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Volumn 12, Issue 2, 2013, Pages 866-882

Quantitative phosphoproteomic analysis of early alterations in protein phosphorylation by 2,3,7,8-tetrachlorodibenzo-p-dioxin

Author keywords

5L cells; ARNT; dioxin; GTPases; phosphoproteomics; protein phosphorylation; SILAC; SIMAC; TCDD; transcriptional regulation

Indexed keywords

2,3,7,8 TETRACHLORODIBENZO PARA DIOXIN; AROMATIC HYDROCARBON RECEPTOR; LYRIC PROTEIN; ONCOPROTEIN; PHOSPHOPROTEIN; SERINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ARNT; UNCLASSIFIED DRUG;

EID: 84873382627     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr3009429     Document Type: Article
Times cited : (6)

References (117)
  • 2
    • 71449114195 scopus 로고    scopus 로고
    • An overview of the effects of dioxins and dioxin-like compounds on vertebrates, as documented in human and ecological epidemiology
    • White, S. S.; Birnbaum, L. S. An overview of the effects of dioxins and dioxin-like compounds on vertebrates, as documented in human and ecological epidemiology J. Environ. Sci. Health, Part C: Environ. Carcinog. Ecotoxicol. Rev. 2009, 27, 197-211
    • (2009) J. Environ. Sci. Health, Part C: Environ. Carcinog. Ecotoxicol. Rev. , vol.27 , pp. 197-211
    • White, S.S.1    Birnbaum, L.S.2
  • 3
    • 34447511096 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor, more than a xenobiotic-interacting protein
    • Barouki, R.; Coumoul, X.; Fernandez-Salguero, P. M. The aryl hydrocarbon receptor, more than a xenobiotic-interacting protein FEBS Lett. 2007, 581, 3608-15
    • (2007) FEBS Lett. , vol.581 , pp. 3608-3615
    • Barouki, R.1    Coumoul, X.2    Fernandez-Salguero, P.M.3
  • 4
    • 0030245635 scopus 로고    scopus 로고
    • Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity
    • Fernandez-Salguero, P. M.; Hilbert, D. M.; Rudikoff, S.; Ward, J. M.; Gonzalez, F. J. Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity Toxicol. Appl. Pharmacol. 1996, 140, 173-9
    • (1996) Toxicol. Appl. Pharmacol. , vol.140 , pp. 173-179
    • Fernandez-Salguero, P.M.1    Hilbert, D.M.2    Rudikoff, S.3    Ward, J.M.4    Gonzalez, F.J.5
  • 5
    • 54349090870 scopus 로고    scopus 로고
    • Abnormal liver development and resistance to 2,3,7,8-tetrachlorodibenzo- p-dioxin toxicity in mice carrying a mutation in the DNA-binding domain of the aryl hydrocarbon receptor
    • Bunger, M. K.; Glover, E.; Moran, S. M.; Walisser, J. A.; Lahvis, G. P.; Hsu, E. L.; Bradfield, C. A. Abnormal liver development and resistance to 2,3,7,8-tetrachlorodibenzo-p-dioxin toxicity in mice carrying a mutation in the DNA-binding domain of the aryl hydrocarbon receptor Toxicol. Sci. 2008, 106, 83-92
    • (2008) Toxicol. Sci. , vol.106 , pp. 83-92
    • Bunger, M.K.1    Glover, E.2    Moran, S.M.3    Walisser, J.A.4    Lahvis, G.P.5    Hsu, E.L.6    Bradfield, C.A.7
  • 6
    • 0035977882 scopus 로고    scopus 로고
    • Molecular biology of the Ah receptor and its role in carcinogenesis
    • Safe, S. Molecular biology of the Ah receptor and its role in carcinogenesis Toxicol. Lett. 2001, 120, 1-7
    • (2001) Toxicol. Lett. , vol.120 , pp. 1-7
    • Safe, S.1
  • 10
    • 59149105386 scopus 로고    scopus 로고
