4
  • 27
    • 17144430928 scopus 로고    scopus 로고
    • β1,6-Branched oligosaccharides are increased in lymph node metastases and predict poor outcome in breast carcinoma
    • Handerson, T., Camp, R., Harigopal, M., Rimm, D., Pawelek, J., β1, 6-Branched oligosaccharides are increased in lymph node metastases and predict poor outcome in breast carcinoma. Clin. Cancer Res. 2005, 11, 2969-2973.
    • (2005) Clin. Cancer Res , vol.11 , pp. 2969-2973
    • Handerson, T.1    Camp, R.2    Harigopal, M.3    Rimm, D.4    Pawelek, J.5
  • 28
    • 0026014062 scopus 로고
    • β1-6 Branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia
    • Fernandes, B., Sagman, U., Auger, M., Demetrio, M., Dennis, J. W., β1-6 Branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia. Cancer Res. 1991, 51, 718-723.
    • (1991) Cancer Res , vol.51 , pp. 718-723
    • Fernandes, B.1    Sagman, U.2    Auger, M.3    Demetrio, M.4    Dennis, J.W.5
  • 29
    • 79953038616 scopus 로고    scopus 로고
    • Differential expression of the alpha2,3-sialic acid residues in breast cancer is associated with metastatic potential
    • Cui, H., Lin, Y., Yue, L., Zhao, X., Liu, J., Differential expression of the alpha2, 3-sialic acid residues in breast cancer is associated with metastatic potential. Oncol. Rep. 2011, 25, 1365-1371.
    • (2011) Oncol. Rep. , vol.25 , pp. 1365-1371
    • Cui, H.1    Lin, Y.2    Yue, L.3    Zhao, X.4    Liu, J.5
  • 30
    • 0029865890 scopus 로고    scopus 로고
    • Expression of L-PHA-binding proteins in breast cancer: reconstitution and molecular characterization of beta 1-6 branched oligosaccharides in three-dimensional cell culture
    • Taeda, Y., Nose, M., Hiraizumi, S., Ohuchi, N., Expression of L-PHA-binding proteins in breast cancer: reconstitution and molecular characterization of beta 1-6 branched oligosaccharides in three-dimensional cell culture. Breast Cancer Res. Treat. 1996, 38, 313-324.
    • (1996) Breast Cancer Res. Treat , vol.38 , pp. 313-324
    • Taeda, Y.1    Nose, M.2    Hiraizumi, S.3    Ohuchi, N.4
  • 31
    • 84878520352 scopus 로고    scopus 로고
    • Associated expression of alpha2,3sialylated type 2 chain structures with lymph node metastasis in distal colorectal cancer
    • Fukasawa, T., Asao, T., Yamauchi, H., Ide, M. et al., Associated expression of alpha2, 3sialylated type 2 chain structures with lymph node metastasis in distal colorectal cancer. Surg. Today 2013, 43, 155-162.
    • (2013) Surg. Today , vol.43 , pp. 155-162
    • Fukasawa, T.1    Asao, T.2    Yamauchi, H.3    Ide, M.4
  • 32
    • 84859562227 scopus 로고    scopus 로고
    • Lectin chromatography/mass spectrometry discovery workflow identifies putative biomarkers of aggressive breast cancers
    • Drake, P. M., Schilling, B., Niles, R. K., Prakobphol, A. et al., Lectin chromatography/mass spectrometry discovery workflow identifies putative biomarkers of aggressive breast cancers. J. Proteome Res. 2012, 11, 2508-2520.
    • (2012) J. Proteome Res , vol.11 , pp. 2508-2520
    • Drake, P.M.1    Schilling, B.2    Niles, R.K.3    Prakobphol, A.4
  • 33
    • 76649133774 scopus 로고    scopus 로고
    • Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis
    • Abbott, K. L., Lim, J. M., Wells, L., Benigno, B. B. et al., Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis. Proteomics 2010, 10, 470-481.
    • (2010) Proteomics , vol.10 , pp. 470-481
    • Abbott, K.L.1    Lim, J.M.2    Wells, L.3    Benigno, B.B.4
  • 34
    • 52949084643 scopus 로고    scopus 로고
    • Characterisation of alpha3beta1 and alpha(v)beta3 integrin N-oligosaccharides in metastatic melanoma WM9 and WM239 cell lines
    • Kremser, M. E., Przybylo, M., Hoja-Lukowicz, D., Pochec, E. et al., Characterisation of alpha3beta1 and alpha(v)beta3 integrin N-oligosaccharides in metastatic melanoma WM9 and WM239 cell lines. Biochim. Biophys. Acta 2008, 1780, 1421-1431.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1421-1431
    • Kremser, M.E.1    Przybylo, M.2    Hoja-Lukowicz, D.3    Pochec, E.4
  • 35
    • 0035964627 scopus 로고    scopus 로고
    • GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
    • Brooks, S. A., Hall, D. M. S., Buley, I., GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane. Br. J. Cancer 2001, 85, 1014-1022.
    • (2001) Br. J. Cancer , vol.85 , pp. 1014-1022
    • Brooks, S.A.1    Hall, D.M.S.2    Buley, I.3
  • 36
    • 84860382308 scopus 로고    scopus 로고
    • The lectin Helix pomatia agglutinin recognises O-GlcNAc containing glycoproteins in human breast cancer
    • Rambaruth, N. D. S., Greenwell, P., Dwek, M. V., The lectin Helix pomatia agglutinin recognises O-GlcNAc containing glycoproteins in human breast cancer. Glycobiology 2012, 22, 839-848.
    • (2012) Glycobiology , vol.22 , pp. 839-848
    • Rambaruth, N.D.S.1    Greenwell, P.2    Dwek, M.V.3
  • 37
    • 0034960028 scopus 로고    scopus 로고
    • Comparison of the lectin-binding pattern in different human melanoma cell lines
    • Litynska, A., Przybylo, M., Pochec, E., Hoja-Lukowicz, D. et al., Comparison of the lectin-binding pattern in different human melanoma cell lines. Melanoma Res. 2001, 11, 205-212.
    • (2001) Melanoma Res. , vol.11 , pp. 205-212
    • Litynska, A.1    Przybylo, M.2    Pochec, E.3    Hoja-Lukowicz, D.4
  • 38
    • 28944439880 scopus 로고    scopus 로고
    • Characterization of glycosylation and adherent properties of melanoma cell lines
    • Laidler, P., Litynska, A., Hoja-Lukowicz, D., Labedz, M. et al., Characterization of glycosylation and adherent properties of melanoma cell lines. Cancer Immunol. Immunother. 2006, 55, 112-118.
    • (2006) Cancer Immunol. Immunother , vol.55 , pp. 112-118
    • Laidler, P.1    Litynska, A.2    Hoja-Lukowicz, D.3    Labedz, M.4
  • 39
    • 34547753416 scopus 로고    scopus 로고
    • Analysis of cell surface carbohydrate expression patterns in normal and tumorigenic human breast cell lines using lectin arrays
    • Chen, S., Zheng, T., Shortreed, M. R., Alexander, C., Smith, L. M., Analysis of cell surface carbohydrate expression patterns in normal and tumorigenic human breast cell lines using lectin arrays. Anal. Chem. 2007, 79, 5698-5702.
    • (2007) Anal. Chem , vol.79 , pp. 5698-5702
    • Chen, S.1    Zheng, T.2    Shortreed, M.R.3    Alexander, C.4    Smith, L.M.5
  • 40
    • 33644874643 scopus 로고    scopus 로고
    • High expression of Lewisy/b antigens is associated with decreased survival in lymph node negative breast carcinomas
    • Madjd, Z., Parsons, T., Watson, N., Spendlove, I. et al., High expression of Lewisy/b antigens is associated with decreased survival in lymph node negative breast carcinomas. Breast Cancer Res. 2005, 7, R780-R787.
    • (2005) Breast Cancer Res , vol.7
    • Madjd, Z.1    Parsons, T.2    Watson, N.3    Spendlove, I.4
  • 41
    • 0022559251 scopus 로고
    • Expression of Lewisa, Lewisb, X, and Y blood group antigens in human colonic tumors and normal tissue and in human tumor-derived cell lines
    • Sakamoto, J., Furukawa, K., Cordon-Cardo, C., Yin, B. W. T. et al., Expression of Lewisa, Lewisb, X, and Y blood group antigens in human colonic tumors and normal tissue and in human tumor-derived cell lines. Cancer Res. 1986, 46, 1553-1561.
    • (1986) Cancer Res , vol.46 , pp. 1553-1561
    • Sakamoto, J.1    Furukawa, K.2    Cordon-Cardo, C.3    Yin, B.W.T.4
  • 42
    • 0024540743 scopus 로고
    • Expression of Tn, sialosyl-Tn, and T antigens in human colon cancer
    • Itzkowitz, S. H., Yuan, M., Montgomery, C. K., Kjeldsen, T. et al., Expression of Tn, sialosyl-Tn, and T antigens in human colon cancer. Cancer Res. 1989, 49, 197-204.
    • (1989) Cancer Res. , vol.49 , pp. 197-204
    • Itzkowitz, S.H.1    Yuan, M.2    Montgomery, C.K.3    Kjeldsen, T.4
  • 43
    • 45549095820 scopus 로고    scopus 로고
    • Targeted glycoproteomic identification of biomarkers for human breast carcinoma
    • Abbott, K. L., Aoki, K., Lim, J.-M., Porterfield, M. et al., Targeted glycoproteomic identification of biomarkers for human breast carcinoma. J. Proteome Res. 2008, 7, 1470-1480.
    • (2008) J. Proteome Res , vol.7 , pp. 1470-1480
    • Abbott, K.L.1    Aoki, K.2    Lim, J.-M.3    Porterfield, M.4
  • 44
    • 77949325755 scopus 로고    scopus 로고
    • Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity
    • North, S. J., Huang, H.-H., Sundaram, S., Jang-Lee, J. et al., Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J. Biol. Chem. 2010, 285, 5759-5775.
    • (2010) J. Biol. Chem , vol.285 , pp. 5759-5775
    • North, S.J.1    Huang, H.-H.2    Sundaram, S.3    Jang-Lee, J.4
  • 46
    • 33846542649 scopus 로고    scopus 로고
    • A serum glycomics approach to breast cancer biomarkers
    • Kirmiz, C., Li, B., An, H. J., Clowers, B. H. et al., A serum glycomics approach to breast cancer biomarkers. Mol. Cel. Proteomics 2007, 6, 43-55.
    • (2007) Mol. Cel. Proteomics , vol.6 , pp. 43-55
    • Kirmiz, C.1    Li, B.2    An, H.J.3    Clowers, B.H.4
  • 47
    • 79551697660 scopus 로고    scopus 로고
    • N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin
    • Machado, E., Kandzia, S., Carilho, R., Altevogt, P. et al., N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin. Glycobiology 2011, 21, 376-386.
    • (2011) Glycobiology , vol.21 , pp. 376-386
    • Machado, E.1    Kandzia, S.2    Carilho, R.3    Altevogt, P.4
  • 48
    • 61849112797 scopus 로고    scopus 로고
    • Expression of a core 3 disialyl-Le(x) hexasaccharide in human colorectal cancers: a potential marker of malignant transformation in colon
    • Robbe-Masselot, C., Herrmann, A., Maes, E., Carlstedt, I. et al., Expression of a core 3 disialyl-Le(x) hexasaccharide in human colorectal cancers: a potential marker of malignant transformation in colon. J. Proteome Res. 2009, 8, 702-711.
