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Volumn 13, Issue 3-4, 2013, Pages 504-511

Characterization of disease-associated N-linked glycoproteins

Author keywords

Disease association; Glycoproteomics; N linked glycoproteins

Indexed keywords

BIOLOGICAL MARKER; BORONIC ACID DERIVATIVE; GLYCOPROTEIN; HYDRAZIDE; SUGAR;

EID: 84873948403     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200333     Document Type: Review
Times cited : (56)

References (85)
  • 2
    • 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
  • 3
    • 77951930076 scopus 로고    scopus 로고
    • Glycoproteomics and clinical applications
    • Tian, Y., Zhang, H., Glycoproteomics and clinical applications. Proteomics Clin. Appl. 2010, 4, 124-132.
    • (2010) Proteomics Clin. Appl. , vol.4 , pp. 124-132
    • Tian, Y.1    Zhang, H.2
  • 4
    • 84863206749 scopus 로고    scopus 로고
    • Application of glycoproteomics for the discovery of biomarkers in lung cancer
    • Kay Li, Q., Gabrielson, E., Zhang, H., Application of glycoproteomics for the discovery of biomarkers in lung cancer. Proteomics Clin. Appl. 2012, 6, 244-256.
    • (2012) Proteomics Clin. Appl. , vol.6 , pp. 244-256
    • Kay Li, Q.1    Gabrielson, E.2    Zhang, H.3
  • 6
    • 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. 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
  • 7
    • 1842414891 scopus 로고    scopus 로고
    • Tumor marker concentrations in normal and malignant tissues of colorectal cancer patients and their prognostic relevance
    • Gebauer, G., Muller-Ruchholtz, W., Tumor marker concentrations in normal and malignant tissues of colorectal cancer patients and their prognostic relevance. Anticancer Res. 1997, 17, 2939-2942.
    • (1997) Anticancer Res. , vol.17 , pp. 2939-2942
    • Gebauer, G.1    Muller-Ruchholtz, W.2
  • 8
    • 0025849053 scopus 로고
    • Measurement of prostate-specific antigen in serum as a screening test for prostate cancer
    • Catalona, W. J., Smith, D. S., Ratliff, T. L., Dodds, K. M. et al., Measurement of prostate-specific antigen in serum as a screening test for prostate cancer. New Engl. J. Med. 1991, 324, 1156-1161.
    • (1991) New Engl. J. Med. , vol.324 , pp. 1156-1161
    • Catalona, W.J.1    Smith, D.S.2    Ratliff, T.L.3    Dodds, K.M.4
  • 9
    • 33645523023 scopus 로고    scopus 로고
    • Serum tumor markers for detection of hepatocellular carcinoma
    • Zhou, L., Liu, J., Luo, F., Serum tumor markers for detection of hepatocellular carcinoma. World J. Gastroentero. 2006, 12, 1175-1181.
    • (2006) World J. Gastroentero. , vol.12 , pp. 1175-1181
    • Zhou, L.1    Liu, J.2    Luo, F.3
  • 10
    • 0035986090 scopus 로고    scopus 로고
    • Nerini Molteni, S., Pallotti, F. , Serum and cerebrospinal fluid human chorionic gonadotropin (hCG) and alpha-fetoprotein (AFP) in intracranial germ cell tumors
    • Seregni, E., Massimino, M., Nerini Molteni, S., Pallotti, F. et al., Serum and cerebrospinal fluid human chorionic gonadotropin (hCG) and alpha-fetoprotein (AFP) in intracranial germ cell tumors. Int. J. Biol. Marker. 2002, 17, 112-118.
    • (2002) Int. J. Biol. Marker. , vol.17 , pp. 112-118
    • Seregni, E.1    Massimino, M.2
  • 11
    • 67649781736 scopus 로고    scopus 로고
    • T-cell growth, cell surface organization, and the galectin-glycoprotein lattice
    • Grigorian, A., Torossian, S., Demetriou, M., T-cell growth, cell surface organization, and the galectin-glycoprotein lattice. Immunol. Rev. 2009, 230, 232-246.
    • (2009) Immunol. Rev. , vol.230 , pp. 232-246
    • Grigorian, A.1    Torossian, S.2    Demetriou, M.3
  • 12
    • 34047099675 scopus 로고    scopus 로고
    • Adjuvant treatment of breast cancer: impact of monoclonal antibody therapy directed against the HER2 receptor
    • Simonds, H. M., Miles, D., Adjuvant treatment of breast cancer: impact of monoclonal antibody therapy directed against the HER2 receptor. Expert Opin. Biol. Ther. 2007, 7, 487-491.
