메뉴 건너뛰기




Volumn 12, Issue 4-5, 2012, Pages 621-637

Affinity-based proteomic profiling: Problems and achievements

Author keywords

Affinity chromatography; Affinity ligands; Cell biology; Chemical proteomics; Pharmacoproteomics; Subproteome isolation

Indexed keywords

CONCANAVALIN A; CYCLIC AMP; CYCLIC GMP; GLYCOPROTEIN; HYDROXYAPATITE; ISATIN; PHOSPHOPROTEIN; PROTEIN KINASE; UBIQUITIN; UBIQUITINATED PROTEIN; WHEAT GERM AGGLUTININ;

EID: 84859219643     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100373     Document Type: Review
Times cited : (38)

References (182)
  • 1
    • 0035895796 scopus 로고    scopus 로고
    • Advances in sample preparation in electromigration, chromatographic and mass spectrometric separation methods
    • Gilar, M., Bouvier, E. S., Compton, B. J., Advances in sample preparation in electromigration, chromatographic and mass spectrometric separation methods. J. Chromatogr. A 2001, 909, 111-135.
    • (2001) J. Chromatogr. A , vol.909 , pp. 111-135
    • Gilar, M.1    Bouvier, E.S.2    Compton, B.J.3
  • 2
    • 0344494027 scopus 로고    scopus 로고
    • Applications of affinity chromatography in proteomics
    • Lee, W. C., Lee, K. H., Applications of affinity chromatography in proteomics. Anal. Biochem. 2004, 324, 1-10.
    • (2004) Anal. Biochem. , vol.324 , pp. 1-10
    • Lee, W.C.1    Lee, K.H.2
  • 3
    • 63049092393 scopus 로고    scopus 로고
    • Affinity prefractionation for MS-based plasma proteomics
    • Pernemalm, M., Lewensohn, R., Lehtio, J., Affinity prefractionation for MS-based plasma proteomics. Proteomics 2009, 9, 1420-1427.
    • (2009) Proteomics , vol.9 , pp. 1420-1427
    • Pernemalm, M.1    Lewensohn, R.2    Lehtio, J.3
  • 4
    • 79551474552 scopus 로고    scopus 로고
    • Protein and peptide fractionation, enrichment and depletion: Tools for the complex proteome
    • Ly, L., Wasinger, V. C., Protein and peptide fractionation, enrichment and depletion: Tools for the complex proteome. Proteomics. 2011, 11, 513-534.
    • (2011) Proteomics. , vol.11 , pp. 513-534
    • Ly, L.1    Wasinger, V.C.2
  • 5
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M. et al., A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 1999, 17, 1030-1032.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4
  • 6
    • 34147217542 scopus 로고    scopus 로고
    • Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map
    • Collins, S. R., Miller, K. M., Maas, N. L., Roguev, A. et al., Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 2007, 446, 806-810.
    • (2007) Nature , vol.446 , pp. 806-810
    • Collins, S.R.1    Miller, K.M.2    Maas, N.L.3    Roguev, A.4
  • 7
    • 43249107694 scopus 로고    scopus 로고
    • Affinity as a tool in life science
    • Uhlén, M., Affinity as a tool in life science. Biotechniques 2008, 44, 649-654.
    • (2008) Biotechniques , vol.44 , pp. 649-654
    • Uhlén, M.1
  • 8
    • 0023280871 scopus 로고
    • Production of factor VIII deficient plasma by immunodepletion using three monoclonal antibodies
    • Takase, T., Rotblat, F., Goodall, A. H., Kernoff, P. B. et al., Production of factor VIII deficient plasma by immunodepletion using three monoclonal antibodies. Br. J. Haematol. 1987, 66, 497-502.
    • (1987) Br. J. Haematol. , vol.66 , pp. 497-502
    • Takase, T.1    Rotblat, F.2    Goodall, A.H.3    Kernoff, P.B.4
  • 9
    • 0037387175 scopus 로고    scopus 로고
    • Multi-component immunoaffinity subtraction chromatography: an innovative step towards a comprehensive survey of the human plasma proteome
    • Pieper, R., Su, Q., Gatlin, C. L., Huang, S. T. et al., Multi-component immunoaffinity subtraction chromatography: an innovative step towards a comprehensive survey of the human plasma proteome. Proteomics 2003, 3, 422-432.
    • (2003) Proteomics , vol.3 , pp. 422-432
    • Pieper, R.1    Su, Q.2    Gatlin, C.L.3    Huang, S.T.4
  • 10
    • 78651426390 scopus 로고    scopus 로고
    • Immunodepletion of high-abundant proteins from acute and chronic wound fluids to elucidate low-abundant regulators in wound healing
    • Steinsträßer, L., Jacobsen, F., Hirsch, T., Kesting, M. et al., Immunodepletion of high-abundant proteins from acute and chronic wound fluids to elucidate low-abundant regulators in wound healing. BMC Res. Notes 2010, 3, 335.
    • (2010) BMC Res. Notes , vol.3 , pp. 335
    • Steinsträßer, L.1    Jacobsen, F.2    Hirsch, T.3    Kesting, M.4
  • 11
    • 77950646738 scopus 로고    scopus 로고
    • Comparison of protein enrichment strategies for proteome analysis of plasma
    • Bandow, J. E., Comparison of protein enrichment strategies for proteome analysis of plasma. Proteomics 2010, 10, 1416-1425.
    • (2010) Proteomics , vol.10 , pp. 1416-1425
    • Bandow, J.E.1
  • 12
    • 33745090847 scopus 로고    scopus 로고
    • Depletion efficiency and recovery of trace markers from a multiparameter immunodepletion column
    • Brand, J., Haslberger, T., Zolg, W., Pestlin, G., Palme, S., Depletion efficiency and recovery of trace markers from a multiparameter immunodepletion column. Proteomics 2006, 6, 3236-3242.
    • (2006) Proteomics , vol.6 , pp. 3236-3242
    • Brand, J.1    Haslberger, T.2    Zolg, W.3    Pestlin, G.4    Palme, S.5
  • 13
    • 23944524368 scopus 로고    scopus 로고
    • Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma
    • Echan, L. A., Tang, H. Y., Ali-Khan, N., Lee, K., Speicher, D.W., Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma. Proteomics 2005, 5, 3292-3303.
    • (2005) Proteomics , vol.5 , pp. 3292-3303
    • Echan, L.A.1    Tang, H.Y.2    Ali-Khan, N.3    Lee, K.4    Speicher, D.W.5
  • 14
    • 26844561626 scopus 로고    scopus 로고
    • Effect of immunoaffinity depletion of human serum during proteomic investigations
    • Yocum, A. K., Yu, K., Oe, T., Blair, I. A., Effect of immunoaffinity depletion of human serum during proteomic investigations. J. Proteome Res. 2005, 4, 1722-1731.
    • (2005) J. Proteome Res. , vol.4 , pp. 1722-1731
    • Yocum, A.K.1    Yu, K.2    Oe, T.3    Blair, I.A.4
  • 15
    • 23944475619 scopus 로고    scopus 로고
    • Differences among techniques for high-abundant protein depletion
    • Zolotarjova, N., Martosella, J., Nicol, G., Bailey, J. et al., Differences among techniques for high-abundant protein depletion. Proteomics 2005, 5, 3304-3313.
    • (2005) Proteomics , vol.5 , pp. 3304-3313
    • Zolotarjova, N.1    Martosella, J.2    Nicol, G.3    Bailey, J.4
  • 16
    • 33744996070 scopus 로고    scopus 로고
    • Different immunoaffinity fractionation strategies to characterize the human plasma proteome
    • Gong, Y., Li, X., Yang, B., Ying, W. et al., Different immunoaffinity fractionation strategies to characterize the human plasma proteome. J. Proteome Res. 2006, 5, 1379-1387.
    • (2006) J. Proteome Res. , vol.5 , pp. 1379-1387
    • Gong, Y.1    Li, X.2    Yang, B.3    Ying, W.4
  • 17
    • 47249106993 scopus 로고    scopus 로고
    • Biomarker discovery for kidney diseases by mass spectrometry
    • Niwa, T., Biomarker discovery for kidney diseases by mass spectrometry. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2008, 870, 148-153.
    • (2008) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.870 , pp. 148-153
    • Niwa, T.1
  • 18
    • 26844512938 scopus 로고    scopus 로고
    • Characterization of proteins in human pancreatic cancer serum using differential gel electrophoresis and tandem mass spectrometry
    • Yu, K. H., Rustgi, A. K., Blair, I. A., Characterization of proteins in human pancreatic cancer serum using differential gel electrophoresis and tandem mass spectrometry. J. Proteome Res. 2005, 4, 1742-1751.
    • (2005) J. Proteome Res. , vol.4 , pp. 1742-1751
    • Yu, K.H.1    Rustgi, A.K.2    Blair, I.A.3
  • 19
    • 26844575524 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatographic prefractionation of immunodepleted human serum proteins to enhance mass spectrometry identification of lower-abundant proteins
    • Martosella, J., Zolotarjova, N., Liu, H., Nicol, G., Boyes, B. E., Reversed-phase high-performance liquid chromatographic prefractionation of immunodepleted human serum proteins to enhance mass spectrometry identification of lower-abundant proteins. J. Proteome Res. 2005, 4, 1522-1537.
