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Volumn 3, Issue 3, 2006, Pages 199-209

Proteomics approach to illustrate drug action mechanisms

Author keywords

Drug mechanism; Drug target; Proteomics

Indexed keywords

2,4 DIMETHYL 5 (2 OXO 1H INDOL 3 YLMETHYLENE) 3 PYRROLEPROPIONIC ACID; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ALCOHOL; ANGIOGENESIS INHIBITOR; ANTINEOPLASTIC AGENT; CALYCULIN A; CISPLATIN; CYANOGINOSIN; CYCLOSPORIN A; DEOXYCHOLIC ACID; FUMAGILLOL CHLOROACETYLCARBAMATE; GEFITINIB; INDISULAM; LONAFARNIB; SOMATOMEDIN BINDING PROTEIN 6; THIOACETAMIDE; VINBLASTINE; VINCRISTINE;

EID: 33947231266     PISSN: 15701638     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016306780136763     Document Type: Review
Times cited : (20)

References (106)
  • 1
    • 27144470222 scopus 로고    scopus 로고
    • Application of immobilized metal affinity chromatography in proteomics
    • Sun X., Chiu J. F., He Q. Y.: Application of immobilized metal affinity chromatography in proteomics. Expert. Rev. Proteomics 2, 649, (2005).
    • (2005) Expert. Rev. Proteomics , vol.2 , pp. 649
    • Sun, X.1    Chiu, J.F.2    He, Q.Y.3
  • 2
    • 0042268086 scopus 로고    scopus 로고
    • Proteomics in biomarker discovery and drug development
    • He Q. Y., Chiu J. F.: Proteomics in biomarker discovery and drug development. J. Cell Biochem. 89, 868, (2003).
    • (2003) J. Cell Biochem , vol.89 , pp. 868
    • He, Q.Y.1    Chiu, J.F.2
  • 4
    • 27744462150 scopus 로고    scopus 로고
    • In vivo drug-response in patients with leukemic non-Hodgkin's lymphomas is associated with in vitro chemosensitivity and gene expression profiling
    • Chow K. U., Nowak D., Kim S. Z., Schneider B., Komor M., Boehrer S., Mitrou P. S., Hoelzer D.: et al. In vivo drug-response in patients with leukemic non-Hodgkin's lymphomas is associated with in vitro chemosensitivity and gene expression profiling. Pharmacol. Res. 53, 49, (2006).
    • (2006) Pharmacol. Res , vol.53 , pp. 49
    • Chow, K.U.1    Nowak, D.2    Kim, S.Z.3    Schneider, B.4    Komor, M.5    Boehrer, S.6    Mitrou, P.S.7    Hoelzer, D.8
  • 5
    • 0029817305 scopus 로고    scopus 로고
    • Modulation of carbachol-induced [Ca2+]i oscillations by Ca2+ influx in single intestinal smooth muscle cells
    • Komori S., Iwata M., Unno T., Ohashi H.: Modulation of carbachol-induced [Ca2+]i oscillations by Ca2+ influx in single intestinal smooth muscle cells. Br. J. Pharmacol. 119, 245, (1996).
    • (1996) Br. J. Pharmacol , vol.119 , pp. 245
    • Komori, S.1    Iwata, M.2    Unno, T.3    Ohashi, H.4
  • 6
    • 0027284485 scopus 로고
    • Classification of mouse liver proteins by immobilized metal affinity chromatography and two-dimensional electrophoresis
    • Jungblut P., Baumeister H., Klose J. Classification of mouse liver proteins by immobilized metal affinity chromatography and two-dimensional electrophoresis. Electrophoresis 14, 638, (1993).
    • (1993) Electrophoresis , vol.14 , pp. 638
    • Jungblut, P.1    Baumeister, H.2    Klose, J.3
  • 9
    • 20844447127 scopus 로고    scopus 로고
    • In vivo dual-tagging proteomic approach in studying signaling pathways in immune response
    • Wang T., Gu S., Ronni T., Du Y. C., Chen X.: In vivo dual-tagging proteomic approach in studying signaling pathways in immune response. J. Proteome. Res. 4, 941, (2005).
    • (2005) J. Proteome. Res , vol.4 , pp. 941
    • Wang, T.1    Gu, S.2    Ronni, T.3    Du, Y.C.4    Chen, X.5
  • 10
    • 0033575719 scopus 로고    scopus 로고
    • Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain
    • Chi S. W., Ayed A., Arrowsmith C. H.: Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain. EMBO J. 18, 4438, (1999).
    • (1999) EMBO J , vol.18 , pp. 4438
    • Chi, S.W.1    Ayed, A.2    Arrowsmith, C.H.3
  • 11
    • 29244451873 scopus 로고    scopus 로고
    • Gold(III) porphyrin 1a induced apoptosis by mitochondrial death pathways related to reactive oxygen species
    • Wang Y., He Q. Y., Sun R. W., Che C. M., Chiu J. F.: Gold(III) porphyrin 1a induced apoptosis by mitochondrial death pathways related to reactive oxygen species. Cancer Res. 65, 11553, (2005).
    • (2005) Cancer Res , vol.65 , pp. 11553
    • Wang, Y.1    He, Q.Y.2    Sun, R.W.3    Che, C.M.4    Chiu, J.F.5
  • 12
    • 31344472931 scopus 로고    scopus 로고
    • Proteomic characterization of the cytotoxic mechanism of gold (III) porphyrin 1a, a potential anticancer drug
    • Wang Y., He Q. Y., Che C. M., Chiu J. F.: Proteomic characterization of the cytotoxic mechanism of gold (III) porphyrin 1a, a potential anticancer drug. Proteomics 6, 131, (2006).
    • (2006) Proteomics , vol.6 , pp. 131
    • Wang, Y.1    He, Q.Y.2    Che, C.M.3    Chiu, J.F.4
  • 13
    • 4644301795 scopus 로고    scopus 로고
    • A proteome analysis of the arsenite response in cultured lung cells: Evidence for in vitro oxidative stress-induced apoptosis
    • Lau A. T., He Q. Y., Chiu J. F.: A proteome analysis of the arsenite response in cultured lung cells: evidence for in vitro oxidative stress-induced apoptosis. Biochem. J. 382, 641, (2004).