    • (2007) Expert Opin. Biol. Ther. , vol.7 , pp. 487-491
    • Simonds, H.M.1    Miles, D.2
  • 13
    • 0020368287 scopus 로고
    • Fractionation of asparagine-linked oligosaccharides by serial lectin-Agarose affinity chromatography. A rapid, sensitive, and specific technique
    • Cummings, R. D., Kornfeld, S., Fractionation of asparagine-linked oligosaccharides by serial lectin-Agarose affinity chromatography. A rapid, sensitive, and specific technique. J. Biol. Chem. 1982, 257, 11235-11240.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11235-11240
    • Cummings, R.D.1    Kornfeld, S.2
  • 14
    • 0001344346 scopus 로고    scopus 로고
    • A guide to the carbohydrate specificities of applied lectins-2 (updated in 2000)
    • Wu, A. M., Song, S. C., Tsai, M. S., Herp, A., A guide to the carbohydrate specificities of applied lectins-2 (updated in 2000). Adv. Exp. Med. Biol. 2001, 491, 551-585.
    • (2001) Adv. Exp. Med. Biol. , vol.491 , pp. 551-585
    • Wu, A.M.1    Song, S.C.2    Tsai, M.S.3    Herp, A.4
  • 15
    • 0036703175 scopus 로고    scopus 로고
    • Plant lectins: occurrence, biochemistry, functions and applications
    • Rudiger, H., Gabius, H. J., Plant lectins: occurrence, biochemistry, functions and applications. Glycoconj. J. 2001, 18, 589-613.
    • (2001) Glycoconj. J. , vol.18 , pp. 589-613
    • Rudiger, H.1    Gabius, H.J.2
  • 16
    • 5444254250 scopus 로고    scopus 로고
    • Lectin-based structural glycomics: glycoproteomics and glycan profiling
    • Hirabayashi, J., Lectin-based structural glycomics: glycoproteomics and glycan profiling. Glycoconj. J. 2004, 21, 35-40.
    • (2004) Glycoconj. J. , vol.21 , pp. 35-40
    • Hirabayashi, J.1
  • 17
    • 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. et al., 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
  • 18
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography
    • Jung, K., Cho, W., Regnier, F. E., Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography. J. Proteome. Res. 2009, 8, 643-650.
    • (2009) J. Proteome. Res. , vol.8 , pp. 643-650
    • Jung, K.1    Cho, W.2    Regnier, F.E.3
  • 19
    • 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 Analyt. Technol. Biomed. Life Sci. 2007, 845, 121-137.
    • (2007) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.845 , pp. 121-137
    • Madera, M.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4
  • 20
    • 77956518417 scopus 로고    scopus 로고
    • Development of serum glycoproteomic profiling technique; simultaneous identification of glycosylation sites and site-specific quantification of glycan structure changes
    • Ueda, K., Takami, S., Saichi, N., Daigo, Y. et al., Development of serum glycoproteomic profiling technique; simultaneous identification of glycosylation sites and site-specific quantification of glycan structure changes. Mol. Cell. Proteomics 2010, 9, 1819-1828.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1819-1828
    • Ueda, K.1    Takami, S.2    Saichi, N.3    Daigo, Y.4
  • 21
    • 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
  • 22
    • 82955161671 scopus 로고    scopus 로고
    • Identification of glycoproteins associated with different histological subtypes of ovarian tumors using quantitative glycoproteomics
    • Tian, Y., Yao, Z., Roden, R. B., Zhang, H., Identification of glycoproteins associated with different histological subtypes of ovarian tumors using quantitative glycoproteomics. Proteomics 2011, 11, 4677-4687.
    • (2011) Proteomics , vol.11 , pp. 4677-4687
    • Tian, Y.1    Yao, Z.2    Roden, R.B.3    Zhang, H.4
  • 23
    • 80052805542 scopus 로고    scopus 로고
    • Quantitative glycoproteomic analysis of optimal cutting temperature-embedded frozen tissues identifying glycoproteins associated with aggressive prostate cancer
    • Tian, Y., Bova, G. S., Zhang, H., Quantitative glycoproteomic analysis of optimal cutting temperature-embedded frozen tissues identifying glycoproteins associated with aggressive prostate cancer. Anal. Chem. 2011, 83, 7013-7019.
    • (2011) Anal. Chem. , vol.83 , pp. 7013-7019
    • Tian, Y.1    Bova, G.S.2    Zhang, H.3
  • 24
    • 78649861704 scopus 로고    scopus 로고
    • Lung cancer serum biomarker discovery using glycoprotein capture and liquid chromatography mass spectrometry
    • Zeng, X., Hood, B. L., Sun, M., Conrads, T. P. et al., Lung cancer serum biomarker discovery using glycoprotein capture and liquid chromatography mass spectrometry. J. Proteome Res. 2010, 9, 6440-6449.
    • (2010) J. Proteome Res. , vol.9 , pp. 6440-6449
    • Zeng, X.1    Hood, B.L.2    Sun, M.3    Conrads, T.P.4
  • 25
    • 62549145382 scopus 로고    scopus 로고
    • Identification of glycoproteins from mouse skin tumors and plasma
    • Tian, Y., Kelly-Spratt, K. S., Kemp, C. J., Zhang, H., Identification of glycoproteins from mouse skin tumors and plasma. Clin. Proteomics 2008, 4, 117-136.
