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Volumn 8, Issue 2, 2009, Pages 287-301

Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; HYDRAZIDE; LECTIN; MEMBRANE PROTEIN; PROTEOME; RESIN; SIALIC ACID;

EID: 61649103556     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800272-MCP200     Document Type: Article
Times cited : (108)

References (61)
  • 1
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H., and Sharon, N. (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473, 4-8
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 2
    • 0026049185 scopus 로고
    • The 'yellow brick road' to branched complex Nglycans
    • Schachter, H. (1991) The 'yellow brick road' to branched complex Nglycans. Glycobiology 1, 453-461
    • (1991) Glycobiology , vol.1 , pp. 453-461
    • Schachter, H.1
  • 3
    • 0022572229 scopus 로고
    • Trafficking of lysosomal enzymes in normal and disease states
    • Kornfeld, S. (1986) Trafficking of lysosomal enzymes in normal and disease states. J. Clin. Investig. 77, 1-6
    • (1986) J. Clin. Investig , vol.77 , pp. 1-6
    • Kornfeld, S.1
  • 4
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta, E. S., and Parodi, A. J. (2003) Quality control and protein folding in the secretory pathway. Annu. Rev. Cell Dev. Biol. 19, 649-676
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 5
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to Mammalian glycan function
    • Lowe, J. B., and Marth, J. D. (2003) A genetic approach to Mammalian glycan function. Annu. Rev. Biochem. 72, 643-691
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 6
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • Hakomori, S. (1996) Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 56, 5309-5318
    • (1996) Cancer Res , vol.56 , pp. 5309-5318
    • Hakomori, S.1
  • 7
    • 0036816590 scopus 로고    scopus 로고
    • Regulation of signal transduction pathways in development by glycosylation
    • Haltiwanger, R. S. (2002) Regulation of signal transduction pathways in development by glycosylation. Curr. Opin. Struct. Biol. 12, 593-598
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 593-598
    • Haltiwanger, R.S.1
  • 8
    • 0042196026 scopus 로고    scopus 로고
    • Glycobiology of neuromuscular disorders
    • Martin, P. T., and Freeze, H. H. (2003) Glycobiology of neuromuscular disorders. Glycobiology 13, 67R-75R
    • (2003) Glycobiology , vol.13
    • Martin, P.T.1    Freeze, H.H.2
  • 9
    • 33645450506 scopus 로고    scopus 로고
    • Mechanisms in protein O-glycan biosynthesis and clinical and molecular aspects of protein O-glycan biosynthesis defects: A review
    • Wopereis, S., Lefeber, D. J., Morava, E., and Wevers, R. A. (2006) Mechanisms in protein O-glycan biosynthesis and clinical and molecular aspects of protein O-glycan biosynthesis defects: a review. Clin. Chem. 52, 574-600
    • (2006) Clin. Chem , vol.52 , pp. 574-600
    • Wopereis, S.1    Lefeber, D.J.2    Morava, E.3    Wevers, R.A.4
  • 10
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • Bard, F., and Malhotra, V. (2006) The formation of TGN-to-plasma-membrane transport carriers. Annu. Rev. Cell Dev. Biol. 22, 439-455
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 12
    • 39049137589 scopus 로고    scopus 로고
    • α2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo
    • Hedlund, M., Ng, E., Varki, A., and Varki, N. M. (2008) α2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo. Cancer Res. 68, 388-394
    • (2008) Cancer Res , vol.68 , pp. 388-394
    • Hedlund, M.1    Ng, E.2    Varki, A.3    Varki, N.M.4
  • 13
    • 0027383298 scopus 로고
    • Cellular sialoglycoconjugates: A histochernical perspective
    • Roth, J. (1993) Cellular sialoglycoconjugates: a histochernical perspective. Histochem. J. 25, 687-710
    • (1993) Histochem. J , vol.25 , pp. 687-710
    • Roth, J.1
