메뉴 건너뛰기




Volumn 1856, Issue 2, 2015, Pages 165-177

Cancer serum biomarkers based on aberrant post-translational modifications of glycoproteins: Clinical value and discovery strategies

Author keywords

Aberrant glycosylation; Cancer biomarkers; Discovery; Glycoproteins; Serum

Indexed keywords

ALPHA FETOPROTEIN; AUTOANTIBODY; BIOLOGICAL MARKER; CA 125 ANTIGEN; CA 15-3 ANTIGEN; CA 19-9 ANTIGEN; CALCITONIN; CARCINOEMBRYONIC ANTIGEN; CHORIONIC GONADOTROPIN BETA SUBUNIT; EPIDERMAL GROWTH FACTOR RECEPTOR 2; ESTROGEN RECEPTOR; GLYCAN; GLYCOGEN; GLYCOPROTEIN; LACTATE DEHYDROGENASE; LECTIN; PROGESTERONE RECEPTOR; PROSTATE SPECIFIC ANTIGEN; THYROGLOBULIN; TRASTUZUMAB; TUMOR MARKER;

EID: 84939785631     PISSN: 0304419X     EISSN: 18792561     Source Type: Journal    
DOI: 10.1016/j.bbcan.2015.07.002     Document Type: Review
Times cited : (25)

References (94)
  • 1
    • 0002448054 scopus 로고
    • On a new substance occurring in the urine with mollities ossium
    • Jones H.B. On a new substance occurring in the urine with mollities ossium. Philos. Trans. R. Soc. Lond. 1848, 138:55-62.
    • (1848) Philos. Trans. R. Soc. Lond. , vol.138 , pp. 55-62
    • Jones, H.B.1
  • 2
    • 53849144620 scopus 로고    scopus 로고
    • Strategies for discovering novel cancer biomarkers through utilization of emerging technologies
    • Kulasingam V., Diamandis E.P. Strategies for discovering novel cancer biomarkers through utilization of emerging technologies. Nat. Clin. Pract. Oncol. 2008, 5:588-599.
    • (2008) Nat. Clin. Pract. Oncol. , vol.5 , pp. 588-599
    • Kulasingam, V.1    Diamandis, E.P.2
  • 3
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • Lis H., Sharon N. Protein glycosylation. Structural and functional aspects. Eur. J. Biochem. 1993, 218:1-27.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 5
    • 0031971883 scopus 로고    scopus 로고
    • Enzyme action in glycoprotein synthesis
    • Sears P., Wong C.H. Enzyme action in glycoprotein synthesis. Cell. Mol. Life Sci. 1998, 54:223-252.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 223-252
    • Sears, P.1    Wong, C.H.2
  • 7
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: new wine in an old bottle
    • Hakomori S. Glycosylation defining cancer malignancy: new wine in an old bottle. Proc. Natl. Acad. Sci. 2002, 99:10231-10233.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 8
    • 0034963231 scopus 로고    scopus 로고
    • Tumor-associated carbohydrate antigens defining tumor malignancy: basis for development of anti-cancer vaccines
    • Hakomori S. Tumor-associated carbohydrate antigens defining tumor malignancy: basis for development of anti-cancer vaccines. Adv. Exp. Med. Biol. 2001, 491:369-402.
    • (2001) Adv. Exp. Med. Biol. , vol.491 , pp. 369-402
    • Hakomori, S.1
  • 9
    • 0026086828 scopus 로고
    • Increased UDP-GlcNAc:Galβ1-3GalNAc-R (GlcNAc to GalNAc) β-1,6-N-acetylgalactosaminyltransferase activity in metastatic murine tumor cell lines. Control of polylactosamine synthesis
    • Yousefi S., Higgins E., Daoling Z., Pollex-Kruger A., Hindsgaul O., Dennis J.W. Increased UDP-GlcNAc:Galβ1-3GalNAc-R (GlcNAc to GalNAc) β-1,6-N-acetylgalactosaminyltransferase activity in metastatic murine tumor cell lines. Control of polylactosamine synthesis. J. Biol. Chem. 1991, 266:1772-1782.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1772-1782
    • Yousefi, S.1    Higgins, E.2    Daoling, Z.3    Pollex-Kruger, A.4    Hindsgaul, O.5    Dennis, J.W.6
  • 10
    • 24744436431 scopus 로고    scopus 로고
    • Molecular basis of incomplete O-glycan synthesis in MCF-7 breast cancer cells: putative role of MUC6 in Tn antigen expression
    • Freire T., Bay S., von Mensdorff-Pouilly S., Osinaga E. Molecular basis of incomplete O-glycan synthesis in MCF-7 breast cancer cells: putative role of MUC6 in Tn antigen expression. Cancer Res. 2005, 65:7880-7887.
    • (2005) Cancer Res. , vol.65 , pp. 7880-7887
    • Freire, T.1    Bay, S.2    von Mensdorff-Pouilly, S.3    Osinaga, E.4
  • 11
    • 0033977912 scopus 로고    scopus 로고
    • The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression
    • Brooks S.A. The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression. Histol. Histopathol. 2000, 15:143-158.
    • (2000) Histol. Histopathol. , vol.15 , pp. 143-158
    • Brooks, S.A.1
  • 12
    • 57449116570 scopus 로고    scopus 로고
    • The prospects of glycan biomarkers for the diagnosis of diseases
    • Lebrilla C.B., An H.J. The prospects of glycan biomarkers for the diagnosis of diseases. Mol. Biosyst. 2009, 5:17-20.