    • (2008) Clin. Proteomics , vol.4 , pp. 117-136
    • Tian, Y.1    Kelly-Spratt, K.S.2    Kemp, C.J.3    Zhang, H.4
  • 26
    • 64349089985 scopus 로고    scopus 로고
    • Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins
    • Wollscheid, B., Bausch-Fluck, D., Henderson, C., O'Brien, R. et al., Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat. Biotechnol. 2009, 27, 378-386.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 378-386
    • Wollscheid, B.1    Bausch-Fluck, D.2    Henderson, C.3    O'Brien, R.4
  • 27
    • 72149120326 scopus 로고    scopus 로고
    • The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation
    • Gundry, R. L., Raginski, K., Tarasova, Y., Tchernyshyov, I. et al., The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation. Mol. Cell. Proteomics 2009, 8, 2555-2569.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2555-2569
    • Gundry, R.L.1    Raginski, K.2    Tarasova, Y.3    Tchernyshyov, I.4
  • 28
    • 84862322594 scopus 로고    scopus 로고
    • Altered expression of sialylated glycoproteins in breast cancer using hydrazide chemistry and mass spectrometry
    • Tian, Y., Esteva, F. J., Song, J., Zhang, H., Altered expression of sialylated glycoproteins in breast cancer using hydrazide chemistry and mass spectrometry. Mol. Cell. Proteomics 2012, 11, M111 011403.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Tian, Y.1    Esteva, F.J.2    Song, J.3    Zhang, H.4
  • 29
    • 84863806531 scopus 로고    scopus 로고
    • Metabolic flux increases glycoprotein sialylation: implications for cell adhesion and cancer metastasis
    • Almaraz, R. T., Tian, Y., Bhattarcharya, R., Tan, E. et al., Metabolic flux increases glycoprotein sialylation: implications for cell adhesion and cancer metastasis. Mol. Cell. Proteomics 2012, 11, M112 017558.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Almaraz, R.T.1    Tian, Y.2    Bhattarcharya, R.3    Tan, E.4
  • 30
    • 70350735945 scopus 로고    scopus 로고
    • Enrichment of glycopeptides for glycan structure and attachment site identification
    • Nilsson, J., Ruetschi, U., Halim, A., Hesse, C. et al., Enrichment of glycopeptides for glycan structure and attachment site identification. Nat. Methods 2009, 6, 809-811.
    • (2009) Nat. Methods , vol.6 , pp. 809-811
    • Nilsson, J.1    Ruetschi, U.2    Halim, A.3    Hesse, C.4
  • 31
    • 84855188603 scopus 로고    scopus 로고
    • Development of glycoprotein capture-based label-free method for the high-throughput screening of differential glycoproteins in hepatocellular carcinoma
    • Chen, R., Tan, Y., Wang, M., Wang, F. et al., Development of glycoprotein capture-based label-free method for the high-throughput screening of differential glycoproteins in hepatocellular carcinoma. Mol. Cell. Proteomics 2011, 10, M110 006445.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Chen, R.1    Tan, Y.2    Wang, M.3    Wang, F.4
  • 32
    • 0022873552 scopus 로고
    • Isolation of 3,4-dihydroxyphenylalanine-containing proteins using boronate affinity chromatography
    • Hawkins, C. J., Lavin, M. F., Parry, D. L., Ross, I. L., Isolation of 3, 4-dihydroxyphenylalanine-containing proteins using boronate affinity chromatography. Anal. Biochem. 1986, 159, 187-190.
    • (1986) Anal. Biochem. , vol.159 , pp. 187-190
    • Hawkins, C.J.1    Lavin, M.F.2    Parry, D.L.3    Ross, I.L.4
  • 33
    • 0033661187 scopus 로고    scopus 로고
    • Boronate affinity chromatography
    • Liu, X. C., Scouten, W. H., Boronate affinity chromatography. Methods Mol. Biol. 2000, 147, 119-128.
    • (2000) Methods Mol. Biol. , vol.147 , pp. 119-128
    • Liu, X.C.1    Scouten, W.H.2
  • 34
    • 67649939045 scopus 로고    scopus 로고
    • Synthesis and application of novel phenylboronate affinity materials based on organic polymer particles for selective trapping of glycoproteins
    • Preinerstorfer, B., Lammerhofer, M., Lindner, W., Synthesis and application of novel phenylboronate affinity materials based on organic polymer particles for selective trapping of glycoproteins. J. Sep. Sci. 2009, 32, 1673-1685.