  • 15
    • 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., and Aebersold, R. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 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
  • 16
    • 34547800600 scopus 로고    scopus 로고
    • Isolation of N-linked glycopeptides from plasma
    • Zhou, Y., Aebersold, R., and Zhang, H. (2007) Isolation of N-linked glycopeptides from plasma. Anal. Chem. 79, 5826-5837
    • (2007) Anal. Chem , vol.79 , pp. 5826-5837
    • Zhou, Y.1    Aebersold, R.2    Zhang, H.3
  • 17
    • 0024278423 scopus 로고
    • The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complextype Asn-linked oligosaccharides containing terminal sialic acid-linked α-2,3 to penultimate galactose residues
    • Wang, W. C., and Cummings, R. D. (1988) The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complextype Asn-linked oligosaccharides containing terminal sialic acid-linked α-2,3 to penultimate galactose residues. J. Biol. Chem. 263, 4576-4585
    • (1988) J. Biol. Chem , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 18
    • 0028299382 scopus 로고
    • Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A
    • Konami, Y., Yamamoto, K., Osawa, T., and Irimura, T. (1994) Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A. FEBS Lett. 342, 334-338
    • (1994) FEBS Lett , vol.342 , pp. 334-338
    • Konami, Y.1    Yamamoto, K.2    Osawa, T.3    Irimura, T.4
  • 19
    • 0034625394 scopus 로고    scopus 로고
    • An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides
    • Imberty, A., Gautier, C., Lescar, J., Perez, S., Wyns, L., and Loris, R. (2000) An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides. J. Biol. Chem. 275, 17541-17548
    • (2000) J. Biol. Chem , vol.275 , pp. 17541-17548
    • Imberty, A.1    Gautier, C.2    Lescar, J.3    Perez, S.4    Wyns, L.5    Loris, R.6
  • 20
    • 0034128749 scopus 로고    scopus 로고
    • Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms
    • Whitfield, M. L., Zheng, L. X., Baldwin, A., Ohta, T., Hurt, M. M., and Marzluff, W. F. (2000) Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol. Cell. Biol. 20, 4188-4198
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4188-4198
    • Whitfield, M.L.1    Zheng, L.X.2    Baldwin, A.3    Ohta, T.4    Hurt, M.M.5    Marzluff, W.F.6
  • 21
    • 38949168914 scopus 로고    scopus 로고
    • Visualization of detergent solubilization of membranes: Implications for the isolation of rafts
    • Garner, A. E., Smith, D. A., and Hooper, N. M. (2008) Visualization of detergent solubilization of membranes: implications for the isolation of rafts. Biophys. J. 94, 1326-1340
    • (2008) Biophys. J , vol.94 , pp. 1326-1340
    • Garner, A.E.1    Smith, D.A.2    Hooper, N.M.3
  • 22
    • 0141955057 scopus 로고    scopus 로고
    • A method for reducing the time required to match protein sequences with tandem mass spectra
    • Craig, R., and Beavis, R. C. (2003) A method for reducing the time required to match protein sequences with tandem mass spectra. Rapid Commun. Mass Spectrom. 17, 2310-2316
    • (2003) Rapid Commun. Mass Spectrom , vol.17 , pp. 2310-2316
    • Craig, R.1    Beavis, R.C.2
  • 23
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 0036549592 scopus 로고    scopus 로고
    • HeLa cells 50 years on: The good, the bad and the ugly
    • Masters, J. R. (2002) HeLa cells 50 years on: the good, the bad and the ugly. Nat. Rev. 2, 315-319
    • (2002) Nat. Rev , vol.2 , pp. 315-319
    • Masters, J.R.1
  • 27
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., Washburn, M. P., and Yates, J. R., III (2001) An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73, 5683-5690
    • (2001) Anal. Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 28
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392
    • (2002) Anal. Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 29