    • (2009) J. Proteome Res. , vol.8 , pp. 702-711
    • Robbe-Masselot, C.1    Herrmann, A.2    Maes, E.3    Carlstedt, I.4
  • 49
    • 80054767981 scopus 로고    scopus 로고
    • Altered O-glycosylation profile of MUC2 mucin occurs in active ulcerative colitis and is associated with increased inflammation
    • Larsson, J. M., Karlsson, H., Crespo, J. G., Johansson, M. E. et al., Altered O-glycosylation profile of MUC2 mucin occurs in active ulcerative colitis and is associated with increased inflammation. Inflamm. Bowel Dis. 2011, 17, 2299-2307.
    • (2011) Inflamm. Bowel Dis. , vol.17 , pp. 2299-2307
    • Larsson, J.M.1    Karlsson, H.2    Crespo, J.G.3    Johansson, M.E.4
  • 50
    • 66249136714 scopus 로고    scopus 로고
    • A complex, but uniform O-glycosylation of the human MUC2 mucin from colonic biopsies analyzed by nanoLC/MSn
    • Holmén Larsson, J. M., Karlsson, H., Sjövall, H., Hansson, G. C., A complex, but uniform O-glycosylation of the human MUC2 mucin from colonic biopsies analyzed by nanoLC/MSn. Glycobiology 2009, 19, 756-766.
    • (2009) Glycobiology , vol.19 , pp. 756-766
    • Holmén Larsson, J.M.1    Karlsson, H.2    Sjövall, H.3    Hansson, G.C.4
  • 51
    • 76149084829 scopus 로고    scopus 로고
    • GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA
    • Deshpande, N., Jensen, P. H., Packer, N. H., Kolarich, D., GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA. J. Proteome Res. 2009, 9, 1063-1075.
    • (2009) J. Proteome Res , vol.9 , pp. 1063-1075
    • Deshpande, N.1    Jensen, P.H.2    Packer, N.H.3    Kolarich, D.4
  • 52
    • 74049091330 scopus 로고    scopus 로고
    • in: Li, J. (Ed.), Humana Press.
    • Apte, A., Meitei, N., in: Li, J. (Ed.), Functional Glycomics, Humana Press 2010, pp. 269-281.
    • (2010) Functional Glycomics , pp. 269-281
    • Apte, A.1    Meitei, N.2
  • 53
    • 50449105825 scopus 로고    scopus 로고
    • Focused glycomic analysis of the N-linked glycan biosynthetic pathway in ovarian cancer
    • Abbott, K. L., Nairn, A. V., Hall, E. M., Horton, M. B. et al., Focused glycomic analysis of the N-linked glycan biosynthetic pathway in ovarian cancer. Proteomics 2008, 8, 3210-3220.
    • (2008) Proteomics , vol.8 , pp. 3210-3220
    • Abbott, K.L.1    Nairn, A.V.2    Hall, E.M.3    Horton, M.B.4
  • 54
    • 28044455199 scopus 로고    scopus 로고
    • Altered mRNA expressions of sialyltransferases in ovarian cancers
    • Wang, P. H., Lee, W. L., Juang, C. M., Yang, Y. H. et al., Altered mRNA expressions of sialyltransferases in ovarian cancers. Gynecol. Oncol. 2005, 99, 631-639.
    • (2005) Gynecol. Oncol. , vol.99 , pp. 631-639
    • Wang, P.H.1    Lee, W.L.2    Juang, C.M.3    Yang, Y.H.4
  • 55
    • 10244252775 scopus 로고    scopus 로고
    • Fucosyltransferase III and sialyl-Le(x) expression correlate in cultured colon carcinoma cells but not in colon carcinoma tissue
    • Hanski, C., Klussmann, E., Wang, J., Bohm, C. et al., Fucosyltransferase III and sialyl-Le(x) expression correlate in cultured colon carcinoma cells but not in colon carcinoma tissue. Glycoconj. J. 1996, 13, 727-733.
    • (1996) Glycoconj. J. , vol.13 , pp. 727-733
    • Hanski, C.1    Klussmann, E.2    Wang, J.3    Bohm, C.4
  • 56
    • 0035283745 scopus 로고    scopus 로고
    • Elevated expression of UDP-N-acetylglucosamine: αmannoside β1,6 N-acetylglucosaminyltransferase is an early event in hepatocarcinogenesis
    • Ito, Y., Miyoshi, E., Sakon, M., Takeda, T. et al., Elevated expression of UDP-N-acetylglucosamine: αmannoside β1, 6 N-acetylglucosaminyltransferase is an early event in hepatocarcinogenesis. Int. J. Cancer 2001, 91, 631-637.
    • (2001) Int. J. Cancer , vol.91 , pp. 631-637
    • Ito, Y.1    Miyoshi, E.2    Sakon, M.3    Takeda, T.4
  • 57
    • 0031824085 scopus 로고    scopus 로고
    • Up-regulation of a set of glycosyltransferase genes in human colorectal cancer
    • Kudo, T., Ikehara, Y., Togayachi, A., Morozumi, K. et al., Up-regulation of a set of glycosyltransferase genes in human colorectal cancer. Lab. Invest. 1998, 78, 797-811.
    • (1998) Lab. Invest. , vol.78 , pp. 797-811
    • Kudo, T.1    Ikehara, Y.2    Togayachi, A.3    Morozumi, K.4
  • 58
    • 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. 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, 130-139.
    • (2011) Int. J. Biochem. Cell Biol , vol.43 , pp. 130-139
    • Trinchera, M.1    Malagolini, N.2    Chiricolo, M.3    Santini, D.4
  • 59
    • 0028564771 scopus 로고
    • Alterations of O-glycan biosynthesis in human colon cancer tissues
    • Yang, J. M., Byrd, J. C., Siddiki, B. B., Chung, Y. S. et al., Alterations of O-glycan biosynthesis in human colon cancer tissues. Glycobiology 1994, 4, 873-884.
    • (1994) Glycobiology , vol.4 , pp. 873-884
    • Yang, J.M.1    Byrd, J.C.2    Siddiki, B.B.3    Chung, Y.S.4
  • 61
    • 3943099388 scopus 로고    scopus 로고
    • Clinical usefulness of alterations in sialic acid, sialyl transferase and sialoproteins in breast cancer
    • Raval, G. N., Parekh, L. J., Patel, D. D., Jha, F. P. et al., Clinical usefulness of alterations in sialic acid, sialyl transferase and sialoproteins in breast cancer. Indian J. Clin. Biochem. 2004, 19, 60-71.
    • (2004) Indian J. Clin. Biochem. , vol.19 , pp. 60-71
    • Raval, G.N.1    Parekh, L.J.2    Patel, D.D.3    Jha, F.P.4
  • 62
    • 0035526308 scopus 로고    scopus 로고
    • Expression of sialyl-Tn antigen in breast cancer cells transfected with the human CMP-Neu5Ac: GalNAc alpha2,6-sialyltransferase (ST6GalNac I) cDNA
    • Julien, S., Krzewinski-Recchi, M. A., Harduin-Lepers, A., Gouyer, V. et al., Expression of sialyl-Tn antigen in breast cancer cells transfected with the human CMP-Neu5Ac: GalNAc alpha2, 6-sialyltransferase (ST6GalNac I) cDNA. Glycoconj. J. 2001, 18, 883-893.
    • (2001) Glycoconj. J. , vol.18 , pp. 883-893
    • Julien, S.1    Krzewinski-Recchi, M.A.2    Harduin-Lepers, A.3    Gouyer, V.4
  • 63
    • 0036351383 scopus 로고    scopus 로고
    • Cell Surface [alpha]2,6-sialylation affects adhesion of breast carcinoma cells
    • Lin, S., Kemmner, W., Grigull, S., Schlag, P. M., Cell Surface [alpha]2, 6-sialylation affects adhesion of breast carcinoma cells. Exp. Cell Res. 2002, 276, 101-110.
    • (2002) Exp. Cell Res , vol.276 , pp. 101-110
    • Lin, S.1    Kemmner, W.2    Grigull, S.3    Schlag, P.M.4
  • 64
    • 0023553530 scopus 로고
    • Characterization of quantitative mucin variants from a human colon cancer cell line
    • Kuan, S. F., Byrd, J. C., Basbaum, C. B., Kim, Y. S., Characterization of quantitative mucin variants from a human colon cancer cell line. Cancer Res. 1987, 47, 5715-5724.
    • (1987) Cancer Res. , vol.47 , pp. 5715-5724
    • Kuan, S.F.1    Byrd, J.C.2    Basbaum, C.B.3    Kim, Y.S.4
  • 65
    • 0034680102 scopus 로고    scopus 로고
    • Molecular portraits of human breast tumours
    • Perou, C., Sorlie, T., Eisen, M., Rijn, M. et al., Molecular portraits of human breast tumours. Nature 2000, 406, 747-752.
    • (2000) Nature , vol.406 , pp. 747-752
    • Perou, C.1    Sorlie, T.2    Eisen, M.3    Rijn, M.4
  • 66
    • 0023255440 scopus 로고
    • Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • Dennis, J., Laferte, S., Waghorne, C., Breitman, M., Kerbel, R., Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science 1987, 236, 582-585.
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.1    Laferte, S.2    Waghorne, C.3    Breitman, M.4    Kerbel, R.5
  • 67
    • 0025858981 scopus 로고
    • Reactivity of anti-CD15 monoclonal antibody PM-81 with breast cancer and elimination of breast cancer cells from human bone marrow by PM-81 and immunomagnetic beads
    • Vredenburgh, J. J., Simpson, W., Memoli, V. A., Ball, E. D., Reactivity of anti-CD15 monoclonal antibody PM-81 with breast cancer and elimination of breast cancer cells from human bone marrow by PM-81 and immunomagnetic beads. Cancer Res. 1991, 51, 2451-2455.
    • (1991) Cancer Res , vol.51 , pp. 2451-2455
    • Vredenburgh, J.J.1    Simpson, W.2    Memoli, V.A.3    Ball, E.D.4
  • 68
    • 0035003195 scopus 로고    scopus 로고
    • Immunohistochemical expression of T, Tn and sialyl-Tn antigens and clinical outcome in human breast carcinoma
    • Imai, J., Ghazizadeh, M., Naito, Z., Asano, G., Immunohistochemical expression of T, Tn and sialyl-Tn antigens and clinical outcome in human breast carcinoma. Anticancer Res. 2001, 21, 1327-1334.
    • (2001) Anticancer Res. , vol.21 , pp. 1327-1334
    • Imai, J.1    Ghazizadeh, M.2    Naito, Z.3    Asano, G.4
  • 69
    • 0030761635 scopus 로고    scopus 로고
    • Endothelial and epithelial expression of sialyl Lewisx and sialyl Lewisa in lesions of breast carcinoma
    • Renkonen, J., Paavonen, T., Renkonen, R., Endothelial and epithelial expression of sialyl Lewisx and sialyl Lewisa in lesions of breast carcinoma. Int. J. Cancer 1997, 74, 296-300.
    • (1997) Int. J. Cancer , vol.74 , pp. 296-300
    • Renkonen, J.1    Paavonen, T.2    Renkonen, R.3
  • 70
    • 47549097733 scopus 로고    scopus 로고
    • Breast cancer diagnosis and prognosis through quantitative measurements of serum glycan profiles
    • Kyselova, Z., Mechref, Y., Kang, P., Goetz, J. A. et al., Breast cancer diagnosis and prognosis through quantitative measurements of serum glycan profiles. Clin. Chem. 2008, 54, 1166-1175.
    • (2008) Clin. Chem , vol.54 , pp. 1166-1175
    • Kyselova, Z.1    Mechref, Y.2    Kang, P.3    Goetz, J.A.4
  • 71
    • 0024493145 scopus 로고
    • Oncodevelopmental expression of -GlcNAcβ1-6Manα1-6Manβ1- branched asparagine-linked oligosaccharides in murine tissues and human breast carcinomas
    • Dennis, J. W., Laferte, S., Oncodevelopmental expression of -GlcNAcβ1-6Manα1-6Manβ1- branched asparagine-linked oligosaccharides in murine tissues and human breast carcinomas. Cancer Res. 1989, 49, 945-950.