    • (2009) J. Sep. Sci. , vol.32 , pp. 1673-1685
    • Preinerstorfer, B.1    Lammerhofer, M.2    Lindner, W.3
  • 35
    • 70350379579 scopus 로고    scopus 로고
    • Synthesis of hydrophilic boronate affinity monolithic capillary for specific capture of glycoproteins by capillary liquid chromatography
    • Ren, L., Liu, Y., Dong, M., Liu, Z., Synthesis of hydrophilic boronate affinity monolithic capillary for specific capture of glycoproteins by capillary liquid chromatography. J. Chromatogr. A 2009, 1216, 8421-8425.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 8421-8425
    • Ren, L.1    Liu, Y.2    Dong, M.3    Liu, Z.4
  • 37
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon, E., Bertozzi, C. R., Cell surface engineering by a modified Staudinger reaction. Science 2000, 287, 2007-2010.
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 38
    • 0041422487 scopus 로고    scopus 로고
    • A chemical approach for identifying O-GlcNAc-modified proteins in cells
    • Vocadlo, D. J., Hang, H. C., Kim, E. J., Hanover, J. A. et al., A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc. Natl. Acad. Sci. USA 2003, 100, 9116-9121.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9116-9121
    • Vocadlo, D.J.1    Hang, H.C.2    Kim, E.J.3    Hanover, J.A.4
  • 39
    • 0345598906 scopus 로고    scopus 로고
    • A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
    • Hang, H. C., Yu, C., Kato, D. L., Bertozzi, C. R., A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc. Natl. Acad. Sci. USA 2003, 100, 14846-14851.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14846-14851
    • Hang, H.C.1    Yu, C.2    Kato, D.L.3    Bertozzi, C.R.4
  • 40
    • 33747618970 scopus 로고    scopus 로고
    • Glycoproteomic probes for fluorescent imaging of fucosylated glycans in vivo
    • Sawa, M., Hsu, T. L., Itoh, T., Sugiyama, M. et al., Glycoproteomic probes for fluorescent imaging of fucosylated glycans in vivo. Proc. Natl. Acad. Sci. USA 2006, 103, 12371-12376.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12371-12376
    • Sawa, M.1    Hsu, T.L.2    Itoh, T.3    Sugiyama, M.4
  • 41
    • 0030929377 scopus 로고    scopus 로고
    • Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis
    • Mahal, L. K., Yarema, K. J., Bertozzi, C. R., Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis. Science 1997, 276, 1125-1128.
    • (1997) Science , vol.276 , pp. 1125-1128
    • Mahal, L.K.1    Yarema, K.J.2    Bertozzi, C.R.3
  • 42
    • 33646589635 scopus 로고    scopus 로고
    • Metabolic installation of thiols into sialic acid modulates adhesion and stem cell biology
    • Sampathkumar, S. G., Li, A. V., Jones, M. B., Sun, Z., Yarema, K. J., Metabolic installation of thiols into sialic acid modulates adhesion and stem cell biology. Nat. Chem. Biol. 2006, 2, 149-152.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 149-152
    • Sampathkumar, S.G.1    Li, A.V.2    Jones, M.B.3    Sun, Z.4    Yarema, K.J.5
  • 43
    • 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
  • 44
    • 0034729576 scopus 로고    scopus 로고
    • Staudinger ligation: a peptide from a thioester and azide
    • Nilsson, B. L., Kiessling, L. L., Raines, R. T., Staudinger ligation: a peptide from a thioester and azide. Org. Lett. 2000, 2, 1939-1941.
    • (2000) Org. Lett. , vol.2 , pp. 1939-1941
    • Nilsson, B.L.1    Kiessling, L.L.2    Raines, R.T.3
  • 45
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A. E., Cravatt, B. F., Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 2004, 11, 535-546.
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 46
    • 9344227358 scopus 로고    scopus 로고
    • A strain-promoted [3 + 2] azide-alkyne cycloaddition for covalent modification of biomolecules in living systems
    • Agard, N. J., Prescher, J. A., Bertozzi, C. R., A strain-promoted [3 + 2] azide-alkyne cycloaddition for covalent modification of biomolecules in living systems. J. Am. Chem. Soc. 2004, 126, 15046-15047.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15046-15047
    • Agard, N.J.1    Prescher, J.A.2    Bertozzi, C.R.3
  • 47
    • 79958002548 scopus 로고    scopus 로고
    • Targeted identification of metastasis-associated cell-surface sialoglycoproteins in prostate cancer
    • Yang, L., Nyalwidhe, J. O., Guo, S., Drake, R. R., Semmes, O. J., Targeted identification of metastasis-associated cell-surface sialoglycoproteins in prostate cancer. Mol. Cell. Proteomics 2011, 10, M110 007294.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Yang, L.1    Nyalwidhe, J.O.2    Guo, S.3    Drake, R.R.4    Semmes, O.J.5
  • 48
    • 80051789064 scopus 로고    scopus 로고
    • Cell surface glycoproteomic analysis of prostate cancer-derived PC-3 cells
    • Hubbard, S. C., Boyce, M., McVaugh, C. T., Peehl, D. M. et al., Cell surface glycoproteomic analysis of prostate cancer-derived PC-3 cells. Bioorg. Med. Chem. Lett. 2011, 21, 4945-4950.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 4945-4950
    • Hubbard, S.C.1    Boyce, M.2    McVaugh, C.T.3    Peehl, D.M.4
  • 49
    • 33644841035 scopus 로고    scopus 로고
    • Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites
    • Alvarez-Manilla, G., Atwood, J., 3rd, Guo, Y., Warren, N. L. et al., Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites. J. Proteome. Res. 2006, 5, 701-708.