    • The significance of the nongenomic pathway in mediating inflammatory signaling of the dioxin-activated Ah receptor to cause toxic effects
    • Matsumura, F. The significance of the nongenomic pathway in mediating inflammatory signaling of the dioxin-activated Ah receptor to cause toxic effects Biochem. Pharmacol. 2009, 77, 608-26
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 608-626
    • Matsumura, F.1
  • 11
    • 0028837970 scopus 로고
    • Evidence for a second pathway in the action mechanism of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Significance of Ah-receptor mediated activation of protein kinase under cell-free conditions
    • Enan, E.; Matsumura, F. Evidence for a second pathway in the action mechanism of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Significance of Ah-receptor mediated activation of protein kinase under cell-free conditions Biochem. Pharmacol. 1995, 49, 249-61
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 249-261
    • Enan, E.1    Matsumura, F.2
  • 12
    • 0342570229 scopus 로고
    • Heart as a target organ in 2,3,7,8-tetrachlorodibenzo-p-dioxin toxicity: Decreased beta-adrenergic responsiveness and evidence of increased intracellular calcium
    • Canga, L.; Levi, R.; Rifkind, A. B. Heart as a target organ in 2,3,7,8-tetrachlorodibenzo-p-dioxin toxicity: decreased beta-adrenergic responsiveness and evidence of increased intracellular calcium Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 905-9
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 905-909
    • Canga, L.1    Levi, R.2    Rifkind, A.B.3
  • 14
    • 0027731279 scopus 로고
    • 2,3,7,8-tetrachlorodibenzo-p-dioxin increases cardiac myocyte intracellular calcium and progressively impairs ventricular contractile responses to isoproterenol and to calcium in chick embryo hearts
    • Canga, L.; Paroli, L.; Blanck, T. J.; Silver, R. B.; Rifkind, A. B. 2,3,7,8-tetrachlorodibenzo-p-dioxin increases cardiac myocyte intracellular calcium and progressively impairs ventricular contractile responses to isoproterenol and to calcium in chick embryo hearts Mol. Pharmacol. 1993, 44, 1142-51
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1142-1151
    • Canga, L.1    Paroli, L.2    Blanck, T.J.3    Silver, R.B.4    Rifkind, A.B.5
  • 15
    • 0030220845 scopus 로고    scopus 로고
    • Stimulation of calcium uptake in cultured rat hippocampal neurons by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Hanneman, W. H.; Legare, M. E.; Barhoumi, R.; Burghardt, R. C.; Safe, S.; Tiffany-Castiglioni, E. Stimulation of calcium uptake in cultured rat hippocampal neurons by 2,3,7,8-tetrachlorodibenzo-p-dioxin Toxicology 1996, 112, 19-28
    • (1996) Toxicology , vol.112 , pp. 19-28
    • Hanneman, W.H.1    Legare, M.E.2    Barhoumi, R.3    Burghardt, R.C.4    Safe, S.5    Tiffany-Castiglioni, E.6
  • 17
    • 39749102799 scopus 로고    scopus 로고
    • Neuronal activity enhances aryl hydrocarbon receptor-mediated gene expression and dioxin neurotoxicity in cortical neurons
    • Lin, C.-H.; Juan, S.-H.; Wang, C. Y.; Sun, Y.-Y.; Chou, C.-M.; Chang, S.-F.; Hu, S.-Y.; Lee, W.-S.; Lee, Y.-H. Neuronal activity enhances aryl hydrocarbon receptor-mediated gene expression and dioxin neurotoxicity in cortical neurons J. Neurochem. 2008, 104, 1415-29
    • (2008) J. Neurochem. , vol.104 , pp. 1415-1429