    • (2009) Mol. Biosyst. , vol.5 , pp. 17-20
    • Lebrilla, C.B.1    An, H.J.2
  • 14
    • 84866511734 scopus 로고    scopus 로고
    • Evaluation of known oncoantibodies, HER2, p53, and cyclin B1, in pre-diagnostic breast cancer sera
    • Lu H., Ladd J., Feng Z., Wu M., Goodell V., Pitteri S.J., et al. Evaluation of known oncoantibodies, HER2, p53, and cyclin B1, in pre-diagnostic breast cancer sera. Cancer Prev. Res. (Phila) 2012, 5:1036-1043.
    • (2012) Cancer Prev. Res. (Phila) , vol.5 , pp. 1036-1043
    • Lu, H.1    Ladd, J.2    Feng, Z.3    Wu, M.4    Goodell, V.5    Pitteri, S.J.6
  • 16
    • 84910095554 scopus 로고    scopus 로고
    • Clinical value of serum tumor markers CA 19-9, CA 125 and CA 72-4 in the diagnosis of pancreatic carcinoma
    • Wang Z., Tian Y. Clinical value of serum tumor markers CA 19-9, CA 125 and CA 72-4 in the diagnosis of pancreatic carcinoma. Mol. Clin. Oncol. 2014, 2:265-268.
    • (2014) Mol. Clin. Oncol. , vol.2 , pp. 265-268
    • Wang, Z.1    Tian, Y.2
  • 18
    • 84868142905 scopus 로고    scopus 로고
    • Early CDT-lung test: improved clinical utility through additional autoantibody assays
    • Chapman C.J., Healey G.F., Murray A., Boyle P., Robertson C., Peek L.J., et al. Early CDT-lung test: improved clinical utility through additional autoantibody assays. Tumour Biol. 2012, 33:1319-1326.
    • (2012) Tumour Biol. , vol.33 , pp. 1319-1326
    • Chapman, C.J.1    Healey, G.F.2    Murray, A.3    Boyle, P.4    Robertson, C.5    Peek, L.J.6
  • 19
    • 84872595604 scopus 로고    scopus 로고
    • Early detection of cancer in the general population - a blinded case control study of p53 auto-antibodies in colorectal cancer
    • Pedersen J.W., Gentry-Maharaj A., Fourkala E.-O., Dawnay A., Burnell M., Zaikin A., et al. Early detection of cancer in the general population - a blinded case control study of p53 auto-antibodies in colorectal cancer. Br. J. Cancer 2013, 108:107-114.
    • (2013) Br. J. Cancer , vol.108 , pp. 107-114
    • Pedersen, J.W.1    Gentry-Maharaj, A.2    Fourkala, E.-O.3    Dawnay, A.4    Burnell, M.5    Zaikin, A.6
  • 20
    • 84878554709 scopus 로고    scopus 로고
    • Autoantibodies to MUC1 glycopeptides cannot be used as a screening assay for early detection of breast, ovarian, lung or pancreatic cancer
    • Burford B., Gentry-Maharaj A., Graham R., Allen D., Pedersen J.W., Nudelman A.S., et al. Autoantibodies to MUC1 glycopeptides cannot be used as a screening assay for early detection of breast, ovarian, lung or pancreatic cancer. Br. J. Cancer 2013, 108:2045-2055.
    • (2013) Br. J. Cancer , vol.108 , pp. 2045-2055
    • Burford, B.1    Gentry-Maharaj, A.2    Graham, R.3    Allen, D.4    Pedersen, J.W.5    Nudelman, A.S.6
  • 21
    • 80053248927 scopus 로고    scopus 로고
    • Autoantibody signatures: progress and perspectives for early cancer detection
    • Desmetz C., Mange A., Maudelonde T., Solassol J. Autoantibody signatures: progress and perspectives for early cancer detection. J. Cell. Mol. Med. 2011, 15:2013-2024.
    • (2011) J. Cell. Mol. Med. , vol.15 , pp. 2013-2024
    • Desmetz, C.1    Mange, A.2    Maudelonde, T.3    Solassol, J.4
  • 22
    • 0030848719 scopus 로고    scopus 로고
    • Immunoreactive T, and Tn epitopes in cancer diagnosis, prognosis and immunotherapy
    • Springer G.F. Immunoreactive T, and Tn epitopes in cancer diagnosis, prognosis and immunotherapy. J. Mol. Med. 1997, 75:594-602.
    • (1997) J. Mol. Med. , vol.75 , pp. 594-602
    • Springer, G.F.1
  • 23
    • 0033787621 scopus 로고    scopus 로고
    • Immunoreactive T, and Tn antigens in malignancy: role in carcinoma diagnosis, prognosis, and immunotherapy
    • Desai P.R. Immunoreactive T, and Tn antigens in malignancy: role in carcinoma diagnosis, prognosis, and immunotherapy. Transfus Med. Rev. 2000, 14:312-325.
    • (2000) Transfus Med. Rev. , vol.14 , pp. 312-325
    • Desai, P.R.1
  • 24
    • 0019168619 scopus 로고
    • Serum glycoproteins in cancer patients: first report of correlations with in vitro and in vivo parameters of cellular immunity
    • Baskies A.M., Chretien P.B., Weiss J.F., Makuch R.W., Beveridge R.A., William A.B., et al. Serum glycoproteins in cancer patients: first report of correlations with in vitro and in vivo parameters of cellular immunity. Cancer 1980, 45:3050-3060.
    • (1980) Cancer , vol.45 , pp. 3050-3060
    • Baskies, A.M.1    Chretien, P.B.2    Weiss, J.F.3    Makuch, R.W.4    Beveridge, R.A.5    William, A.B.6
  • 25
    • 77956851321 scopus 로고    scopus 로고
    • Measurement of biomarker proteins for point-of-care early detection and monitoring of cancer
    • Rusling J.F., Kumar C.V., Gutkind J.S., Patel V. Measurement of biomarker proteins for point-of-care early detection and monitoring of cancer. Analyst 2010, 135:2496-2511.