    • (2005) J. Proteome Res. , vol.4 , pp. 1522-1537
    • Martosella, J.1    Zolotarjova, N.2    Liu, H.3    Nicol, G.4    Boyes, B.E.5
  • 20
    • 78649901550 scopus 로고    scopus 로고
    • Tandem affinity depletion: a combination of affinity fractionation and immunoaffinity depletion allows the detection of low-abundance components in the complex proteomes of body fluids
    • Mortezai, N., Harder, S., Schnabel, C., Moors, E. et al., Tandem affinity depletion: a combination of affinity fractionation and immunoaffinity depletion allows the detection of low-abundance components in the complex proteomes of body fluids. J. Proteome Res. 2010, 9, 6126-6134.
    • (2010) J. Proteome Res. , vol.9 , pp. 6126-6134
    • Mortezai, N.1    Harder, S.2    Schnabel, C.3    Moors, E.4
  • 21
    • 33750728385 scopus 로고    scopus 로고
    • Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications
    • Qian, W. J., Jacobs, J. M., Liu, T., Camp, D. G., 2nd, Smith, R. D., Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications. Mol. Cell. Proteomics 2006, 5, 1727-1744.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1727-1744
    • Qian, W.J.1    Jacobs, J.M.2    Liu, T.3    Camp II, D.G.4    Smith, R.D.5
  • 22
    • 65249123492 scopus 로고    scopus 로고
    • Liquid-phase-based separation systems for depletion, prefractionation and enrichment of proteins in biological fluids for in-depth proteomics analysis
    • Jmeian, Y., El Rassi, Z., Liquid-phase-based separation systems for depletion, prefractionation and enrichment of proteins in biological fluids for in-depth proteomics analysis. Electrophoresis 2009, 30, 249-261.
    • (2009) Electrophoresis , vol.30 , pp. 249-261
    • Jmeian, Y.1    El Rassi, Z.2
  • 23
    • 63049092393 scopus 로고    scopus 로고
    • Affinity prefractionation for MS-based plasma proteomics
    • Pernemalm, M., Lewensohn, R., Lehtiö, J., Affinity prefractionation for MS-based plasma proteomics. Proteomics 2009, 9, 1420-1427.
    • (2009) Proteomics , vol.9 , pp. 1420-1427
    • Pernemalm, M.1    Lewensohn, R.2    Lehtiö, J.3
  • 24
    • 33745054119 scopus 로고    scopus 로고
    • Analysis of the cGMP/cAMP interactome using a chemical proteomics approach in mammalian heart tissue validates sphingosine kinase type 1-interacting protein as a genuine and highly abundant AKAP
    • Scholten, A., Poh, M. K., van Veen, T. A., van Breukelen, B. et al., Analysis of the cGMP/cAMP interactome using a chemical proteomics approach in mammalian heart tissue validates sphingosine kinase type 1-interacting protein as a genuine and highly abundant AKAP. J. Proteome Res. 2006, 5, 1435-1447.
    • (2006) J. Proteome Res. , vol.5 , pp. 1435-1447
    • Scholten, A.1    Poh, M.K.2    van Veen, T.A.3    van Breukelen, B.4
  • 25
    • 67449105851 scopus 로고    scopus 로고
    • Selectivity in enrichment of cAMP-dependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins
    • Aye, T. T., Mohammed, Sh., van den Toorn, H. W. P., van Veen, T. A. B. et al., Selectivity in enrichment of cAMP-dependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins. Mol. Cell. Proteomics 2009, 8, 1016-1028.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1016-1028
    • Aye, T.T.1    Mohammed, S.2    van den Toorn, H.W.P.3    van Veen, T.A.B.4
  • 26
    • 63349102805 scopus 로고    scopus 로고
    • Chemical tools selectively target components of the PKA system
    • DOI: 10.1186/1472-6769-9-3.
    • Bertinetti, D., Schweinsberg, S., Hanke, S. E., Schwede, F. et al., Chemical tools selectively target components of the PKA system. BMC Chem. Biol. 2009, 9, 3. DOI: 10.1186/1472-6769-9-3.
    • (2009) BMC Chem. Biol. , vol.9 , pp. 3
    • Bertinetti, D.1    Schweinsberg, S.2    Hanke, S.E.3    Schwede, F.4
  • 27
    • 33748686575 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases: Molecular regulation to clinical use
    • Bender, A. T., Beavo, J. A., Cyclic nucleotide phosphodiesterases: Molecular regulation to clinical use. Pharmacol. Rev. 2006, 58, 488-520.
    • (2006) Pharmacol. Rev. , vol.58 , pp. 488-520
    • Bender, A.T.1    Beavo, J.A.2
  • 28
    • 65349151273 scopus 로고    scopus 로고
    • A chemical proteomics based enrichment technique targeting the interactome of the PDE5 inhibitor PF-4540124w
    • Dadvar, P., O'Flaherty, M., Scholten, A., Rumpel, K., Heck, A. J. R., A chemical proteomics based enrichment technique targeting the interactome of the PDE5 inhibitor PF-4540124w. Mol. BioSyst. 2009, 5, 472-482.
    • (2009) Mol. BioSyst. , vol.5 , pp. 472-482
    • Dadvar, P.1    O'Flaherty, M.2    Scholten, A.3    Rumpel, K.4    Heck, A.J.R.5
  • 29
    • 78349236592 scopus 로고    scopus 로고
    • Target profiling of a small library of phosphodiesterase 5 (PDE5) inhibitors using chemical proteomics
    • Raijmakers, R., Dadvar, P., Pelletier, S., Gouw, J. et al., Target profiling of a small library of phosphodiesterase 5 (PDE5) inhibitors using chemical proteomics. ChemMedChem. 2010, 5, 1927-1936.
    • (2010) ChemMedChem. , vol.5 , pp. 1927-1936
    • Raijmakers, R.1    Dadvar, P.2    Pelletier, S.3    Gouw, J.4
  • 30
    • 19944433530 scopus 로고    scopus 로고
    • Chemical proteomic analysis reveals alternative modes of action for pyrido[2,3-d]pyrimidine kinase inhibitors
    • Wissing, J., Godl, K., Brehmer, D., Blencke, S. et al., Chemical proteomic analysis reveals alternative modes of action for pyrido[2, 3-d]pyrimidine kinase inhibitors. Mol. Cell. Proteomics 2004, 3, 1181-1193.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1181-1193
    • Wissing, J.1    Godl, K.2    Brehmer, D.3    Blencke, S.4
  • 32
    • 9144219693 scopus 로고    scopus 로고
    • An efficient proteomics method to identify the cellular targets of protein kinase inhibitors
    • Godl, K., Wissing, J., Kurtenbach, A., Habenberger, P. et al., An efficient proteomics method to identify the cellular targets of protein kinase inhibitors. Proc. Natl. Acad. Sci. USA 2003, 100, 15434-15439.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15434-15439
    • Godl, K.1    Wissing, J.2    Kurtenbach, A.3    Habenberger, P.4
  • 33
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: an update
    • Bain, J., McLauchlan, H., Elliott, M., Cohen, P., The specificities of protein kinase inhibitors: an update. Biochem. J. 2003, 371, 199-204.
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 34
    • 36549040859 scopus 로고    scopus 로고
    • The selectivity of protein kinase inhibitors: a further update
    • Bain, J., Plater, L., Elliott, M., Shpiro, N. et al., The selectivity of protein kinase inhibitors: a further update. Biochem. J. 2007, 408, 297-315.
    • (2007) Biochem. J. , vol.408 , pp. 297-315
    • Bain, J.1    Plater, L.2    Elliott, M.3    Shpiro, N.4
  • 35
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M., Cohen, P., Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 2000, 351, 95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 37
    • 19944433530 scopus 로고    scopus 로고
    • Chemical proteomic analysis reveals alternative modes of action for pyrido[2,3-d]pyrimidine kinase inhibitors
    • Wissing, J., Godl, K., Brehmer, D., Blencke, S. et al., Chemical proteomic analysis reveals alternative modes of action for pyrido[2, 3-d]pyrimidine kinase inhibitors. Mol. Cell. Proteomics 2004, 3, 1181-1193.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1181-1193
    • Wissing, J.1    Godl, K.2    Brehmer, D.3    Blencke, S.4
  • 38
    • 34147163563 scopus 로고    scopus 로고
    • Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry
    • Wissing, J., Jansch, L., Nimtz, M., Dieterich, G. et al., Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol. Cell. Proteomics 2007, 6, 537-547.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 537-547
    • Wissing, J.1    Jansch, L.2    Nimtz, M.3    Dieterich, G.4
  • 39
    • 27444431599 scopus 로고    scopus 로고
    • Phosphorylation of Numb family proteins. Possible involvement of Ca2+/calmodulin-dependent protein kinases
    • Tokumitsu, H., Hatano, N., Inuzuka, H., Sueyoshi, Y. et al., Phosphorylation of Numb family proteins. Possible involvement of Ca2+/calmodulin-dependent protein kinases. J. Biol. Chem. 2005, 280, 35108-35118.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35108-35118
    • Tokumitsu, H.1    Hatano, N.2    Inuzuka, H.3    Sueyoshi, Y.4
  • 40
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders, J., Sickmann, A., State-of-the-art in phosphoproteomics. Proteomics 2005, 5, 4052-4061.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 41
    • 0037131411 scopus 로고    scopus 로고
    • Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs
    • Zhang, H., Zha, X., Tan, Y., Hornbeck, P.V., Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs. J. Biol. Chem. 2002, 277, 39379-39387.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39379-39387
    • Zhang, H.1    Zha, X.2    Tan, Y.3    Hornbeck, P.V.4
  • 42
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm, T. E., Jensen, O. N., Larsen, M. R., Analytical strategies for phosphoproteomics. Proteomics 2009, 9, 1451-1468.
