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Volumn 80, Issue 5, 2010, Pages 739-747

Methods for investigation of targeted kinase inhibitor therapy using chemical proteomics and phosphorylation profiling

Author keywords

Drug resistance; Drug response; Mass spectrometry; Phosphoproteomics; Phosphorylation; Targeted therapy

Indexed keywords

PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTRANSFERASE INHIBITOR; PHOSPHOTYROSINE;

EID: 77954216493     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.03.027     Document Type: Review
Times cited : (16)

References (86)
  • 1
    • 20444370016 scopus 로고
    • The cleavage products of vitellin
    • Levene P.A., Alsberg C.L. The cleavage products of vitellin. J Biol Chem 1906, 2(1):127-133.
    • (1906) J Biol Chem , vol.2 , Issue.1 , pp. 127-133
    • Levene, P.A.1    Alsberg, C.L.2
  • 2
    • 0000685288 scopus 로고
    • Serinephosphoric acid obtained on hydrolysis of vitellinic acid
    • Lipmann F.A., Levene P.A. Serinephosphoric acid obtained on hydrolysis of vitellinic acid. J Biol Chem 1932, 98(1):109-114.
    • (1932) J Biol Chem , vol.98 , Issue.1 , pp. 109-114
    • Lipmann, F.A.1    Levene, P.A.2
  • 3
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Burnett G., Kennedy E.P. The enzymatic phosphorylation of proteins. J Biol Chem 1954, 211(2):969-980.
    • (1954) J Biol Chem , vol.211 , Issue.2 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 4
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P., Hunter T. Oncogenic kinase signalling. Nature 2001, 411(6835):355-365.
    • (2001) Nature , vol.411 , Issue.6835 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 5
    • 72849127628 scopus 로고    scopus 로고
    • Kinase mutations in human disease: interpreting genotype-phenotype relationships
    • Lahiry P., Torkamani A., Schork N.J., Hegele R.A. Kinase mutations in human disease: interpreting genotype-phenotype relationships. Nat Rev Genet 2010, 11(1):60-74.
    • (2010) Nat Rev Genet , vol.11 , Issue.1 , pp. 60-74
    • Lahiry, P.1    Torkamani, A.2    Schork, N.J.3    Hegele, R.A.4
  • 6
    • 13844321724 scopus 로고    scopus 로고
    • Chasing mutations in the epidermal growth factor in lung cancer
    • Dowell J.E., Minna J.D. Chasing mutations in the epidermal growth factor in lung cancer. N Engl J Med 2005, 352(8):830-832.
    • (2005) N Engl J Med , vol.352 , Issue.8 , pp. 830-832
    • Dowell, J.E.1    Minna, J.D.2
  • 8
    • 40849147041 scopus 로고    scopus 로고
    • EGFR antagonists in cancer treatment
    • Ciardiello F., Tortora G. EGFR antagonists in cancer treatment. N Engl J Med 2008, 358(11):1160-1174.
    • (2008) N Engl J Med , vol.358 , Issue.11 , pp. 1160-1174
    • Ciardiello, F.1    Tortora, G.2
  • 9
    • 33750989362 scopus 로고    scopus 로고
    • 2-Aminothiazole as a novel kinase inhibitor template. Structure-activity relationship studies toward the discovery of N-(2-chloro-6-methylphenyl)-2-[[6-[4-(2-hydroxyethyl)-1-piperazinyl)]-2-methyl-4-pyrimidinyl]amino)]-1,3-thiazole-5-carboxamide (dasatinib, BMS-354825) as a potent pan-Src kinase inhibitor
    • Das J., Chen P., Norris D., Padmanabha R., Lin J., Moquin R.V., et al. 2-Aminothiazole as a novel kinase inhibitor template. Structure-activity relationship studies toward the discovery of N-(2-chloro-6-methylphenyl)-2-[[6-[4-(2-hydroxyethyl)-1-piperazinyl)]-2-methyl-4-pyrimidinyl]amino)]-1,3-thiazole-5-carboxamide (dasatinib, BMS-354825) as a potent pan-Src kinase inhibitor. J Med Chem 2006, 49(23):6819-6832.