    • (2010) Analyst , vol.135 , pp. 2496-2511
    • Rusling, J.F.1    Kumar, C.V.2    Gutkind, J.S.3    Patel, V.4
  • 26
    • 46049092019 scopus 로고    scopus 로고
    • Detection of pancreatic cancer using antibody microarray-based serum protein profiling
    • Ingvarsson J., Wingren C., Carlsson A., Ellmark P., Wahren B., Engström G., et al. Detection of pancreatic cancer using antibody microarray-based serum protein profiling. Proteomics 2008, 8:2211-2219.
    • (2008) Proteomics , vol.8 , pp. 2211-2219
    • Ingvarsson, J.1    Wingren, C.2    Carlsson, A.3    Ellmark, P.4    Wahren, B.5    Engström, G.6
  • 27
    • 38749122786 scopus 로고    scopus 로고
    • Serum proteome profiling of metastatic breast cancer using recombinant antibody microarrays
    • Carlsson A., Wingren C., Ingvarsson J., Ellmark P., Baldertorp B., Fernö M., et al. Serum proteome profiling of metastatic breast cancer using recombinant antibody microarrays. Eur. J. Cancer 2008, 44:472-480.
    • (2008) Eur. J. Cancer , vol.44 , pp. 472-480
    • Carlsson, A.1    Wingren, C.2    Ingvarsson, J.3    Ellmark, P.4    Baldertorp, B.5    Fernö, M.6
  • 28
    • 33745570110 scopus 로고    scopus 로고
    • Role of proteomics in translational research in cervical cancer
    • Yim E.K., Park J.S. Role of proteomics in translational research in cervical cancer. Expert Rev. Proteomics 2006, 3:21-36.
    • (2006) Expert Rev. Proteomics , vol.3 , pp. 21-36
    • Yim, E.K.1    Park, J.S.2
  • 30
    • 84939799305 scopus 로고    scopus 로고
    • Prognostic and predictive markers in early detection of different types of cancers for selected organ sites
    • Marella S. Prognostic and predictive markers in early detection of different types of cancers for selected organ sites. IOSR J. Pharm. Biol. Sci. 2013, 8:25-42.
    • (2013) IOSR J. Pharm. Biol. Sci. , vol.8 , pp. 25-42
    • Marella, S.1
  • 32
    • 84939807909 scopus 로고    scopus 로고
    • Circulating IgG antibody against FOXP3 may be a potential biomarker for lung cancer
    • Wang W., Ye L., Li X., Guan S., Sun S., Wang M., et al. Circulating IgG antibody against FOXP3 may be a potential biomarker for lung cancer. Adv. Lung Cancer 2013, 2:79-83.
    • (2013) Adv. Lung Cancer , vol.2 , pp. 79-83
    • Wang, W.1    Ye, L.2    Li, X.3    Guan, S.4    Sun, S.5    Wang, M.6
  • 33
    • 3242680643 scopus 로고    scopus 로고
    • Biomarkers in breast cancer
    • Kurebayashi J. Biomarkers in breast cancer. Gan To Kagaku Ryoho 2004, 31:1021-1026.
    • (2004) Gan To Kagaku Ryoho , vol.31 , pp. 1021-1026
    • Kurebayashi, J.1
  • 34
    • 34247282875 scopus 로고    scopus 로고
    • Contribution of oncoproteomics to cancer biomarker discovery
    • Cho W.C.S. Contribution of oncoproteomics to cancer biomarker discovery. Mol. Cancer 2007, 6:25.
    • (2007) Mol. Cancer , vol.6 , pp. 25
    • Cho, W.C.S.1
  • 35
    • 23944439913 scopus 로고    scopus 로고
    • So, you want to look for biomarkers
    • Labaer J. So, you want to look for biomarkers. J. Proteome Res. 2005, 4:1053-1059.
    • (2005) J. Proteome Res. , vol.4 , pp. 1053-1059
    • Labaer, J.1
  • 36
    • 84858701322 scopus 로고    scopus 로고
    • Carbohydrate-protein interactions and their biosensing applications
    • Zeng X., Andrade C.A.S., Oliveira M.D.L., Sun X. Carbohydrate-protein interactions and their biosensing applications. Anal. Bioanal. Chem. 2012, 402:3161-3176.
    • (2012) Anal. Bioanal. Chem. , vol.402 , pp. 3161-3176
    • Zeng, X.1    Andrade, C.A.S.2    Oliveira, M.D.L.3    Sun, X.4
  • 37
    • 0000250138 scopus 로고
    • Carbohydrate-protein interactions in antibodies and lectins
    • Bundle D.R., Young N.M. Carbohydrate-protein interactions in antibodies and lectins. Curr. Opin. Struct. Biol. 1992, 2:666-673.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 666-673
    • Bundle, D.R.1    Young, N.M.2
  • 38
    • 0001697163 scopus 로고
    • Protein-carbohydrate interaction. II. Inhibition studies on the interaction of concanavalin A with polysaccharides
    • Goldstein I.J., Hollerman C.E., Smith E.E. Protein-carbohydrate interaction. II. Inhibition studies on the interaction of concanavalin A with polysaccharides. Biochemistry 1965, 4:876-883.
    • (1965) Biochemistry , vol.4 , pp. 876-883
    • Goldstein, I.J.1    Hollerman, C.E.2    Smith, E.E.3
  • 39
    • 0034628502 scopus 로고    scopus 로고
    • Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands
    • Kitov P.I., Sadowska J.M., Mulvey G., Armstrong G.D., Ling H., Pannu N.S., et al. Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands. Nature 2000, 403:669-672.