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 43
    • 0033562834 scopus 로고    scopus 로고
    • Iron(III)-immobilized metal ion affinity chromatography and mass spectrometry for the purification and characterization of synthetic phosphopeptides
    • Li, S., Dass, C., Iron(III)-immobilized metal ion affinity chromatography and mass spectrometry for the purification and characterization of synthetic phosphopeptides. Anal. Biochem. 1999, 270, 9-14.
    • (1999) Anal. Biochem. , vol.270 , pp. 9-14
    • Li, S.1    Dass, C.2
  • 44
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz, M. C., Tempst, P., Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal. Chem. 1999, 71, 2883-2892.
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 45
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nuhse, T. S., Stensballe, A., Jensen, O. N., Peck, S. C., Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 2003, 2, 1234-1243.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 46
    • 34548128405 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses
    • Nuhse, T. S., Bottrill, A. R., Jones, A. M., Peck, S. C., Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses. Plant J. 2007, 51, 931-940.
    • (2007) Plant J. , vol.51 , pp. 931-940
    • Nuhse, T.S.1    Bottrill, A.R.2    Jones, A.M.3    Peck, S.C.4
  • 47
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P. et al., Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol. Cell. Proteomics 2005, 4, 310-327.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 310-327
    • Gruhler, A.1    Olsen, J.V.2    Mohammed, S.3    Mortensen, P.4
  • 48
    • 84862908545 scopus 로고    scopus 로고
    • Stability of metal ion complexes formed with methyl phosphate and hydrogen phosphate
    • Saha, A., Saha, N., Ji, L. N., Zhao, J. et al., Stability of metal ion complexes formed with methyl phosphate and hydrogen phosphate. J. Biol. Inorg. Chem. 1996, 1, 231-238.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 231-238
    • Saha, A.1    Saha, N.2    Ji, L.N.3    Zhao, J.4
  • 49
    • 31644451099 scopus 로고    scopus 로고
    • Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease
    • D'Ambrosio, C., Arena, S., Fulcoli, G., Scheinfeld, M. H. et al., Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease. Mol. Cell. Proteomics 2006, 5, 97-113.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 97-113
    • D'Ambrosio, C.1    Arena, S.2    Fulcoli, G.3    Scheinfeld, M.H.4
  • 50
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • McNulty, D. E., Annan, R. S., Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol. Cell. Proteomics 2008, 7, 971-980.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 51
    • 79953716847 scopus 로고    scopus 로고
    • Large-scale phosphoproteomics analysis of whole saliva reveals a distinct phosphorylation pattern
    • Stone, M. D., Chen, X., McGowan, T., Bandhakavi, S. et al., Large-scale phosphoproteomics analysis of whole saliva reveals a distinct phosphorylation pattern. J. Proteome Res. 2011, 10, 1728-1736.
    • (2011) J. Proteome Res. , vol.10 , pp. 1728-1736
    • Stone, M.D.1    Chen, X.2    McGowan, T.3    Bandhakavi, S.4
  • 52
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J. et al., Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 2002, 20, 301-305.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 301-305
    • Ficarro, S.B.1    McCleland, M.L.2    Stukenberg, P.T.3    Burke, D.J.4
  • 53
    • 78649803436 scopus 로고    scopus 로고
    • Phosphoproteomics profiling of human skin fibroblast cells reveals pathways and proteins affected by low doses of ionizing radiation
    • Yang, F., Waters, K. M., Miller, J. H., Gritsenko, M. A. et al., Phosphoproteomics profiling of human skin fibroblast cells reveals pathways and proteins affected by low doses of ionizing radiation. PLoS One 2010, 5, e14152.
    • (2010) PLoS One , vol.5
    • Yang, F.1    Waters, K.M.2    Miller, J.H.3    Gritsenko, M.A.4
  • 54
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., Jorgensen, T. J., Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 2005, 4, 873-886.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 55
    • 36248934589 scopus 로고    scopus 로고
    • Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques
    • Jensen, S. S., Larsen, M. R., Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques. Rapid Comm. Mass Spectrom. 2007, 21, 3635-3645.
    • (2007) Rapid Comm. Mass Spectrom. , vol.21 , pp. 3635-3645
    • Jensen, S.S.1    Larsen, M.R.2
  • 56
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • Thingholm, T. E., Jorgensen, T. J., Jensen, O. N., Larsen, M. R., Highly selective enrichment of phosphorylated peptides using titanium dioxide. Nat. Protoc. 2006, 1, 1929-1935.
    • (2006) Nat. Protoc. , vol.1 , pp. 1929-1935
    • Thingholm, T.E.1    Jorgensen, T.J.2    Jensen, O.N.3    Larsen, M.R.4
  • 57
    • 53049101603 scopus 로고    scopus 로고
    • TiO(2)-based phosphoproteomic analysis of the plasma membrane and the effects of phosphatase inhibitor treatment
    • Thingholm, T. E., Larsen, M. R., Ingrell, C. R., Kassem, M., Jensen, O. N., TiO(2)-based phosphoproteomic analysis of the plasma membrane and the effects of phosphatase inhibitor treatment. J. Proteome Res. 2008, 7, 3304-3313.
    • (2008) J. Proteome Res. , vol.7 , pp. 3304-3313
    • Thingholm, T.E.1    Larsen, M.R.2    Ingrell, C.R.3    Kassem, M.4    Jensen, O.N.5
  • 58
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller, B., Mueller, L. N., Mueller, M., Domon, B., Aebersold, R., Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 2007, 4, 231-237.
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 59
    • 33847713391 scopus 로고    scopus 로고
    • Phosphoproteins of the chicken eggshell calcified layer
    • Mann, K., Olsen, J. V., Macek, B., Gnad, F., Mann, M., Phosphoproteins of the chicken eggshell calcified layer. Proteomics 2007, 7, 106-115.
    • (2007) Proteomics , vol.7 , pp. 106-115
    • Mann, K.1    Olsen, J.V.2    Macek, B.3    Gnad, F.4    Mann, M.5
  • 60
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H., Horn, D. M., Tang, N., Mathivanan, S., Pandey, A., Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. USA 2007, 104, 2199-2204.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 61
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006, 127, 635-648.
    • (2006) Cell. , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4
  • 63
    • 37249050876 scopus 로고    scopus 로고
    • Quantitative mass spectrometry to investigate epidermal growth factor receptor phosphorylation dynamics
    • Schuchardt, S., Borlak, J., Quantitative mass spectrometry to investigate epidermal growth factor receptor phosphorylation dynamics. Mass Spectrom. Rev. 2008, 27, 51-65.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 51-65
    • Schuchardt, S.1    Borlak, J.2
  • 64
    • 66649127498 scopus 로고    scopus 로고
    • Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks
    • Reiland, S., Messerli, G., Baerenfaller, K., Gerrits, B. et al., Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks. Plant Physiol. 2009, 150, 889-903.
    • (2009) Plant Physiol. , vol.150 , pp. 889-903
    • Reiland, S.1    Messerli, G.2    Baerenfaller, K.3    Gerrits, B.4
  • 65
    • 70349759983 scopus 로고    scopus 로고
    • Isotope-labeling and affinity enrichment of phosphopeptides for proteomic analysis using liquid chromatography-tandem mass spectrometry
    • Kota, U., Chien, K. Y., Goshe, M. B., Isotope-labeling and affinity enrichment of phosphopeptides for proteomic analysis using liquid chromatography-tandem mass spectrometry. Methods Mol Biol. 2009, 564, 303-321.
    • (2009) Methods Mol Biol. , vol.564 , pp. 303-321
    • Kota, U.1    Chien, K.Y.2    Goshe, M.B.3
  • 66
    • 65349130025 scopus 로고    scopus 로고
    • Enrichment and characterization of phosphopeptides by immobilized metal affinity chromatography (IMAC) and mass spectrometry
    • xi.
    • Thingholm, T. E., Jensen, O. N., Enrichment and characterization of phosphopeptides by immobilized metal affinity chromatography (IMAC) and mass spectrometry. Methods Mol Biol. 2009a, 527, 47-56, xi.
    • (2009) Methods Mol Biol. , vol.527 , pp. 47-56
    • Thingholm, T.E.1    Jensen, O.N.2
  • 67
    • 0032765337 scopus 로고    scopus 로고
    • Phosphopeptide analysis by on-line immobilized metal-ion affinity chromatography-capillary electrophoresis-electrospray ionization mass spectrometry
    • Cao, P., Stults, J. T., Phosphopeptide analysis by on-line immobilized metal-ion affinity chromatography-capillary electrophoresis-electrospray ionization mass spectrometry. J. Chromatogr. A 1999, 853, 225-235.