    • (2006) J. Proteome. Res. , vol.5 , pp. 701-708
    • Alvarez-Manilla, G.1    Atwood 3rd, J.2    Guo, Y.3    Warren, N.L.4
  • 50
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N. et al., A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J. Proteome. Res. 2004, 3, 556-566.
    • (2004) J. Proteome. Res. , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4
  • 51
    • 80054984666 scopus 로고    scopus 로고
    • Online combination of reversed-phase/reversed-phase and porous graphitic carbon liquid chromatography for multicomponent separation of proteomics and glycoproteomics samples
    • Lam, M. P., Lau, E., Siu, S. O., Ng, D. C. et al., Online combination of reversed-phase/reversed-phase and porous graphitic carbon liquid chromatography for multicomponent separation of proteomics and glycoproteomics samples. Electrophoresis 2011, 32, 2930-2940.
    • (2011) Electrophoresis , vol.32 , pp. 2930-2940
    • Lam, M.P.1    Lau, E.2    Siu, S.O.3    Ng, D.C.4
  • 52
    • 8744300809 scopus 로고    scopus 로고
    • Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness
    • Ge, Y., Rajkumar, L., Guzman, R. C., Nandi, S. et al., Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness. Proteomics 2004, 4, 3464-3467.
    • (2004) Proteomics , vol.4 , pp. 3464-3467
    • Ge, Y.1    Rajkumar, L.2    Guzman, R.C.3    Nandi, S.4
  • 53
    • 80052805542 scopus 로고    scopus 로고
    • Quantitative glycoproteomic analysis of optimal cutting temperature-embedded frozen tissues identifying glycoproteins associated with aggressive prostate cancer
    • Tian, Y., Bova, G. S., Zhang, H., Quantitative glycoproteomic analysis of optimal cutting temperature-embedded frozen tissues identifying glycoproteins associated with aggressive prostate cancer. Anal. Chem. 2011, 83, 7013-7019.
    • (2011) Anal. Chem. , vol.83 , pp. 7013-7019
    • Tian, Y.1    Bova, G.S.2    Zhang, H.3
  • 54
    • 82955161671 scopus 로고    scopus 로고
    • Identification of glycoproteins associated with different histological subtypes of ovarian tumors using quantitative glycoproteomics
    • Tian, Y., Yao, Z., Roden, R. B., Zhang, H., Identification of glycoproteins associated with different histological subtypes of ovarian tumors using quantitative glycoproteomics. Proteomics 2011, 11, 4677-4687.
    • (2011) Proteomics , vol.11 , pp. 4677-4687
    • Tian, Y.1    Yao, Z.2    Roden, R.B.3    Zhang, H.4
  • 55
    • 0032536822 scopus 로고    scopus 로고
    • Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin
    • Sasaki, T., Brakebusch, C., Engel, J., Timpl, R., Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. EMBO J. 1998, 17, 1606-1613.
    • (1998) EMBO J. , vol.17 , pp. 1606-1613
    • Sasaki, T.1    Brakebusch, C.2    Engel, J.3    Timpl, R.4
  • 56
    • 76749118044 scopus 로고    scopus 로고
    • The tumor-associated antigen 90K/Mac-2-binding protein secreted by human colon carcinoma cells enhances extracellular levels of promatrilysin and is a novel substrate of matrix metalloproteinases-2, -7 (matrilysin) and -9: Implications of proteolytic cleavage
    • Ulmer, T. A., Keeler, V., Andre, S., Gabius, H. J. et al., The tumor-associated antigen 90K/Mac-2-binding protein secreted by human colon carcinoma cells enhances extracellular levels of promatrilysin and is a novel substrate of matrix metalloproteinases-2, -7 (matrilysin) and -9: Implications of proteolytic cleavage. Biochim. Biophys. Acta. 2010, 1800, 336-343.
    • (2010) Biochim. Biophys. Acta. , vol.1800 , pp. 336-343
    • Ulmer, T.A.1    Keeler, V.2    Andre, S.3    Gabius, H.J.4
  • 57
    • 67650451085 scopus 로고    scopus 로고
    • The multifaceted role of periostin in tumorigenesis
    • Ruan, K., Bao, S., Ouyang, G., The multifaceted role of periostin in tumorigenesis. Cell. Mol. Life Sci. 2009, 66, 2219-2230.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2219-2230
    • Ruan, K.1    Bao, S.2    Ouyang, G.3
  • 58
    • 34247882685 scopus 로고    scopus 로고
    • Periostin regulates collagen fibrillogenesis and the biomechanical properties of connective tissues
    • Norris, R. A., Damon, B., Mironov, V., Kasyanov, V. et al., Periostin regulates collagen fibrillogenesis and the biomechanical properties of connective tissues. J. Cell. Biochem. 2007, 101, 695-711.