    • (1989) Cancer Res , vol.49 , pp. 945-950
    • Dennis, J.W.1    Laferte, S.2
  • 72
    • 0033233461 scopus 로고    scopus 로고
    • An alpha2,3 sialyltransferase (ST3Gal I) is elevated in primary breast carcinomas
    • Burchell, J., Poulsom, R., Hanby, A., Whitehouse, C. et al., An alpha2, 3 sialyltransferase (ST3Gal I) is elevated in primary breast carcinomas. Glycobiology 1999, 9, 1307-1311.
    • (1999) Glycobiology , vol.9 , pp. 1307-1311
    • Burchell, J.1    Poulsom, R.2    Hanby, A.3    Whitehouse, C.4
  • 73
    • 77950545117 scopus 로고    scopus 로고
    • N-Acetylgalactosaminyltransferase-14 as a potential biomarker for breast cancer by immunohistochemistry
    • Wu, C., Guo, X., Wang, W., Wang, Y. et al., N-Acetylgalactosaminyltransferase-14 as a potential biomarker for breast cancer by immunohistochemistry. BMC Cancer 2010, 10, 123.
    • (2010) BMC Cancer , vol.10 , pp. 123
    • Wu, C.1    Guo, X.2    Wang, W.3    Wang, Y.4
  • 74
    • 0032530423 scopus 로고    scopus 로고
    • Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer
    • Recchi, M. A., Hebbar, M., Hornez, L., Harduin-Lepers, A. et al., Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer. Cancer Res. 1998, 58, 4066-4070.
    • (1998) Cancer Res. , vol.58 , pp. 4066-4070
    • Recchi, M.A.1    Hebbar, M.2    Hornez, L.3    Harduin-Lepers, A.4
  • 75
    • 0036271329 scopus 로고    scopus 로고
    • Expression of ABH/Lewis-related antigens as prognostic factors in patients with breast cancer
    • Nakagoe, T., Fukushima, K., Itoyanagi, N., Ikuta, Y. et al., Expression of ABH/Lewis-related antigens as prognostic factors in patients with breast cancer. J. Cancer Res. Clin. Oncol. 2002, 128, 257-264.
    • (2002) J. Cancer Res. Clin. Oncol. , vol.128 , pp. 257-264
    • Nakagoe, T.1    Fukushima, K.2    Itoyanagi, N.3    Ikuta, Y.4
  • 76
    • 57049137606 scopus 로고    scopus 로고
    • A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression
    • Abd Hamid, U. M., Royle, L., Saldova, R., Radcliffe, C. M. et al., A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression. Glycobiology 2008, 18, 1105-1118.
    • (2008) Glycobiology , vol.18 , pp. 1105-1118
    • Abd Hamid, U.M.1    Royle, L.2    Saldova, R.3    Radcliffe, C.M.4
  • 77
    • 79551481037 scopus 로고    scopus 로고
    • Levels of specific serum N-glycans identify breast cancer patients with higher circulating tumor cell counts
    • Saldova, R., Reuben, J. M., Abd Hamid, U. M., Rudd, P. M., Cristofanilli, M., Levels of specific serum N-glycans identify breast cancer patients with higher circulating tumor cell counts. Ann. Oncol. 2011, 22, 1113-1119.
    • (2011) Ann. Oncol. , vol.22 , pp. 1113-1119
    • Saldova, R.1    Reuben, J.M.2    Abd Hamid, U.M.3    Rudd, P.M.4    Cristofanilli, M.5
  • 78
    • 77953555196 scopus 로고    scopus 로고
    • Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: a potential methodology for cancer-biomarker discovery
    • Alley, W. R., Madera, M., Mechref, Y., Novotny, M. V., Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: a potential methodology for cancer-biomarker discovery. Anal. Chem. 2010, 82, 5095-5106.
    • (2010) Anal. Chem , vol.82 , pp. 5095-5106
    • Alley, W.R.1    Madera, M.2    Mechref, Y.3    Novotny, M.V.4
  • 80
    • 80051717722 scopus 로고    scopus 로고
    • The emerging importance of alpha-L-fucose in human breast cancer: a review
    • Listinsky, J. J., Siegal, G. P., Listinsky, C. M., The emerging importance of alpha-L-fucose in human breast cancer: a review. Am. J. Transl. Res. 2011, 3, 292-322.
    • (2011) Am. J. Transl. Res. , vol.3 , pp. 292-322
    • Listinsky, J.J.1    Siegal, G.P.2    Listinsky, C.M.3
  • 81
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H., Sharon, N., On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473, 4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 82
    • 67049095491 scopus 로고    scopus 로고
    • Comprehensive clinico-glycomic study of 16 colorectal cancer specimens: elucidation of aberrant glycosylation and its mechanistic causes in colorectal cancer cells
    • Misonou, Y., Shida, K., Korekane, H., Seki, Y. et al., Comprehensive clinico-glycomic study of 16 colorectal cancer specimens: elucidation of aberrant glycosylation and its mechanistic causes in colorectal cancer cells. J. Proteome Res. 2009, 8, 2990-3005.
    • (2009) J. Proteome Res. , vol.8 , pp. 2990-3005
    • Misonou, Y.1    Shida, K.2    Korekane, H.3    Seki, Y.4
  • 83
    • 35448992849 scopus 로고    scopus 로고
    • Blood markers for early detection of colorectal cancer: a systematic review
    • Hundt, S., Haug, U., Brenner, H., Blood markers for early detection of colorectal cancer: a systematic review. Cancer Epidemiol. Biomarkers Prev. 2007, 16, 1935-1953.
    • (2007) Cancer Epidemiol. Biomarkers Prev. , vol.16 , pp. 1935-1953
    • Hundt, S.1    Haug, U.2    Brenner, H.3
  • 84
    • 0029863463 scopus 로고    scopus 로고
    • Enhanced sialylation of mucin-associated carbohydrate structures in human colon cancer metastasis
    • Bresalier, R. S., Ho, S. B., Schoeppner, H. L., Kim, Y. S. et al., Enhanced sialylation of mucin-associated carbohydrate structures in human colon cancer metastasis. Gastroenterology 1996, 110, 1354-1367.
    • (1996) Gastroenterology , vol.110 , pp. 1354-1367
    • Bresalier, R.S.1    Ho, S.B.2    Schoeppner, H.L.3    Kim, Y.S.4
  • 85
    • 34447345132 scopus 로고    scopus 로고
    • Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon
    • Malagolini, N., Santini, D., Chiricolo, M., Dall'Olio, F., Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon. Glycobiology 2007, 17, 688-697.
    • (2007) Glycobiology , vol.17 , pp. 688-697
    • Malagolini, N.1    Santini, D.2    Chiricolo, M.3    Dall'Olio, F.4
  • 86
    • 62049084618 scopus 로고    scopus 로고
    • Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4
    • Uemura, T., Shiozaki, K., Yamaguchi, K., Miyazaki, S. et al., Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4. Oncogene 2009, 28, 1218-1229.
    • (2009) Oncogene , vol.28 , pp. 1218-1229
    • Uemura, T.1    Shiozaki, K.2    Yamaguchi, K.3    Miyazaki, S.4
  • 87
    • 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. et al., Core fucosylation of E-cadherin enhances cell-cell adhesion in human colon carcinoma WiDr cells. Cancer Sci. 2009, 100, 888-895.
    • (2009) Cancer Sci , vol.100 , pp. 888-895
    • Osumi, D.1    Takahashi, M.2    Miyoshi, E.3    Yokoe, S.4
  • 88
    • 80051591721 scopus 로고    scopus 로고
    • Caco-2 and LS174T cell lines provide different models for studying mucin expression in colon cancer
    • Bu, X. D., Li, N., Tian, X. Q., Huang, P. L., Caco-2 and LS174T cell lines provide different models for studying mucin expression in colon cancer. Tissue Cell 2011, 43, 201-206.
    • (2011) Tissue Cell , vol.43 , pp. 201-206
    • Bu, X.D.1    Li, N.2    Tian, X.Q.3    Huang, P.L.4
  • 89
    • 0025778637 scopus 로고
    • Mucin production by human colonic carcinoma cells correlates with their metastatic potential in animal models of colon cancer metastasis
    • Bresalier, R. S., Niv, Y., Byrd, J. C., Duh, Q. Y. et al., Mucin production by human colonic carcinoma cells correlates with their metastatic potential in animal models of colon cancer metastasis. J. Clin. Invest. 1991, 87, 1037-1045.
    • (1991) J. Clin. Invest , vol.87 , pp. 1037-1045
    • Bresalier, R.S.1    Niv, Y.2    Byrd, J.C.3    Duh, Q.Y.4
  • 90
    • 0028235332 scopus 로고
    • O-Glycan biosynthesis in human colorectal adenoma cells during progression to cancer
    • Vavasseur, F., Dole, K., Yang, J., Matta, K. L. et al., O-Glycan biosynthesis in human colorectal adenoma cells during progression to cancer. Eur. J. Biochem. 1994, 222, 415-424.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 415-424
    • Vavasseur, F.1    Dole, K.2    Yang, J.3    Matta, K.L.4
  • 91
    • 84881373126 scopus 로고    scopus 로고
    • Relevant markers of cancer stem cells indicate a poor prognosis in hepatocellular carcinoma patients: a meta-analysis
    • Ma, Y. C., Yang, J. Y., Yan, L. N., Relevant markers of cancer stem cells indicate a poor prognosis in hepatocellular carcinoma patients: a meta-analysis. Eur. J. Gastroenterol. Hepatol. 2013, 25, 1007-1016.
    • (2013) Eur. J. Gastroenterol. Hepatol , vol.25 , pp. 1007-1016
    • Ma, Y.C.1    Yang, J.Y.2    Yan, L.N.3
  • 92
    • 34250020201 scopus 로고    scopus 로고
    • Hepatocellular carcinoma: epidemiology and molecular carcinogenesis
    • El-Serag, H. B., Rudolph, K. L., Hepatocellular carcinoma: epidemiology and molecular carcinogenesis. Gastroenterology 2007, 132, 2557-2576.
    • (2007) Gastroenterology , vol.132 , pp. 2557-2576
    • El-Serag, H.B.1    Rudolph, K.L.2
  • 93
    • 84874600175 scopus 로고    scopus 로고
    • Management of small hepatocellular carcinoma in cirrhosis: focus on portal hypertension
    • Hernandez-Gea, V., Turon, F., Berzigotti, A., Villanueva, A., Management of small hepatocellular carcinoma in cirrhosis: focus on portal hypertension. World J. Gastroenterol. 2013, 19, 1193-1199.
    • (2013) World J. Gastroenterol , vol.19 , pp. 1193-1199
    • Hernandez-Gea, V.1    Turon, F.2    Berzigotti, A.3    Villanueva, A.4
  • 94
    • 84876267925 scopus 로고    scopus 로고
    • Recent advances in the treatment of hepatocellular carcinoma
    • Padhya, K. T., Marrero, J. A., Singal, A. G., Recent advances in the treatment of hepatocellular carcinoma. Curr. Opin. Gastroenterol. 2013, 29, 285-292.
    • (2013) Curr. Opin. Gastroenterol , vol.29 , pp. 285-292
    • Padhya, K.T.1    Marrero, J.A.2    Singal, A.G.3
  • 96
    • 80053158728 scopus 로고    scopus 로고
    • Highly sensitive lens culinaris agglutinin-reactive alpha-fetoprotein is useful for early detection of hepatocellular carcinoma in patients with chronic liver disease
    • Oda, K., Ido, A., Tamai, T., Matsushita, M. et al., Highly sensitive lens culinaris agglutinin-reactive alpha-fetoprotein is useful for early detection of hepatocellular carcinoma in patients with chronic liver disease. Oncol. Rep. 2011, 26, 1227-1233.