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658
    • (2003) Anal. Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 30
    • 0023803163 scopus 로고
    • Oncodevelopmental expression and structure of alkaline phosphatase genes
    • Millan, J. L. (1988) Oncodevelopmental expression and structure of alkaline phosphatase genes. Anticancer Res. 8, 995-1004
    • (1988) Anticancer Res , vol.8 , pp. 995-1004
    • Millan, J.L.1
  • 31
    • 1242338794 scopus 로고    scopus 로고
    • Emmprin promotes anchorage-independent growth in human mammary carcinoma cells by stimulating hyaluronan production
    • Marieb, E. A., Zoltan-Jones, A., Li, R., Misra, S., Ghatak, S., Cao, J., Zucker, S., and Toole, B. P. (2004) Emmprin promotes anchorage-independent growth in human mammary carcinoma cells by stimulating hyaluronan production. Cancer Res. 64, 1229-1232
    • (2004) Cancer Res , vol.64 , pp. 1229-1232
    • Marieb, E.A.1    Zoltan-Jones, A.2    Li, R.3    Misra, S.4    Ghatak, S.5    Cao, J.6    Zucker, S.7    Toole, B.P.8
  • 32
    • 33750619371 scopus 로고    scopus 로고
    • Identification and validation of mannose 6-phosphate glycoproteins in human plasma reveal a wide range of lysosomal and non-lysosomal proteins
    • Sleat, D. E., Wang, Y., Sohar, I., Lackland, H., Li, Y., Li, H., Zheng, H., and Lobel, P. (2006) Identification and validation of mannose 6-phosphate glycoproteins in human plasma reveal a wide range of lysosomal and non-lysosomal proteins. Mol. Cell. Proteomics 5, 1942-1956
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1942-1956
    • Sleat, D.E.1    Wang, Y.2    Sohar, I.3    Lackland, H.4    Li, Y.5    Li, H.6    Zheng, H.7    Lobel, P.8
  • 34
    • 39749200034 scopus 로고    scopus 로고
    • Imaging and imagination: Understanding the endo-lysosomal system
    • van Meel, E., and Klumperman, J. (2008) Imaging and imagination: understanding the endo-lysosomal system. Histochem. Cell Biol. 129, 253-266
    • (2008) Histochem. Cell Biol , vol.129 , pp. 253-266
    • van Meel, E.1    Klumperman, J.2
  • 35
    • 1842499791 scopus 로고    scopus 로고
    • Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry
    • Schirle, M., Heurtier, M. A., and Kuster, B. (2003) Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry. Mol. Cell. Proteomics 2, 1297-1305
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1297-1305
    • Schirle, M.1    Heurtier, M.A.2    Kuster, B.3
  • 36
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • Ramachandran, P., Boontheung, P., Xie, Y., Sondej, M., Wong, D. T., and Loo, J. A. (2006) Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J. Proteome Res. 5, 1493-1503
    • (2006) J. Proteome Res , vol.5 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4    Wong, D.T.5    Loo, J.A.6
  • 37
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu, T., Qian, W. J., Gritsenko, M. A., Camp, D. G., II, Monroe, M. E., Moore, R. J., and Smith, R. D. (2005) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 4, 2070-2080
    • (2005) J. Proteome Res , vol.4 , pp. 2070-2080
    • Liu, T.1    Qian, W.J.2    Gritsenko, M.A.3    Camp II, D.G.4    Monroe, M.E.5    Moore, R.J.6    Smith, R.D.7
  • 38
    • 33644690335 scopus 로고    scopus 로고
    • Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach
    • Lewandrowski, U., Moebius, J., Walter, U., and Sickmann, A. (2006) Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol. Cell. Proteomics 5, 226-233
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 226-233
    • Lewandrowski, U.1    Moebius, J.2    Walter, U.3    Sickmann, A.4
  • 40
    • 0022366024 scopus 로고
    • Ricin-binding properties of acid hydrolases from isolated lysosomes implies prior processing by terminal transferases of the trans-Golgi apparatus