    • Lin, C.-H.1    Juan, S.-H.2    Wang, C.Y.3    Sun, Y.-Y.4    Chou, C.-M.5    Chang, S.-F.6    Hu, S.-Y.7    Lee, W.-S.8    Lee, Y.-H.9
  • 18
    • 0026648792 scopus 로고
    • Dioxin induces expression of c-fos and c-jun proto-oncogenes and a large increase in transcription factor AP-1
    • Puga, A.; Nebert, D. W.; Carrier, F. Dioxin induces expression of c-fos and c-jun proto-oncogenes and a large increase in transcription factor AP-1 DNA Cell Biol. 1992, 11, 269-81
    • (1992) DNA Cell Biol. , vol.11 , pp. 269-281
    • Puga, A.1    Nebert, D.W.2    Carrier, F.3
  • 19
    • 0030694636 scopus 로고    scopus 로고
    • Sustained increase in intracellular free calcium and activation of cyclooxygenase-2 expression in mouse hepatoma cells treated with dioxin
    • Puga, A.; Hoffer, A.; Zhou, S.; Bohm, J. M.; Leikauf, G. D.; Shertzer, H. G. Sustained increase in intracellular free calcium and activation of cyclooxygenase-2 expression in mouse hepatoma cells treated with dioxin Biochem. Pharmacol. 1997, 54, 1287-96
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 1287-1296
    • Puga, A.1    Hoffer, A.2    Zhou, S.3    Bohm, J.M.4    Leikauf, G.D.5    Shertzer, H.G.6
  • 20
    • 40849088103 scopus 로고    scopus 로고
    • Dioxin-mediated up-regulation of aryl hydrocarbon receptor target genes is dependent on the calcium/calmodulin/CaMKIalpha pathway
    • Monteiro, P.; Gilot, D.; Le Ferrec, E.; Rauch, C.; Lagadic-Gossmann, D.; Fardel, O. Dioxin-mediated up-regulation of aryl hydrocarbon receptor target genes is dependent on the calcium/calmodulin/CaMKIalpha pathway Mol. Pharmacol. 2008, 73, 769-77
    • (2008) Mol. Pharmacol. , vol.73 , pp. 769-777
    • Monteiro, P.1    Gilot, D.2    Le Ferrec, E.3    Rauch, C.4    Lagadic-Gossmann, D.5    Fardel, O.6
  • 21
    • 45749119506 scopus 로고    scopus 로고
    • Roles of cytosolic phospholipase A2 and Src kinase in the early action of 2,3,7,8-tetrachlorodibenzo-p-dioxin through a nongenomic pathway in MCF10A cells
    • Dong, B.; Matsumura, F. Roles of cytosolic phospholipase A2 and Src kinase in the early action of 2,3,7,8-tetrachlorodibenzo-p-dioxin through a nongenomic pathway in MCF10A cells Mol. Pharmacol. 2008, 74, 255-63
    • (2008) Mol. Pharmacol. , vol.74 , pp. 255-263
    • Dong, B.1    Matsumura, F.2
  • 22
    • 58849106775 scopus 로고    scopus 로고
    • Significance of the nongenomic, inflammatory pathway in mediating the toxic action of TCDD to induce rapid and long-term cellular responses in 3T3-L1 adipocytes
    • Li, W.; Matsumura, F. Significance of the nongenomic, inflammatory pathway in mediating the toxic action of TCDD to induce rapid and long-term cellular responses in 3T3-L1 adipocytes Biochemistry 2008, 47, 13997-4008
    • (2008) Biochemistry , vol.47 , pp. 13997-14008
    • Li, W.1    Matsumura, F.2
  • 23
    • 70449658819 scopus 로고    scopus 로고
    • TCDD-induced cyclooxygenase-2 expression is mediated by the nongenomic pathway in mouse MMDD1 macula densa cells and kidneys
    • Dong, B.; Nishimura, N.; Vogel, C. F.; Tohyama, C.; Matsumura, F. TCDD-induced cyclooxygenase-2 expression is mediated by the nongenomic pathway in mouse MMDD1 macula densa cells and kidneys Biochem. Pharmacol. 2010, 79, 487-97
    • (2010) Biochem. Pharmacol. , vol.79 , pp. 487-497