    • (2011) Oncol. Rep. , vol.26 , pp. 1227-1233
    • Oda, K.1    Ido, A.2    Tamai, T.3    Matsushita, M.4
  • 97
    • 84875884309 scopus 로고    scopus 로고
    • Fucosylated fraction of alpha-fetoprotein as a serological marker of early hepatocellular carcinoma
    • Moriya, S., Morimoto, M., Numata, K., Nozaki, A. et al., Fucosylated fraction of alpha-fetoprotein as a serological marker of early hepatocellular carcinoma. Anticancer Res. 2013, 33, 997-1001.
    • (2013) Anticancer Res , vol.33 , pp. 997-1001
    • Moriya, S.1    Morimoto, M.2    Numata, K.3    Nozaki, A.4
  • 98
    • 50449096184 scopus 로고    scopus 로고
    • Toward cancer biomarker discovery using the glycomics approach
    • Taniguchi, N., Toward cancer biomarker discovery using the glycomics approach. Proteomics 2008, 8, 3205-3208.
    • (2008) Proteomics , vol.8 , pp. 3205-3208
    • Taniguchi, N.1
  • 99
    • 70449970103 scopus 로고    scopus 로고
    • Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein markers
    • Dai, Z., Zhou, J., Qiu, S. J., Liu, Y. K., Fan, J., Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein markers. Electrophoresis 2009, 30, 2957-2966.
    • (2009) Electrophoresis , vol.30 , pp. 2957-2966
    • Dai, Z.1    Zhou, J.2    Qiu, S.J.3    Liu, Y.K.4    Fan, J.5
  • 100
    • 47649102850 scopus 로고    scopus 로고
    • Diagnosing and monitoring hepatocellular carcinoma with alpha-fetoprotein: new aspects and applications
    • Debruyne, E. N., Delanghe, J. R., Diagnosing and monitoring hepatocellular carcinoma with alpha-fetoprotein: new aspects and applications. Clin. Chim. Acta 2008, 395, 19-26.
    • (2008) Clin. Chim. Acta , vol.395 , pp. 19-26
    • Debruyne, E.N.1    Delanghe, J.R.2
  • 101
    • 0033226804 scopus 로고    scopus 로고
    • Usefulness of Lens culinaris agglutinin A-reactive fraction of alpha-fetoprotein (AFP-L3) as a marker of distant metastasis from hepatocellular carcinoma
    • Yamashiki, N., Seki, T., Wakabayashi, M., Nakagawa, T. et al., Usefulness of Lens culinaris agglutinin A-reactive fraction of alpha-fetoprotein (AFP-L3) as a marker of distant metastasis from hepatocellular carcinoma. Oncol. Rep. 1999, 6, 1229-1232.
    • (1999) Oncol. Rep. , vol.6 , pp. 1229-1232
    • Yamashiki, N.1    Seki, T.2    Wakabayashi, M.3    Nakagawa, T.4
  • 102
    • 0032951103 scopus 로고    scopus 로고
    • Clinical utility of Lens culinaris agglutinin-reactive alpha-fetoprotein in small hepatocellular carcinoma: special reference to imaging diagnosis
    • Kumada, T., Nakano, S., Takeda, I., Kiriyama, S. et al., Clinical utility of Lens culinaris agglutinin-reactive alpha-fetoprotein in small hepatocellular carcinoma: special reference to imaging diagnosis. J. Hepatol. 1999, 30, 125-130.
    • (1999) J. Hepatol , vol.30 , pp. 125-130
    • Kumada, T.1    Nakano, S.2    Takeda, I.3    Kiriyama, S.4
  • 103
    • 0027422524 scopus 로고
    • A collaborative study for the evaluation of lectin-reactive alpha-fetoproteins in early detection of hepatocellular carcinoma
    • Taketa, K., Endo, Y., Sekiya, C., Tanikawa, K. et al., A collaborative study for the evaluation of lectin-reactive alpha-fetoproteins in early detection of hepatocellular carcinoma. Cancer Res. 1993, 53, 5419-5423.
    • (1993) Cancer Res. , vol.53 , pp. 5419-5423
    • Taketa, K.1    Endo, Y.2    Sekiya, C.3    Tanikawa, K.4
  • 104
    • 0034749063 scopus 로고    scopus 로고
    • AFP-L3: a new generation of tumor marker for hepatocellular carcinoma
    • Li, D., Mallory, T., Satomura, S., AFP-L3: a new generation of tumor marker for hepatocellular carcinoma. Clin. Chim. Acta 2001, 313, 15-19.
    • (2001) Clin. Chim. Acta , vol.313 , pp. 15-19
    • Li, D.1    Mallory, T.2    Satomura, S.3
  • 105
    • 0027398098 scopus 로고
    • Contribution of carbohydrate antigens sialyl Lewis A and sialyl Lewis X to adhesion of human cancer cells to vascular endothelium
    • Takada, A., Ohmori, K., Yoneda, T., Tsuyuoka, K. et al., Contribution of carbohydrate antigens sialyl Lewis A and sialyl Lewis X to adhesion of human cancer cells to vascular endothelium. Cancer Res. 1993, 53, 354-361.
    • (1993) Cancer Res. , vol.53 , pp. 354-361
    • Takada, A.1    Ohmori, K.2    Yoneda, T.3    Tsuyuoka, K.4
  • 106
    • 0742306881 scopus 로고    scopus 로고
    • Expression of β-galactoside α2,6 sialyltransferase and of α2,6-sialylated glycoconjugates in normal human liver, hepatocarcinoma, and cirrhosis
    • Dall'Olio, F., Chiricolo, M., D'Errico, A., Gruppioni, E. et al., Expression of β-galactoside α2, 6 sialyltransferase and of α2, 6-sialylated glycoconjugates in normal human liver, hepatocarcinoma, and cirrhosis. Glycobiology 2004, 14, 39-49.
    • (2004) Glycobiology , vol.14 , pp. 39-49
    • Dall'Olio, F.1    Chiricolo, M.2    D'Errico, A.3    Gruppioni, E.4
  • 107
    • 84862846021 scopus 로고    scopus 로고
    • Increased levels of tetra-antennary N-linked glycan but not core fucosylation are associated with hepatocellular carcinoma tissue
    • Mehta, A., Norton, P., Liang, H., Comunale, M. A. et al., Increased levels of tetra-antennary N-linked glycan but not core fucosylation are associated with hepatocellular carcinoma tissue. Cancer Epidemiol. Biomarkers Prev. 2012, 21, 925-933.
    • (2012) Cancer Epidemiol. Biomarkers Prev. , vol.21 , pp. 925-933
    • Mehta, A.1    Norton, P.2    Liang, H.3    Comunale, M.A.4
  • 109
    • 0025803638 scopus 로고
    • Fucosyltransferases: differential plasma and tissue alterations in hepatocellular carcinoma and cirrhosis
    • Hutchinson, W. L., Du, M.-Q., Johnson, P. J., Williams, R., Fucosyltransferases: differential plasma and tissue alterations in hepatocellular carcinoma and cirrhosis. Hepatology 1991, 13, 683-688.
    • (1991) Hepatology , vol.13 , pp. 683-688
    • Hutchinson, W.L.1    Du, M.-Q.2    Johnson, P.J.3    Williams, R.4
  • 110
    • 0031934239 scopus 로고    scopus 로고
    • Elevated activity of N-acetylglucosaminyltransferase V in human hepatocellular carcinoma
    • Yao, M., Zhou, D.-P., Jiang, S.-M., Wang, Q.-H. et al., Elevated activity of N-acetylglucosaminyltransferase V in human hepatocellular carcinoma. J. Cancer Res. Clin. Oncol. 1998, 124, 27-30.
    • (1998) J. Cancer Res. Clin. Oncol. , vol.124 , pp. 27-30
    • Yao, M.1    Zhou, D.-P.2    Jiang, S.-M.3    Wang, Q.-H.4
  • 111
    • 0024278682 scopus 로고
    • Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures
    • Passaniti, A., Hart, G. W., Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures. J. Biol. Chem. 1988, 263, 7591-7603.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7591-7603
    • Passaniti, A.1    Hart, G.W.2
  • 112
    • 0025939031 scopus 로고
    • N-linked sugar chains of mouse B16 melanoma cells and their low-metastasizing variant selected by wheat germ agglutinin
    • Kawano, T., Takasaki, S., Tao, T. W., Kobata, A., N-linked sugar chains of mouse B16 melanoma cells and their low-metastasizing variant selected by wheat germ agglutinin. Glycobiology 1991, 1, 375-385.
    • (1991) Glycobiology , vol.1 , pp. 375-385
    • Kawano, T.1    Takasaki, S.2    Tao, T.W.3    Kobata, A.4
  • 113
    • 0031023592 scopus 로고    scopus 로고
    • Reduction of metastatic properties of BL6 melanoma cells expressing terminal fucose(alpha)1-2-galactose after alpha1,2-fucosyltransferase cDNA transfection
    • Gorelik, E., Xu, F., Henion, T., Anaraki, F., Galili, U., Reduction of metastatic properties of BL6 melanoma cells expressing terminal fucose(alpha)1-2-galactose after alpha1, 2-fucosyltransferase cDNA transfection. Cancer Res. 1997, 57, 332-336.
    • (1997) Cancer Res. , vol.57 , pp. 332-336
    • Gorelik, E.1    Xu, F.2    Henion, T.3    Anaraki, F.4    Galili, U.5
  • 114
    • 13544255695 scopus 로고    scopus 로고
    • N-glycoproteins bearing beta1-6 branched oligosaccharides from the A375 human melanoma cell line analysed by tandem mass spectrometry
    • Ochwat, D., Hoja-Lukowicz, D., Litynska, A., N-glycoproteins bearing beta1-6 branched oligosaccharides from the A375 human melanoma cell line analysed by tandem mass spectrometry. Melanoma Res. 2004, 14, 479-485.
    • (2004) Melanoma Res. , vol.14 , pp. 479-485
    • Ochwat, D.1    Hoja-Lukowicz, D.2    Litynska, A.3
  • 115
    • 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, 13811-13815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 117
    • 0036178190 scopus 로고    scopus 로고
    • Current understanding of the epidemiology and clinical implications of BRCA1 and BRCA2 mutations for ovarian cancer
    • Narod, S. A., Boyd, J., Current understanding of the epidemiology and clinical implications of BRCA1 and BRCA2 mutations for ovarian cancer. Curr. Opin. Obstet. Gynecol. 2002, 14, 19-26.
    • (2002) Curr. Opin. Obstet. Gynecol. , vol.14 , pp. 19-26
    • Narod, S.A.1    Boyd, J.2
  • 118
    • 33751427410 scopus 로고    scopus 로고
    • Proceedings of a GOG workshop on intraperitoneal therapy for ovarian cancer
    • Alberts, D. S., Markman, M., Muggia, F., Ozols, R. F. et al., Proceedings of a GOG workshop on intraperitoneal therapy for ovarian cancer. Gynecol. Oncol. 2006, 103, 783-792.
    • (2006) Gynecol. Oncol. , vol.103 , pp. 783-792
    • Alberts, D.S.1    Markman, M.2    Muggia, F.3    Ozols, R.F.4
  • 119
    • 0036361955 scopus 로고    scopus 로고
    • The scientific basis of early detection of epithelial ovarian cancer: the National Ovarian Cancer Early Detection Program (NOCEDP)
    • Fishman, D. A., Bozorgi, K., The scientific basis of early detection of epithelial ovarian cancer: the National Ovarian Cancer Early Detection Program (NOCEDP). Cancer Treat Res. 2002, 107, 3-28.