    • (1999) J. Chromatogr. A , vol.853 , pp. 225-235
    • Cao, P.1    Stults, J.T.2
  • 68
    • 36349013239 scopus 로고    scopus 로고
    • Preparation of Fe3O4@ZrO2 core-shell microspheres as affinity probes for selective enrichment and direct determination of phosphopeptides using matrix-assisted laser desorption ionization mass spectrometry
    • Li, Y., Leng, T., Lin, H., Deng, C. et al., Preparation of Fe3O4@ZrO2 core-shell microspheres as affinity probes for selective enrichment and direct determination of phosphopeptides using matrix-assisted laser desorption ionization mass spectrometry. J. Proteome Res. 2007, 6, 4498-4510.
    • (2007) J. Proteome Res. , vol.6 , pp. 4498-4510
    • Li, Y.1    Leng, T.2    Lin, H.3    Deng, C.4
  • 69
    • 34447498653 scopus 로고    scopus 로고
    • Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis
    • Zhou, H., Tian, R., Ye, M., Xu, S. et al., Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis. Electrophoresis 2007, 28, 2201-2215.
    • (2007) Electrophoresis , vol.28 , pp. 2201-2215
    • Zhou, H.1    Tian, R.2    Ye, M.3    Xu, S.4
  • 70
    • 74249098455 scopus 로고    scopus 로고
    • Enrichment and analysis of phosphopeptides under different experimental conditions using titanium dioxide affinity chromatography and mass spectrometry
    • Aryal, U. K., Ross, A. R., Enrichment and analysis of phosphopeptides under different experimental conditions using titanium dioxide affinity chromatography and mass spectrometry. Rapid Commun. Mass Spectrom. 2010, 24, 219-231.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 219-231
    • Aryal, U.K.1    Ross, A.R.2
  • 71
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • Thingholm, T. E., Jensen, O. N., Robinson, P. J., Larsen, M. R., SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides. Mol. Cell. Proteomics 2008a, 7, 661-671.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 661-671
    • Thingholm, T.E.1    Jensen, O.N.2    Robinson, P.J.3    Larsen, M.R.4
  • 72
    • 65349125322 scopus 로고    scopus 로고
    • Enrichment and separation of mono- and multiply phosphorylated peptides using sequential elution from IMAC prior to mass spectrometric analysis
    • Thingholm, T. E., Jensen, O. N., Larsen, M. R., Enrichment and separation of mono- and multiply phosphorylated peptides using sequential elution from IMAC prior to mass spectrometric analysis. Methods Mol. Biol. 2009b, 527, 67-78.
    • (2009) Methods Mol. Biol. , vol.527 , pp. 67-78
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 73
    • 76649129012 scopus 로고    scopus 로고
    • Hydroxyapatite affinity chromatography for the highly selective enrichment of mono- and multi-phosphorylated peptides in phosphoproteome analysis
    • Mamone, G., Picariello, G., Ferranti, P., Addeo, F., Hydroxyapatite affinity chromatography for the highly selective enrichment of mono- and multi-phosphorylated peptides in phosphoproteome analysis. Proteomics 2010, 10, 380-393.
    • (2010) Proteomics , vol.10 , pp. 380-393
    • Mamone, G.1    Picariello, G.2    Ferranti, P.3    Addeo, F.4
  • 74
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate
    • Gronborg, M., Kristiansen, T. Z., Stensballe, A., Andersen, J. S., A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate. Mol. Cell. Proteomics 2002, 1, 517-527.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 517-527
    • Gronborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4
  • 75
    • 34548392335 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation on a proteome-scale
    • Collins, M. O., Yu, L., Choudhary, J. S., Analysis of protein phosphorylation on a proteome-scale. Proteomics 2007, 7, 2751-2768.
    • (2007) Proteomics , vol.7 , pp. 2751-2768
    • Collins, M.O.1    Yu, L.2    Choudhary, J.S.3
  • 76
    • 0037501375 scopus 로고    scopus 로고
    • Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation
    • Ficarro, S., Chertihin, O., Westbrook, V. A., White, F., Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. J. Biol. Chem. 2003, 278, 11579-11589.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11579-11589
    • Ficarro, S.1    Chertihin, O.2    Westbrook, V.A.3    White, F.4
  • 77
    • 21144445429 scopus 로고    scopus 로고
    • Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography
    • Zheng, H., Hu, P., Quinn, D. F., Wang, Y. K., Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography. Mol. Cell. Proteomics 2005, 4, 721-730.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 721-730
    • Zheng, H.1    Hu, P.2    Quinn, D.F.3    Wang, Y.K.4
  • 78
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J., Moritz, A., Lee, K. A., Guo, A., Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 2005, 23, 94-101.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4
  • 79
    • 0037059770 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A., Mann, M., Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J. Biol. Chem. 2002, 277, 1031-1039.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1031-1039
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 80
    • 79960951711 scopus 로고    scopus 로고
    • Use of a tandem affinity purification assay to detect interactions between West Nile and dengue viral proteins and proteins of the mosquito vector
    • Colpitts, T. M., Cox, J., Nguyen, A., Feitosa, F. et al., Use of a tandem affinity purification assay to detect interactions between West Nile and dengue viral proteins and proteins of the mosquito vector. Virology 2011, 417, 179-187.
    • (2011) Virology , vol.417 , pp. 179-187
    • Colpitts, T.M.1    Cox, J.2    Nguyen, A.3    Feitosa, F.4
  • 81
    • 80052790750 scopus 로고    scopus 로고
    • Tandem affinity purification and identification of GPCR-associated protein complexes
    • Daulat, A. M., Maurice, P., Jockers, R., Tandem affinity purification and identification of GPCR-associated protein complexes. Methods Mol Biol. 2011, 746, 399-409.
    • (2011) Methods Mol Biol. , vol.746 , pp. 399-409
    • Daulat, A.M.1    Maurice, P.2    Jockers, R.3
  • 82
    • 80053098274 scopus 로고    scopus 로고
    • Identifying protein complexes by affinity purification and mass spectrometry analysis in the rice blast fungus
    • Liu, W., Iliuk, A., Tao, A., Ding, S., Identifying protein complexes by affinity purification and mass spectrometry analysis in the rice blast fungus. Methods Mol Biol. 2011, 722, 157-166.
    • (2011) Methods Mol Biol. , vol.722 , pp. 157-166
    • Liu, W.1    Iliuk, A.2    Tao, A.3    Ding, S.4
  • 83
    • 61349126317 scopus 로고    scopus 로고
    • Tandem affinity purification of proteins
    • Günzl, A., Schimanski, B., Tandem affinity purification of proteins. Curr. Protoc. Protein Sci. 2009, 55, 19.19.1-19.19.16.
    • (2009) Curr. Protoc. Protein Sci. , vol.55 , pp. 19191-191916
    • Günzl, A.1    Schimanski, B.2
  • 84
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling
    • Angrand, P. O., Segura, I., Völkel, P., Ghidelli, S. et al., Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol. Cell. Proteomics 2006, 5, 2211-2227.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1    Segura, I.2    Völkel, P.3    Ghidelli, S.4
  • 85
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T., Chait, B.T., Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 2001, 19, 379-382.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 86
    • 0036468952 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins
    • Goshe, M. B., Veenstra, T. D., Panisko, E. A., Conrads, T. P. et al., Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins. Anal. Chem. 2002, 74, 607-616.
    • (2002) Anal. Chem. , vol.74 , pp. 607-616
    • Goshe, M.B.1    Veenstra, T.D.2    Panisko, E.A.3    Conrads, T.P.4
  • 87
    • 79960026710 scopus 로고    scopus 로고
    • Tools for phospho- and glycoproteomics of plasma membranes
    • Wisniewski, J. R., Tools for phospho- and glycoproteomics of plasma membranes. Amino Acids 2010, 41, 223-233.
    • (2010) Amino Acids , vol.41 , pp. 223-233
    • Wisniewski, J.R.1
  • 88
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
    • Wells, L., Vosseller, K., Hart, G. W., Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 2001, 291, 2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 89
    • 0028033725 scopus 로고
    • New-type of linkage between a carbohydrate and a protein C-glycosylation of a specific tryptophan residue in human
    • Hofsteenge, J., Muller, D. R., Debeer, T., New-type of linkage between a carbohydrate and a protein C-glycosylation of a specific tryptophan residue in human. RNase Us. Biochemistry 1994, 33, 13524-13530.
    • (1994) RNase Us. Biochemistry , vol.33 , pp. 13524-13530
    • Hofsteenge, J.1    Muller, D.R.2    Debeer, T.3
  • 90
    • 77956014533 scopus 로고    scopus 로고
    • The lectin riddle: glycoproteins fractionated from complex mixtures have similar glycomic profiles
    • Lee, A., Nakano, M., Hincapie, M., Kolarich, D. et al., The lectin riddle: glycoproteins fractionated from complex mixtures have similar glycomic profiles. J. Integr. Biol. 2010, 14, 487-499.
    • (2010) J. Integr. Biol. , vol.14 , pp. 487-499
    • Lee, A.1    Nakano, M.2    Hincapie, M.3    Kolarich, D.4
  • 91
    • 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
  • 92
    • 0034640419 scopus 로고    scopus 로고
    • Binding of multivalent carbohydrates to concanavalin A and Diocleagrandiflora lectin: thermodynamic analysis of the "multivalency effect"
    • Dam, T. K., Roy, R., Das, S. K., Oscarson, S., Brewer, C. F., Binding of multivalent carbohydrates to concanavalin A and Diocleagrandiflora lectin: thermodynamic analysis of the "multivalency effect". J. Biol. Chem. 2000, 275, 14223-14230.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14223-14230
    • Dam, T.K.1    Roy, R.2    Das, S.K.3    Oscarson, S.4    Brewer, C.F.5
  • 93
    • 0016411842 scopus 로고
    • Studies on the combining sites of concanavalin A
    • Goldstein, I. J., Studies on the combining sites of concanavalin A. Adv. Exp. Med. Biol. 1975, 55, 35-53.