    • Dong, B.1    Nishimura, N.2    Vogel, C.F.3    Tohyama, C.4    Matsumura, F.5
  • 24
    • 60649085971 scopus 로고    scopus 로고
    • Characterization of the pattern of the nongenomic signaling pathway through which TCDD-induces early inflammatory responses in U937 human macrophages
    • Sciullo, E. M.; Dong, B.; Vogel, C. F. A.; Matsumura, F. Characterization of the pattern of the nongenomic signaling pathway through which TCDD-induces early inflammatory responses in U937 human macrophages Chemosphere 2009, 74, 1531-7
    • (2009) Chemosphere , vol.74 , pp. 1531-1537
    • Sciullo, E.M.1    Dong, B.2    Vogel, C.F.A.3    Matsumura, F.4
  • 25
    • 12844257378 scopus 로고    scopus 로고
    • Studies on the mechanism of rapid activation of protein tyrosine phosphorylation activities, particularly c-Src kinase, by TCDD in MCF10A
    • Mazina, O.; Park, S.; Sano, H.; Wong, P.; Matsumura, F. Studies on the mechanism of rapid activation of protein tyrosine phosphorylation activities, particularly c-Src kinase, by TCDD in MCF10A J. Biochem. Mol. Toxicol. 2004, 18, 313-21
    • (2004) J. Biochem. Mol. Toxicol. , vol.18 , pp. 313-321
    • Mazina, O.1    Park, S.2    Sano, H.3    Wong, P.4    Matsumura, F.5
  • 28
    • 0029125761 scopus 로고
    • Human calcium-calmodulin dependent protein kinase I: CDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase i kinase
    • Haribabu, B.; Hook, S. S.; Selbert, M. A.; Goldstein, E. G.; Tomhave, E. D.; Edelman, A. M.; Snyderman, R.; Means, A. R. Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase EMBO J. 1995, 14, 3679-86
    • (1995) EMBO J. , vol.14 , pp. 3679-3686
    • Haribabu, B.1    Hook, S.S.2    Selbert, M.A.3    Goldstein, E.G.4    Tomhave, E.D.5    Edelman, A.M.6    Snyderman, R.7    Means, A.R.8
  • 29
    • 0025676130 scopus 로고
    • Inhibition of growth by 2,3,7,8-tetrachlorodibenzo-p-dioxin in 5L rat hepatoma cells is associated with the presence of Ah receptor
    • Göttlicher, M.; Cikryt, P.; Wiebel, F. J. Inhibition of growth by 2,3,7,8-tetrachlorodibenzo-p-dioxin in 5L rat hepatoma cells is associated with the presence of Ah receptor Carcinogenesis 1990, 11, 2205-10
    • (1990) Carcinogenesis , vol.11 , pp. 2205-2210
    • Göttlicher, M.1    Cikryt, P.2    Wiebel, F.J.3
  • 30
    • 0026316443 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin causes unbalanced growth in 5L rat hepatoma cells
    • Göttlicher, M.; Wiebel, F. J. 2,3,7,8-Tetrachlorodibenzo-p-dioxin causes unbalanced growth in 5L rat hepatoma cells Toxicol. Appl. Pharmacol. 1991, 111, 496-503
    • (1991) Toxicol. Appl. Pharmacol. , vol.111 , pp. 496-503
    • Göttlicher, M.1    Wiebel, F.J.2
  • 31
    • 0026021837 scopus 로고
    • Toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin in vitro: H4IIEC3-derived 5L hepatoma cells as a model system
    • Wiebel, F. J.; Klose, U.; Kiefer, F. Toxicity of 2,3,7,8- tetrachlorodibenzo-p-dioxin in vitro: H4IIEC3-derived 5L hepatoma cells as a model system Toxicol. Lett. 1991, 55, 161-9
    • (1991) Toxicol. Lett. , vol.55 , pp. 161-169
    • Wiebel, F.J.1    Klose, U.2    Kiefer, F.3
  • 33
    • 0001459262 scopus 로고    scopus 로고
    • Complementation of Ah receptor deficiency in hepatoma cells: Negative feedback regulation and cell cycle control by the Ah receptor