    • (2000) Nature , vol.403 , pp. 669-672
    • Kitov, P.I.1    Sadowska, J.M.2    Mulvey, G.3    Armstrong, G.D.4    Ling, H.5    Pannu, N.S.6
  • 40
    • 0026772958 scopus 로고
    • N-glycosylation of serum proteins in disease and its investigation using lectins
    • Turner G.A. N-glycosylation of serum proteins in disease and its investigation using lectins. Clin. Chim. Acta 1992, 208:149-171.
    • (1992) Clin. Chim. Acta , vol.208 , pp. 149-171
    • Turner, G.A.1
  • 41
    • 65549120632 scopus 로고    scopus 로고
    • Comparative glycoproteomics: approaches and applications
    • Wei X., Li L. Comparative glycoproteomics: approaches and applications. Brief. Funct. Genomic. Proteomic. 2008, 8:104-113.
    • (2008) Brief. Funct. Genomic. Proteomic. , vol.8 , pp. 104-113
    • Wei, X.1    Li, L.2
  • 42
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • Yang Z., Hancock W.S. Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J. Chromatogr. A 2004, 1053:79-88.
    • (2004) J. Chromatogr. A , vol.1053 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 43
    • 34247866397 scopus 로고    scopus 로고
    • Lectin-immobilization strategies for affinity purification and separation of glycoconjugates
    • Monzo A., Bonn G.K., Guttman A. Lectin-immobilization strategies for affinity purification and separation of glycoconjugates. TrAC 2007, 26:423-432.
    • (2007) TrAC , vol.26 , pp. 423-432
    • Monzo, A.1    Bonn, G.K.2    Guttman, A.3
  • 44
    • 79957491752 scopus 로고    scopus 로고
    • Affinity entrapment of oligosaccharides and glycopeptides using free lectin solution
    • Yodoshi M., Oyama T., Masaki K., Kakehi K., Hayakawa T., Suzuki S. Affinity entrapment of oligosaccharides and glycopeptides using free lectin solution. Anal. Sci. 2011, 27:395-400.
    • (2011) Anal. Sci. , vol.27 , pp. 395-400
    • Yodoshi, M.1    Oyama, T.2    Masaki, K.3    Kakehi, K.4    Hayakawa, T.5    Suzuki, S.6
  • 45
    • 0037176224 scopus 로고    scopus 로고
    • Use of a lectin affinity selector in the search for unusual glycosylation on proteomics
    • Xiong L., Regnier F.E. Use of a lectin affinity selector in the search for unusual glycosylation on proteomics. J. Chromatogr. B 2002, 782:405-418.
    • (2002) J. Chromatogr. B , vol.782 , pp. 405-418
    • Xiong, L.1    Regnier, F.E.2
  • 46
    • 33745827045 scopus 로고    scopus 로고
    • Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum
    • Zhao J., Simeone D.M., Heidt D., Anderson M.A., Lubman D.M. Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum. J. Proteome Res. 2006, 5:1792-1802.
    • (2006) J. Proteome Res. , vol.5 , pp. 1792-1802
    • Zhao, J.1    Simeone, D.M.2    Heidt, D.3    Anderson, M.A.4    Lubman, D.M.5
  • 47
    • 55249118407 scopus 로고    scopus 로고
    • Glycoproteomic analyses of ovarian cancer cell lines and sera from ovarian cancer patients show distinct glycosylation changes in individual proteins
    • Li B., An H.J., Kirmiz C., Lebrilla C.B., Lam K.S., Miyamoto S. Glycoproteomic analyses of ovarian cancer cell lines and sera from ovarian cancer patients show distinct glycosylation changes in individual proteins. J. Proteome Res. 2008, 7:3776-3788.
    • (2008) J. Proteome Res. , vol.7 , pp. 3776-3788
    • Li, B.1    An, H.J.2    Kirmiz, C.3    Lebrilla, C.B.4    Lam, K.S.5    Miyamoto, S.6
  • 48
    • 80054078249 scopus 로고    scopus 로고
    • Multi-sequential surface plasmon resonance analysis of haptoglobin-lectin complex in sera of patients with malignant and benign prostate diseases
    • Kazuno S., Fujimura T., Arai T., Ueno T., Nagao K., Fujime M., et al. Multi-sequential surface plasmon resonance analysis of haptoglobin-lectin complex in sera of patients with malignant and benign prostate diseases. Anal. Biochem. 2011, 419:241-249.
    • (2011) Anal. Biochem. , vol.419 , pp. 241-249
    • Kazuno, S.1    Fujimura, T.2    Arai, T.3    Ueno, T.4    Nagao, K.5    Fujime, M.6
  • 49
    • 15744387329 scopus 로고    scopus 로고
    • Monitoring glycosylation pattern changes of glycoproteins using multi-lectin affinity chromatography
    • Yang Z., Hancock W.S. Monitoring glycosylation pattern changes of glycoproteins using multi-lectin affinity chromatography. J. Chromatogr. A 2005, 1070:57-64.
    • (2005) J. Chromatogr. A , vol.1070 , pp. 57-64
    • Yang, Z.1    Hancock, W.S.2
  • 50
    • 21644459777 scopus 로고    scopus 로고
    • Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides
    • Madera M., Mechref Y., Novotny M.V. Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides. Anal. Chem. 2005, 77:4081-4090.