    • (1975) Adv. Exp. Med. Biol. , vol.55 , pp. 35-53
    • Goldstein, I.J.1
  • 94
    • 0022899468 scopus 로고
    • Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study
    • Brewer, C. F., Bhattacharyya, L., Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study. J. Biol. Chem. 1986, 261, 7306-7310.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7306-7310
    • Brewer, C.F.1    Bhattacharyya, L.2
  • 95
    • 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
  • 96
    • 0025804302 scopus 로고
    • The amino acid sequences of jacalin and the Maclura pomifera agglutinin
    • Young, N. M., Johnston, R. A., Watson, D.C., The amino acid sequences of jacalin and the Maclura pomifera agglutinin. FEBS Lett. 1991, 282, 382-384.
    • (1991) FEBS Lett. , vol.282 , pp. 382-384
    • Young, N.M.1    Johnston, R.A.2    Watson, D.C.3
  • 97
    • 0037093547 scopus 로고    scopus 로고
    • Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose
    • Bourne, Y., Astoul, C. H., Zamboni, V., Peumans, W. J. et al., Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose. Biochem. J. 2002, 364, 173-180.
    • (2002) Biochem. J. , vol.364 , pp. 173-180
    • Bourne, Y.1    Astoul, C.H.2    Zamboni, V.3    Peumans, W.J.4
  • 99
    • 0032498117 scopus 로고    scopus 로고
    • Jacalin interacts with Asn-linked glycopeptides containing multi-antennary oligosaccharide structure with terminal alpha-linked galactose
    • Do, S. I., Lee, K. Y., Jacalin interacts with Asn-linked glycopeptides containing multi-antennary oligosaccharide structure with terminal alpha-linked galactose. FEBS Lett. 1998, 421, 169-173.
    • (1998) FEBS Lett. , vol.421 , pp. 169-173
    • Do, S.I.1    Lee, K.Y.2
  • 100
    • 0016190847 scopus 로고
    • Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding
    • Nagata, Y., Burger, M. M., Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J. Biol. Chem. 1974, 249, 3116-3122.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3116-3122
    • Nagata, Y.1    Burger, M.M.2
  • 101
    • 59749086716 scopus 로고    scopus 로고
    • Specificity analysis of lectins and antibodies using remodeled glycoproteins
    • Iskratsch, T., Braun, A., Paschinger, K., Wilson, I. B., Specificity analysis of lectins and antibodies using remodeled glycoproteins. Anal. Biochem. 2009, 386, 133-146.
    • (2009) Anal. Biochem. , vol.386 , pp. 133-146
    • Iskratsch, T.1    Braun, A.2    Paschinger, K.3    Wilson, I.B.4
  • 102
    • 33749145859 scopus 로고    scopus 로고
    • Multilectin affinity chromatography for characterization of multiple glycoprotein biomarker candidates in serum from breast cancer patients
    • Yang, Z., Harris, L. E., Palmer-Toy, D. E., Hancock, W. S., Multilectin affinity chromatography for characterization of multiple glycoprotein biomarker candidates in serum from breast cancer patients. Clin. Chem. 2006, 52, 1897-1905.
    • (2006) Clin. Chem. , vol.52 , pp. 1897-1905
    • Yang, Z.1    Harris, L.E.2    Palmer-Toy, D.E.3    Hancock, W.S.4
  • 103
    • 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
  • 104
    • 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
  • 105
    • 39049137589 scopus 로고    scopus 로고
    • 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo
    • Hedlund, M., Ng, E., Varki, A., Varki, N. M., 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo. Cancer Res. 2008, 68, 388-394.
    • (2008) Cancer Res. , vol.68 , pp. 388-394
    • Hedlund, M.1    Ng, E.2    Varki, A.3    Varki, N.M.4
  • 106
    • 0027383298 scopus 로고
    • Cellular sialoglycoconjugates: a histochemical perspective
    • Roth, J., Cellular sialoglycoconjugates: a histochemical perspective. Histochem. J. 1993, 25, 687-710.
    • (1993) Histochem. J. , vol.25 , pp. 687-710
    • Roth, J.1
  • 107
    • 61649103556 scopus 로고    scopus 로고
    • Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome
    • McDonald, C. A., Yang, J. Y., Marathe, V., Yen, T. Y., Macher, B. A., Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome. Mol. Cell. Proteomics 2009, 8, 287-301.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 287-301
    • McDonald, C.A.1    Yang, J.Y.2    Marathe, V.3    Yen, T.Y.4    Macher, B.A.5
  • 108
    • 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 d-2,3 to penultimate galactose residues
    • Wang, W. C., Cummings, R. D., The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complextype Asn-linked oligosaccharides containing terminal sialic acid-linked d-2, 3 to penultimate galactose residues. J. Biol. Chem. 1988, 263, 4576-4585.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 109
    • 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. et al., An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides. J. Biol. Chem. 2000, 275, 17541-17548.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17541-17548
    • Imberty, A.1    Gautier, C.2    Lescar, J.3    Perez, S.4
  • 110
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells, L., Vosseller, K., Cole, R. N., Cronshaw, J. M. et al., Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell. Proteomics 2002, 1, 791-804.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4
  • 111
    • 0035567107 scopus 로고    scopus 로고
    • Identification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry
    • Chalkley, R. J., Burlingame, A. L., Identification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 2001, 12, 1106-1113.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 1106-1113
    • Chalkley, R.J.1    Burlingame, A.L.2
  • 112
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-Glc-NAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry
    • Greis, K. D., Hayes, B. K., Comer, F. I., Kirk, M. et al., Selective detection and site-analysis of O-Glc-NAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry. Anal. Biochem. 1996, 234, 38-49.
    • (1996) Anal. Biochem. , vol.234 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4
  • 113
    • 0034329621 scopus 로고    scopus 로고
    • Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry
    • Haynes, P. A., Aebersold, R., Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry. Anal. Chem. 2000, 72, 5402-5410.
    • (2000) Anal. Chem. , vol.72 , pp. 5402-5410
    • Haynes, P.A.1    Aebersold, R.2
  • 114
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann, M., Ong, S. E., Gronborg, M., Steen, H. et al., Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 2002, 20, 261-268.
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4
  • 115
    • 0036490141 scopus 로고    scopus 로고
    • Mass spectrometry-based methods for phosphorylation site mapping of hyperphosphorylated proteins applied to Net1, a regulator of exit from mitosis in yeast
    • Loughrey Chen, S., Huddleston, M. J., Shou, W., Deshaies, R. J. et al., Mass spectrometry-based methods for phosphorylation site mapping of hyperphosphorylated proteins applied to Net1, a regulator of exit from mitosis in yeast. Mol. Cell. Proteomics 2002, 1, 186-196.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 186-196
    • Loughrey Chen, S.1    Huddleston, M.J.2    Shou, W.3    Deshaies, R.J.4
  • 117
    • 57049177106 scopus 로고    scopus 로고
    • Identification of structural and functional O-linked N-acetylglucosamine-bearing proteins in Xenopus laevis oocyte
    • Dehennaut, V., Slomianny, M. C., Page, A., Vercoutter-Edouart, A. S. et al., Identification of structural and functional O-linked N-acetylglucosamine-bearing proteins in Xenopus laevis oocyte. Mol. Cell. Proteomics 2008, 7, 2229-2245.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2229-2245
    • Dehennaut, V.1    Slomianny, M.C.2    Page, A.3    Vercoutter-Edouart, A.S.4
  • 118
    • 77955981009 scopus 로고    scopus 로고
    • Boronic acid lectin affinity chromatography (BLAC). 3. Temperature dependence of glycoprotein isolation and enrichment
    • Olajos, M., Szekrényes, á., Hajos, P., Gjerde, D. T., Guttman, A., Boronic acid lectin affinity chromatography (BLAC). 3. Temperature dependence of glycoprotein isolation and enrichment. Anal. Bioanal. Chem. 2010, 397, 2401-2407.
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 2401-2407
    • Olajos, M.1    Szekrényes, Á.2    Hajos, P.3    Gjerde, D.T.4    Guttman, A.5
  • 119
    • 36649037780 scopus 로고    scopus 로고
    • Boronic acid-lectin affinity chromatography. 1. Simultaneous glycoprotein binding with selective or combined elution
    • Monzo, A., Bonn, G. K., Guttman, A., Boronic acid-lectin affinity chromatography. 1. Simultaneous glycoprotein binding with selective or combined elution. Anal. Bioanal. Chem. 2007, 389, 2097-2102.
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 2097-2102
    • Monzo, A.1    Bonn, G.K.2    Guttman, A.3
  • 120
    • 58149134069 scopus 로고    scopus 로고
    • Improved methods for the enrichment and analysis of glycated peptides
    • Zhang, Q., Schepmoes, A. A., Brock, J. W. C., Wu, S. et al., Improved methods for the enrichment and analysis of glycated peptides. Anal. Chem. 2008, 24, 9822-9829.