    • (2006) J Med Chem , vol.49 , Issue.23 , pp. 6819-6832
    • Das, J.1    Chen, P.2    Norris, D.3    Padmanabha, R.4    Lin, J.5    Moquin, R.V.6
  • 10
    • 0037322376 scopus 로고    scopus 로고
    • Safety and activity of docetaxel and trastuzumab in HER2 overexpressing metastatic breast cancer: a pilot phase II study
    • Montemurro F., Choa G., Faggiuolo R., Sperti E., Capaldi A., Donadio M., et al. Safety and activity of docetaxel and trastuzumab in HER2 overexpressing metastatic breast cancer: a pilot phase II study. Am J Clin Oncol 2003, 26(1):95-97.
    • (2003) Am J Clin Oncol , vol.26 , Issue.1 , pp. 95-97
    • Montemurro, F.1    Choa, G.2    Faggiuolo, R.3    Sperti, E.4    Capaldi, A.5    Donadio, M.6
  • 11
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 2007, 131(6):1190-1203.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 12
    • 40849130043 scopus 로고    scopus 로고
    • Proteomic methods for drug target discovery
    • Sleno L., Emili A. Proteomic methods for drug target discovery. Curr Opin Chem Biol 2008, 12(1):46-54.
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.1 , pp. 46-54
    • Sleno, L.1    Emili, A.2
  • 13
    • 0014348411 scopus 로고
    • Selective enzyme purification by affinity chromatography
    • Cuatrecasas P., Wilchek M., Anfinsen C.B. Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci USA 1968, 61(2):636-643.
    • (1968) Proc Natl Acad Sci USA , vol.61 , Issue.2 , pp. 636-643
    • Cuatrecasas, P.1    Wilchek, M.2    Anfinsen, C.B.3
  • 14
    • 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(9):616-624.
    • (2009) Nat Chem Biol , vol.5 , Issue.9 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 15
    • 42049123098 scopus 로고    scopus 로고
    • Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib
    • Hantschel O., Rix U., Superti-Furga G. Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib. Leuk Lymphoma 2008, 49(4):615-619.
    • (2008) Leuk Lymphoma , vol.49 , Issue.4 , pp. 615-619
    • Hantschel, O.1    Rix, U.2    Superti-Furga, G.3
  • 16
    • 29144453813 scopus 로고    scopus 로고
    • Characterisation of kinase-selective inhibitors by chemical proteomics
    • Daub H. Characterisation of kinase-selective inhibitors by chemical proteomics. Biochim Biophys Acta 2005, 1754(1-2):183-190.
    • (2005) Biochim Biophys Acta , vol.1754 , Issue.1-2 , pp. 183-190
    • Daub, H.1
  • 17
    • 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., Blencke S., Gutbrod H., et al. An efficient proteomics method to identify the cellular targets of protein kinase inhibitors. Proc Natl Acad Sci USA 2003, 100(26):15434-15439.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.26 , pp. 15434-15439
    • Godl, K.1    Wissing, J.2    Kurtenbach, A.3    Habenberger, P.4    Blencke, S.5    Gutbrod, H.6
  • 18
    • 37049014938 scopus 로고    scopus 로고
    • Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets
    • Rix U., Hantschel O., Dürnberger G., Remsing Rix L.L., Planyavsky M., Fernbach N.V., et al. Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets. Blood 2007, 110(12):4055-4063.
    • (2007) Blood , vol.110 , Issue.12 , pp. 4055-4063
    • Rix, U.1    Hantschel, O.2    Dürnberger, G.3    Remsing Rix, L.L.4    Planyavsky, M.5    Fernbach, N.V.6
  • 19
    • 34147163563 scopus 로고    scopus 로고
    • Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry
    • Wissing J., Jänsch L., Nimtz M., Dieterich G., Hornberger R., Kéri G., et al. Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics 2007, 6(3):537-547.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.3 , pp. 537-547
    • Wissing, J.1    Jänsch, L.2    Nimtz, M.3    Dieterich, G.4    Hornberger, R.5    Kéri, G.6
  • 20
    • 34948875686 scopus 로고    scopus 로고
    • Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors
    • Bantscheff M., Eberhard D., Abraham Y., Bastuck S., Boesche M., Hobson S., et al. Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat Biotechnol 2007, 25(9):1035-1044.