    • (2005) Anal. Chem. , vol.77 , pp. 4081-4090
    • Madera, M.1    Mechref, Y.2    Novotny, M.V.3
  • 51
    • 33751529259 scopus 로고    scopus 로고
    • High-sensitivity profiling of glycoproteins from human blood serum through multiple-lectin affinity chromatography and liquid chromatography/tandem mass spectrometry
    • Madera M., Mechref Y., Klouckova I., Novotny M.V. High-sensitivity profiling of glycoproteins from human blood serum through multiple-lectin affinity chromatography and liquid chromatography/tandem mass spectrometry. J. Chromatogr. B 2007, 845:121-137.
    • (2007) J. Chromatogr. B , vol.845 , pp. 121-137
    • Madera, M.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 52
    • 0001140423 scopus 로고
    • Theoretical investigation of the potentialities of the use of a multidimensional column in chromatography
    • Guiochon G., Beaver L.A., Gonnord M.F., Siouffi A.M., Zakaria M. Theoretical investigation of the potentialities of the use of a multidimensional column in chromatography. J. Chromatogr. A 1983, 255:415-437.
    • (1983) J. Chromatogr. A , vol.255 , pp. 415-437
    • Guiochon, G.1    Beaver, L.A.2    Gonnord, M.F.3    Siouffi, A.M.4    Zakaria, M.5
  • 53
    • 0346158492 scopus 로고    scopus 로고
    • The proteomics approach to find biomarkers in gastric cancer
    • Ryu J., Kim H., Lee Y., Myong N., Hwang C., Lee G., et al. The proteomics approach to find biomarkers in gastric cancer. J. Korean Med. Sci. 2003, 18:505-509.
    • (2003) J. Korean Med. Sci. , vol.18 , pp. 505-509
    • Ryu, J.1    Kim, H.2    Lee, Y.3    Myong, N.4    Hwang, C.5    Lee, G.6
  • 54
    • 4344560133 scopus 로고    scopus 로고
    • Identification of tumor markers using two-dimensional electrophoresis in gastric carcinoma
    • Wang K., Wang R., Zhang J. Identification of tumor markers using two-dimensional electrophoresis in gastric carcinoma. World J. Gastroenterol. 2004, 10:2179-2183.
    • (2004) World J. Gastroenterol. , vol.10 , pp. 2179-2183
    • Wang, K.1    Wang, R.2    Zhang, J.3
  • 55
    • 84908873236 scopus 로고    scopus 로고
    • Comprehensive N-glycome profiling of cultured human epithelial breast cells identifies unique secretome N-glycosylation signatures enabling tumorigenic subtype classification
    • Lee L.Y., Thaysen-Andersen M., Baker M.S., Packer N.H., Hancock W.S., Fanayan S. Comprehensive N-glycome profiling of cultured human epithelial breast cells identifies unique secretome N-glycosylation signatures enabling tumorigenic subtype classification. J. Proteome Res. 2014, 13:4783-4795.
    • (2014) J. Proteome Res. , vol.13 , pp. 4783-4795
    • Lee, L.Y.1    Thaysen-Andersen, M.2    Baker, M.S.3    Packer, N.H.4    Hancock, W.S.5    Fanayan, S.6
  • 56
    • 84908884009 scopus 로고    scopus 로고
    • LC-MS profiling of N-glycans derived from human serum samples for biomarker discovery in hepatocellular carcinoma
    • Tsai T., Wang M., Di Poto C., Hu Y., Zhou S., Zhao Y., et al. LC-MS profiling of N-glycans derived from human serum samples for biomarker discovery in hepatocellular carcinoma. J. Proteome Res. 2014, 13:4859-4868.
    • (2014) J. Proteome Res. , vol.13 , pp. 4859-4868
    • Tsai, T.1    Wang, M.2    Di Poto, C.3    Hu, Y.4    Zhou, S.5    Zhao, Y.6
  • 57
    • 84908584273 scopus 로고    scopus 로고
    • Liquid chromatography-selected reaction monitoring (LC-SRM) approach for the separation and quantitation of sialylated N-glycans linkage isomers
    • Tao S., Huang Y., Boyes B.E., Orlando R. Liquid chromatography-selected reaction monitoring (LC-SRM) approach for the separation and quantitation of sialylated N-glycans linkage isomers. Anal. Chem. 2014, 86:10584-10590.
    • (2014) Anal. Chem. , vol.86 , pp. 10584-10590
    • Tao, S.1    Huang, Y.2    Boyes, B.E.3    Orlando, R.4
  • 58
    • 84939840284 scopus 로고    scopus 로고
    • A combined shotgun and targeted mass spectrometry strategy for breast cancer biomarker discovery
    • Sjöström M., Ossola R., Breslin T., Rinner O., Malmström L., Schmidt A., et al. A combined shotgun and targeted mass spectrometry strategy for breast cancer biomarker discovery. J. Proteome Res. 2015, 14:2807-2818.
    • (2015) J. Proteome Res. , vol.14 , pp. 2807-2818
    • Sjöström, M.1    Ossola, R.2    Breslin, T.3    Rinner, O.4    Malmström, L.5    Schmidt, A.6
  • 59
    • 84907828149 scopus 로고    scopus 로고
    • Confident assignment of site-specific glycosylation in complex glycoproteins in a single step
    • Khatri K., Staples G.O., Leymarie N., Leon D.R., Turiák L., Yu Huang, et al. Confident assignment of site-specific glycosylation in complex glycoproteins in a single step. J. Proteome Res. 2014, 13:4347-4355.
    • (2014) J. Proteome Res. , vol.13 , pp. 4347-4355
    • Khatri, K.1    Staples, G.O.2    Leymarie, N.3    Leon, D.R.4    Turiák, L.5    Yu, H.6
  • 60
    • 22044449363 scopus 로고    scopus 로고
    • The mass spectrometric analysis of glycoproteins and their glycan structures
    • Morelle W., Michalski J. The mass spectrometric analysis of glycoproteins and their glycan structures. Curr. Anal. Chem. 2005, 1:29-57.