    • (2004) Biochem. J , vol.382 , pp. 641
    • Lau, A.T.1    He, Q.Y.2    Chiu, J.F.3
  • 14
    • 27944502074 scopus 로고    scopus 로고
    • Combination of solid-phase affinity capture on magnetic beads and mass spectrometry to study non-covalent interactions: Example of minor groove binding drugs
    • Schlosser G., Vekey K., Malorni A., Pocsfalvi G.: Combination of solid-phase affinity capture on magnetic beads and mass spectrometry to study non-covalent interactions: example of minor groove binding drugs. Rapid Commun. Mass Spectrom. 19, 3307, (2005).
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 3307
    • Schlosser, G.1    Vekey, K.2    Malorni, A.3    Pocsfalvi, G.4
  • 15
    • 23844509794 scopus 로고    scopus 로고
    • Insulin-like growth factor binding protein-5 is a target of matrix metalloproteinase-7: Implications for epithelial-mesenchymal signaling
    • Hemers E., Duval C., McCaig C., Handley M., Dockray G. J., Varro A. Insulin-like growth factor binding protein-5 is a target of matrix metalloproteinase-7: implications for epithelial-mesenchymal signaling. Cancer Res. 65, 7363, (2005).
    • (2005) Cancer Res , vol.65 , pp. 7363
    • Hemers, E.1    Duval, C.2    McCaig, C.3    Handley, M.4    Dockray, G.J.5    Varro, A.6
  • 16
    • 24944514702 scopus 로고    scopus 로고
    • Identification of placental transforming growth factor-beta and bikunin metabolites as contaminants of pharmaceutical human chorionic gonadotrophin preparations by proteomic techniques
    • Malatos S., Neubert H., Kicman A. T., Iles R. K.: Identification of placental transforming growth factor-beta and bikunin metabolites as contaminants of pharmaceutical human chorionic gonadotrophin preparations by proteomic techniques. Mol. Cell Proteomics 4, 984, (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 984
    • Malatos, S.1    Neubert, H.2    Kicman, A.T.3    Iles, R.K.4
  • 18
    • 26844465529 scopus 로고    scopus 로고
    • Proteomic evidence for roles for nucleolin and poly[ADP-ribosyl] transferase in drug resistance
    • Fu Z., Fenselau C.: Proteomic evidence for roles for nucleolin and poly[ADP-ribosyl] transferase in drug resistance. J. Proteome. Res. 4, 1583, (2005).
    • (2005) J. Proteome. Res , vol.4 , pp. 1583
    • Fu, Z.1    Fenselau, C.2
  • 19
    • 23044510618 scopus 로고    scopus 로고
    • Proteomic characterization of the angiogenesis inhibitor SU6668 reveals multiple impacts on cellular kinase signaling
    • Godl K., Gruss O. J., Eickhoff J., Wissing J., Blencke S., Weber M., Degen H., Brehmer D.: et al. Proteomic characterization of the angiogenesis inhibitor SU6668 reveals multiple impacts on cellular kinase signaling. Cancer Res. 65, 6919, (2005).
    • (2005) Cancer Res , vol.65 , pp. 6919
    • Godl, K.1    Gruss, O.J.2    Eickhoff, J.3    Wissing, J.4    Blencke, S.5    Weber, M.6    Degen, H.7    Brehmer, D.8
  • 20
    • 21344455298 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitor SCH66336 induces rapid phosphorylation of eukaryotic translation elongation factor 2 in head and neck squamous cell carcinoma cells
    • Ren H., Tai S. K., Khuri F., Chu Z., Mao L.: Farnesyltransferase inhibitor SCH66336 induces rapid phosphorylation of eukaryotic translation elongation factor 2 in head and neck squamous cell carcinoma cells. Cancer Res. 65, 5841, (2005).
    • (2005) Cancer Res , vol.65 , pp. 5841
    • Ren, H.1    Tai, S.K.2    Khuri, F.3    Chu, Z.4    Mao, L.5
  • 21
    • 23144436273 scopus 로고    scopus 로고
    • Age-dependent variations of cell response to oxidative stress: Proteomic approach to protein expression and phosphorylation
    • Miura Y., Kano M., Abe K., Urano S., Suzuki S., Toda T.: Age-dependent variations of cell response to oxidative stress: proteomic approach to protein expression and phosphorylation. Electrophoresis 26, 2786, (2005).
    • (2005) Electrophoresis , vol.26 , pp. 2786
    • Miura, Y.1    Kano, M.2    Abe, K.3    Urano, S.4    Suzuki, S.5    Toda, T.6
  • 22
    • 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 4, 721, (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 721
    • Zheng, H.1    Hu, P.2    Quinn, D.F.3    Wang, Y.K.4
  • 23
    • 24144490686 scopus 로고    scopus 로고
    • Proteomics in acute myelogenous leukaemia (AML): Methodological strategies and identification of protein targets for novel antileukaemic therapy
    • Sjoholt G., Anensen N., Wergeland L., Mc C. E., Bruserud O., Gjertsen B. T.: Proteomics in acute myelogenous leukaemia (AML): methodological strategies and identification of protein targets for novel antileukaemic therapy. Curr. Drug Targets. 6, 631, (2005).
    • (2005) Curr. Drug Targets , vol.6 , pp. 631
    • Sjoholt, G.1    Anensen, N.2    Wergeland, L.3    Mc, C.E.4    Bruserud, O.5    Gjertsen, B.T.6
  • 24
    • 25144493129 scopus 로고    scopus 로고
    • VeloceGenomics: An accelerated in vivo drug discovery approach to rapidly predict the biologic, drug-like activity of compounds, proteins, or genes
    • Papoian R., Scherer A., Saulnier M., Staedtler F., Cordier A., Legay F., Maurer G., Staeheli J.: et al. VeloceGenomics: an accelerated in vivo drug discovery approach to rapidly predict the biologic, drug-like activity of compounds, proteins, or genes. Pharm. Res. 22, 1597, (2005).