    • Fedde, K. N., and Sly, W. S. (1985) Ricin-binding properties of acid hydrolases from isolated lysosomes implies prior processing by terminal transferases of the trans-Golgi apparatus. Biochem. Biophys. Res. Commun. 133, 614-620
    • (1985) Biochem. Biophys. Res. Commun , vol.133 , pp. 614-620
    • Fedde, K.N.1    Sly, W.S.2
  • 41
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J., De Hoog, C. L., and Mann, M. (2003) Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. U. S. A. 100, 5813-5818
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 42
    • 27144462628 scopus 로고    scopus 로고
    • Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation
    • Foster, L. J., Zeemann, P. A., Li, C., Mann, M., Jensen, O. N., and Kassem, M. (2005) Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation. Stem Cells 23, 1367-1377
    • (2005) Stem Cells , vol.23 , pp. 1367-1377
    • Foster, L.J.1    Zeemann, P.A.2    Li, C.3    Mann, M.4    Jensen, O.N.5    Kassem, M.6
  • 43
    • 34547222017 scopus 로고    scopus 로고
    • Identification of candidate biomarker proteins released by human endometrial and cervical cancer cells using two-dimensional liquid chromatography/tandem mass spectrometry
    • Li, H., DeSouza, L. V., Ghanny, S., Li, W., Romaschin, A. D., Colgan, T. J., and Siu, K. W. (2007) Identification of candidate biomarker proteins released by human endometrial and cervical cancer cells using two-dimensional liquid chromatography/tandem mass spectrometry. J. Proteome Res. 6, 2615-2622
    • (2007) J. Proteome Res , vol.6 , pp. 2615-2622
    • Li, H.1    DeSouza, L.V.2    Ghanny, S.3    Li, W.4    Romaschin, A.D.5    Colgan, T.J.6    Siu, K.W.7
  • 44
    • 39749125069 scopus 로고    scopus 로고
    • Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis
    • Masuda, T., Tomita, M., and Ishihama, Y. (2008) Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis. J. Proteome Res. 7, 731-740
    • (2008) J. Proteome Res , vol.7 , pp. 731-740
    • Masuda, T.1    Tomita, M.2    Ishihama, Y.3
  • 45
    • 33846488076 scopus 로고    scopus 로고
    • Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics
    • Sun, B., Ranish, J. A., Utleg, A. G., White, J. T., Yan, X., Lin, B., and Hood, L. (2007) Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics. Mol. Cell. Proteomics 6, 141-149
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 141-149
    • Sun, B.1    Ranish, J.A.2    Utleg, A.G.3    White, J.T.4    Yan, X.5    Lin, B.6    Hood, L.7
  • 46
    • 33645795446 scopus 로고    scopus 로고
    • Modification-specific proteomics of plasma membrane proteins: Identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment
    • Elortza, F., Mohammed, S., Bunkenborg, J., Foster, L. J., Nuhse, T. S., Brodbeck, U., Peck, S. C., and Jensen, O. N. (2006) Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J. Proteome Res. 5, 935-943
    • (2006) J. Proteome Res , vol.5 , pp. 935-943
    • Elortza, F.1    Mohammed, S.2    Bunkenborg, J.3    Foster, L.J.4    Nuhse, T.S.5    Brodbeck, U.6    Peck, S.C.7    Jensen, O.N.8
  • 47
    • 32044432615 scopus 로고    scopus 로고
    • Membrane complement regulatory proteins
    • Kim, D. D., and Song, W. C. (2006) Membrane complement regulatory proteins. Clin. Immunol. 118, 127-136
    • (2006) Clin. Immunol , vol.118 , pp. 127-136
    • Kim, D.D.1    Song, W.C.2
  • 48
    • 0242456170 scopus 로고    scopus 로고
    • Axis of evil: Molecular mechanisms of cancer metastasis
    • Bogenrieder, T., and Herlyn, M. (2002) Axis of evil: molecular mechanisms of cancer metastasis. Oncogene 22, 6524-6536
    • (2002) Oncogene , vol.22 , pp. 6524-6536
    • Bogenrieder, T.1    Herlyn, M.2
  • 49
    • 0036713311 scopus 로고    scopus 로고
    • Specific down-modulation of Notch1 signaling in cervical cancer cells is required for sustained HPV-E6/E7 expression and late steps of malignant transformation