    • (2008) Anal. Chem. , vol.24 , pp. 9822-9829
    • Zhang, Q.1    Schepmoes, A.A.2    Brock, J.W.C.3    Wu, S.4
  • 121
    • 75849121168 scopus 로고    scopus 로고
    • Synthesis and carbohydrate binding studies of fluorescent α-amidoboronic acids and the corresponding bisboronic acids
    • Jin, S., Zhu, C., Cheng, Y., Li, M., Wang, B., Synthesis and carbohydrate binding studies of fluorescent α-amidoboronic acids and the corresponding bisboronic acids. Bioorg. Med. Chem. 2010a, 4, 1449-1455.
    • (2010) Bioorg. Med. Chem. , vol.4 , pp. 1449-1455
    • Jin, S.1    Zhu, C.2    Cheng, Y.3    Li, M.4    Wang, B.5
  • 122
    • 24144443786 scopus 로고    scopus 로고
    • Boronolectins and fluorescent boronolectins: an examination of the detailed chemistry issues important for the design
    • Yan, J., Fang, H., Wang, B., Boronolectins and fluorescent boronolectins: an examination of the detailed chemistry issues important for the design. Med. Res. Rev. 2005, 5, 490-520.
    • (2005) Med. Res. Rev. , vol.5 , pp. 490-520
    • Yan, J.1    Fang, H.2    Wang, B.3
  • 123
    • 4344582978 scopus 로고    scopus 로고
    • Fluorescent chemosensors for carbohydrates: a decade's worth of bright spies for saccharides in review
    • Cao, H., Heagy, M. D., Fluorescent chemosensors for carbohydrates: a decade's worth of bright spies for saccharides in review. J. Fluoresc. 2004, 5, 569-584.
    • (2004) J. Fluoresc. , vol.5 , pp. 569-584
    • Cao, H.1    Heagy, M.D.2
  • 124
    • 61349150697 scopus 로고    scopus 로고
    • Identification of the First fluorescent α-amidoboronic acids that change fluorescent properties upon sugar binding
    • Jin, S., Zhu, C., Li, M., Wang, B., Identification of the First fluorescent α-amidoboronic acids that change fluorescent properties upon sugar binding. Bioorg. Med. Chem. Lett. 2009, 6, 1596-1599.
    • (2009) Bioorg. Med. Chem. Lett. , vol.6 , pp. 1596-1599
    • Jin, S.1    Zhu, C.2    Li, M.3    Wang, B.4
  • 125
    • 0025891612 scopus 로고
    • New ligands for boronate affinity chromatography: synthesis and properties
    • Singhal, R. P., Ramamurthy, B., Govindraj, N., Sarwar, Y., New ligands for boronate affinity chromatography: synthesis and properties. J. Chromatogr. 1991, 543, 17-38.
    • (1991) J. Chromatogr. , vol.543 , pp. 17-38
    • Singhal, R.P.1    Ramamurthy, B.2    Govindraj, N.3    Sarwar, Y.4
  • 126
    • 0033525458 scopus 로고    scopus 로고
    • Selective fructose transport through supported liquid membranes containing diboronic acid or conjugated monoboronic acid-quaternary ammonium carriers
    • Gardiner, S. J., Smith, B. D., Duggan, P. J., Karpa, M. J., Griffin, G. J., Selective fructose transport through supported liquid membranes containing diboronic acid or conjugated monoboronic acid-quaternary ammonium carriers. Tetrahedron 1999, 55, 2857-2864.
    • (1999) Tetrahedron , vol.55 , pp. 2857-2864
    • Gardiner, S.J.1    Smith, B.D.2    Duggan, P.J.3    Karpa, M.J.4    Griffin, G.J.5
  • 127
    • 0002014775 scopus 로고    scopus 로고
    • Functional group compatibilities in boronic ester chemistry
    • Matteson, D. S., Functional group compatibilities in boronic ester chemistry. J. Organomet. Chem. 1999, 581, 51-65.
    • (1999) J. Organomet. Chem. , vol.581 , pp. 51-65
    • Matteson, D.S.1
  • 128
    • 36048977494 scopus 로고    scopus 로고
    • Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection
    • Sparbier, K., Asperger, A., Resemann, A., Kessler, I. et al., Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection. J. Biomol. Tech. 2007, 18, 252-258.
    • (2007) J. Biomol. Tech. , vol.18 , pp. 252-258
    • Sparbier, K.1    Asperger, A.2    Resemann, A.3    Kessler, I.4
  • 129
    • 33645748520 scopus 로고    scopus 로고
    • Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles
    • Sparbier, K., Koch, S., Kessler, I., Wenzel, T., Kostrzewa, M., Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles. J. Biomol. Techn. 2005, 16, 407-413.
    • (2005) J. Biomol. Techn. , vol.16 , pp. 407-413
    • Sparbier, K.1    Koch, S.2    Kessler, I.3    Wenzel, T.4    Kostrzewa, M.5
  • 130
    • 11144328866 scopus 로고    scopus 로고
    • Validation by a mass spectrometric reference method of use of boronate affinity chromatography to measure glycohemoglobin in the presence of hemoglobin S and C Traits
    • Little, R. R., Vesper, H., Rohlfing, C. L., Ospina, M. et al., Validation by a mass spectrometric reference method of use of boronate affinity chromatography to measure glycohemoglobin in the presence of hemoglobin S and C Traits. Clin. Chem. 2005, 51, 264-265.
    • (2005) Clin. Chem. , vol.51 , pp. 264-265
    • Little, R.R.1    Vesper, H.2    Rohlfing, C.L.3    Ospina, M.4
  • 131
    • 77649169235 scopus 로고    scopus 로고
    • Glycation isotopic labeling with 13C-reducing sugars for quantitative analysis of glycated proteins in human plasma
    • Priego-Capote, F., Scherl, A., Müller, M., Waridel, P. et al., Glycation isotopic labeling with 13C-reducing sugars for quantitative analysis of glycated proteins in human plasma. Mol. Cell. Proteomics 2010, 3, 579-592.
    • (2010) Mol. Cell. Proteomics , vol.3 , pp. 579-592
    • Priego-Capote, F.1    Scherl, A.2    Müller, M.3    Waridel, P.4
  • 132
    • 70449732843 scopus 로고    scopus 로고
    • Characterization of anti-advanced glycation end product antibodies to nonenzymatically lysine-derived and arginine-derived glycated products
    • Choi, Y. G., Lim, S., Characterization of anti-advanced glycation end product antibodies to nonenzymatically lysine-derived and arginine-derived glycated products. J. Immunoassay Immonochem. 2009, 4, 386-399.
    • (2009) J. Immunoassay Immonochem. , vol.4 , pp. 386-399
    • Choi, Y.G.1    Lim, S.2
  • 134
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology
    • Schwartz, A. L., Ciechanover, A., Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu. Rev. Pharmacol. Toxicol. 2009, 49, 73-96.
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 136
    • 42049091467 scopus 로고    scopus 로고
    • Evaluation of proteomic strategies for analyzing ubiquitinated proteins
    • Peng, J., Evaluation of proteomic strategies for analyzing ubiquitinated proteins. BMB Rep. 2008, 41, 177-183.
    • (2008) BMB Rep. , vol.41 , pp. 177-183
    • Peng, J.1
  • 137
    • 25144443718 scopus 로고    scopus 로고
    • The ubiquitin system for protein degradation and some of its roles in the control of the cell-division cycle (Nobel lecture)
    • Hershko, A., The ubiquitin system for protein degradation and some of its roles in the control of the cell-division cycle (Nobel lecture). Angew. Chem. Int. Ed. Engl. 2005, 44, 5932-5943.
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 5932-5943
    • Hershko, A.1
  • 139
    • 34247342702 scopus 로고    scopus 로고
    • Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants
    • Maor, R., Jones, A., Nühse, T. S., Studholme, D. J. et al., Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants. Mol. Cell. Proteomics 2007, 6, 601-610.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 601-610
    • Maor, R.1    Jones, A.2    Nühse, T.S.3    Studholme, D.J.4
  • 140
    • 23144452492 scopus 로고    scopus 로고
    • Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics
    • Kirkpatrick, D. S., Denison, C., Gygi, S. P., Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics. Nat. Cell. Biol. 2005, 7, 750-757.
    • (2005) Nat. Cell. Biol. , vol.7 , pp. 750-757
    • Kirkpatrick, D.S.1    Denison, C.2    Gygi, S.P.3
  • 141
    • 0242300110 scopus 로고    scopus 로고
    • A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery
    • Hitchcock, A. L., Auld, K., Gygi, S. P., Silver, P. A., A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl. Acad. Sci. USA 2003, 100, 12735-12740.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12735-12740
    • Hitchcock, A.L.1    Auld, K.2    Gygi, S.P.3    Silver, P.A.4
  • 142
    • 34247528121 scopus 로고    scopus 로고
    • A proteomics approach to identify the ubiquitinated proteins in mouse heart
    • Jeon, H. B., Choi, E. S., Yoon, J. H., Hwang, J. H. et al., A proteomics approach to identify the ubiquitinated proteins in mouse heart. Biochem. Biophys. Res. Commun. 2007, 357, 731-736.