    • (2007) J. Cell. Biochem. , vol.101 , pp. 695-711
    • Norris, R.A.1    Damon, B.2    Mironov, V.3    Kasyanov, V.4
  • 59
    • 33745394558 scopus 로고    scopus 로고
    • Periostin: a novel component of subepithelial fibrosis of bronchial asthma downstream of IL-4 and IL-13 signals
    • Takayama, G., Arima, K., Kanaji, T., Toda, S. et al., Periostin: a novel component of subepithelial fibrosis of bronchial asthma downstream of IL-4 and IL-13 signals. J. Allergy Clin. Immunol. 2006, 118, 98-104.
    • (2006) J. Allergy Clin. Immunol. , vol.118 , pp. 98-104
    • Takayama, G.1    Arima, K.2    Kanaji, T.3    Toda, S.4
  • 60
    • 34249289041 scopus 로고    scopus 로고
    • Snail, Zeb and bHLH factors in tumour progression: an alliance against the epithelial phenotype
    • Peinado, H., Olmeda, D., Cano, A., Snail, Zeb and bHLH factors in tumour progression: an alliance against the epithelial phenotype? Nat. Rev. Cancer 2007, 7, 415-428.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 415-428
    • Peinado, H.1    Olmeda, D.2    Cano, A.3
  • 61
    • 33244463813 scopus 로고    scopus 로고
    • Complex networks orchestrate epithelial-mesenchymal transitions
    • Thiery, J. P., Sleeman, J. P., Complex networks orchestrate epithelial-mesenchymal transitions. Nat. Rev. Mol. Cell Biol. 2006, 7, 131-142.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 131-142
    • Thiery, J.P.1    Sleeman, J.P.2
  • 62
    • 0036595629 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in tumour progression
    • Thiery, J. P., Epithelial-mesenchymal transitions in tumour progression. Nat. Rev. Cancer 2002, 2, 442-454.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 442-454
    • Thiery, J.P.1
  • 63
    • 58149335431 scopus 로고    scopus 로고
    • Prognostic significance of epithelial-mesenchymal and mesenchymal-epithelial transition protein expression in non-small cell lung cancer
    • Soltermann, A., Tischler, V., Arbogast, S., Braun, J. et al., Prognostic significance of epithelial-mesenchymal and mesenchymal-epithelial transition protein expression in non-small cell lung cancer. Clin. Cancer Res. 2008, 14, 7430-7437.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 7430-7437
    • Soltermann, A.1    Tischler, V.2    Arbogast, S.3    Braun, J.4
  • 64
    • 0036775241 scopus 로고    scopus 로고
    • Versican: a versatile extracellular matrix proteoglycan in cell biology
    • Wight, T. N., Versican: a versatile extracellular matrix proteoglycan in cell biology. Curr. Opin. Cell. Biol. 2002, 14, 617-623.
    • (2002) Curr. Opin. Cell. Biol. , vol.14 , pp. 617-623
    • Wight, T.N.1
  • 65
    • 33847281322 scopus 로고    scopus 로고
    • Prognostic significance of stromal versican expression in human endometrial cancer
    • Kodama, J., Hasengaowa, Kusumoto, T., Seki, N. et al., Prognostic significance of stromal versican expression in human endometrial cancer. Ann. Oncol. 2007, 18, 269-274.
    • (2007) Ann. Oncol. , vol.18 , pp. 269-274
    • Kodama, J.1    Hasengaowa, K.T.2    Seki, N.3
  • 66
    • 0035880704 scopus 로고    scopus 로고
    • Serum level of the periostin, a homologue of an insect cell adhesion molecule, as a prognostic marker in nonsmall cell lung carcinomas
    • Sasaki, H., Dai, M., Auclair, D., Fukai, I. et al., Serum level of the periostin, a homologue of an insect cell adhesion molecule, as a prognostic marker in nonsmall cell lung carcinomas. Cancer 2001, 92, 843-848.
    • (2001) Cancer , vol.92 , pp. 843-848
    • Sasaki, H.1    Dai, M.2    Auclair, D.3    Fukai, I.4
  • 67
    • 0012579234 scopus 로고    scopus 로고
    • Prostate-specific antigen and the early diagnosis of prostate cancer
    • Caplan, A., Kratz, A., Prostate-specific antigen and the early diagnosis of prostate cancer. Am. J. Clin. Pathol. 2002, 117, S104-S108.
    • (2002) Am. J. Clin. Pathol. , vol.117
    • Caplan, A.1    Kratz, A.2
  • 68
    • 80755138399 scopus 로고    scopus 로고
    • Parameters to improve the specificity of the prostate-specific antigen. Early detection of prostate cancer
    • Borgermann, C., Kliner, S., Swoboda, A., Luboldt, H. J. et al., Parameters to improve the specificity of the prostate-specific antigen. Early detection of prostate cancer. Urologe A 2011, 50, 1095-1100.