    • (2005) Curr. Anal. Chem. , vol.1 , pp. 29-57
    • Morelle, W.1    Michalski, J.2
  • 61
    • 84907938355 scopus 로고    scopus 로고
    • High-throughput determination of the site-specific N-sialoglycan occupancy rates by differential oxidation of glycoproteins followed with quantitative glycoproteomics analysis
    • Zhang Z., Sun Z., Zhu J., Liu J., Huang G., Ye M., et al. High-throughput determination of the site-specific N-sialoglycan occupancy rates by differential oxidation of glycoproteins followed with quantitative glycoproteomics analysis. Anal. Chem. 2014, 86:9830-9837.
    • (2014) Anal. Chem. , vol.86 , pp. 9830-9837
    • Zhang, Z.1    Sun, Z.2    Zhu, J.3    Liu, J.4    Huang, G.5    Ye, M.6
  • 62
    • 84908878410 scopus 로고    scopus 로고
    • Label-free glycopeptide quantification for biomarker discovery in human sera
    • Mayampurath A., Song E., Mathur A., Yu C., Hammoud Z., Mechref Y., et al. Label-free glycopeptide quantification for biomarker discovery in human sera. J. Proteome Res. 2014, 13:4821-4832.
    • (2014) J. Proteome Res. , vol.13 , pp. 4821-4832
    • Mayampurath, A.1    Song, E.2    Mathur, A.3    Yu, C.4    Hammoud, Z.5    Mechref, Y.6
  • 63
    • 33845449090 scopus 로고
    • Global methods for protein glycosylation analysis by mass spectrometry
    • Budnik B.A., Lee R.S., Steen J.A.J. Global methods for protein glycosylation analysis by mass spectrometry. Biochim. Biophys. Acta 1764, 2006:1870-1880.
    • (1764) Biochim. Biophys. Acta , vol.2006 , pp. 1870-1880
    • Budnik, B.A.1    Lee, R.S.2    Steen, J.A.J.3
  • 64
    • 1842426801 scopus 로고    scopus 로고
    • Concanavalin A chromatography coupled to two-dimensional gel electrophoresis improves protein expression studies of the serum proteome
    • Rodríguez-Piñero A.M., Ayude D., Rodríguez-Berrocal F.J., Cadena M.P. Concanavalin A chromatography coupled to two-dimensional gel electrophoresis improves protein expression studies of the serum proteome. J. Chromatogr. B 2004, 803:337-343.
    • (2004) J. Chromatogr. B , vol.803 , pp. 337-343
    • Rodríguez-Piñero, A.M.1    Ayude, D.2    Rodríguez-Berrocal, F.J.3    Cadena, M.P.4
  • 65
    • 33750620940 scopus 로고    scopus 로고
    • Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers
    • Drake R.R., Schwegler E.E., Malik G., Diaz J., Block T., Mehta A., et al. Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers. Mol. Cell. Proteomics 2006, 5:1957-1967.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1957-1967
    • Drake, R.R.1    Schwegler, E.E.2    Malik, G.3    Diaz, J.4    Block, T.5    Mehta, A.6
  • 66
    • 84920278040 scopus 로고    scopus 로고
    • Glycomic analysis of membrane glycoproteins with bisecting glycosylation from ovarian cancer tissues reveals novel structures and functions
    • Allam H., Aoki K., Benigno B.B., McDonald J.F., Mackintosh S.G., Tiemeyer M., et al. Glycomic analysis of membrane glycoproteins with bisecting glycosylation from ovarian cancer tissues reveals novel structures and functions. J. Proteome Res. 2015, 14:434-446.
    • (2015) J. Proteome Res. , vol.14 , pp. 434-446
    • Allam, H.1    Aoki, K.2    Benigno, B.B.3    McDonald, J.F.4    Mackintosh, S.G.5    Tiemeyer, M.6
  • 67
    • 57049137606 scopus 로고    scopus 로고
    • A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression
    • Hamid U.M.A., Royle L., Saldova R., Radcliffe C.M., Harvey D.J., Storr S.J., 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
    • Hamid, U.M.A.1    Royle, L.2    Saldova, R.3    Radcliffe, C.M.4    Harvey, D.J.5    Storr, S.J.6
  • 68
    • 33846818820 scopus 로고    scopus 로고
    • Chemical methods for glycoprotein discovery
    • Bond M.R., Kohler J.J. Chemical methods for glycoprotein discovery. Curr. Opin. Chem. Biol. 2007, 11:52-58.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 52-58
    • Bond, M.R.1    Kohler, J.J.2
  • 69
    • 4444337997 scopus 로고    scopus 로고
    • Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain
    • Khidekel N., Ficarro S.B., Peters E.C., Hsieh-Wilson L.C. Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proc. Natl. Acad. Sci. 2004, 101:13132-13137.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 13132-13137
    • Khidekel, N.1    Ficarro, S.B.2    Peters, E.C.3    Hsieh-Wilson, L.C.4
  • 70
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H., Li X.J., Martin D.B., Aebersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 2003, 21:660-666.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 71
    • 84928957864 scopus 로고    scopus 로고
    • Identification of glycoproteins containing specific glycans using a lectin-chemical method
    • Li Y., Shah P., De Marzo A.M., Van Eyk J.E., Li Q., Chan D.W., et al. Identification of glycoproteins containing specific glycans using a lectin-chemical method. Anal. Chem. 2015, 87:4683-4687.
    • (2015) Anal. Chem. , vol.87 , pp. 4683-4687
    • Li, Y.1    Shah, P.2    De Marzo, A.M.3    Van Eyk, J.E.4    Li, Q.5    Chan, D.W.6
  • 72
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu T., Qian W., Gritsenko M.A., Camp D.G., Monroe M.E., Moore R.J., et al. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 2005, 4:2070-2080.