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 731-736
    • Jeon, H.B.1    Choi, E.S.2    Yoon, J.H.3    Hwang, J.H.4
  • 143
    • 0035380584 scopus 로고    scopus 로고
    • Purification of poly-ubiquitinated proteins by S5a-affinity chromatography
    • Layfield, R., Tooth, D., Landon, M., Dawson, S. et al., Purification of poly-ubiquitinated proteins by S5a-affinity chromatography. Proteomics 2001, 1, 773-777.
    • (2001) Proteomics , vol.1 , pp. 773-777
    • Layfield, R.1    Tooth, D.2    Landon, M.3    Dawson, S.4
  • 144
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    • Hiyama, H., Yokoi, M., Masutani, C., Sugasawa, K. et al., Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. J. Biol. Chem. 1999, 274, 28019-28025.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28019-28025
    • Hiyama, H.1    Yokoi, M.2    Masutani, C.3    Sugasawa, K.4
  • 145
    • 67649823451 scopus 로고    scopus 로고
    • The ubiquitin-interacting motif protein, S5a, is ubiquitinated by all types of ubiquitin ligases by a mechanism different from typical substrate recognition
    • Uchiki, T., Kim, H. T., Zhai, B., Gygi, S. P. et al., The ubiquitin-interacting motif protein, S5a, is ubiquitinated by all types of ubiquitin ligases by a mechanism different from typical substrate recognition. J. Biol. Chem. 2009, 284, 12622-12632.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12622-12632
    • Uchiki, T.1    Kim, H.T.2    Zhai, B.3    Gygi, S.P.4
  • 146
    • 42649095634 scopus 로고    scopus 로고
    • A protocol for immunoaffinity separation of the accumulated ubiquitin-protein conjugates solubilized with sodium dodecyl sulfate
    • Shimada, Y., Fukuda, T., Aoki, K., Yukawa, T. et al., A protocol for immunoaffinity separation of the accumulated ubiquitin-protein conjugates solubilized with sodium dodecyl sulfate. Anal. Biochem. 2008, 377, 77-82.
    • (2008) Anal. Biochem. , vol.377 , pp. 77-82
    • Shimada, Y.1    Fukuda, T.2    Aoki, K.3    Yukawa, T.4
  • 147
    • 48949106092 scopus 로고    scopus 로고
    • Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells
    • Tan, F., Lu, L., Cai, Y., Wang, J. et al., Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells. Proteomics 2008, 8, 2885-2896.
    • (2008) Proteomics , vol.8 , pp. 2885-2896
    • Tan, F.1    Lu, L.2    Cai, Y.3    Wang, J.4
  • 148
    • 70449084692 scopus 로고    scopus 로고
    • Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities
    • Hjerpe, R., Aillet, F., Lopitz-Otsoa, F., Lang, V. et al., Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. EMBO Rep. 2009, 10, 1250-1258.
    • (2009) EMBO Rep. , vol.10 , pp. 1250-1258
    • Hjerpe, R.1    Aillet, F.2    Lopitz-Otsoa, F.3    Lang, V.4
  • 149
    • 0037472654 scopus 로고    scopus 로고
    • Ubiquitin binding proteins protect ubiquitin conjugates from disassembly
    • Hartmann-Petersen, R., Hendil, K. B., Gordon, C., Ubiquitin binding proteins protect ubiquitin conjugates from disassembly. FEBS Lett. 2003, 535, 77-81.
    • (2003) FEBS Lett. , vol.535 , pp. 77-81
    • Hartmann-Petersen, R.1    Hendil, K.B.2    Gordon, C.3
  • 150
    • 21044460108 scopus 로고    scopus 로고
    • Two-step affinity purification of multiubiquitylated proteins from Saccharomyces cerevisiae
    • Mayor, T., Deshaies, R. J., Two-step affinity purification of multiubiquitylated proteins from Saccharomyces cerevisiae. Methods Enzymol. 2005, 399, 385-392.
    • (2005) Methods Enzymol. , vol.399 , pp. 385-392
    • Mayor, T.1    Deshaies, R.J.2
  • 151
    • 0033814819 scopus 로고    scopus 로고
    • Purification of proteins using polyhistidine affinity tags
    • Bornhorst, J. A., Falke, J. J., Purification of proteins using polyhistidine affinity tags. Methods Enzymol. 2000, 326, 245-254.
    • (2000) Methods Enzymol. , vol.326 , pp. 245-254
    • Bornhorst, J.A.1    Falke, J.J.2
  • 152
    • 79955780605 scopus 로고    scopus 로고
    • A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development
    • 10, M110.002188.
    • Franco, M., Seyfried, N. T., Brand, A. H., Peng, J., Mayor, U., A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development. Mol. Cell. Proteomics 2011, 10, M110.002188.
    • (2011) Mol. Cell. Proteomics
    • Franco, M.1    Seyfried, N.T.2    Brand, A.H.3    Peng, J.4    Mayor, U.5
  • 153
    • 0038811689 scopus 로고    scopus 로고
    • The biotin enzyme family: Conserved structural motifs and domain rearrangements
    • Jitrapakdee, S., Wallace, J. C., The biotin enzyme family: Conserved structural motifs and domain rearrangements. Curr. Protein Pept. Sci. 2003, 4, 217-229.
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 217-229
    • Jitrapakdee, S.1    Wallace, J.C.2
  • 154
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking
    • Tagwerker, C., Flick, K., Cui, M., Guerrero, C. et al., A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol. Cell. Proteomics 2006, 5, 737-748.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4
  • 155
    • 34247166669 scopus 로고    scopus 로고
    • A new method of purification of proteasome substrates reveals polyubiquitination of 20S proteasome subunits
    • Ventadour, S., Jarzaguet, M., Wing, S. S., Chambon, C. et al., A new method of purification of proteasome substrates reveals polyubiquitination of 20S proteasome subunits. J. Biol. Chem. 2007, 282, 5302-5309.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5302-5309
    • Ventadour, S.1    Jarzaguet, M.2    Wing, S.S.3    Chambon, C.4
  • 156
    • 77449137513 scopus 로고    scopus 로고
    • Proteomic analysis of protein phosphorylation and ubiquitination in Alzheimer's disease
    • Thomas, S. N., Cripps, D., Yang, A. J., Proteomic analysis of protein phosphorylation and ubiquitination in Alzheimer's disease. Methods Mol. Biol. 2009, 566, 109-121.
    • (2009) Methods Mol. Biol. , vol.566 , pp. 109-121
    • Thomas, S.N.1    Cripps, D.2    Yang, A.J.3
  • 157
    • 78751496279 scopus 로고    scopus 로고
    • Proteomic snapshot of the EGF-induced ubiquitin network
    • Argenzio, E., Bange, T., Oldrini, B., Bianchi, F. et al., Proteomic snapshot of the EGF-induced ubiquitin network. Mol. Syst. Biol. 2011, 7, 462.
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 462
    • Argenzio, E.1    Bange, T.2    Oldrini, B.3    Bianchi, F.4
  • 158
    • 0030055633 scopus 로고    scopus 로고
    • Isatin - a link between natriuretic peptides and monoamines
    • Medvedev, A. E., Clow, A., Sandler, M., Glover, V., Isatin - a link between natriuretic peptides and monoamines. Biochem. Pharmacol. 1996, 52, 385-391.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 385-391
    • Medvedev, A.E.1    Clow, A.2    Sandler, M.3    Glover, V.4
  • 160
    • 57349102719 scopus 로고    scopus 로고
    • Biological targets for isatin and its analogues: implications for therapy
    • Medvedev, A., Buneeva, O., Glover, V., Biological targets for isatin and its analogues: implications for therapy. Biol. Targets Therap. 2007, 1, 151-162.
    • (2007) Biol. Targets Therap. , vol.1 , pp. 151-162
    • Medvedev, A.1    Buneeva, O.2    Glover, V.3
  • 161
    • 17644424572 scopus 로고    scopus 로고
    • Biological activities of isatin and its derivatives
    • Pandeya, S. N., Smitha, S., Jyoti, M., Sridhar, S. K., Biological activities of isatin and its derivatives. Acta Pharm. 2005, 55, 27-46.
    • (2005) Acta Pharm. , vol.55 , pp. 27-46
    • Pandeya, S.N.1    Smitha, S.2    Jyoti, M.3    Sridhar, S.K.4
  • 162
    • 0030048086 scopus 로고    scopus 로고
    • The relationship between isatin and monoamine oxidase-B inhibitory activity in urine
    • Pang, F. Y., Hucklebridge, F. H., Forster, G., Tan, K., Clow, A., The relationship between isatin and monoamine oxidase-B inhibitory activity in urine. Stress Med. 1996, 12, 35-42.
    • (1996) Stress Med. , vol.12 , pp. 35-42
    • Pang, F.Y.1    Hucklebridge, F.H.2    Forster, G.3    Tan, K.4    Clow, A.5
  • 163
    • 0033561573 scopus 로고    scopus 로고
    • Efficacy of isatin analogues as antagonists of rat brain and heart atrial natriuretic peptide receptors coupled to particulate guanylyl cyclase
    • Medvedev, A. E., Goodwin, B. L., Sandler, M., Glover, V., Efficacy of isatin analogues as antagonists of rat brain and heart atrial natriuretic peptide receptors coupled to particulate guanylyl cyclase. Biochem. Pharmacol. 1999, 57, 913-915.