    • (2007) Nat Biotechnol , vol.25 , Issue.9 , pp. 1035-1044
    • Bantscheff, M.1    Eberhard, D.2    Abraham, Y.3    Bastuck, S.4    Boesche, M.5    Hobson, S.6
  • 21
    • 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., Weber M., Habenberger P., et al. Chemical proteomic analysis reveals alternative modes of action for pyrido[2,3-d]pyrimidine kinase inhibitors. Mol Cell Proteomics 2004, 3(12):1181-1193.
    • (2004) Mol Cell Proteomics , vol.3 , Issue.12 , pp. 1181-1193
    • Wissing, J.1    Godl, K.2    Brehmer, D.3    Blencke, S.4    Weber, M.5    Habenberger, P.6
  • 24
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: principles and applications
    • Macek B., Mann M., Olsen J.V. Global and site-specific quantitative phosphoproteomics: principles and applications. Annu Rev Pharmacol Toxicol 2009, 49:199-221.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 25
    • 56649106671 scopus 로고    scopus 로고
    • IPEP: an in silico tool to examine proteolytic peptides for mass spectrometry
    • Lu D., Liu R.Z., Izumi V., Fenstermacher D., Haura E.B., Koomen J., et al. IPEP: an in silico tool to examine proteolytic peptides for mass spectrometry. Bioinformatics 2008, 24(23):2801-2802.
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2801-2802
    • Lu, D.1    Liu, R.Z.2    Izumi, V.3    Fenstermacher, D.4    Haura, E.B.5    Koomen, J.6
  • 26
    • 0022029557 scopus 로고
    • Electrospray interface for liquid chromatographs and mass spectrometers
    • Whitehouse C.M., Dreyer R.N., Yamashita M., Fenn J.B. Electrospray interface for liquid chromatographs and mass spectrometers. Anal Chem 1985, 57(3):675-679.
    • (1985) Anal Chem , vol.57 , Issue.3 , pp. 675-679
    • Whitehouse, C.M.1    Dreyer, R.N.2    Yamashita, M.3    Fenn, J.B.4
  • 27
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100 000 by laser ionization time-of flight mass spectrometry
    • Tanaka K., Waki H., Ido Y., Akita S., Yoshida Y., Yoshida T. Protein and polymer analyses up to m/z 100 000 by laser ionization time-of flight mass spectrometry. Rapid Commun Mass Spectrom 1988, 2(20):151-153.
    • (1988) Rapid Commun Mass Spectrom , vol.2 , Issue.20 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 28
    • 84885653762 scopus 로고
    • Ein neues Massenspektrometer ohne Magnetfeld
    • Paul W., Steinwedel H. Ein neues Massenspektrometer ohne Magnetfeld. Zeitschrift für Naturforschung 1953, A8(7):448-450.
    • (1953) Zeitschrift für Naturforschung , vol.A8 , Issue.7 , pp. 448-450
    • Paul, W.1    Steinwedel, H.2
  • 29
    • 0032237775 scopus 로고    scopus 로고
    • Fragmentation of phosphopeptides in an ion trap mass spectrometer
    • DeGnore J.P., Qin J. Fragmentation of phosphopeptides in an ion trap mass spectrometer. J Am Soc Mass Spectrom 1998, 9(11):1175-1188.
    • (1998) J Am Soc Mass Spectrom , vol.9 , Issue.11 , pp. 1175-1188
    • DeGnore, J.P.1    Qin, J.2
  • 30
    • 55849122284 scopus 로고    scopus 로고
    • Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation analysis
    • Villén J., Beausoleil S.A., Gygi S.P. Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation analysis. Proteomics 2008, 8(21):4444-4452.