    • (2005) Pharm. Res , vol.22 , pp. 1597
    • Papoian, R.1    Scherer, A.2    Saulnier, M.3    Staedtler, F.4    Cordier, A.5    Legay, F.6    Maurer, G.7    Staeheli, J.8
  • 26
    • 14844295744 scopus 로고    scopus 로고
    • Systematic peptide array-based delineation of the differential beta-catenin interaction with Tcf4, E-cadherin, and adeno-matous polyposis coli
    • Gail R., Frank R., Wittinghofer A.: Systematic peptide array-based delineation of the differential beta-catenin interaction with Tcf4, E-cadherin, and adeno-matous polyposis coli. J. Biol. Chem. 280, 7107, (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 7107
    • Gail, R.1    Frank, R.2    Wittinghofer, A.3
  • 27
    • 3543028591 scopus 로고    scopus 로고
    • FGF-2 induced by interleukin-1 beta through the action of phosphatidylinositol 3-kinase mediates endothelial mesenchymal transformation in corneal endothelial cells
    • Lee H. T., Lee J. G., Na M., Kay E. P.: FGF-2 induced by interleukin-1 beta through the action of phosphatidylinositol 3-kinase mediates endothelial mesenchymal transformation in corneal endothelial cells. J. Biol. Chem. 279, 32325, (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 32325
    • Lee, H.T.1    Lee, J.G.2    Na, M.3    Kay, E.P.4
  • 28
    • 3242688104 scopus 로고    scopus 로고
    • Surface plasmon resonance studies of the direct interaction between a drug/intestinal brush border membrane
    • Kim K., Cho S., Park J. H., Byun Y., Chung H., Kwon I. C., Jeong S. Y.: Surface plasmon resonance studies of the direct interaction between a drug/intestinal brush border membrane. Pharm. Res. 21, 1233, (2004).
    • (2004) Pharm. Res , vol.21 , pp. 1233
    • Kim, K.1    Cho, S.2    Park, J.H.3    Byun, Y.4    Chung, H.5    Kwon, I.C.6    Jeong, S.Y.7
  • 29
    • 8444252965 scopus 로고    scopus 로고
    • Genomic and proteomic technologies for individualisation and improvement of cancer treatment
    • Wulfkuhle J., Espina V., Liotta L., Petricoin E.: Genomic and proteomic technologies for individualisation and improvement of cancer treatment. Eur. J. Cancer 40, 2623, (2004).
    • (2004) Eur. J. Cancer , vol.40 , pp. 2623
    • Wulfkuhle, J.1    Espina, V.2    Liotta, L.3    Petricoin, E.4
  • 30
    • 21744453318 scopus 로고    scopus 로고
    • ERK phosphorylation is linked to VEGFR2 expression and Ets-2 phosphorylation in breast cancer and is associated with tamoxifen treatment resistance and small tumours with good prognosis
    • Svensson S., Jirstrom K., Ryden L., Roos G., Emdin S., Ostrowski M. C., Landberg G.: ERK phosphorylation is linked to VEGFR2 expression and Ets-2 phosphorylation in breast cancer and is associated with tamoxifen treatment resistance and small tumours with good prognosis. Oncogene 24, 4370, (2005).
    • (2005) Oncogene , vol.24 , pp. 4370
    • Svensson, S.1    Jirstrom, K.2    Ryden, L.3    Roos, G.4    Emdin, S.5    Ostrowski, M.C.6    Landberg, G.7
  • 31
    • 20444366189 scopus 로고    scopus 로고
    • Pb2+ exposure alters the lens alpha A-crystallin protein profile in vivo and induces cataract formation in lens organ culture
    • Neal R., Aykin-Burns N., Ercal N., Zigler J. S., Jr.: Pb2+ exposure alters the lens alpha A-crystallin protein profile in vivo and induces cataract formation in lens organ culture. Toxicology 212, 1, (2005).
    • (2005) Toxicology , vol.212 , pp. 1
    • Neal, R.1    Aykin-Burns, N.2    Ercal, N.3    Zigler Jr., J.S.4
  • 33
    • 33745543989 scopus 로고    scopus 로고
    • In vitro evaluation of adenosine 5'-monophosphate as an imaging agent of tumor metabolism
    • Cho S. Y., Polster J., Engles J. M., Hilton J., Abraham E. H., Wahl R. L.: In vitro evaluation of adenosine 5'-monophosphate as an imaging agent of tumor metabolism. J. Nucl. Med. 47, 837, (2006).
    • (2006) J. Nucl. Med , vol.47 , pp. 837
    • Cho, S.Y.1    Polster, J.2    Engles, J.M.3    Hilton, J.4    Abraham, E.H.5    Wahl, R.L.6
  • 34
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert J. D., Pisitkun T., Wang G., Shen R. F., Knepper M. A.: Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites. Proc. Natl. Acad. Sci. USA 103, 7159, (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7159
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.3    Shen, R.F.4    Knepper, M.A.5
  • 35
    • 33745621292 scopus 로고    scopus 로고
    • Absolute quantification of multi-site phosphorylation by selective reaction monitoring mass spectrometry: Determination of inhibitory phosphorylation status of cyclin dependent kinases
    • Mayya V., Rezaul K., Wu L., Fong M. B., Han D. K.: Absolute quantification of multi-site phosphorylation by selective reaction monitoring mass spectrometry: Determination of inhibitory phosphorylation status of cyclin dependent kinases. Mol. Cell Proteomics 5, 1146, (2006).
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1146
    • Mayya, V.1    Rezaul, K.2    Wu, L.3    Fong, M.B.4    Han, D.K.5
  • 36
    • 33645102888 scopus 로고    scopus 로고
    • D'Astous M., Mendez P., Morissette M., Garcia-Segura L. M., Di Paolo T.: Implication of the phosphatidylinositol-3 kinase/protein kinase B signaling pathway in the neuroprotective effect of estradiol in the striatum of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mice. Mol. Pharmacol. 69, 1492, (2006).