    • (2005) J. Proteome Res. , vol.4 , pp. 2070-2080
    • Liu, T.1    Qian, W.2    Gritsenko, M.A.3    Camp, D.G.4    Monroe, M.E.5    Moore, R.J.6
  • 73
    • 84908871089 scopus 로고    scopus 로고
    • LC-MS/MS quantitation of esophagus disease blood serum glycoproteins by enrichment with hydrazide chemistry and lectin affinity chromatograph
    • Song E., Zhu R., Hammoud Z.T., Mechref Y. LC-MS/MS quantitation of esophagus disease blood serum glycoproteins by enrichment with hydrazide chemistry and lectin affinity chromatograph. J. Proteome Res. 2014, 13:4808-4820.
    • (2014) J. Proteome Res. , vol.13 , pp. 4808-4820
    • Song, E.1    Zhu, R.2    Hammoud, Z.T.3    Mechref, Y.4
  • 74
    • 84934978195 scopus 로고    scopus 로고
    • Rapid assignment of core versus antenna fucosylation types in protein N-glycosylation via procainamide labeling and tandem mass spectrometry
    • Nwosu C., Yau H.K., Becht S. Rapid assignment of core versus antenna fucosylation types in protein N-glycosylation via procainamide labeling and tandem mass spectrometry. Anal. Chem. 2015, 87:5905-5913.
    • (2015) Anal. Chem. , vol.87 , pp. 5905-5913
    • Nwosu, C.1    Yau, H.K.2    Becht, S.3
  • 75
    • 34547599483 scopus 로고    scopus 로고
    • Biomedical and clinical applications of immunoassays and immunosensors for tumor markers
    • Wu J., Fu Z., Yan F., Ju H. Biomedical and clinical applications of immunoassays and immunosensors for tumor markers. TrAC 2007, 26:679-688.
    • (2007) TrAC , vol.26 , pp. 679-688
    • Wu, J.1    Fu, Z.2    Yan, F.3    Ju, H.4
  • 76
    • 26444452697 scopus 로고    scopus 로고
    • Thomsen-Friedenreich and Tn antigens in nipple fluid: carbohydrate biomarkers for breast cancer detection
    • Kumar S.R., Sauter E.R., Quinn T.P., Deutscher S.L. Thomsen-Friedenreich and Tn antigens in nipple fluid: carbohydrate biomarkers for breast cancer detection. Clin. Cancer Res. 2005, 11:6868-6871.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 6868-6871
    • Kumar, S.R.1    Sauter, E.R.2    Quinn, T.P.3    Deutscher, S.L.4
  • 77
    • 27144513329 scopus 로고    scopus 로고
    • Multiplexed electrical detection of cancer markers with nanowire sensor arrays
    • Zheng G.F., Patolsky F., Cui Y., Wang W.U., Lieber C.M. Multiplexed electrical detection of cancer markers with nanowire sensor arrays. Nat. Biotechnol. 2005, 10:1294-1301.
    • (2005) Nat. Biotechnol. , vol.10 , pp. 1294-1301
    • Zheng, G.F.1    Patolsky, F.2    Cui, Y.3    Wang, W.U.4    Lieber, C.M.5
  • 78
    • 34548703594 scopus 로고    scopus 로고
    • Identification of tumor antigens by using proteomics. Methods in Molecular Biology, vol 360, Target discovery and validation reviews and protocols, vol 1
    • M.Sioud, Humana Press Inc., Totowa, NJ
    • Le Naour F. Identification of tumor antigens by using proteomics. Methods in Molecular Biology, vol 360, Target discovery and validation reviews and protocols, vol 1. Emerging Strategies for Targets and Biomarker Discovery 2007, 327-334. M.Sioud, Humana Press Inc., Totowa, NJ.
    • (2007) Emerging Strategies for Targets and Biomarker Discovery , pp. 327-334
    • Le Naour, F.1
  • 79
    • 84922978673 scopus 로고    scopus 로고
    • Simple and robust antibody microarray-based immunoassay platform for sensitive and selective detection of PSA and hK2 toward accurate diagnosis of prostate cancer
    • Lee S.W., Hosokawa K., Kim S., Laurell T., Maeda M. Simple and robust antibody microarray-based immunoassay platform for sensitive and selective detection of PSA and hK2 toward accurate diagnosis of prostate cancer. Sens. Bio-Sens. Res. 2015, 3:105-111.
    • (2015) Sens. Bio-Sens. Res. , vol.3 , pp. 105-111
    • Lee, S.W.1    Hosokawa, K.2    Kim, S.3    Laurell, T.4    Maeda, M.5
  • 80
    • 84930608347 scopus 로고    scopus 로고
    • Upregulation of glycans containing 3' fucose in a subset of pancreatic cancers uncovered using fusion-tagged lectins
    • Singh S., Pal K., Yadav J., Tang H., Partyka K., Kletter D., et al. Upregulation of glycans containing 3' fucose in a subset of pancreatic cancers uncovered using fusion-tagged lectins. J. Proteome Res. 2015, 14:2594-2605.
    • (2015) J. Proteome Res. , vol.14 , pp. 2594-2605
    • Singh, S.1    Pal, K.2    Yadav, J.3    Tang, H.4    Partyka, K.5    Kletter, D.6
  • 82
    • 0037434981 scopus 로고    scopus 로고
    • Disease proteomics
    • Hanash S. Disease proteomics. Nature 2003, 422:226-232.