    • (2008) Proteomics , vol.8 , Issue.21 , pp. 4444-4452
    • Villén, J.1    Beausoleil, S.A.2    Gygi, S.P.3
  • 31
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema P.J., Mohammed S., Heck A.J. Phosphopeptide fragmentation and analysis by mass spectrometry. J Mass Spectrom 2009, 44(6):861-878.
    • (2009) J Mass Spectrom , vol.44 , Issue.6 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.3
  • 33
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka J.E., Coon J.J., Schroeder M.J., Shabanowitz J., Hunt D.F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci USA 2004, 101(26):9528-9533.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.26 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 34
    • 33847778786 scopus 로고    scopus 로고
    • Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry
    • Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E., Bai D.L., et al. Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc Natl Acad Sci USA 2007, 104(7):2193-2198.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.7 , pp. 2193-2198
    • Chi, A.1    Huttenhower, C.2    Geer, L.Y.3    Coon, J.J.4    Syka, J.E.5    Bai, D.L.6
  • 35
    • 59049086847 scopus 로고    scopus 로고
    • Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry
    • Swaney D.L., Wenger C.D., Thomson J.A., Coon J.J. Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 2009, 106(4):995-1000.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.4 , pp. 995-1000
    • Swaney, D.L.1    Wenger, C.D.2    Thomson, J.A.3    Coon, J.J.4
  • 36
    • 0001268221 scopus 로고
    • Fourier transform ion cyclotron resonance spectroscopy
    • Comisarow M.B., Marshall A.G. Fourier transform ion cyclotron resonance spectroscopy. Chem Phys Lett 1974, 25(2):282-283.
    • (1974) Chem Phys Lett , vol.25 , Issue.2 , pp. 282-283
    • Comisarow, M.B.1    Marshall, A.G.2
  • 37
    • 0041408938 scopus 로고    scopus 로고
    • Electrostatic axially harmonic orbital trapping: a high-performance technique of mass analysis
    • Makarov A. Electrostatic axially harmonic orbital trapping: a high-performance technique of mass analysis. Anal Chem 2000, 72(6):1156-1162.
    • (2000) Anal Chem , vol.72 , Issue.6 , pp. 1156-1162
    • Makarov, A.1
  • 40
    • 35648969575 scopus 로고    scopus 로고
    • The effects of mass accuracy, data acquisition speed, and search algorithm choice on peptide identification rates in phosphoproteomics
    • Bakalarski C.E., Haas W., Dephoure N.E., Gygi S.P. The effects of mass accuracy, data acquisition speed, and search algorithm choice on peptide identification rates in phosphoproteomics. Anal Bioanal Chem 2007, 389(5):1409-1419.
    • (2007) Anal Bioanal Chem , vol.389 , Issue.5 , pp. 1409-1419
    • Bakalarski, C.E.1    Haas, W.2    Dephoure, N.E.3    Gygi, S.P.4
  • 41
    • 0022541790 scopus 로고
    • 3+) affinity chromatography
    • 3+) affinity chromatography. Anal Biochem 1986, 154(1):250-254.
    • (1986) Anal Biochem , vol.154 , Issue.1 , pp. 250-254
    • Andersson, L.1    Parath, J.2
  • 42
    • 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(14):2883-2892.
    • (1999) Anal Chem , vol.71 , Issue.14 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 43
    • 0028062116 scopus 로고
    • Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70
    • Watts J.D., Affolter M., Krebs D.L., Wange R.L., Samelson L.E., Aebersold R. Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70. J Biol Chem 1994, 269(47):29520-29529.
    • (1994) J Biol Chem , vol.269 , Issue.47 , pp. 29520-29529
    • Watts, J.D.1    Affolter, M.2    Krebs, D.L.3    Wange, R.L.4    Samelson, L.E.5    Aebersold, R.6
  • 44
  • 45
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nühse 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(11):1234-1243.