    • D'Astous M., Mendez P., Morissette M., Garcia-Segura L. M., Di Paolo T.: Implication of the phosphatidylinositol-3 kinase/protein kinase B signaling pathway in the neuroprotective effect of estradiol in the striatum of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mice. Mol. Pharmacol. 69, 1492, (2006).
  • 37
    • 31644441420 scopus 로고    scopus 로고
    • Proteomic analysis of lysosomal acid hydrolases secreted by osteoclasts: Implications for lytic enzyme transport and bone metabolism
    • Czupalla C., Mansukoski H., Riedl T., Thiel D., Krause E., Hoflack B.: Proteomic analysis of lysosomal acid hydrolases secreted by osteoclasts: implications for lytic enzyme transport and bone metabolism. Mol. Cell Proteomics 5, 134, (2006).
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 134
    • Czupalla, C.1    Mansukoski, H.2    Riedl, T.3    Thiel, D.4    Krause, E.5    Hoflack, B.6
  • 38
    • 23944500826 scopus 로고    scopus 로고
    • Extended Range Proteomic Analysis (ERPA): A new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications- comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)
    • Wu S. L., Kim J., Hancock W. S., Karger B.: Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications- comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR). J. Proteome. Res. 4, 1155, (2005).
    • (2005) J. Proteome. Res , vol.4 , pp. 1155
    • Wu, S.L.1    Kim, J.2    Hancock, W.S.3    Karger, B.4
  • 39
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates
    • Tam E. M., Morrison C. J., Wu Y. I., Stack M. S., Overall C. M.: Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. USA 101, 6917, (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6917
    • Tam, E.M.1    Morrison, C.J.2    Wu, Y.I.3    Stack, M.S.4    Overall, C.M.5
  • 43
    • 0038361307 scopus 로고    scopus 로고
    • Discovering potent and selective reversible inhibitors of enzymes in complex proteomes
    • Leung D., Hardouin C., Boger D. L., Cravatt B. F.: Discovering potent and selective reversible inhibitors of enzymes in complex proteomes. Nat. Biotechnol. 21, 687, (2003).
    • (2003) Nat. Biotechnol , vol.21 , pp. 687
    • Leung, D.1    Hardouin, C.2    Boger, D.L.3    Cravatt, B.F.4
  • 44
    • 0042034151 scopus 로고    scopus 로고
    • A new method to estimate ligand-receptor energetics
    • Bock J. R., Gough D. A.: A new method to estimate ligand-receptor energetics. Mol. Cell Proteomics 1, 904, (2002).
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 904
    • Bock, J.R.1    Gough, D.A.2
  • 45
    • 7444271412 scopus 로고    scopus 로고
    • Proteomic analysis identifies that 14-3-3zeta interacts with beta-catenin and facilitates its activation by Akt
    • Tian Q., Feetham M. C., Tao W. A., He X. C., Li L., Aebersold R., Hood L.: Proteomic analysis identifies that 14-3-3zeta interacts with beta-catenin and facilitates its activation by Akt. Proc. Natl. Acad. Sci. USA 101, 15370, (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15370
    • Tian, Q.1    Feetham, M.C.2    Tao, W.A.3    He, X.C.4    Li, L.5    Aebersold, R.6    Hood, L.7
  • 46
    • 0038391227 scopus 로고    scopus 로고
    • Approaches to define antigen receptor-induced serine kinase signal transduction pathways
    • Astoul E., Laurence A. D., Totty N., Beer S., Alexander D. R., Cantrell D. A.: Approaches to define antigen receptor-induced serine kinase signal transduction pathways. J. Biol. Chem. 278, 9267, (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 9267
    • Astoul, E.1    Laurence, A.D.2    Totty, N.3    Beer, S.4    Alexander, D.R.5    Cantrell, D.A.6
  • 47
    • 0142157658 scopus 로고    scopus 로고
    • Proteomic profiling drug-induced apoptosis in non-small cell lung carcinoma: Identification of RS/DJ-1 and RhoGDIalpha
    • MacKeigan J. P., Clements C. M., Lich J. D., Pope R. M., Hod Y., Ting J. P.: Proteomic profiling drug-induced apoptosis in non-small cell lung carcinoma: identification of RS/DJ-1 and RhoGDIalpha. Cancer Res. 63, 6928, (2003).
    • (2003) Cancer Res , vol.63 , pp. 6928
    • MacKeigan, J.P.1    Clements, C.M.2    Lich, J.D.3    Pope, R.M.4    Hod, Y.5    Ting, J.P.6
  • 48
    • 18244370796 scopus 로고    scopus 로고
    • How molecular profiling could revolutionize drug discovery
    • Stoughton R. B., Friend S. H.: How molecular profiling could revolutionize drug discovery. Nat. Rev. Drug Discov. 4, 345, (2005).
    • (2005) Nat. Rev. Drug Discov , vol.4 , pp. 345
    • Stoughton, R.B.1    Friend, S.H.2
  • 49
    • 1642602773 scopus 로고    scopus 로고
    • Drug target identification: A question of biology
    • Smith C.: Drug target identification: a question of biology. Nature 428, 225, (2004).
    • (2004) Nature , vol.428 , pp. 225
    • Smith, C.1
  • 50
    • 14944338732 scopus 로고    scopus 로고
    • Volume-sensitive organic osmolyte/anion channels in cancer: Novel approaches to studying channel modulation employing proteomics technologies
    • Davies A. R., Belsey M. J., Kozlowski R. Z.: Volume-sensitive organic osmolyte/anion channels in cancer: novel approaches to studying channel modulation employing proteomics technologies. Ann. N. Y. Acad. Sci. 1028, 38, (2004).