    • (2002) Cancer Treat Res. , vol.107 , pp. 3-28
    • Fishman, D.A.1    Bozorgi, K.2
  • 120
    • 33646560022 scopus 로고    scopus 로고
    • Systemic therapy for ovarian cancer: current status and new treatments
    • Ozols, R. F., Systemic therapy for ovarian cancer: current status and new treatments. Semin. Oncol. 2006, 33, S3-S11.
    • (2006) Semin. Oncol. , vol.33
    • Ozols, R.F.1
  • 122
    • 33644845467 scopus 로고    scopus 로고
    • Does aggressive surgery only benefit patients with less advanced ovarian cancer? Results from an international comparison within the SCOTROC-1 Trial
    • Crawford, S. C., Vasey, P. A., Paul, J., Hay, A. et al., Does aggressive surgery only benefit patients with less advanced ovarian cancer? Results from an international comparison within the SCOTROC-1 Trial. J. Clin. Oncol. 2005, 23, 8802-8811.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 8802-8811
    • Crawford, S.C.1    Vasey, P.A.2    Paul, J.3    Hay, A.4
  • 123
    • 7444262835 scopus 로고    scopus 로고
    • Factors associated with cytoreducibility among women with ovarian carcinoma
    • Eltabbakh, G. H., Mount, S. L., Beatty, B., Simmons-Arnold, L. et al., Factors associated with cytoreducibility among women with ovarian carcinoma. Gynecol. Oncol. 2004, 95, 377-383.
    • (2004) Gynecol. Oncol. , vol.95 , pp. 377-383
    • Eltabbakh, G.H.1    Mount, S.L.2    Beatty, B.3    Simmons-Arnold, L.4
  • 124
    • 33745602539 scopus 로고    scopus 로고
    • Diagnosis and management of epithelial ovarian cancer
    • Bhoola, S., Hoskins, W. J., Diagnosis and management of epithelial ovarian cancer. Obstet. Gynecol. 2006, 107, 1399-1410.
    • (2006) Obstet. Gynecol. , vol.107 , pp. 1399-1410
    • Bhoola, S.1    Hoskins, W.J.2
  • 125
    • 33947258908 scopus 로고    scopus 로고
    • Phase II study of carboplatin followed by sequential gemcitabine and paclitaxel as first-line treatment for advanced ovarian cancer
    • Friedlander, M., Buck, M., Wyld, D., Findlay, M. et al., Phase II study of carboplatin followed by sequential gemcitabine and paclitaxel as first-line treatment for advanced ovarian cancer. Int. J. Gynecol. Cancer 2007, 17, 350-358.
    • (2007) Int. J. Gynecol. Cancer , vol.17 , pp. 350-358
    • Friedlander, M.1    Buck, M.2    Wyld, D.3    Findlay, M.4
  • 126
    • 0032963634 scopus 로고    scopus 로고
    • Selection of carbohydrate antigens in human epithelial ovarian cancers as targets for immunotherapy: serous and mucinous tumors exhibit distinctive patterns of expression
    • Federici, M. F., Kudryashov, V., Saigo, P. E., Finstad, C. L., Lloyd, K. O., Selection of carbohydrate antigens in human epithelial ovarian cancers as targets for immunotherapy: serous and mucinous tumors exhibit distinctive patterns of expression. Int. J. Cancer 1999, 81, 193-198.
    • (1999) Int. J. Cancer , vol.81 , pp. 193-198
    • Federici, M.F.1    Kudryashov, V.2    Saigo, P.E.3    Finstad, C.L.4    Lloyd, K.O.5
  • 127
    • 75149122087 scopus 로고    scopus 로고
    • Proteogenomic studies in epithelial ovarian cancer: established knowledge and future needs
    • Jacob, F., Goldstein, D. R., Fink, D., Heinzelmann-Schwarz, V., Proteogenomic studies in epithelial ovarian cancer: established knowledge and future needs. Biomark. Med. 2009, 3, 743-756.
    • (2009) Biomark. Med. , vol.3 , pp. 743-756
    • Jacob, F.1    Goldstein, D.R.2    Fink, D.3    Heinzelmann-Schwarz, V.4
  • 129
    • 50349091687 scopus 로고    scopus 로고
    • The early detection of ovarian cancer: from traditional methods to proteomics. Can we really do better than serum CA-125
    • Nossov, V., Amneus, M., Su, F., Lang, J. et al., The early detection of ovarian cancer: from traditional methods to proteomics. Can we really do better than serum CA-125? Am. J. Obstet. Gynecol. 2008, 199, 215-223.
    • (2008) Am. J. Obstet. Gynecol. , vol.199 , pp. 215-223
    • Nossov, V.1    Amneus, M.2    Su, F.3    Lang, J.4
  • 130
    • 81055154923 scopus 로고    scopus 로고
    • 5-AZA-2'-deoxycytidine induced demethylation influences N-glycosylation of secreted glycoproteins in ovarian cancer
    • Saldova, R., Dempsey, E., Perez-Garay, M., Marino, K. et al., 5-AZA-2'-deoxycytidine induced demethylation influences N-glycosylation of secreted glycoproteins in ovarian cancer. Epigenetics 2011, 6, 1362-1372.
    • (2011) Epigenetics , vol.6 , pp. 1362-1372
    • Saldova, R.1    Dempsey, E.2    Perez-Garay, M.3    Marino, K.4
  • 131
    • 0042206865 scopus 로고    scopus 로고
    • Characterization of the oligosaccharides associated with the human ovarian tumor marker CA125
    • Kui Wong, N., Easton, R. L., Panico, M., Sutton-Smith, M. et al., Characterization of the oligosaccharides associated with the human ovarian tumor marker CA125. J. Biol. Chem. 2003, 278, 28619-28634.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28619-28634
    • Kui Wong, N.1    Easton, R.L.2    Panico, M.3    Sutton-Smith, M.4
  • 132
    • 67349087158 scopus 로고    scopus 로고
    • ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function
    • doi: 10.1186/1757-2215-1-3.
    • Christie, D. R., Shaikh, F. M., Lucas, J. A. t., Lucas, J. A., 3rd, Bellis, S. L., ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function. J. Ovarian. Res. 2008, 1, 3. doi: 10.1186/1757-2215-1-3.
    • (2008) J. Ovarian. Res. , vol.1 , pp. 3
    • Christie, D.R.1    Shaikh, F.M.2    Lucas, J.A.t.3    Lucas III, J.A.4    Bellis, S.L.5
  • 133
    • 84878831802 scopus 로고    scopus 로고
    • Priming mass spectrometry-based sulfoglycomic mapping for identification of terminal sulfated lacdiNAc glycotope
    • Yu, S. Y., Chang, L. Y., Cheng, C. W., Chou, C. C. et al., Priming mass spectrometry-based sulfoglycomic mapping for identification of terminal sulfated lacdiNAc glycotope. Glycoconj. J. 2013, 30, 183-194.
    • (2013) Glycoconj. J. , vol.30 , pp. 183-194
    • Yu, S.Y.1    Chang, L.Y.2    Cheng, C.W.3    Chou, C.C.4
  • 134
    • 33749360659 scopus 로고    scopus 로고
    • Different expression levels of alpha3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines
    • Escrevente, C., Machado, E., Brito, C., Reis, C. A. et al., Different expression levels of alpha3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines. Int. J. Oncol. 2006, 29, 557-566.
    • (2006) Int. J. Oncol. , vol.29 , pp. 557-566
    • Escrevente, C.1    Machado, E.2    Brito, C.3    Reis, C.A.4
  • 135
    • 67650996838 scopus 로고    scopus 로고
    • Analysis of the human cancer glycome identifies a novel group of tumor-associated N-acetylglucosamine glycan antigens
    • Satomaa, T., Heiskanen, A., Leonardsson, I., Angstrom, J. et al., Analysis of the human cancer glycome identifies a novel group of tumor-associated N-acetylglucosamine glycan antigens. Cancer Res. 2009, 69, 5811-5819.
    • (2009) Cancer Res. , vol.69 , pp. 5811-5819
    • Satomaa, T.1    Heiskanen, A.2    Leonardsson, I.3    Angstrom, J.4
  • 136
    • 33846624310 scopus 로고    scopus 로고
    • Intraepithelial carcinoma of the fimbria and pelvic serous carcinoma: evidence for a causal relationship
    • Kindelberger, D. W., Lee, Y., Miron, A., Hirsch, M. S. et al., Intraepithelial carcinoma of the fimbria and pelvic serous carcinoma: evidence for a causal relationship. Am. J. Surg. Pathol. 2007, 31, 161-169.
    • (2007) Am. J. Surg. Pathol. , vol.31 , pp. 161-169
    • Kindelberger, D.W.1    Lee, Y.2    Miron, A.3    Hirsch, M.S.4
  • 137
    • 33846187651 scopus 로고    scopus 로고
    • A candidate precursor to serous carcinoma that originates in the distal fallopian tube
    • Lee, Y., Miron, A., Drapkin, R., Nucci, M. R. et al., A candidate precursor to serous carcinoma that originates in the distal fallopian tube. J. Pathol. 2007, 211, 26-35.
    • (2007) J. Pathol. , vol.211 , pp. 26-35
    • Lee, Y.1    Miron, A.2    Drapkin, R.3    Nucci, M.R.4
  • 138
    • 39349116737 scopus 로고    scopus 로고
    • Serous carcinogenesis in the fallopian tube: a descriptive classification
    • Jarboe, E., Folkins, A., Nucci, M. R., Kindelberger, D. et al., Serous carcinogenesis in the fallopian tube: a descriptive classification. Int. J. Gynecol. Pathol. 2008, 27, 1-9.
    • (2008) Int. J. Gynecol. Pathol. , vol.27 , pp. 1-9
    • Jarboe, E.1    Folkins, A.2    Nucci, M.R.3    Kindelberger, D.4
  • 139
    • 80054732170 scopus 로고    scopus 로고
    • Serum antiglycan antibody detection of nonmucinous ovarian cancers by using a printed glycan array
    • Jacob, F., Goldstein, D. R., Bovin, N. V., Pochechueva, T. et al., Serum antiglycan antibody detection of nonmucinous ovarian cancers by using a printed glycan array. Int. J. Cancer. 2012, 130, 138-146.
    • (2012) Int. J. Cancer , vol.130 , pp. 138-146
    • Jacob, F.1    Goldstein, D.R.2    Bovin, N.V.3    Pochechueva, T.4
  • 140
    • 77954340426 scopus 로고    scopus 로고
    • Newly diagnosed and relapsed epithelial ovarian carcinoma: ESMO Clinical Practice Guidelines for diagnosis, treatment and follow-up
    • Colombo, N., Peiretti, M., Parma, G., Lapresa, M. et al., Newly diagnosed and relapsed epithelial ovarian carcinoma: ESMO Clinical Practice Guidelines for diagnosis, treatment and follow-up. Ann. Oncol. 2010, 21 (Suppl 5), v23-v30.
    • (2010) Ann. Oncol. , vol.21 , Issue.SUPPL. 5
    • Colombo, N.1    Peiretti, M.2    Parma, G.3    Lapresa, M.4
  • 141
    • 31444433687 scopus 로고    scopus 로고
    • Altered glycosylation in cancer: sialic acids and sialyltransferases
    • Wang, P. H., Altered glycosylation in cancer: sialic acids and sialyltransferases. J. Cancer Mol. 2005, 1, 73-81.
    • (2005) J. Cancer Mol. , vol.1 , pp. 73-81
    • Wang, P.H.1
  • 142
    • 0004106191 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY).
    • Varki, A., Schauer, R., Essentials of Glycobiology, Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY) 2009.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Schauer, R.2
  • 143
    • 0029758363 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of sialyltransferases
    • Tsuji, S., Molecular cloning and functional analysis of sialyltransferases. J. Biochem. 1996, 120, 1-13.