    • (2003) Mol Cell Proteomics , vol.2 , Issue.11 , pp. 1234-1243
    • Nühse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 46
    • 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., Jørgensen T.J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 2005, 4(7):873-886.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.7 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.5
  • 47
    • 38049035341 scopus 로고    scopus 로고
    • Global profiling of phosphopeptides by titania affinity enrichment
    • Wu J., Shakey Q., Liu W., Schuller A., Follettie M.T. Global profiling of phosphopeptides by titania affinity enrichment. J Proteome Res 2007, 6(12):4684-4689.
    • (2007) J Proteome Res , vol.6 , Issue.12 , pp. 4684-4689
    • Wu, J.1    Shakey, Q.2    Liu, W.3    Schuller, A.4    Follettie, M.T.5
  • 48
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse M.W., Uitto P.M., Hilhorst M.J., Ooms B., Heck A.J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem 2004, 76(14):3935-3943.
    • (2004) Anal Chem , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 49
    • 34547869591 scopus 로고    scopus 로고
    • Identification of phosphoproteins and determination of phosphorylation sites by zirconium dioxide enrichment and SELDI-MS/MS
    • Cuccurullo M., Schlosser G., Cacace G., Malorni L., Pocsfalvi G. Identification of phosphoproteins and determination of phosphorylation sites by zirconium dioxide enrichment and SELDI-MS/MS. J Mass Spectrom 2007, 42(8):1069-1078.
    • (2007) J Mass Spectrom , vol.42 , Issue.8 , pp. 1069-1078
    • Cuccurullo, M.1    Schlosser, G.2    Cacace, G.3    Malorni, L.4    Pocsfalvi, G.5
  • 50
    • 28444487185 scopus 로고    scopus 로고
    • Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC)
    • Wolschin F., Wienkoop S., Weckwerth W. Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC). Proteomics 2005, 5(17):4389-4397.
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4389-4397
    • Wolschin, F.1    Wienkoop, S.2    Weckwerth, W.3
  • 51
    • 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(4):379-382.
    • (2001) Nat Biotechnol , vol.19 , Issue.4 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 52
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H., Watts J.D., Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol 2001, 19(4):375-378.
    • (2001) Nat Biotechnol , vol.19 , Issue.4 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 53
  • 54
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A., Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990, 61(2):203-212.
    • (1990) Cell , vol.61 , Issue.2 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 55
    • 0028964465 scopus 로고
    • Cytokine signaling through nonreceptor protein tyrosine kinases
    • Taniguchi T. Cytokine signaling through nonreceptor protein tyrosine kinases. Science 1995, 268(5208):251-255.
    • (1995) Science , vol.268 , Issue.5208 , pp. 251-255
    • Taniguchi, T.1
  • 56
    • 0024953236 scopus 로고
    • Protein modification: phosphorylation on tyrosine residues
    • Hunter T. Protein modification: phosphorylation on tyrosine residues. Curr Opin Cell Biol 1989, 1(6):1168-1181.
    • (1989) Curr Opin Cell Biol , vol.1 , Issue.6 , pp. 1168-1181
    • Hunter, T.1
  • 57
    • 0141723426 scopus 로고    scopus 로고
    • Gleevec resistance: lessons for target-directed drug development
    • Daley G.Q. Gleevec resistance: lessons for target-directed drug development. Cell Cycle 2003, 2(3):190-191.
    • (2003) Cell Cycle , vol.2 , Issue.3 , pp. 190-191
    • Daley, G.Q.1
  • 58
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter T., Sefton B.M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 1980, 77(3):1311-1315.
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.3 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 59
    • 0034624002 scopus 로고    scopus 로고
    • Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways
    • Pandey A., Fernandez M.M., Steen H., Blagoev B., Nielsen M.M., Roche S., et al. Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways. J Biol Chem 2000, 275(49):38633-38639.