    • Weiss, C.; Kolluri, S. K.; Kiefer, F.; Göttlicher, M. Complementation of Ah receptor deficiency in hepatoma cells: negative feedback regulation and cell cycle control by the Ah receptor Exp. Cell Res. 1996, 226, 154-63
    • (1996) Exp. Cell Res. , vol.226 , pp. 154-163
    • Weiss, C.1    Kolluri, S.K.2    Kiefer, F.3    Göttlicher, M.4
  • 34
    • 0032575589 scopus 로고    scopus 로고
    • A direct interaction between the aryl hydrocarbon receptor and retinoblastoma protein. Linking dioxin signaling to the cell cycle
    • Ge, N. L.; Elferink, C. J. A direct interaction between the aryl hydrocarbon receptor and retinoblastoma protein. Linking dioxin signaling to the cell cycle J. Biol. Chem. 1998, 273, 22708-13
    • (1998) J. Biol. Chem. , vol.273 , pp. 22708-22713
    • Ge, N.L.1    Elferink, C.J.2
  • 35
    • 0032841577 scopus 로고    scopus 로고
    • Suppression of cell cycle progression by flavonoids: Dependence on the aryl hydrocarbon receptor
    • Reiners, J.; J J; Clift, R.; Mathieu, P. Suppression of cell cycle progression by flavonoids: Dependence on the aryl hydrocarbon receptor Carcinogenesis 1999, 20, 1561-6
    • (1999) Carcinogenesis , vol.20 , pp. 1561-1566
    • Reiners, J.J.J.1    Clift, R.2    Mathieu, P.3
  • 36
    • 0035065262 scopus 로고    scopus 로고
    • Maximal aryl hydrocarbon receptor activity depends on an interaction with the retinoblastoma protein
    • Elferink, C. J.; Ge, N. L.; Levine, A. Maximal aryl hydrocarbon receptor activity depends on an interaction with the retinoblastoma protein Mol. Pharmacol. 2001, 59, 664-73
    • (2001) Mol. Pharmacol. , vol.59 , pp. 664-673
    • Elferink, C.J.1    Ge, N.L.2    Levine, A.3
  • 37
    • 1642579495 scopus 로고    scopus 로고
    • Cytochrome P4501A1 promotes G1 phase cell cycle progression by controlling aryl hydrocarbon receptor activity
    • Levine-Fridman, A.; Chen, L.; Elferink, C. J. Cytochrome P4501A1 promotes G1 phase cell cycle progression by controlling aryl hydrocarbon receptor activity Mol. Pharmacol. 2004, 65, 461-9
    • (2004) Mol. Pharmacol. , vol.65 , pp. 461-469
    • Levine-Fridman, A.1    Chen, L.2    Elferink, C.J.3
  • 38
    • 17744408754 scopus 로고    scopus 로고
    • Contribution of the Ah receptor to the phenolic antioxidant-mediated expression of human and rat UDP-glucuronosyltransferase UGT1A6 in Caco-2 and rat hepatoma 5L cells
    • Münzel, P. A.; Schmohl, S.; Buckler, F.; Jaehrling, J.; Raschko, F. T.; Köhle, C.; Bock, K. W. Contribution of the Ah receptor to the phenolic antioxidant-mediated expression of human and rat UDP-glucuronosyltransferase UGT1A6 in Caco-2 and rat hepatoma 5L cells Biochem. Pharmacol. 2003, 66, 841-7
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 841-847
    • Münzel, P.A.1    Schmohl, S.2    Buckler, F.3    Jaehrling, J.4    Raschko, F.T.5    Köhle, C.6    Bock, K.W.7
  • 39
    • 43849083916 scopus 로고    scopus 로고
    • Cytochrome P450 2C11 5′-flanking region and promoter: Regulation by aromatic hydrocarbons in vitro
    • Sawaya, R. M.; Riddick, D. S. Cytochrome P450 2C11 5′-flanking region and promoter: Regulation by aromatic hydrocarbons in vitro Toxicology 2008, 248, 104-12
    • (2008) Toxicology , vol.248 , pp. 104-112
    • Sawaya, R.M.1    Riddick, D.S.2
  • 42
    • 0035576809 scopus 로고    scopus 로고