    • (1996) J. Biochem. , vol.120 , pp. 1-13
    • Tsuji, S.1
  • 144
    • 0040668346 scopus 로고    scopus 로고
    • Sialyl Lewis(a): a tumor-associated carbohydrate antigen involved in adhesion and metastatic potential of cancer cells
    • Ugorski, M., Laskowska, A., Sialyl Lewis(a): a tumor-associated carbohydrate antigen involved in adhesion and metastatic potential of cancer cells. Acta Biochim. Pol. 2002, 49, 303-311.
    • (2002) Acta Biochim. Pol. , vol.49 , pp. 303-311
    • Ugorski, M.1    Laskowska, A.2
  • 145
    • 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. 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, 3632-3637.
    • (1993) Cancer Res. , vol.53 , pp. 3632-3637
    • Nakamori, S.1    Kameyama, M.2    Imaoka, S.3    Furukawa, H.4
  • 146
    • 0030910463 scopus 로고    scopus 로고
    • Endothelial-selectin ligands sialyl Lewis(x) and sialyl Lewis(a) are differentiation antigens immunogenic in human melanoma
    • Ravindranath, M. H., Amiri, A. A., Bauer, P. M., Kelley, M. C. et al., Endothelial-selectin ligands sialyl Lewis(x) and sialyl Lewis(a) are differentiation antigens immunogenic in human melanoma. Cancer 1997, 79, 1686-1697.
    • (1997) Cancer , vol.79 , pp. 1686-1697
    • Ravindranath, M.H.1    Amiri, A.A.2    Bauer, P.M.3    Kelley, M.C.4
  • 147
    • 0030761635 scopus 로고    scopus 로고
    • Endothelial and epithelial expression of sialyl Lewis(x) and sialyl Lewis(a) in lesions of breast carcinoma
    • Renkonen, J., Paavonen, T., Renkonen, R., Endothelial and epithelial expression of sialyl Lewis(x) and sialyl Lewis(a) in lesions of breast carcinoma. Int. J. Cancer 1997, 74, 296-300.
    • (1997) Int. J. Cancer , vol.74 , pp. 296-300
    • Renkonen, J.1    Paavonen, T.2    Renkonen, R.3
  • 148
    • 0027210907 scopus 로고
    • Association of expression of blood group-related carbohydrate antigens with prognosis in breast cancer
    • Narita, T., Funahashi, H., Satoh, Y., Watanabe, T. et al., Association of expression of blood group-related carbohydrate antigens with prognosis in breast cancer. Cancer 1993, 71, 3044-3053.
    • (1993) Cancer , vol.71 , pp. 3044-3053
    • Narita, T.1    Funahashi, H.2    Satoh, Y.3    Watanabe, T.4
  • 149
    • 21244447444 scopus 로고    scopus 로고
    • Expression of sialyl lewis X, sialyl Lewis A, E-cadherin and cathepsin-D in human breast cancer: immunohistochemical analysis in mammary carcinoma in situ, invasive carcinomas and their lymph node metastasis
    • Jeschke, U., Mylonas, I., Shabani, N., Kunert-Keil, C. et al., Expression of sialyl lewis X, sialyl Lewis A, E-cadherin and cathepsin-D in human breast cancer: immunohistochemical analysis in mammary carcinoma in situ, invasive carcinomas and their lymph node metastasis. Anticancer Res. 2005, 25, 1615-1622.
    • (2005) Anticancer Res. , vol.25 , pp. 1615-1622
    • Jeschke, U.1    Mylonas, I.2    Shabani, N.3    Kunert-Keil, C.4
  • 150
    • 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. 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, 753-760.
    • (2000) Can. J. Gastroenterol. , vol.14 , pp. 753-760
    • Nakagoe, T.1    Fukushima, K.2    Nanashima, A.3    Sawai, T.4
  • 151
    • 0026634013 scopus 로고
    • Expression of sialylated Lewis(x) antigen in chronic and neoplastic liver diseases
    • Jagirdar, J., Thung, S. N., Shah, K. D., Nudelman, E. et al., Expression of sialylated Lewis(x) antigen in chronic and neoplastic liver diseases. Arch. Pathol. Lab. Med. 1992, 116, 643-648.
    • (1992) Arch. Pathol. Lab. Med. , vol.116 , pp. 643-648
    • Jagirdar, J.1    Thung, S.N.2    Shah, K.D.3    Nudelman, E.4
  • 152
    • 0033559260 scopus 로고    scopus 로고
    • Dual roles of sialyl Lewis X oligosaccharides in tumor metastasis and rejection by natural killer cells
    • Ohyama, C., Tsuboi, S., Fukuda, M., Dual roles of sialyl Lewis X oligosaccharides in tumor metastasis and rejection by natural killer cells. EMBO J. 1999, 18, 1516-1525.
    • (1999) EMBO J. , vol.18 , pp. 1516-1525
    • Ohyama, C.1    Tsuboi, S.2    Fukuda, M.3
  • 153
    • 0041699690 scopus 로고    scopus 로고
    • Prognostic value of tumoral sialyltransferase expression and circulating E-selectin concentrations in node-negative breast cancer patients
    • Hebbar, M., Krzewinski-Recchi, M. A., Hornez, L., Verdiere, A. et al., Prognostic value of tumoral sialyltransferase expression and circulating E-selectin concentrations in node-negative breast cancer patients. Int. J. Biol. Markers 2003, 18, 116-122.
    • (2003) Int. J. Biol. Markers , vol.18 , pp. 116-122
    • Hebbar, M.1    Krzewinski-Recchi, M.A.2    Hornez, L.3    Verdiere, A.4
  • 154
    • 0034351214 scopus 로고    scopus 로고
    • The sialyl-α2,6-lactosaminyl-structure: Biosynthesis and functional role
    • Dall'Olio, F., The sialyl-α2, 6-lactosaminyl-structure: Biosynthesis and functional role. Glycoconj. J. 2000, 17, 669-676.
    • (2000) Glycoconj. J , vol.17 , pp. 669-676
    • Dall'Olio, F.1
  • 155
    • 0029666070 scopus 로고    scopus 로고
    • Unique alpha 2, 8-polysialylated glycoproteins in breast cancer and leukemia cells
    • Martersteck, C. M., Kedersha, N. L., Drapp, D. A., Tsui, T. G., Colley, K. J., Unique alpha 2, 8-polysialylated glycoproteins in breast cancer and leukemia cells. Glycobiology 1996, 6, 289-301.
    • (1996) Glycobiology , vol.6 , pp. 289-301
    • Martersteck, C.M.1    Kedersha, N.L.2    Drapp, D.A.3    Tsui, T.G.4    Colley, K.J.5
  • 156
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: biosynthesis and biological function in mammals
    • Becker, D. J., Lowe, J. B., Fucose: biosynthesis and biological function in mammals. Glycobiology 2003, 13, 41R-53R.
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 157
    • 44449153943 scopus 로고    scopus 로고
    • Functional roles of N-glycans in cell signaling and cell adhesion in cancer
    • Zhao, Y.-Y., Takahashi, M., Gu, J.-G., Miyoshi, E. et al., Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci. 2008, 99, 1304-1310.
    • (2008) Cancer Sci , vol.99 , pp. 1304-1310
    • Zhao, Y.-Y.1    Takahashi, M.2    Gu, J.-G.3    Miyoshi, E.4
  • 158
    • 79960978002 scopus 로고    scopus 로고
    • Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells
    • Liu, Y.-C., Yen, H.-Y., Chen, C.-Y., Chen, C.-H. et al., Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells. Proc. Natl. Acad. Sci. 2011, 108, 11332-11337.
    • (2011) Proc. Natl. Acad. Sci , vol.108 , pp. 11332-11337
    • Liu, Y.-C.1    Yen, H.-Y.2    Chen, C.-Y.3    Chen, C.-H.4
  • 159
    • 84859560597 scopus 로고    scopus 로고
    • N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients
    • Alley, W. R., Jr., Vasseur, J. A., Goetz, J. A., Svoboda, M. et al., N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients. J. Proteome Res. 2012, 11, 2282-2300.
    • (2012) J. Proteome Res. , vol.11 , pp. 2282-2300
    • Alley Jr, W.R.1    Vasseur, J.A.2    Goetz, J.A.3    Svoboda, M.4
  • 160
    • 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, 725-729.
    • (2008) J. Biochem. , vol.143 , pp. 725-729
    • Miyoshi, E.1    Moriwaki, K.2    Nakagawa, T.3
  • 161
    • 84876697786 scopus 로고    scopus 로고
    • Expression of alpha 1,6-fucosyltransferase 8 in hepatitis B virus-related hepatocellular carcinoma influences tumour progression
    • Ji, J., Gu, X., Fang, M., Zhao, Y. et al., Expression of alpha 1, 6-fucosyltransferase 8 in hepatitis B virus-related hepatocellular carcinoma influences tumour progression. Digest. Liver Dis. 2013, 45, 414-421.
    • (2013) Digest. Liver Dis. , vol.45 , pp. 414-421
    • Ji, J.1    Gu, X.2    Fang, M.3    Zhao, Y.4
  • 162
    • 0026502517 scopus 로고
    • Mucin synthesis and secretion in relation to spontaneous differentiation of colon cancer cells in vitro
    • Niv, Y., Byrd, J. C., Ho, S. B., Dahiya, R., Kim, Y. S., Mucin synthesis and secretion in relation to spontaneous differentiation of colon cancer cells in vitro. Int. J. Cancer 1992, 50, 147-152.
    • (1992) Int. J. Cancer , vol.50 , pp. 147-152
    • Niv, Y.1    Byrd, J.C.2    Ho, S.B.3    Dahiya, R.4    Kim, Y.S.5
  • 164
    • 0018759548 scopus 로고
    • Characterization of WiDr: a human colon carcinoma cell line
    • Noguchi, P., Wallace, R., Johnson, J., Earley, E. M. et al., Characterization of WiDr: a human colon carcinoma cell line. In Vitro 1979, 15, 401-408.
    • (1979) In Vitro , vol.15 , pp. 401-408
    • Noguchi, P.1    Wallace, R.2    Johnson, J.3    Earley, E.M.4
  • 165
    • 62349133903 scopus 로고    scopus 로고
    • Highly fucosylated N-glycan ligands for mannan-binding protein expressed specifically on CD26 (DPPVI) isolated from a human colorectal carcinoma cell line, SW1116
    • Kawasaki, N., Lin, C. W., Inoue, R., Khoo, K. H. et al., Highly fucosylated N-glycan ligands for mannan-binding protein expressed specifically on CD26 (DPPVI) isolated from a human colorectal carcinoma cell line, SW1116. Glycobiology 2009, 19, 437-450.
    • (2009) Glycobiology , vol.19 , pp. 437-450
    • Kawasaki, N.1    Lin, C.W.2    Inoue, R.3    Khoo, K.H.4
  • 166
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose
    • Ferrara, C., Grau, S., Jäger, C., Sondermann, P. et al., Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose. Proc. Natl. Acad. Sci. 2011, 108, 12669-12674.
    • (2011) Proc. Natl. Acad. Sci , vol.108 , pp. 12669-12674
    • Ferrara, C.1    Grau, S.2    Jäger, C.3    Sondermann, P.4
  • 167
    • 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, 725-729.
    • (2008) J. Biochem , vol.143 , pp. 725-729
    • Miyoshi, E.1    Moriwaki, K.2    Nakagawa, T.3
  • 168
    • 70249098332 scopus 로고    scopus 로고
    • Taniguchi, N., Honke, K., Fukuda, M., Clausen, H., Eds.), Springer, Japan.
    • Kannagi, R., in: Taniguchi, N., Honke, K., Fukuda, M., Clausen, H., et al. (Eds.), Handbook of Glycosyltransferases and Related Genes, Springer, Japan 2002, pp. 237-245.