    • (2004) Ann. N. Y. Acad. Sci , vol.1028 , pp. 38
    • Davies, A.R.1    Belsey, M.J.2    Kozlowski, R.Z.3
  • 51
    • 0345598923 scopus 로고    scopus 로고
    • Redox regulation of surface protein thiols: Identification of integrin alpha-4 as a molecular target by using redox proteomics
    • Laragione T., Bonetto V., Casoni F., Massignan T., Bianchi G., Gianazza E., Ghezzi P.: Redox regulation of surface protein thiols: identification of integrin alpha-4 as a molecular target by using redox proteomics. Proc. Natl. Acad. Sci. USA 100, 14737, (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14737
    • Laragione, T.1    Bonetto, V.2    Casoni, F.3    Massignan, T.4    Bianchi, G.5    Gianazza, E.6    Ghezzi, P.7
  • 52
    • 13844319935 scopus 로고    scopus 로고
    • Drug bioactivation, covalent binding to target proteins and toxicity relevance
    • Zhou S., Chan E., Duan W., Huang M., Chen Y. Z.: Drug bioactivation, covalent binding to target proteins and toxicity relevance. Drug Metab. Rev. 37, 41, (2005).
    • (2005) Drug Metab. Rev , vol.37 , pp. 41
    • Zhou, S.1    Chan, E.2    Duan, W.3    Huang, M.4    Chen, Y.Z.5
  • 53
    • 10644250718 scopus 로고    scopus 로고
    • A proteomic analysis of thioacetamide-induced hepa-totoxicity and cirrhosis in rat livers
    • Low T. Y., Leow C. K., Salto-Tellez M., Chung M. C.: A proteomic analysis of thioacetamide-induced hepa-totoxicity and cirrhosis in rat livers. Proteomics 4, 3960, (2004).
    • (2004) Proteomics , vol.4 , pp. 3960
    • Low, T.Y.1    Leow, C.K.2    Salto-Tellez, M.3    Chung, M.C.4
  • 56
    • 0031823995 scopus 로고    scopus 로고
    • New insights into cyclosporine A nephrotoxicity by proteome analysis
    • Aicher L., Wahl D., Arce A., Grenet O., Steiner S.: New insights into cyclosporine A nephrotoxicity by proteome analysis. Electrophoresis 19, 1998, (1998).
    • (1998) Electrophoresis , vol.19 , pp. 1998
    • Aicher, L.1    Wahl, D.2    Arce, A.3    Grenet, O.4    Steiner, S.5
  • 57
    • 33646251378 scopus 로고    scopus 로고
    • Proteomic approach to study the cytotoxicity of dioscin (saponin)
    • Wang Y., Cheung Y. H., Yang Z., Chiu J. F., Che C. M., He Q. Y.: Proteomic approach to study the cytotoxicity of dioscin (saponin). Proteomics 6, 2422, (2006).
    • (2006) Proteomics , vol.6 , pp. 2422
    • Wang, Y.1    Cheung, Y.H.2    Yang, Z.3    Chiu, J.F.4    Che, C.M.5    He, Q.Y.6
  • 58
    • 26844495728 scopus 로고    scopus 로고
    • Proteomic identification of insulin-like growth factor-binding protein-6 induced by sublethal H2O2 stress from human diploid fibroblasts
    • Xie L., Tsaprailis G., Chen Q. M.: Proteomic identification of insulin-like growth factor-binding protein-6 induced by sublethal H2O2 stress from human diploid fibroblasts. Mol. Cell Proteomics 4, 1273, (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1273
    • Xie, L.1    Tsaprailis, G.2    Chen, Q.M.3
  • 59
    • 21244457292 scopus 로고    scopus 로고
    • Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine- containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry
    • Kanski J., Hong S. J., Schoneich C.: Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine- containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry. J. Biol. Chem. 280, 24261, (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 24261
    • Kanski, J.1    Hong, S.J.2    Schoneich, C.3
  • 60
    • 15744388954 scopus 로고    scopus 로고
    • Target identification and validation in drug discovery: The role of proteomics
    • Kopec K. K., Bozyczko-Coyne D., Williams M.: Target identification and validation in drug discovery: the role of proteomics. Biochem. Pharmacol. 69, 1133, (2005).
    • (2005) Biochem. Pharmacol , vol.69 , pp. 1133
    • Kopec, K.K.1    Bozyczko-Coyne, D.2    Williams, M.3
  • 61
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux D. L., Korsmeyer S. J.: Cell death in development. Cell 96, 245, (1999).
    • (1999) Cell , vol.96 , pp. 245
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 63
    • 11144267126 scopus 로고    scopus 로고
    • Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1
    • O'Neill E., Rushworth L., Baccarini M., Kolch W.: Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1. Science 306, 2267, (2004).
    • (2004) Science , vol.306 , pp. 2267
    • O'Neill, E.1    Rushworth, L.2    Baccarini, M.3    Kolch, W.4
  • 65
    • 15944413138 scopus 로고    scopus 로고
    • Identification of dynamic proteome changes upon ligand activation of Trk-receptors using two-dimensional fluorescence difference gel electrophoresis and mass spectrometry
    • Sitek B., Apostolov O., Stuhler K., Pfeiffer K., Meyer H. E., Eggert A., Schramm A.: Identification of dynamic proteome changes upon ligand activation of Trk-receptors using two-dimensional fluorescence difference gel electrophoresis and mass spectrometry. Mol. Cell Proteomics 4, 291, (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 291
    • Sitek, B.1    Apostolov, O.2    Stuhler, K.3    Pfeiffer, K.4    Meyer, H.E.5    Eggert, A.6    Schramm, A.7
  • 66
    • 33646362301 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of myc-induced apoptosis: A direct role for Myc induction of the mitochondrial chloride ion channel, mtCLIC/CLIC4
    • Shiio Y., Suh K. S., Lee H., Yuspa S. H., Eisenman R. N., Aebersold R.: Quantitative proteomic analysis of myc-induced apoptosis: a direct role for Myc induction of the mitochondrial chloride ion channel, mtCLIC/CLIC4. J. Biol. Chem. 281, 2750, (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 2750
    • Shiio, Y.1    Suh, K.S.2    Lee, H.3    Yuspa, S.H.4    Eisenman, R.N.5    Aebersold, R.6
  • 68
    • 33745600824 scopus 로고    scopus 로고
    • A proteomic investigation into a human gastric cancer cell line BGC823 treated with diallyl trisulfide
    • Li N., Guo R., Li W., Shao J., Li S., Zhao K., Chen X., Xu N. et al.: A proteomic investigation into a human gastric cancer cell line BGC823 treated with diallyl trisulfide. Carcinogenesis, 27, 1222, (2006).