    • (2011) Urologe A , vol.50 , pp. 1095-1100
    • Borgermann, C.1    Kliner, S.2    Swoboda, A.3    Luboldt, H.J.4
  • 69
    • 20044377211 scopus 로고    scopus 로고
    • Use of targeted glycoproteomics to identify serum glycoproteins that correlate with liver cancer in woodchucks and humans
    • Block, T. M., Comunale, M. A., Lowman, M., Steel, L. F. et al., Use of targeted glycoproteomics to identify serum glycoproteins that correlate with liver cancer in woodchucks and humans. Proc. Natl. Acad. Sci. USA 2005, 102, 779-784.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 779-784
    • Block, T.M.1    Comunale, M.A.2    Lowman, M.3    Steel, L.F.4
  • 70
    • 79956282745 scopus 로고    scopus 로고
    • Glycoproteomics analysis to identify a glycoform on haptoglobin associated with lung cancer
    • Tsai, H. Y., Boonyapranai, K., Sriyam, S., Yu, C. J. et al., Glycoproteomics analysis to identify a glycoform on haptoglobin associated with lung cancer. Proteomics 2011, 11, 2162-2170.
    • (2011) Proteomics , vol.11 , pp. 2162-2170
    • Tsai, H.Y.1    Boonyapranai, K.2    Sriyam, S.3    Yu, C.J.4
  • 71
    • 0034131162 scopus 로고    scopus 로고
    • Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring
    • Durand, G., Seta, N., Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring. Clin. Chem. 2000, 46, 795-805.
    • (2000) Clin. Chem. , vol.46 , pp. 795-805
    • Durand, G.1    Seta, N.2
  • 72
    • 75849140063 scopus 로고    scopus 로고
    • Sweetening the pot: adding glycosylation to the biomarker discovery equation
    • Drake, P. M., Cho, W., Li, B., Prakobphol, A. et al., Sweetening the pot: adding glycosylation to the biomarker discovery equation. Clin. Chem. 2010, 56, 223-236.
    • (2010) Clin. Chem. , vol.56 , pp. 223-236
    • Drake, P.M.1    Cho, W.2    Li, B.3    Prakobphol, A.4
  • 73
    • 34247853422 scopus 로고    scopus 로고
    • Chemical glycosylation in the synthesis of glycoconjugate antitumour vaccines
    • Galonic, D. P., Gin, D. Y., Chemical glycosylation in the synthesis of glycoconjugate antitumour vaccines. Nature 2007, 446, 1000-1007.
    • (2007) Nature , vol.446 , pp. 1000-1007
    • Galonic, D.P.1    Gin, D.Y.2
  • 74
    • 50449087746 scopus 로고    scopus 로고
    • Clinical application of functional glycoproteomics - dissection of glycotopes carried by soluble CD44 variants in sera of patients with cancers
    • Lim, K. T., Miyazaki, K., Kimura, N., Izawa, M. et al., Clinical application of functional glycoproteomics - dissection of glycotopes carried by soluble CD44 variants in sera of patients with cancers. Proteomics 2008, 8, 3263-3273.
    • (2008) Proteomics , vol.8 , pp. 3263-3273
    • Lim, K.T.1    Miyazaki, K.2    Kimura, N.3    Izawa, M.4
  • 75
    • 61849174789 scopus 로고    scopus 로고
    • Glycoproteomics for prostate cancer detection: changes in serum PSA glycosylation patterns
    • Meany, D. L., Zhang, Z., Sokoll, L. J., Zhang, H. et al., Glycoproteomics for prostate cancer detection: changes in serum PSA glycosylation patterns. J. Proteome. Res. 2009, 8, 613-619.
    • (2009) J. Proteome. Res. , vol.8 , pp. 613-619
    • Meany, D.L.1    Zhang, Z.2    Sokoll, L.J.3    Zhang, H.4
  • 76
    • 81255146498 scopus 로고    scopus 로고
    • Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays
    • Li, Y., Tao, S. C., Bova, G. S., Liu, A. Y. et al., Detection and verification of glycosylation patterns of glycoproteins from clinical specimens using lectin microarrays and lectin-based immunosorbent assays. Anal. Chem. 2011, 83, 8509-8516.
    • (2011) Anal. Chem. , vol.83 , pp. 8509-8516
    • Li, Y.1    Tao, S.C.2    Bova, G.S.3    Liu, A.Y.4
  • 77
    • 78650796888 scopus 로고    scopus 로고
    • Simultaneous analysis of glycosylated and sialylated prostate-specific antigen revealing differential distribution of glycosylated prostate-specific antigen isoforms in prostate cancer tissues
    • Li, Y., Tian, Y., Rezai, T., Prakash, A. et al., Simultaneous analysis of glycosylated and sialylated prostate-specific antigen revealing differential distribution of glycosylated prostate-specific antigen isoforms in prostate cancer tissues. Anal. Chem. 2011, 83, 240-245.