    • (2002) Handbook of Glycosyltransferases and Related Genes , pp. 237-245
    • Kannagi, R.1
  • 169
    • 11544370976 scopus 로고    scopus 로고
    • Gene expression of fucosyl- and sialyl-transferases which synthesize sialyl Lewis(x), the carbohydrate ligands for E-selectin, in human breast cancer
    • Matsuura, N., Narita, T., Hiraiwa, N., Hiraiwa, M. et al., Gene expression of fucosyl- and sialyl-transferases which synthesize sialyl Lewis(x), the carbohydrate ligands for E-selectin, in human breast cancer. Int. J. Oncol. 1998, 12, 1157-1164.
    • (1998) Int. J. Oncol , vol.12 , pp. 1157-1164
    • Matsuura, N.1    Narita, T.2    Hiraiwa, N.3    Hiraiwa, M.4
  • 170
    • 0026547034 scopus 로고
    • Quantitative dot blot analyses of blood-group-related antigens in paired normal and malignant human breast tissues
    • Ura, Y., Dion, A. S., Williams, C. J., Olsen, B. D. et al., Quantitative dot blot analyses of blood-group-related antigens in paired normal and malignant human breast tissues. Int. J. Cancer 1992, 50, 57-63.
    • (1992) Int. J. Cancer , vol.50 , pp. 57-63
    • Ura, Y.1    Dion, A.S.2    Williams, C.J.3    Olsen, B.D.4
  • 172
    • 80053611914 scopus 로고    scopus 로고
    • The effect of overexpression of α1,3-fucosyltransferase VII on adhesive capability of human colon carcinoma HT-29 cells to HUVECs
    • Yue, L., Yu, H., Zhang, C., Liu, J., The effect of overexpression of α1, 3-fucosyltransferase VII on adhesive capability of human colon carcinoma HT-29 cells to HUVECs. Adv. Mat. Res. 2012, 345, 250-256.
    • (2012) Adv. Mat. Res , vol.345 , pp. 250-256
    • Yue, L.1    Yu, H.2    Zhang, C.3    Liu, J.4
  • 173
    • 0023183073 scopus 로고
    • Presence of tumor-associated antigens in epidermal growth factor receptors from different human carcinomas
    • Basu, A., Murthy, U., Rodeck, U., Herlyn, M. et al., Presence of tumor-associated antigens in epidermal growth factor receptors from different human carcinomas. Cancer Res. 1987, 47, 2531-2536.
    • (1987) Cancer Res. , vol.47 , pp. 2531-2536
    • Basu, A.1    Murthy, U.2    Rodeck, U.3    Herlyn, M.4
  • 174
    • 0029931120 scopus 로고    scopus 로고
    • Serological and immunochemical analysis of Lewis y (Ley) blood group antigen expression in epithelial ovarian cancer
    • Yin, B. W., Finstad, C. L., Kitamura, K., Federici, M. G. et al., Serological and immunochemical analysis of Lewis y (Ley) blood group antigen expression in epithelial ovarian cancer. Int. J. Cancer 1996, 65, 406-412.
    • (1996) Int. J. Cancer , vol.65 , pp. 406-412
    • Yin, B.W.1    Finstad, C.L.2    Kitamura, K.3    Federici, M.G.4
  • 175
    • 14144255432 scopus 로고    scopus 로고
    • Alterations in the glycolipid composition and cellular properties of ovarian carcinoma-derived RMG-1 cells on transfection of the alpha1,2-fucosyltransferase gene
    • Iwamori, M., Tanaka, K., Kubushiro, K., Lin, B. et al., Alterations in the glycolipid composition and cellular properties of ovarian carcinoma-derived RMG-1 cells on transfection of the alpha1, 2-fucosyltransferase gene. Cancer Sci. 2005, 96, 26-30.
    • (2005) Cancer Sci. , vol.96 , pp. 26-30
    • Iwamori, M.1    Tanaka, K.2    Kubushiro, K.3    Lin, B.4
  • 176
    • 0034741234 scopus 로고    scopus 로고
    • Relationship between metastasis-associated phenotypes and N-glycan structure of surface glycoproteins in human hepatocarcinoma cells
    • Guo, H.-B., Zhang, Y., Chen, H.-L., Relationship between metastasis-associated phenotypes and N-glycan structure of surface glycoproteins in human hepatocarcinoma cells. J. Cancer Res. Clin. Oncol. 2001, 127, 231-236.
    • (2001) J. Cancer Res. Clin. Oncol , vol.127 , pp. 231-236
    • Guo, H.-B.1    Zhang, Y.2    Chen, H.-L.3
  • 177
    • 0033031839 scopus 로고    scopus 로고
    • Control of metastasis by Asn-linked, β1-6 branched oligosaccharides in mouse mammary cancer cells
    • Seberger, P. J., Chaney, W. G., Control of metastasis by Asn-linked, β1-6 branched oligosaccharides in mouse mammary cancer cells. Glycobiology 1999, 9, 235-241.
    • (1999) Glycobiology , vol.9 , pp. 235-241
    • Seberger, P.J.1    Chaney, W.G.2
  • 178
    • 34547610472 scopus 로고    scopus 로고
    • Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase
    • Guo, H. B., Randolph, M., Pierce, M., Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase. J. Biol. Chem. 2007, 282, 22150-22162.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22150-22162
    • Guo, H.B.1    Randolph, M.2    Pierce, M.3
  • 179
    • 78650451823 scopus 로고    scopus 로고
    • Specific posttranslational modification regulates early events in mammary carcinoma formation
    • Guo, H.-B., Johnson, H., Randolph, M., Nagy, T. et al., Specific posttranslational modification regulates early events in mammary carcinoma formation. Proc. Natl. Acad. Sci. 2010, 107, 21116-21121.
    • (2010) Proc. Natl. Acad. Sci , vol.107 , pp. 21116-21121
    • Guo, H.-B.1    Johnson, H.2    Randolph, M.3    Nagy, T.4
  • 180
    • 39049105125 scopus 로고    scopus 로고
    • Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1
    • Kim, Y. S., Hwang, S. Y., Kang, H. Y., Sohn, H. et al., Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1. Mol. Cell. Proteomics 2008, 7, 1-14.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1-14
    • Kim, Y.S.1    Hwang, S.Y.2    Kang, H.Y.3    Sohn, H.4
  • 181
    • 34547844244 scopus 로고    scopus 로고
    • Identification of proteins bearing beta1-6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis
    • Przybylo, M., Martuszewska, D., Pochec, E., Hoja-Lukowicz, D., Litynska, A., Identification of proteins bearing beta1-6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis. Biochim. Biophys. Acta 2007, 1770, 1427-1435.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 1427-1435
    • Przybylo, M.1    Martuszewska, D.2    Pochec, E.3    Hoja-Lukowicz, D.4    Litynska, A.5
  • 182
    • 5144234312 scopus 로고    scopus 로고
    • Addition of β1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin
    • Ihara, S., Miyoshi, E., Nakahara, S., Sakiyama, H. et al., Addition of β1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. Glycobiology 2004, 14, 139-146.
    • (2004) Glycobiology , vol.14 , pp. 139-146
    • Ihara, S.1    Miyoshi, E.2    Nakahara, S.3    Sakiyama, H.4
  • 183
    • 0036894568 scopus 로고    scopus 로고
    • Aberrant N-glycosylation of β1 integrin causes reduced α5β1 integrin clustering and stimulates cell migration
    • Guo, H.-B., Lee, I., Kamar, M., Akiyama, S. K., Pierce, M., Aberrant N-glycosylation of β1 integrin causes reduced α5β1 integrin clustering and stimulates cell migration. Cancer Res. 2002, 62, 6837-6845.
    • (2002) Cancer Res , vol.62 , pp. 6837-6845
    • Guo, H.-B.1    Lee, I.2    Kamar, M.3    Akiyama, S.K.4    Pierce, M.5
  • 184
    • 28644451894 scopus 로고    scopus 로고
    • Coexpression of beta1,6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome
    • Siddiqui, S. F., Pawelek, J., Handerson, T., Lin, C. Y. et al., Coexpression of beta1, 6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome. Cancer Epidemiol. Biomarkers Prev. 2005, 14, 2517-2523.
    • (2005) Cancer Epidemiol. Biomarkers Prev. , vol.14 , pp. 2517-2523
    • Siddiqui, S.F.1    Pawelek, J.2    Handerson, T.3    Lin, C.Y.4
  • 185
    • 50449107493 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex
    • Akama, R., Sato, Y., Kariya, Y., Isaji, T. et al., N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex. Proteomics 2008, 8, 3221-3228.
    • (2008) Proteomics , vol.8 , pp. 3221-3228
    • Akama, R.1    Sato, Y.2    Kariya, Y.3    Isaji, T.4
  • 186
    • 0024847844 scopus 로고
    • N-Acetylglucosaminyltransferase III in human serum, and liver and hepatoma tissues: Increased activity in liver cirrhosis and hepatoma patients
    • Ishibashi, K., Nishikawa, A., Hayashi, N., Kasahara, A. et al., N-Acetylglucosaminyltransferase III in human serum, and liver and hepatoma tissues: Increased activity in liver cirrhosis and hepatoma patients. Clin. Chim. Acta 1989, 185, 325-332.
    • (1989) Clin. Chim. Acta , vol.185 , pp. 325-332
    • Ishibashi, K.1    Nishikawa, A.2    Hayashi, N.3    Kasahara, A.4
  • 187
    • 62049085785 scopus 로고    scopus 로고
    • E-cadherin directly contributes to PI3K/AKT activation by engaging the PI3K-p85 regulatory subunit to adherens junctions of ovarian carcinoma cells
    • De Santis, G., Miotti, S., Mazzi, M., Canevari, S., Tomassetti, A., E-cadherin directly contributes to PI3K/AKT activation by engaging the PI3K-p85 regulatory subunit to adherens junctions of ovarian carcinoma cells. Oncogene 2009, 28, 1206-1217.
    • (2009) Oncogene , vol.28 , pp. 1206-1217
    • De Santis, G.1    Miotti, S.2    Mazzi, M.3    Canevari, S.4    Tomassetti, A.5
  • 188
    • 0030466993 scopus 로고    scopus 로고
    • Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells
    • Lloyd, K. O., Burchell, J., Kudryashov, V., Yin, B. W., Taylor-Papadimitriou, J., Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells. J. Biol. Chem. 1996, 271, 33325-33334.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33325-33334
    • Lloyd, K.O.1    Burchell, J.2    Kudryashov, V.3    Yin, B.W.4    Taylor-Papadimitriou, J.5
  • 189
    • 84876473766 scopus 로고    scopus 로고
    • Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity
    • Lavrsen, K., Madsen, C. B., Rasch, M. G., Woetmann, A. et al., Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity. Glycoconj. J. 2013, 30, 227-236.
    • (2013) Glycoconj. J. , vol.30 , pp. 227-236
    • Lavrsen, K.1    Madsen, C.B.2    Rasch, M.G.3    Woetmann, A.4
  • 190
    • 0030485053 scopus 로고    scopus 로고
    • Expression of sialyl-Tn in breast cancer. Correlation with prognostic parameters
    • Soares, R., Marinho, A., Schmitt, F., Expression of sialyl-Tn in breast cancer. Correlation with prognostic parameters. Pathol. Res. Pract. 1996, 192, 1181-1186.
    • (1996) Pathol. Res. Pract. , vol.192 , pp. 1181-1186
    • Soares, R.1    Marinho, A.2    Schmitt, F.3
  • 191
    • 0028895533 scopus 로고
    • Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin
    • Campbell, B. J., Finnie, I. A., Hounsell, E. F., Rhodes, J. M., Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin. J. Clin. Invest. 1995, 95, 571-576.