    • (2006) Carcinogenesis , vol.27 , pp. 1222
    • Li, N.1    Guo, R.2    Li, W.3    Shao, J.4    Li, S.5    Zhao, K.6    Chen, X.7    Xu, N.8
  • 69
    • 9644302485 scopus 로고    scopus 로고
    • Proteomic analysis of antiproliferative effects by treatment of 5-fluorouracil in cervical cancer cells
    • Yim E. K., Lee K. H., Bae J. S., Namkoong S. E., Um S. J., Park J. S.: Proteomic analysis of antiproliferative effects by treatment of 5-fluorouracil in cervical cancer cells. DNA Cell Biol. 23, 769, (2004).
    • (2004) DNA Cell Biol , vol.23 , pp. 769
    • Yim, E.K.1    Lee, K.H.2    Bae, J.S.3    Namkoong, S.E.4    Um, S.J.5    Park, J.S.6
  • 70
    • 11144274440 scopus 로고    scopus 로고
    • Large-scale quantitative proteomic study of PUMA-induced apoptosis using two-dimensional liquid chromatography-mass spectrometry coupled with amino acid-coded mass tagging
    • Gu S., Du Y., Chen J., Liu Z., Bradbury E. M., Hu C. A., Chen X.: Large-scale quantitative proteomic study of PUMA-induced apoptosis using two-dimensional liquid chromatography-mass spectrometry coupled with amino acid-coded mass tagging. J. Proteome. Res. 3, 1191, (2004).
    • (2004) J. Proteome. Res , vol.3 , pp. 1191
    • Gu, S.D.Y.1    Chen, J.2    Liu, Z.3    Bradbury, E.M.4    Hu, C.A.5    Chen, X.6
  • 71
    • 24144451321 scopus 로고    scopus 로고
    • Protein fingerprints of anti-cancer effects of cyclin-dependent kinase inhibition: Identiication of candidate biomarkers using 2-D liquid phase separation coupled to mass spectrometry
    • Skalnikova H., Halada P., Dzubak P., Hajduch M., Kovarova H.: Protein fingerprints of anti-cancer effects of cyclin-dependent kinase inhibition: identiication of candidate biomarkers using 2-D liquid phase separation coupled to mass spectrometry. Technol. Cancer Res. Treat. 4, 447, (2005).
    • (2005) Technol. Cancer Res. Treat , vol.4 , pp. 447
    • Skalnikova, H.1    Halada, P.2    Dzubak, P.3    Hajduch, M.4    Kovarova, H.5
  • 72
    • 24944453273 scopus 로고    scopus 로고
    • Induction of apoptosis in mouse liver by microcystin-LR: A combined transcriptomic, proteomic, and simulation strategy
    • Chen T., Wang Q., Cui J., Yang W., Shi Q., Hua Z., Ji J., Shen P.: Induction of apoptosis in mouse liver by microcystin-LR: a combined transcriptomic, proteomic, and simulation strategy. Mol. Cell Proteomics 4, 958, (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 958
    • Chen, T.1    Wang, Q.2    Cui, J.3    Yang, W.4    Shi, Q.5    Hua, Z.6    Ji, J.7    Shen, P.8
  • 73
    • 29144480597 scopus 로고    scopus 로고
    • Analysis of protein expression during oxidative stress in breast epithelial cells using a stable isotope labeled proteome internal standard
    • Yan Y., Weaver V. M., Blair I. A.: Analysis of protein expression during oxidative stress in breast epithelial cells using a stable isotope labeled proteome internal standard. J. Proteome. Res. 4, 2007, (2005).
    • (2005) J. Proteome. Res , vol.4 , pp. 2007
    • Yan, Y.1    Weaver, V.M.2    Blair, I.A.3
  • 74
    • 27144518454 scopus 로고    scopus 로고
    • Proteomic analysis of human O6-methylguanine-DNA methyltransferase by affinity chromatography and tandem mass spectrometry
    • Niture S. K., Doneanu C. E., Velu C. S., Bailey N. I., Srivenugopal K. S.: Proteomic analysis of human O6-methylguanine-DNA methyltransferase by affinity chromatography and tandem mass spectrometry. Biochem. Biophys. Res. Commun. 337, 1176, (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.337 , pp. 1176
    • Niture, S.K.1    Doneanu, C.E.2    Velu, C.S.3    Bailey, N.I.4    Srivenugopal, K.S.5
  • 75
    • 0141953996 scopus 로고    scopus 로고
    • Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin
    • Keezer S. M., Ivie S. E., Krutzsch H. C., Tandle A., Libutti S. K., Roberts D. D.: Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin. Cancer Res. 63, 6405, (2003).
    • (2003) Cancer Res , vol.63 , pp. 6405
    • Keezer, S.M.1    Ivie, S.E.2    Krutzsch, H.C.3    Tandle, A.4    Libutti, S.K.5    Roberts, D.D.6
  • 77
    • 27544493101 scopus 로고    scopus 로고
    • Cerebrospinal fluid proteomic analysis reveals dysregulation of methionine amino-peptidase-2 expression in human and mouse neurofibromatosis 1-associated glioma
    • Dasgupta B., Yi Y., Hegedus B., Weber J. D., Gutmann D. H.: Cerebrospinal fluid proteomic analysis reveals dysregulation of methionine amino-peptidase-2 expression in human and mouse neurofibromatosis 1-associated glioma. Cancer Res. 65, 9843, (2005).