    • (2003) Nature , vol.422 , pp. 226-232
    • Hanash, S.1
  • 83
    • 20444501805 scopus 로고    scopus 로고
    • Development of a lectin microarray for the rapid analysis of protein glycopatterns
    • Pilobello K.T. Development of a lectin microarray for the rapid analysis of protein glycopatterns. ChemBioChem 2005, 6:1-4.
    • (2005) ChemBioChem , vol.6 , pp. 1-4
    • Pilobello, K.T.1
  • 84
    • 73649112112 scopus 로고    scopus 로고
    • A strategy for discovery of cancer glyco-biomarkers in serum using newly developed technologies for glycoproteomics
    • Narimatsu H., Sawaki H., Kuno A., Kaji H., Ito H., Ikehara Y. A strategy for discovery of cancer glyco-biomarkers in serum using newly developed technologies for glycoproteomics. FEBS J. 2010, 277:95-105.
    • (2010) FEBS J. , vol.277 , pp. 95-105
    • Narimatsu, H.1    Sawaki, H.2    Kuno, A.3    Kaji, H.4    Ito, H.5    Ikehara, Y.6
  • 85
    • 84866135063 scopus 로고    scopus 로고
    • Identification and confirmation of differentially expressed fucosylated glycoproteins in the serum of ovarian cancer patients using a lectin array and LC-MS/MS
    • Wu J., Xie X., Liu Y., He J., Benitez R., Buckanovich R.J., et al. Identification and confirmation of differentially expressed fucosylated glycoproteins in the serum of ovarian cancer patients using a lectin array and LC-MS/MS. J. Proteome Res. 2012, 11:4541-4552.
    • (2012) J. Proteome Res. , vol.11 , pp. 4541-4552
    • Wu, J.1    Xie, X.2    Liu, Y.3    He, J.4    Benitez, R.5    Buckanovich, R.J.6
  • 86
    • 84990177206 scopus 로고    scopus 로고
    • Glycoprofiling of cancer biomarkers: label-free electrochemical lectin-based biosensors
    • Pihíková D., Kasák P., Tkac J. Glycoprofiling of cancer biomarkers: label-free electrochemical lectin-based biosensors. Open Chem. 2015, 13:636-655.
    • (2015) Open Chem. , vol.13 , pp. 636-655
    • Pihíková, D.1    Kasák, P.2    Tkac, J.3
  • 87
    • 83755205413 scopus 로고    scopus 로고
    • High-throughput lectin magnetic bead array-coupled tandem mass spectrometry for glycoprotein biomarker discovery
    • Choi E., Loo D., Dennis J.W., O'Leary C.A., Hill M.M. High-throughput lectin magnetic bead array-coupled tandem mass spectrometry for glycoprotein biomarker discovery. Electrophoresis 2011, 32:3564-3575.
    • (2011) Electrophoresis , vol.32 , pp. 3564-3575
    • Choi, E.1    Loo, D.2    Dennis, J.W.3    O'Leary, C.A.4    Hill, M.M.5
  • 88
    • 70349159332 scopus 로고    scopus 로고
    • The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays
    • Yue T., Goldstein I.J., Hollingsworth M.A., Kaul K., Brand R.E., Haab B.B. The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays. Mol. Cell. Proteomics 2009, 8:1697-1707.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1697-1707
    • Yue, T.1    Goldstein, I.J.2    Hollingsworth, M.A.3    Kaul, K.4    Brand, R.E.5    Haab, B.B.6
  • 89
    • 59149091977 scopus 로고    scopus 로고
    • Focused differential glycan analysis with the platform antibody-assisted lectin profiling for glycan-related biomarker verification
    • Kuno A., Kato Y., Matsuda A., Kaneko M.K., Ito H., Amano K., et al. Focused differential glycan analysis with the platform antibody-assisted lectin profiling for glycan-related biomarker verification. Mol. Cell. Proteomics 2009, 8:99-108.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 99-108
    • Kuno, A.1    Kato, Y.2    Matsuda, A.3    Kaneko, M.K.4    Ito, H.5    Amano, K.6
  • 90
    • 48749083261 scopus 로고    scopus 로고
    • Concept, strategy and realization of lectin-based glycan profiling
    • Hirabayashi J. Concept, strategy and realization of lectin-based glycan profiling. J. Biochem. 2008, 144:139-147.
    • (2008) J. Biochem. , vol.144 , pp. 139-147
    • Hirabayashi, J.1
  • 91
    • 79953005786 scopus 로고    scopus 로고
    • Multiplexed antibody arrays for the discovery and validation of glycosylated protein biomarkers
    • Nelson B.P. Multiplexed antibody arrays for the discovery and validation of glycosylated protein biomarkers. Bioanalysis 2009, 1:1431-1444.
    • (2009) Bioanalysis , vol.1 , pp. 1431-1444
    • Nelson, B.P.1
  • 92
    • 20544478148 scopus 로고    scopus 로고
    • Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands
    • Thulasiraman V., Lin S., Gheorghiu L., Lathrop J., Lomas L., Hammond D., et al. Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands. Electrophoresis 2005, 26:3561-3571.
    • (2005) Electrophoresis , vol.26 , pp. 3561-3571
    • Thulasiraman, V.1    Lin, S.2    Gheorghiu, L.3    Lathrop, J.4    Lomas, L.5    Hammond, D.6
  • 93
    • 33750112796 scopus 로고    scopus 로고
    • Protein Equalizer Technology*: the quest for a "democratic proteome"
    • Righetti P.G., Boschetti E., Lomas L., Citterio A. Protein Equalizer Technology*: the quest for a "democratic proteome". Proteomics 2006, 6:3980-3992.
    • (2006) Proteomics , vol.6 , pp. 3980-3992
    • Righetti, P.G.1    Boschetti, E.2    Lomas, L.3    Citterio, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.