    • (1995) J. Clin. Invest. , vol.95 , pp. 571-576
    • Campbell, B.J.1    Finnie, I.A.2    Hounsell, E.F.3    Rhodes, J.M.4
  • 192
    • 0029948573 scopus 로고    scopus 로고
    • Tn and sialyl-Tn antigens as potential prognostic markers in human ovarian carcinoma
    • Ogawa, H., Ghazizadeh, M., Araki, T., Tn and sialyl-Tn antigens as potential prognostic markers in human ovarian carcinoma. Gynecol. Obstet. Invest. 1996, 41, 278-283.
    • (1996) Gynecol. Obstet. Invest. , vol.41 , pp. 278-283
    • Ogawa, H.1    Ghazizadeh, M.2    Araki, T.3
  • 193
    • 0026344051 scopus 로고
    • Expression of Tn and sialyl-Tn antigens in tumor tissues of the ovary
    • Inoue, M., Ton, S. M., Ogawa, H., Tanizawa, O., Expression of Tn and sialyl-Tn antigens in tumor tissues of the ovary. Am. J. Clin. Pathol. 1991, 96, 711-716.
    • (1991) Am. J. Clin. Pathol. , vol.96 , pp. 711-716
    • Inoue, M.1    Ton, S.M.2    Ogawa, H.3    Tanizawa, O.4
  • 194
    • 33845924961 scopus 로고    scopus 로고
    • Expression of Tn and sialyl-Tn antigens in endometrial cancer: its relationship with tumor-produced cyclooxygenase-2, tumor-infiltrated lymphocytes and patient prognosis
    • Ohno, S., Ohno, Y., Nakada, H., Suzuki, N. et al., Expression of Tn and sialyl-Tn antigens in endometrial cancer: its relationship with tumor-produced cyclooxygenase-2, tumor-infiltrated lymphocytes and patient prognosis. Anticancer Res. 2006, 26, 4047-4053.
    • (2006) Anticancer Res. , vol.26 , pp. 4047-4053
    • Ohno, S.1    Ohno, Y.2    Nakada, H.3    Suzuki, N.4
  • 195
    • 0033002055 scopus 로고    scopus 로고
    • Sialyl Tn antigen expression is associated with the prognosis of patients with advanced colorectal cancer
    • Imada, T., Rino, Y., Hatori, S., Takahashi, M. et al., Sialyl Tn antigen expression is associated with the prognosis of patients with advanced colorectal cancer. Hepato-gastroenterology 1999, 46, 208-214.
    • (1999) Hepato-gastroenterology , vol.46 , pp. 208-214
    • Imada, T.1    Rino, Y.2    Hatori, S.3    Takahashi, M.4
  • 196
    • 4444225031 scopus 로고    scopus 로고
    • Differences in prognosis of colorectal cancer patients based on the expression of sialyl Lewisa, sialyl Lewisx and sialyl Tn antigens in serum and tumor tissue
    • Akamine, S., Nakagoe, T., Sawai, T., Tsuji, T. et al., Differences in prognosis of colorectal cancer patients based on the expression of sialyl Lewisa, sialyl Lewisx and sialyl Tn antigens in serum and tumor tissue. Anticancer Res. 2004, 24, 2541-2546.
    • (2004) Anticancer Res. , vol.24 , pp. 2541-2546
    • Akamine, S.1    Nakagoe, T.2    Sawai, T.3    Tsuji, T.4
  • 197
    • 0025048023 scopus 로고
    • Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients
    • Itzkowitz, S. H., Bloom, E. J., Kokal, W. A., Modin, G. et al., Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients. Cancer 1990, 66, 1960-1966.
    • (1990) Cancer , vol.66 , pp. 1960-1966
    • Itzkowitz, S.H.1    Bloom, E.J.2    Kokal, W.A.3    Modin, G.4
  • 198
    • 0028265079 scopus 로고
    • Expression of sialosyl-Tn antigen (monoclonal antibody MLS102 reactive) in normal tissues and malignant tumors of the digestive tract
    • Ohshio, G., Yoshioka, H., Manabe, T., Sakahara, H. et al., Expression of sialosyl-Tn antigen (monoclonal antibody MLS102 reactive) in normal tissues and malignant tumors of the digestive tract. J. Cancer Res. Clin. Oncol. 1994, 120, 325-330.
    • (1994) J. Cancer Res. Clin. Oncol , vol.120 , pp. 325-330
    • Ohshio, G.1    Yoshioka, H.2    Manabe, T.3    Sakahara, H.4
  • 199
    • 0022457641 scopus 로고
    • Distribution of Oncofetal Antigen Tumor-associated Glycoprotein-72 Defined by Monoclonal Antibody B72.3
    • Thor, A., Ohuchi, N., Szpak, C. A., Johnston, W. W., Schlom, J., Distribution of Oncofetal Antigen Tumor-associated Glycoprotein-72 Defined by Monoclonal Antibody B72.3. Cancer Res. 1986, 46, 3118-3124.
    • (1986) Cancer Res. , vol.46 , pp. 3118-3124
    • Thor, A.1    Ohuchi, N.2    Szpak, C.A.3    Johnston, W.W.4    Schlom, J.5
  • 200
    • 33646846653 scopus 로고    scopus 로고
    • Characterization of the glycosylation profile of the human breast cancer cell line, MDA-231, and a bone colonizing variant
    • Carcel-Trullols, J., Stanley, J. S., Saha, R., Shaaf, S. et al., Characterization of the glycosylation profile of the human breast cancer cell line, MDA-231, and a bone colonizing variant. Int. J. Oncol. 2006, 28, 1173-1183.
    • (2006) Int. J. Oncol. , vol.28 , pp. 1173-1183
    • Carcel-Trullols, J.1    Stanley, J.S.2    Saha, R.3    Shaaf, S.4
  • 201
    • 0028075832 scopus 로고
    • Expression of sialyl-Tn predicts the effect of adjuvant chemotherapy in node-positive breast cancer
    • Miles, D. W., Happerfield, L. C., Smith, P., Gillibrand, R. et al., Expression of sialyl-Tn predicts the effect of adjuvant chemotherapy in node-positive breast cancer. Br. J. Cancer 1994, 70, 1272-1275.
    • (1994) Br. J. Cancer , vol.70 , pp. 1272-1275
    • Miles, D.W.1    Happerfield, L.C.2    Smith, P.3    Gillibrand, R.4
  • 202
    • 60849107267 scopus 로고    scopus 로고
    • The role of cell adhesion molecules in the progression of colorectal cancer and the development of liver metastasis
    • Paschos, K. A., Canovas, D., Bird, N. C., The role of cell adhesion molecules in the progression of colorectal cancer and the development of liver metastasis. Cell. Signal. 2009, 21, 665-674.
    • (2009) Cell. Signal. , vol.21 , pp. 665-674
    • Paschos, K.A.1    Canovas, D.2    Bird, N.C.3
  • 203
    • 0031979657 scopus 로고    scopus 로고
    • Liver metastasis and adhesion to the sinusoidal endothelium by human colon cancer cells is related to mucin carbohydrate chain length
    • Bresalier, R. S., Byrd, J. C., Brodt, P., Ogata, S. et al., Liver metastasis and adhesion to the sinusoidal endothelium by human colon cancer cells is related to mucin carbohydrate chain length. Int. J. Cancer 1998, 76, 556-562.
    • (1998) Int. J. Cancer , vol.76 , pp. 556-562
    • Bresalier, R.S.1    Byrd, J.C.2    Brodt, P.3    Ogata, S.4
  • 204
    • 0028145764 scopus 로고
    • Use of model cell lines to study the biosynthesis and biological role of cancer-associated sialosyl-Tn antigen
    • Ogata, S., Chen, A., Itzkowitz, S. H., Use of model cell lines to study the biosynthesis and biological role of cancer-associated sialosyl-Tn antigen. Cancer Res. 1994, 54, 4036-4044.
    • (1994) Cancer Res. , vol.54 , pp. 4036-4044
    • Ogata, S.1    Chen, A.2    Itzkowitz, S.H.3
  • 206
    • 62449091054 scopus 로고    scopus 로고
    • Enhanced immune recognition of cryptic glycan markers in human tumors
    • Newsom-Davis, T. E., Wang, D., Steinman, L., Chen, P. F. et al., Enhanced immune recognition of cryptic glycan markers in human tumors. Cancer Res. 2009, 69, 2018-2025.
    • (2009) Cancer Res. , vol.69 , pp. 2018-2025
    • Newsom-Davis, T.E.1    Wang, D.2    Steinman, L.3    Chen, P.F.4
  • 207
  • 208
    • 0035073535 scopus 로고    scopus 로고
    • Differential distribution of sialic acid in α2,3 and α2,6 linkages in the apical membrane of cultured epithelial cells and tissues
    • Ulloa, F., Real, F. X., Differential distribution of sialic acid in α2, 3 and α2, 6 linkages in the apical membrane of cultured epithelial cells and tissues. J. Histochem. Cytochem. 2001, 49, 501-509.
    • (2001) J. Histochem. Cytochem , vol.49 , pp. 501-509
    • Ulloa, F.1    Real, F.X.2
  • 209
    • 0030951441 scopus 로고    scopus 로고
    • Involvement of carbohydrate antigen sialyl Lewis X in colorectal cancer metastasis
    • Nakamori, S., Kameyama, M., Imaoka, S., Furukawa, H. et al., Involvement of carbohydrate antigen sialyl Lewis X in colorectal cancer metastasis. Dis. Colon Rectum 1997, 40, 420-431.
    • (1997) Dis. Colon Rectum , vol.40 , pp. 420-431
    • Nakamori, S.1    Kameyama, M.2    Imaoka, S.3    Furukawa, H.4
  • 210
    • 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. 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, 3632-3637.
    • (1993) Cancer Res , vol.53 , pp. 3632-3637
    • Nakamori, S.1    Kameyama, M.2    Imaoka, S.3    Furukawa, H.4
  • 211
    • 0031883324 scopus 로고    scopus 로고
    • Different modes of sialyl-Tn expression during malignant transformation of human colonic mucosa
    • Ogata, S., Koganty, R., Reddish, M., Michael Longenecker, B. et al., Different modes of sialyl-Tn expression during malignant transformation of human colonic mucosa. Glycoconj. J. 1998, 15, 29-35.
    • (1998) Glycoconj. J. , vol.15 , pp. 29-35
    • Ogata, S.1    Koganty, R.2    Reddish, M.3    Michael Longenecker, B.4
  • 212
    • 0030979567 scopus 로고    scopus 로고
    • Altered mRNA expression of specific molecular species of fucosyl- and sialyl-transferases in human colorectal cancer tissues
    • Ito, H., Hiraiwa, N., Sawada-Kasugai, M., Akamatsu, S. et al., Altered mRNA expression of specific molecular species of fucosyl- and sialyl-transferases in human colorectal cancer tissues. Int. J. Cancer 1997, 71, 556-564.
    • (1997) Int. J. Cancer , vol.71 , pp. 556-564
    • Ito, H.1    Hiraiwa, N.2    Sawada-Kasugai, M.3    Akamatsu, S.4
  • 213
    • 0034021674 scopus 로고    scopus 로고
    • Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases
    • Petretti, T., Kemmner, W., Schulze, B., Schlag, P. M., Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases. Gut 2000, 46, 359-366.
    • (2000) Gut , vol.46 , pp. 359-366
    • Petretti, T.1    Kemmner, W.2    Schulze, B.3    Schlag, P.M.4
  • 214
    • 84865229984 scopus 로고    scopus 로고
    • Developmental expression of the neuron-specific N-acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V
    • Lee, J. K., Matthews, R. T., Lim, J. M., Swanier, K. et al., Developmental expression of the neuron-specific N-acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V. J. Biol. Chem. 2012, 287, 28526-28536.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28526-28536
    • Lee, J.K.1    Matthews, R.T.2    Lim, J.M.3    Swanier, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.