    • Novel target genes of the Ah (dioxin) receptor: Transcriptional induction of N-myristoyltransferase 2
    • Kolluri, S. K.; Balduf, C.; Hofmann, M.; Göttlicher, M. Novel target genes of the Ah (dioxin) receptor: transcriptional induction of N-myristoyltransferase 2 Cancer Res. 2001, 61, 8534-9
    • (2001) Cancer Res. , vol.61 , pp. 8534-8539
    • Kolluri, S.K.1    Balduf, C.2    Hofmann, M.3    Göttlicher, M.4
  • 43
    • 0033166447 scopus 로고    scopus 로고
    • P27(Kip1) induction and inhibition of proliferation by the intracellular Ah receptor in developing thymus and hepatoma cells
    • Kolluri, S. K.; Weiss, C.; Koff, A.; Göttlicher, M. p27(Kip1) induction and inhibition of proliferation by the intracellular Ah receptor in developing thymus and hepatoma cells Genes Dev. 1999, 13, 1742-53
    • (1999) Genes Dev. , vol.13 , pp. 1742-1753
    • Kolluri, S.K.1    Weiss, C.2    Koff, A.3    Göttlicher, M.4
  • 45
    • 0001315455 scopus 로고
    • A transplantable bile-secreting hepatocellular carcinoma in the rat
    • Reuber, M. D. A transplantable bile-secreting hepatocellular carcinoma in the rat J. Natl. Cancer Inst. 1961, 26, 891-9
    • (1961) J. Natl. Cancer Inst. , vol.26 , pp. 891-899
    • Reuber, M.D.1
  • 46
    • 34548356772 scopus 로고    scopus 로고
    • An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics
    • Van Hoof, D.; Pinkse, M. W. H.; Oostwaard, D. W.-V.; Mummery, C. L.; Heck, A. J. R.; Krijgsveld, J. An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics Nat. Methods 2007, 4, 677-8
    • (2007) Nat. Methods , vol.4 , pp. 677-678
    • Van Hoof, D.1    Pinkse, M.W.H.2    Oostwaard, D.W.-V.3    Mummery, C.L.4    Heck, A.J.R.5    Krijgsveld, J.6
  • 47
    • 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 2008, 7, 661-71
    • (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
  • 48
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom, J.; Nordhoff, E.; Mirgorodskaya, E.; Ekman, R.; Roepstorff, P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry J. Mass Spectrom. 1999, 34, 105-16
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 49
    • 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. D. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns Mol. Cell. Proteomics 2005, 4, 873-86
    • (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.D.5
  • 50
    • 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 Commun. Mass Spectrom. 2007, 21, 3635-45
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3635-3645
    • Jensen, S.S.1    Larsen, M.R.2
  • 51
    • 3042824849 scopus 로고    scopus 로고
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry
    • Schroeder, M. J.; Shabanowitz, J.; Schwartz, J. C.; Hunt, D. F.; Coon, J. J. A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry Anal. Chem. 2004, 76, 3590-8
    • (2004) Anal. Chem. , vol.76 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 53
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • Olsen, J. V.; Mann, M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 13417-22
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 54
    • 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.; Mann, M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 2006, 127, 635-48
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 55