    • (2000) J Biol Chem , vol.275 , Issue.49 , pp. 38633-38639
    • Pandey, A.1    Fernandez, M.M.2    Steen, H.3    Blagoev, B.4    Nielsen, M.M.5    Roche, S.6
  • 60
    • 3042626249 scopus 로고    scopus 로고
    • Selective tyrosine hyperphosphorylation of cytoskeletal and stress proteins in primary human breast cancers: implications for adjuvant use of kinase-inhibitory drugs
    • Lim Y.P., Wong C.Y., Ooi L.L., Druker B.J., Epstein R.J. Selective tyrosine hyperphosphorylation of cytoskeletal and stress proteins in primary human breast cancers: implications for adjuvant use of kinase-inhibitory drugs. Clin Cancer Res 2004, 10(12 Pt 1):3980-3987.
    • (2004) Clin Cancer Res , vol.10 , Issue.12 PART 1 , pp. 3980-3987
    • Lim, Y.P.1    Wong, C.Y.2    Ooi, L.L.3    Druker, B.J.4    Epstein, R.J.5
  • 61
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol 2005, 23(1):94-101.
    • (2005) Nat Biotechnol , vol.23 , Issue.1 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4    Goss, V.L.5    Spek, E.J.6
  • 62
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
    • Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci USA 2007, 104(14):5860-5865.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.14 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 65
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villén J., Gygi S.P. The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat Protoc 2008, 3(10):1630-1638.
    • (2008) Nat Protoc , vol.3 , Issue.10 , pp. 1630-1638
    • Villén, J.1    Gygi, S.P.2
  • 66
    • 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., Kumar C., Mortensen P., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127(3):635-648.
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6
  • 68
    • 70349621112 scopus 로고    scopus 로고
    • Systems-wide analysis of a phosphatase knock-down by quantitative proteomics and phosphoproteomics
    • Hilger M., Bonaldi T., Gnad F., Mann M. Systems-wide analysis of a phosphatase knock-down by quantitative proteomics and phosphoproteomics. Mol Cell Proteomics 2009, 8(8):1908-1920.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.8 , pp. 1908-1920
    • Hilger, M.1    Bonaldi, T.2    Gnad, F.3    Mann, M.4
  • 69
    • 49549116189 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of signaling network dynamics
    • White F.M. Quantitative phosphoproteomic analysis of signaling network dynamics. Curr Opin Biotechnol 2008, 19(4):404-409.
    • (2008) Curr Opin Biotechnol , vol.19 , Issue.4 , pp. 404-409
    • White, F.M.1
  • 70
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev B., Ong S.E., Kratchmarova I., Mann M. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat Biotechnol 2004, 22(9):1139-1145.
    • (2004) Nat Biotechnol , vol.22 , Issue.9 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 71
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 2002, 1(5):376-386.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 72
    • 0242569349 scopus 로고    scopus 로고
    • A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture
    • Ibarrola N., Kalume D.E., Gronborg M., Iwahori A., Pandey A. A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture. Anal Chem 2003, 75(22):6043-6049.
    • (2003) Anal Chem , vol.75 , Issue.22 , pp. 6043-6049
    • Ibarrola, N.1    Kalume, D.E.2    Gronborg, M.3    Iwahori, A.4    Pandey, A.5
  • 73
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 2008, 26(12):1367-1372.
    • (2008) Nat Biotechnol , vol.26 , Issue.12 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 74
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N., Marchese J.N., Williamson B., Parker K., Hattan S., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 2004, 3(12):1154-1169.
    • (2004) Mol Cell Proteomics , vol.3 , Issue.12 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattan, S.6
  • 75
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., et al. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics 2005, 4(9):1240-1250.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.9 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6
  • 76
    • 33746730389 scopus 로고    scopus 로고
    • Phosphoproteomic approaches to elucidate cellular signaling networks
    • Schmelzle K., White F.M. Phosphoproteomic approaches to elucidate cellular signaling networks. Curr Opin Biotechnol 2006, 17(4):406-414.