    • Talora, C., Sgroi, D. C., Crum, C. P., and Dotto, G. P. (2002) Specific down-modulation of Notch1 signaling in cervical cancer cells is required for sustained HPV-E6/E7 expression and late steps of malignant transformation. Genes Dev. 16, 2252-2263
    • (2002) Genes Dev , vol.16 , pp. 2252-2263
    • Talora, C.1    Sgroi, D.C.2    Crum, C.P.3    Dotto, G.P.4
  • 50
    • 34247895766 scopus 로고    scopus 로고
    • Presenilin/-secretase-mediated cleavage regulates association of leukocyte-common antigen-related (LAR) receptor tyrosine phosphatase with β-catenin
    • Haapasalo, A., Kim, D. Y., Carey, B. W., Turunen, M. K., Pettingell, W. H., and Kovacs, D. M. (2007) Presenilin/-secretase-mediated cleavage regulates association of leukocyte-common antigen-related (LAR) receptor tyrosine phosphatase with β-catenin. J. Biol. Chem. 282, 9063-9072
    • (2007) J. Biol. Chem , vol.282 , pp. 9063-9072
    • Haapasalo, A.1    Kim, D.Y.2    Carey, B.W.3    Turunen, M.K.4    Pettingell, W.H.5    Kovacs, D.M.6
  • 51
    • 29244477844 scopus 로고    scopus 로고
    • Uhlen, M, Bjorling, E, Agaton, C, Szigyarto, C. A, Amini, B, Andersen, E, Andersson, A. C, Angelidou, P, Asplund, A, Asplund, C, Berglund, L, Bergstrom, K, Brumer, H, Cerjan, D, Ekstrom, M, Elobeid, A, Eriksson, C, Fagerberg, L, Falk, R, Fall, J, Forsberg, M, Bjorklund, M. G, Gumbel, K, Halimi, A, Hallin, I, Hamsten, C, Hansson, M, Hedhammar, M, Hercules, G, Kampf, C, Larsson, K, Lindskog, M, Lodewyckx, W, Lund, J, Lundeberg, J, Magnusson, K, Malm, E, Nilsson, P, Odling, J, Oksvold, P, Olsson, I, Oster, E, Ottosson, J, Paavilainen, L, Persson, A, Rimini, R, Rockberg, J, Runeson, M, Sivertsson, A, Skollermo, A, Steen, J, Stenvall, M, Sterky, F, Stromberg, S, Sundberg, M, Tegel, H, Tourle, S, Wahlund, E, Walden, A, Wan, J, Wernerus, H, Westberg, J, Wester, K, Wrethagen, U, Xu, L. L, Hober, S, and Ponten, F, 2005 A human protein atlas for normal and cancer tissues based on antibody proteomics. Mol. Cell. Proteomics
    • Uhlen, M., Bjorling, E., Agaton, C., Szigyarto, C. A., Amini, B., Andersen, E., Andersson, A. C., Angelidou, P., Asplund, A., Asplund, C., Berglund, L., Bergstrom, K., Brumer, H., Cerjan, D., Ekstrom, M., Elobeid, A., Eriksson, C., Fagerberg, L., Falk, R., Fall, J., Forsberg, M., Bjorklund, M. G., Gumbel, K., Halimi, A., Hallin, I., Hamsten, C., Hansson, M., Hedhammar, M., Hercules, G., Kampf, C., Larsson, K., Lindskog, M., Lodewyckx, W., Lund, J., Lundeberg, J., Magnusson, K., Malm, E., Nilsson, P., Odling, J., Oksvold, P., Olsson, I., Oster, E., Ottosson, J., Paavilainen, L., Persson, A., Rimini, R., Rockberg, J., Runeson, M., Sivertsson, A., Skollermo, A., Steen, J., Stenvall, M., Sterky, F., Stromberg, S., Sundberg, M., Tegel, H., Tourle, S., Wahlund, E., Walden, A., Wan, J., Wernerus, H., Westberg, J., Wester, K., Wrethagen, U., Xu, L. L., Hober, S., and Ponten, F. (2005) A human protein atlas for normal and cancer tissues based on antibody proteomics. Mol. Cell. Proteomics 4, 1920-1932
  • 52
    • 0034861071 scopus 로고    scopus 로고
    • Enhanced 3-O-sulfation of galactose in Asn-linked glycans and Maackia amurensis lectin binding in a new Chinese hamster ovary cell line
    • Bai, X., Brown, J. R., Varki, A., and Esko, J. D. (2001) Enhanced 3-O-sulfation of galactose in Asn-linked glycans and Maackia amurensis lectin binding in a new Chinese hamster ovary cell line. Glycobiology 11, 621-632
    • (2001) Glycobiology , vol.11 , pp. 621-632
    • Bai, X.1    Brown, J.R.2    Varki, A.3    Esko, J.D.4
  • 53
    • 0036534774 scopus 로고    scopus 로고
    • Effects of sialic acid substitutions on recognition by Sambucus nigra agglutinin and Maackia amurensis hemagglutinin
    • Brinkman-Van der Linden, E. C., Sonnenburg, J. L., and Varki, A. (2002) Effects of sialic acid substitutions on recognition by Sambucus nigra agglutinin and Maackia amurensis hemagglutinin. Anal. Biochem. 303, 98-104
    • (2002) Anal. Biochem , vol.303 , pp. 98-104