    • (2005) Cancer Res , vol.65 , pp. 9843
    • Dasgupta, B.1    Yi, Y.2    Hegedus, B.3    Weber, J.D.4    Gutmann, D.H.5
  • 78
    • 29644445975 scopus 로고    scopus 로고
    • Proteomic Analysis of Vascular Endothelial Growth Factor-induced Endothelial Cell Differentiation Reveals a Role for Chloride Intracellular Channel 4 (CLIC4) in Tubular Morphogenesis
    • Bohman S., Matsumoto T., Suh K., Dimberg A., Jakobsson L., Yuspa S., Claesson-Welsh L.: Proteomic Analysis of Vascular Endothelial Growth Factor-induced Endothelial Cell Differentiation Reveals a Role for Chloride Intracellular Channel 4 (CLIC4) in Tubular Morphogenesis. J. Biol. Chem. 280, 42397, (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 42397
    • Bohman, S.1    Matsumoto, T.2    Suh, K.3    Dimberg, A.4    Jakobsson, L.5    Yuspa, S.6    Claesson-Welsh, L.7
  • 80
    • 13644254794 scopus 로고    scopus 로고
    • Molecular mechanisms of drug resistance
    • Longley D. B., Johnston P. G.: Molecular mechanisms of drug resistance. J. Pathol. 205, 275, (2005).
    • (2005) J. Pathol , vol.205 , pp. 275
    • Longley, D.B.1    Johnston, P.G.2
  • 83
    • 0242413674 scopus 로고    scopus 로고
    • Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations
    • Verrills N. M., Walsh B. J., Cobon G. S., Hains P. G., Kavallaris M.: Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations. J. Biol. Chem. 278, 45082, (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 45082
    • Verrills, N.M.1    Walsh, B.J.2    Cobon, G.S.3    Hains, P.G.4    Kavallaris, M.5
  • 84
    • 0032006059 scopus 로고    scopus 로고
    • Microtubules and actin filaments: Dynamic targets for cancer chemotherapy
    • Jordan M. A., Wilson L.: Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr. Opin. Cell Biol. 10, 123, (1998).
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 123
    • Jordan, M.A.1    Wilson, L.2
  • 85
    • 0034714438 scopus 로고    scopus 로고
    • Cytoskeletal disruption accelerates caspase-3 activation and alters the intracellular membrane reorganization in DNA damage-induced apoptosis
    • Yamazaki Y., Tsuruga M., Zhou D., Fujita Y., Shang X., Dang Y., Kawasaki K., Oka S.: Cytoskeletal disruption accelerates caspase-3 activation and alters the intracellular membrane reorganization in DNA damage-induced apoptosis. Exp. Cell Res. 259, 64, (2000).
    • (2000) Exp. Cell Res , vol.259 , pp. 64
    • Yamazaki, Y.1    Tsuruga, M.2    Zhou, D.3    Fujita, Y.4    Shang, X.5    Dang, Y.6    Kawasaki, K.7    Oka, S.8
  • 86
    • 85047683345 scopus 로고    scopus 로고
    • Apoptosis induced by disruption of the actin cytoskeleton is mediated via activation of CD95 (Fas/APO-1)
    • Kulms D., Dussmann H., Poppelmann B., Stander S., Schwarz A., Schwarz T.: Apoptosis induced by disruption of the actin cytoskeleton is mediated via activation of CD95 (Fas/APO-1). Cell Death. Differ. 9, 598, (2002).
    • (2002) Cell Death. Differ , vol.9 , pp. 598
    • Kulms, D.1    Dussmann, H.2    Poppelmann, B.3    Stander, S.4    Schwarz, A.5    Schwarz, T.6
  • 87
    • 0036176510 scopus 로고    scopus 로고
    • Mechanisms of cancer drug resistance
    • Gottesman M. M.: Mechanisms of cancer drug resistance. Annu. Rev. Med. 53, 615, (2002).
    • (2002) Annu. Rev. Med , vol.53 , pp. 615
    • Gottesman, M.M.1
  • 88
    • 0035489609 scopus 로고    scopus 로고
    • Proteomics for studying cancer cells and the development of chemoresistance
    • Hutter G., Sinha P.: Proteomics for studying cancer cells and the development of chemoresistance. Proteomics 1, 1233, (2001).
    • (2001) Proteomics , vol.1 , pp. 1233
    • Hutter, G.1    Sinha, P.2
  • 90
    • 17144430514 scopus 로고    scopus 로고
    • Down-regulation of mitochondrial F1F0-ATP synthase in human colon cancer cells with induced 5-fluorouracil resistance
    • Shin Y. K., Yoo B. C., Chang H. J., Jeon E., Hong S. H., Jung M. S., Lim S. J., Park J. G.: Down-regulation of mitochondrial F1F0-ATP synthase in human colon cancer cells with induced 5-fluorouracil resistance. Cancer Res. 65, 3162, (2005).
    • (2005) Cancer Res , vol.65 , pp. 3162
    • Shin, Y.K.1    Yoo, B.C.2    Chang, H.J.3    Jeon, E.4    Hong, S.H.5    Jung, M.S.6    Lim, S.J.7    Park, J.G.8
  • 91
    • 24044453711 scopus 로고    scopus 로고
    • Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia
    • Morand J. P., Macri J., Adeli K.: Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia. J. Biol. Chem. 280, 17626, (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 17626
    • Morand, J.P.1    Macri, J.2    Adeli, K.3
  • 92
    • 4444331337 scopus 로고    scopus 로고
    • Characterization of the Salmonella typhimurium proteome by semi-automated two dimensional HPLC-mass spectrometry: Detection of proteins implicated in multiple antibiotic resistance
    • Coldham N. G., Woodward M. J.: Characterization of the Salmonella typhimurium proteome by semi-automated two dimensional HPLC-mass spectrometry: detection of proteins implicated in multiple antibiotic resistance. J. Proteome. Res. 3, 595, (2004).