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.4 , pp. 406-414
    • Schmelzle, K.1    White, F.M.2
  • 77
    • 0035923582 scopus 로고    scopus 로고
    • Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding
    • Nollau P., Mayer B.J. Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding. Proc Natl Acad Sci USA 2001, 98(24):13531-13536.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.24 , pp. 13531-13536
    • Nollau, P.1    Mayer, B.J.2
  • 78
    • 10944257339 scopus 로고    scopus 로고
    • Profiling the global tyrosine phosphorylation state
    • Machida K., Mayer B.J., Nollau P. Profiling the global tyrosine phosphorylation state. Mol Cell Proteomics 2003, 2(4):215-233.
    • (2003) Mol Cell Proteomics , vol.2 , Issue.4 , pp. 215-233
    • Machida, K.1    Mayer, B.J.2    Nollau, P.3
  • 79
    • 0027690228 scopus 로고
    • Biotinylated isocoumarins, new inhibitors and reagents for detection, localization, and isolation of serine proteases
    • Kam C.M., Abuelyaman A.S., Li Z., Hudig D., Powers J.C. Biotinylated isocoumarins, new inhibitors and reagents for detection, localization, and isolation of serine proteases. Bioconjug Chem 1993, 4(6):560-567.
    • (1993) Bioconjug Chem , vol.4 , Issue.6 , pp. 560-567
    • Kam, C.M.1    Abuelyaman, A.S.2    Li, Z.3    Hudig, D.4    Powers, J.C.5
  • 80
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: the serine hydrolases
    • Liu Y., Patricelli M.P., Cravatt B.F. Activity-based protein profiling: the serine hydrolases. Proc Natl Acad Sci USA 1999, 96:14694-14699.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 81
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum D., Medzihradszky K.F., Burlingame A., Bogyo M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem Biol 2000, 7(8):569-581.
    • (2000) Chem Biol , vol.7 , Issue.8 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 82
    • 24044520992 scopus 로고    scopus 로고
    • A streamlined platform for high-content functional proteomics of primary human specimens
    • Jessani N., Niessen S., Wei B.Q., Nicolau M., Humphrey M., Ji Y., et al. A streamlined platform for high-content functional proteomics of primary human specimens. Nat Methods 2005, 2(9):691-697.
    • (2005) Nat Methods , vol.2 , Issue.9 , pp. 691-697
    • Jessani, N.1    Niessen, S.2    Wei, B.Q.3    Nicolau, M.4    Humphrey, M.5    Ji, Y.6
  • 83
    • 0036678119 scopus 로고    scopus 로고
    • Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness
    • Jessani N., Liu Y., Humphrey M., Cravatt B.F. Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc Natl Acad Sci USA 2002, 99(16):10335-10340.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.16 , pp. 10335-10340
    • Jessani, N.1    Liu, Y.2    Humphrey, M.3    Cravatt, B.F.4
  • 84
    • 0036391485 scopus 로고    scopus 로고
    • Design and synthesis of class-selective activity probes for protein tyrosine phosphatases
    • Lo L.C., Pang T.L., Kuo C.H., Chiang Y.L., Wang H.Y., Lin J.J. Design and synthesis of class-selective activity probes for protein tyrosine phosphatases. J Proteome Res 2002, 1(1):35-40.
    • (2002) J Proteome Res , vol.1 , Issue.1 , pp. 35-40
    • Lo, L.C.1    Pang, T.L.2    Kuo, C.H.3    Chiang, Y.L.4    Wang, H.Y.5    Lin, J.J.6
  • 86
    • 35348839586 scopus 로고    scopus 로고
    • PhosphoPep - a phosphoproteome resource for systems biology research in Drosophila Kc167 cells
    • Bodenmiller B., Malmstrom J., Gerrits B., Campbell D., Lam H., Schmidt A., et al. PhosphoPep - a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Mol Syst Biol 2007, 3:139.
    • (2007) Mol Syst Biol , vol.3 , pp. 139
    • Bodenmiller, B.1    Malmstrom, J.2    Gerrits, B.3    Campbell, D.4    Lam, H.5    Schmidt, A.6


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