    • Brinkman-Van der Linden, E.C.1    Sonnenburg, J.L.2    Varki, A.3
  • 54
    • 38949198075 scopus 로고    scopus 로고
    • Genome-wide transcriptional analysis of the human cell cycle identifies genes differentially regulated in normal and cancer cells
    • Bar-Joseph, Z., Siegfried, Z., Brandeis, M., Brors, B., Lu, Y., Eils, R., Dynlacht, B. D., and Simon, I. (2008) Genome-wide transcriptional analysis of the human cell cycle identifies genes differentially regulated in normal and cancer cells. Proc. Natl. Acad. Sci. U. S. A. 105, 955-960
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 955-960
    • Bar-Joseph, Z.1    Siegfried, Z.2    Brandeis, M.3    Brors, B.4    Lu, Y.5    Eils, R.6    Dynlacht, B.D.7    Simon, I.8
  • 55
    • 20844439353 scopus 로고    scopus 로고
    • Global protein shotgun expression profiling of proliferating mcf-7 breast cancer cells
    • Sandhu, C., Connor, M., Kislinger, T., Slingerland, J., and Emili, A. (2005) Global protein shotgun expression profiling of proliferating mcf-7 breast cancer cells. J. Proteome Res. 4, 674-689
    • (2005) J. Proteome Res , vol.4 , pp. 674-689
    • Sandhu, C.1    Connor, M.2    Kislinger, T.3    Slingerland, J.4    Emili, A.5
  • 56
    • 4344668062 scopus 로고    scopus 로고
    • Links between CD147 function, glycosylation, and caveolin-1
    • Tang, W., Chang, S. B., and Hemler, M. E. (2004) Links between CD147 function, glycosylation, and caveolin-1. Mol. Biol. Cell 15, 4043-4050
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4043-4050
    • Tang, W.1    Chang, S.B.2    Hemler, M.E.3
  • 57
    • 0035665602 scopus 로고    scopus 로고
    • Heteromeric amino acid transporters: Biochemistry, genetics, and physiology
    • Chillaron, J., Roca, R., Valencia, A., Zorzano, A., and Palacin, M. (2001) Heteromeric amino acid transporters: biochemistry, genetics, and physiology. Am. J. Physiol. 281, F995-F1018
    • (2001) Am. J. Physiol , vol.281
    • Chillaron, J.1    Roca, R.2    Valencia, A.3    Zorzano, A.4    Palacin, M.5
  • 58
    • 0034142172 scopus 로고    scopus 로고
    • Surface antigen CD98(4F2): Not a single membrane protein, but a family of proteins with multiple functions
    • Deves, R., and Boyd, C. A. (2000) Surface antigen CD98(4F2): not a single membrane protein, but a family of proteins with multiple functions. J. Membr. Biol. 173, 165-177
    • (2000) J. Membr. Biol , vol.173 , pp. 165-177
    • Deves, R.1    Boyd, C.A.2
  • 59
    • 3042777493 scopus 로고    scopus 로고
    • β1 integrins show specific association with CD98 protein in low density membranes
    • Kolesnikova, T. V., Mannion, B. A., Berditchevski, F., and Hemler, M. E. (2001) β1 integrins show specific association with CD98 protein in low density membranes. BMC Biochem. 2, 10
    • (2001) BMC Biochem , vol.2 , pp. 10
    • Kolesnikova, T.V.1    Mannion, B.A.2    Berditchevski, F.3    Hemler, M.E.4
  • 60
    • 0035914363 scopus 로고    scopus 로고
    • CD98-mediated links between amino acid transport and β1 integrin distribution in polarized columnar epithelia
    • Merlin, D., Sitaraman, S., Liu, X., Eastburn, K., Sun, J., Kucharzik, T., Lewis, B., and Madara, J. L. (2001) CD98-mediated links between amino acid transport and β1 integrin distribution in polarized columnar epithelia. J. Biol. Chem. 276, 39282-39289
    • (2001) J. Biol. Chem , vol.276 , pp. 39282-39289
    • Merlin, D.1    Sitaraman, S.2    Liu, X.3    Eastburn, K.4    Sun, J.5    Kucharzik, T.6    Lewis, B.7    Madara, J.L.8
  • 61
    • 24044511771 scopus 로고    scopus 로고
    • Metabolic activation-related CD147-CD98 complex
    • Xu, D., and Hemler, M. E. (2005) Metabolic activation-related CD147-CD98 complex. Mol. Cell. Proteomics 4, 1061-1071
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1061-1071
    • Xu, D.1    Hemler, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.