    • (2004) J. Proteome. Res , vol.3 , pp. 595
    • Coldham, N.G.1    Woodward, M.J.2
  • 93
    • 4043094169 scopus 로고    scopus 로고
    • Differential protein expression analysis of Leishmania major reveals novel roles for methionine adenosyltransferase and S-adenosylmethionine in methotrexate resistance
    • Drummelsmith J., Girard I., Trudel N., Ouellette M.: Differential protein expression analysis of Leishmania major reveals novel roles for methionine adenosyltransferase and S-adenosylmethionine in methotrexate resistance. J. Biol. Chem. 279, 33273, (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 33273
    • Drummelsmith, J.1    Girard, I.2    Trudel, N.3    Ouellette, M.4
  • 94
    • 24944483028 scopus 로고    scopus 로고
    • Proteomic analysis on multi-drug resistant cells HL-60/DOX of acute myeloblastic leukemia
    • Chen C. Y., Jia J. H., Zhang M. X., Meng Y. S., Kong D. X., Pan X. L., Yu X. P.: Proteomic analysis on multi-drug resistant cells HL-60/DOX of acute myeloblastic leukemia. Chin J. Physiol. 48, 115, (2005).
    • (2005) Chin J. Physiol , vol.48 , pp. 115
    • Chen, C.Y.1    Jia, J.H.2    Zhang, M.X.3    Meng, Y.S.4    Kong, D.X.5    Pan, X.L.6    Yu, X.P.7
  • 95
    • 2542550392 scopus 로고    scopus 로고
    • Comparison of proteomic and genomic analyses of the human breast cancer cell line T47D and the antiestrogen- resistant derivative T47D-r
    • Huber M., Bahr I., Kratzschmar J. R., Becker A., Muller E. C., Donner P., Pohlenz H. D., Schneider M. R. et al.: Comparison of proteomic and genomic analyses of the human breast cancer cell line T47D and the antiestrogen- resistant derivative T47D-r. Mol. Cell Proteomics 3, 43, (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 43
    • Huber, M.1    Bahr, I.2    Kratzschmar, J.R.3    Becker, A.4    Muller, E.C.5    Donner, P.6    Pohlenz, H.D.7    Schneider, M.R.8
  • 96
    • 21144441198 scopus 로고    scopus 로고
    • Systems analysis of transcriptome and proteome in retinoic acid/arsenic trioxide-induced cell differentiation/ apoptosis of promyelocytic leukemia
    • Zheng P. Z., Wang K. K., Zhang Q. Y., Huang Q. H., Du Y. Z., Zhang Q. H., Xiao D. K., Shen S. H. et al.: Systems analysis of transcriptome and proteome in retinoic acid/arsenic trioxide-induced cell differentiation/ apoptosis of promyelocytic leukemia. Proc. Natl. Acad. Sci. USA 102, 7653, (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7653
    • Zheng, P.Z.1    Wang, K.K.2    Zhang, Q.Y.3    Huang, Q.H.4    Du, Y.Z.5    Zhang, Q.H.6    Xiao, D.K.7    Shen, S.H.8
  • 97
    • 2642521977 scopus 로고    scopus 로고
    • Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line
    • Shu H., Chen S., Bi Q., Mumby M., Brekken D. L.: Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. Mol. Cell Proteomics 3, 279, (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 279
    • Shu, H.1    Chen, S.2    Bi, Q.3    Mumby, M.4    Brekken, D.L.5
  • 98
    • 29144449939 scopus 로고    scopus 로고
    • Proteomic analysis of cellular response to microcystin in human amnion FL cells
    • Fu W. Y., Xu L. H., Yu Y. N.: Proteomic analysis of cellular response to microcystin in human amnion FL cells. J. Proteome. Res. 4, 2207, (2005).
    • (2005) J. Proteome. Res , vol.4 , pp. 2207
    • Fu, W.Y.1    Xu, L.H.2    Yu, Y.N.3
  • 99
    • 4644220424 scopus 로고    scopus 로고
    • Proteomic identification of 14-3-3 sigma as a common component of the androgen receptor and the epidermal growth factor receptor signaling pathways of the human prostate epithelial cell line M12
    • Huang D., Liu X., Plymate S. R., Idowu M., Grimes M., Best A. M., McKinney J. L., Ware J. L.: Proteomic identification of 14-3-3 sigma as a common component of the androgen receptor and the epidermal growth factor receptor signaling pathways of the human prostate epithelial cell line M12. Oncogene 23, 6881, (2004).
    • (2004) Oncogene , vol.23 , pp. 6881
    • Huang, D.1    Liu, X.2    Plymate, S.R.3    Idowu, M.4    Grimes, M.5    Best, A.M.6    McKinney, J.L.7    Ware, J.L.8
  • 101
    • 15744376979 scopus 로고    scopus 로고
    • Signaling cascades activated upon antibody cross-linking of myelin oligodendrocyte glycoprotein: Potential implications for multiple sclerosis
    • Marta C. B., Montano M. B., Taylor C. M., Taylor A. L., Bansal R., Pfeiffer S. E.: Signaling cascades activated upon antibody cross-linking of myelin oligodendrocyte glycoprotein: potential implications for multiple sclerosis. J. Biol. Chem. 280, 8985, (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 8985
    • Marta, C.B.1    Montano, M.B.2    Taylor, C.M.3    Taylor, A.L.4    Bansal, R.5    Pfeiffer, S.E.6
  • 102
    • 4744350841 scopus 로고    scopus 로고
    • Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate
    • Ueda K., Kosako H., Fukui Y., Hattori S.: Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate. J. Biol. Chem. 279, 41815, (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 41815
    • Ueda, K.1    Kosako, H.2    Fukui, Y.3    Hattori, S.4
  • 104
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B., Kratchmarova I., Ong S. E., Nielsen M., Foster L. J., Mann M.: A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315, (2003).
    • (2003) Nat. Biotechnol , vol.21 , pp. 315
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 105
    • 4444243475 scopus 로고    scopus 로고
    • Quantitative proteomic and transcriptional analysis of the response to the p38 mitogen-activated protein kinase inhibitor SB203580 in transformed follicular lymphoma cells
    • Lin Z., Crockett D. K., Jenson S. D., Lim M. S., Elenitoba-Johnson K. S.: Quantitative proteomic and transcriptional analysis of the response to the p38 mitogen-activated protein kinase inhibitor SB203580 in transformed follicular lymphoma cells. Mol. Cell Proteomics 3, 820, (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 820
    • Lin, Z.1    Crockett, D.K.2    Jenson, S.D.3    Lim, M.S.4    Elenitoba-Johnson, K.S.5


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