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 913-915
    • Medvedev, A.E.1    Goodwin, B.L.2    Sandler, M.3    Glover, V.4
  • 164
    • 0036052087 scopus 로고    scopus 로고
    • Study of the tissue and subcellular distribution of isatin-binding proteins with optical biosensor
    • Ivanov, Iu. D., Panova, N. G., Gnedenko, O. V., Bineeva, O. A. et al., Study of the tissue and subcellular distribution of isatin-binding proteins with optical biosensor. Vopr. Med. Khim. 2002, 48, 73-83.
    • (2002) Vopr. Med. Khim. , vol.48 , pp. 73-83
    • Ivanov, I.D.1    Panova, N.G.2    Gnedenko, O.V.3    Bineeva, O.A.4
  • 165
    • 70449469388 scopus 로고    scopus 로고
    • Isatin binding proteins in rat brain: in situ imaging, quantitative characterization of specific [3H]isatin dinding, and proteomic profiling
    • Crumeyrolle-Arias, M., Buneeva, O., Zgoda, V., Kopylov, A. et al., Isatin binding proteins in rat brain: in situ imaging, quantitative characterization of specific [3H]isatin dinding, and proteomic profiling. J. Neurosci. Res. 2009, 87, 2763-2772.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 2763-2772
    • Crumeyrolle-Arias, M.1    Buneeva, O.2    Zgoda, V.3    Kopylov, A.4
  • 166
    • 73549095291 scopus 로고    scopus 로고
    • Isatin binding proteins of rat and mouse brain: proteomic identification and optical biosensor validation
    • Buneeva, O., Gnedenko, O., Zgoda, V., Kopylov, A. et al., Isatin binding proteins of rat and mouse brain: proteomic identification and optical biosensor validation. Proteomics 2010, 10, 23-37.
    • (2010) Proteomics , vol.10 , pp. 23-37
    • Buneeva, O.1    Gnedenko, O.2    Zgoda, V.3    Kopylov, A.4
  • 167
    • 34248550988 scopus 로고    scopus 로고
    • Isatin interaction with glyceraldehyde-3-phosphate dehydrogenase, a putative target of neuroprotective drugs: partial agonism with deprenyl
    • Medvedev, A., Buneeva, O., Gnedenko, V., Fedchenko, M. et al., Isatin interaction with glyceraldehyde-3-phosphate dehydrogenase, a putative target of neuroprotective drugs: partial agonism with deprenyl. J. Neural Transm. 2006, 71, 195-203.
    • (2006) J. Neural Transm. , vol.71 , pp. 195-203
    • Medvedev, A.1    Buneeva, O.2    Gnedenko, V.3    Fedchenko, M.4
  • 169
    • 0036817905 scopus 로고    scopus 로고
    • Proteomic technologies in modern biomedical science
    • Govorun, V. M., Archakov, A. I., Proteomic technologies in modern biomedical science. Biochemistry (Moscow) 2002, 67, 1109-1123.
    • (2002) Biochemistry (Moscow) , vol.67 , pp. 1109-1123
    • Govorun, V.M.1    Archakov, A.I.2
  • 170
    • 19944408971 scopus 로고    scopus 로고
    • Limitations of current proteomics technologies
    • Garbis, S., Lubec, G., Fountoulakis, M., Limitations of current proteomics technologies. J. Chromatogr. 2005, 1077, 1-18.
    • (2005) J. Chromatogr. , vol.1077 , pp. 1-18
    • Garbis, S.1    Lubec, G.2    Fountoulakis, M.3
  • 171
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics
    • Butterfield, D. A., Perluigi, M., Sultana, R., Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur. J. Pharmacol. 2006, 545, 39-50.
    • (2006) Eur. J. Pharmacol. , vol.545 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 172
    • 0028871164 scopus 로고
    • Behavioral effects of isatin on open field activity and immobility in the forced swim test in rats
    • Abel, E. L., Behavioral effects of isatin on open field activity and immobility in the forced swim test in rats. Physiol. Behav. 1995, 57, 611-613.
    • (1995) Physiol. Behav. , vol.57 , pp. 611-613
    • Abel, E.L.1
  • 173
    • 80051650502 scopus 로고    scopus 로고
    • Pharmaco-proteomic analysis of a novel cell-permeable peptide inhibitor of tumor-induced angiogenesis
    • 10, M110.005264.
    • Bang, J. Y., Kim, E. Y., Kang, D. K., Chang, S. I. et al., Pharmaco-proteomic analysis of a novel cell-permeable peptide inhibitor of tumor-induced angiogenesis. Mol. Cell. Proteomics 2011, 10, M110.005264.
    • (2011) Mol. Cell. Proteomics
    • Bang, J.Y.1    Kim, E.Y.2    Kang, D.K.3    Chang, S.I.4
  • 174
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix, U., Superti-Furga, G., Target profiling of small molecules by chemical proteomics. Nat. Chem. Biol. 2009, 5, 616-624.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 175
    • 48849086000 scopus 로고    scopus 로고
    • The Proteominer and the Fortyniners: searching for gold nuggets in the proteomic arena
    • Righetti, P. G., Boschetti, E., The Proteominer and the Fortyniners: searching for gold nuggets in the proteomic arena. Mass Spectrom. Rev. 2008, 27, 596-608.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 596-608
    • Righetti, P.G.1    Boschetti, E.2
  • 176
    • 79954497190 scopus 로고    scopus 로고
    • Combinatorial peptide ligand libraries: the conquest of the "hidden proteome" advances at great strides
    • Righetti, P. G., Fasoli, E., Boschetti, E., Combinatorial peptide ligand libraries: the conquest of the "hidden proteome" advances at great strides. Electrophoresis 2011, 32, 960-966.
    • (2011) Electrophoresis , vol.32 , pp. 960-966
    • Righetti, P.G.1    Fasoli, E.2    Boschetti, E.3
  • 177
    • 77955857651 scopus 로고    scopus 로고
    • Combinatorial peptide ligand library plasma treatment: advantages for accessing low abundance proteins
    • Beseme, O., Fertin, M., Drobecq, H., Amouyel, P., Pinet, F., Combinatorial peptide ligand library plasma treatment: advantages for accessing low abundance proteins. Electrophoresis 2010, 31, 2697-2704.
    • (2010) Electrophoresis , vol.31 , pp. 2697-2704
    • Beseme, O.1    Fertin, M.2    Drobecq, H.3    Amouyel, P.4    Pinet, F.5
  • 178
    • 58849127707 scopus 로고    scopus 로고
    • Combinatorial peptide ligand libraries and plant proteomics: a winning strategy at a price
    • Boschetti, E., Bindschedler, L. V., Tang, C., Fasoli, E., Righetti, P. G., Combinatorial peptide ligand libraries and plant proteomics: a winning strategy at a price. J. Chromatogr. A 2009, 1216, 1215-1222.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 1215-1222
    • Boschetti, E.1    Bindschedler, L.V.2    Tang, C.3    Fasoli, E.4    Righetti, P.G.5
  • 179
    • 58949100303 scopus 로고    scopus 로고
    • Chicken egg yolk cytoplasmic proteome, mined via combinatorial peptide ligand libraries
    • Farinazzo, A., Restuccia, U., Bachi, A., Guerrier, L. et al., Chicken egg yolk cytoplasmic proteome, mined via combinatorial peptide ligand libraries. J. Chromatogr. A 2009, 1216, 1241-1252.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 1241-1252
    • Farinazzo, A.1    Restuccia, U.2    Bachi, A.3    Guerrier, L.4
  • 180
    • 77249155980 scopus 로고    scopus 로고
    • Exploring the venom proteome of the African puff adder, Bitis arietans, using a combinatorial peptide ligand library approach at different pHs
    • Fasoli, E., Sanz, L., Wagstaff, S., Harrison, R. A. et al., Exploring the venom proteome of the African puff adder, Bitis arietans, using a combinatorial peptide ligand library approach at different pHs. J. Proteomics 2010, 73, 932-942.
    • (2010) J. Proteomics , vol.73 , pp. 932-942
    • Fasoli, E.1    Sanz, L.2    Wagstaff, S.3    Harrison, R.A.4
  • 181
    • 82355185805 scopus 로고    scopus 로고
    • Low abundance protein enrichment for discovery of candidate plasma protein biomarkers for early detection of breast cancer
    • Meng, R., Gormley, M., Bhat, V. B., Rosenberg, A., Quong, A. A., Low abundance protein enrichment for discovery of candidate plasma protein biomarkers for early detection of breast cancer. J. Proteomics 2011, 75, 366-374.
    • (2011) J. Proteomics , vol.75 , pp. 366-374
    • Meng, R.1    Gormley, M.2    Bhat, V.B.3    Rosenberg, A.4    Quong, A.A.5
  • 182
    • 80053541929 scopus 로고    scopus 로고
    • Capturing and amplifying impurities from recombinant therapeutic proteins via combinatorial peptide libraries: a proteomic approach
    • Righetti, P. G., Boschetti, E., Fasoli, E., Capturing and amplifying impurities from recombinant therapeutic proteins via combinatorial peptide libraries: a proteomic approach. Curr. Pharm. Biotechnol. 2011, 12, 1537-1547.
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 1537-1547
    • Righetti, P.G.1    Boschetti, E.2    Fasoli, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.