    • (2011) Anal. Chem. , vol.83 , pp. 240-245
    • Li, Y.1    Tian, Y.2    Rezai, T.3    Prakash, A.4
  • 78
    • 0038618896 scopus 로고    scopus 로고
    • Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins
    • Peracaula, R., Tabares, G., Royle, L., Harvey, D. J. et al., Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins. Glycobiology 2003, 13, 457-470.
    • (2003) Glycobiology , vol.13 , pp. 457-470
    • Peracaula, R.1    Tabares, G.2    Royle, L.3    Harvey, D.J.4
  • 79
    • 35448955641 scopus 로고    scopus 로고
    • Cancer biomarker discovery in plasma using a tissue-targeted proteomic approach
    • Zhang, H., Chan, D. W., Cancer biomarker discovery in plasma using a tissue-targeted proteomic approach. Cancer Epidem Biomar 2007, 16, 1915-1917.
    • (2007) Cancer Epidem Biomar , vol.16 , pp. 1915-1917
    • Zhang, H.1    Chan, D.W.2
  • 80
    • 78149399037 scopus 로고    scopus 로고
    • Mapping tissue-specific expression of extracellular proteins using systematic glycoproteomic analysis of different mouse tissues
    • Tian, Y., Kelly-Spratt, K. S., Kemp, C. J., Zhang, H., Mapping tissue-specific expression of extracellular proteins using systematic glycoproteomic analysis of different mouse tissues. J. Proteome. Res. 2010, 9, 5837-5847.
    • (2010) J. Proteome. Res. , vol.9 , pp. 5837-5847
    • Tian, Y.1    Kelly-Spratt, K.S.2    Kemp, C.J.3    Zhang, H.4
  • 81
    • 80052024809 scopus 로고    scopus 로고
    • Development of quantitative plasma N-glycoproteomics using label-free 2D LC-MALDI MS and its applicability for biomarker discovery in hepatocellular carcinoma
    • Ishihara, T., Fukuda, I., Morita, A., Takinami, Y. et al., Development of quantitative plasma N-glycoproteomics using label-free 2D LC-MALDI MS and its applicability for biomarker discovery in hepatocellular carcinoma. J. Proteomics 2011, 74, 2159-2168.
    • (2011) J. Proteomics , vol.74 , pp. 2159-2168
    • Ishihara, T.1    Fukuda, I.2    Morita, A.3    Takinami, Y.4
  • 82
    • 77958190741 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin variants in plasma from HIV-infected patients revealed by proteomic and glycoproteomic analysis
    • Zhang, L., Jia, X., Zhang, X., Cao, J. et al., Alpha-1 antitrypsin variants in plasma from HIV-infected patients revealed by proteomic and glycoproteomic analysis. Electrophoresis 2010, 31, 3437-3445.
    • (2010) Electrophoresis , vol.31 , pp. 3437-3445
    • Zhang, L.1    Jia, X.2    Zhang, X.3    Cao, J.4
  • 83
    • 77249130649 scopus 로고    scopus 로고
    • Glycoproteomics of paclitaxel resistance in human epithelial ovarian cancer cell lines: towards the identification of putative biomarkers
    • Di Michele, M., Marcone, S., Cicchillitti, L., Della Corte, A. et al., Glycoproteomics of paclitaxel resistance in human epithelial ovarian cancer cell lines: towards the identification of putative biomarkers. J. Proteomics 2010, 73, 879-898.
    • (2010) J. Proteomics , vol.73 , pp. 879-898
    • Di Michele, M.1    Marcone, S.2    Cicchillitti, L.3    Della Corte, A.4
  • 84
    • 77956518417 scopus 로고    scopus 로고
    • Development of serum glycoproteomic profiling technique; simultaneous identification of glycosylation sites and site-specific quantification of glycan structure changes
    • Ueda, K., Takami, S., Saichi, N., Daigo, Y. et al., Development of serum glycoproteomic profiling technique; simultaneous identification of glycosylation sites and site-specific quantification of glycan structure changes. Mol. Cell. Proteomics 2010.
    • (2010) Mol. Cell. Proteomics
    • Ueda, K.1    Takami, S.2    Saichi, N.3    Daigo, Y.4
  • 85
    • 79951574929 scopus 로고    scopus 로고
    • Up-regulation of prohibitin 1 is involved in the proliferation and migration of liver cancer cells
    • Xu, Z., Wu, J., Zha, X., Up-regulation of prohibitin 1 is involved in the proliferation and migration of liver cancer cells. Sci. China Life Sci. 2011, 54, 121-127.
    • (2011) Sci. China Life Sci. , vol.54 , pp. 121-127
    • Xu, Z.1    Wu, J.2    Zha, X.3


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