    • 0019219257 scopus 로고
    • A rapid method for assaying the metabolism of 7-ethoxyresorufin by microsomal subcellular fractions
    • Pohl, R. J.; Fouts, J. R. A rapid method for assaying the metabolism of 7-ethoxyresorufin by microsomal subcellular fractions Anal. Biochem. 1980, 107, 150-5
    • (1980) Anal. Biochem. , vol.107 , pp. 150-155
    • Pohl, R.J.1    Fouts, J.R.2
  • 56
    • 0031669934 scopus 로고    scopus 로고
    • Establishment of a simple cleanup procedure and bioassay for determining 2,3,7,8-tetrachlorodibenzo-p-dioxin toxicity equivalents of environmental samples
    • Schwirzer, S. M.; Hofmaier, A. M.; Kettrup, A.; Nerdinger, P. E.; Schramm, K. W.; Thoma, H.; Wegenke, M.; Wiebel, F. J. Establishment of a simple cleanup procedure and bioassay for determining 2,3,7,8-tetrachlorodibenzo-p- dioxin toxicity equivalents of environmental samples Ecotoxicol. Environ. Saf. 1998, 41, 77-82
    • (1998) Ecotoxicol. Environ. Saf. , vol.41 , pp. 77-82
    • Schwirzer, S.M.1    Hofmaier, A.M.2    Kettrup, A.3    Nerdinger, P.E.4    Schramm, K.W.5    Thoma, H.6    Wegenke, M.7    Wiebel, F.J.8
  • 59
    • 0032765048 scopus 로고    scopus 로고
    • Signaling from beta-adrenoceptor to L-type calcium channel: Identification of a novel cardiac protein kinase A target possessing similarities to AHNAK
    • Haase, H.; Podzuweit, T.; Lutsch, G.; Hohaus, A.; Kostka, S.; Lindschau, C.; Kott, M.; Kraft, R.; Morano, I. Signaling from beta-adrenoceptor to L-type calcium channel: identification of a novel cardiac protein kinase A target possessing similarities to AHNAK FASEB J. 1999, 13, 2161-72
    • (1999) FASEB J. , vol.13 , pp. 2161-2172
    • Haase, H.1    Podzuweit, T.2    Lutsch, G.3    Hohaus, A.4    Kostka, S.5    Lindschau, C.6    Kott, M.7    Kraft, R.8    Morano, I.9
  • 61
    • 1842529581 scopus 로고    scopus 로고
    • Calcium current in rat cardiomyocytes is modulated by the carboxyl-terminal ahnak domain
    • Alvarez, J.; Hamplova, J.; Hohaus, A.; Morano, I.; Haase, H.; Vassort, G. Calcium current in rat cardiomyocytes is modulated by the carboxyl-terminal ahnak domain J. Biol. Chem. 2004, 279, 12456-61
    • (2004) J. Biol. Chem. , vol.279 , pp. 12456-12461
    • Alvarez, J.1    Hamplova, J.2    Hohaus, A.3    Morano, I.4    Haase, H.5    Vassort, G.6
  • 64
    • 0033003606 scopus 로고    scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD)-mediated membrane translocation of c-Src protein kinase in liver WB-F344 cells
    • Kohle, C.; Gschaidmeier, H.; Lauth, D.; Topell, S.; Zitzer, H.; Bock, K. W. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD)-mediated membrane translocation of c-Src protein kinase in liver WB-F344 cells Arch. Toxicol. 1999, 73, 152-8
    • (1999) Arch. Toxicol. , vol.73 , pp. 152-158
    • Kohle, C.1    Gschaidmeier, H.2    Lauth, D.3    Topell, S.4    Zitzer, H.5    Bock, K.W.6
  • 65
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas, S. M.; Brugge, J. S. Cellular functions regulated by Src family kinases Annu. Rev. Cell. Dev. Biol. 1997, 13, 513-609
    • (1997) Annu. Rev. Cell. Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 66
    • 0031012543 scopus 로고    scopus 로고
    • Peroxovanadate induces tyrosine phosphorylation of multiple signaling proteins in mouse liver and kidney
    • Ruff, S. J.; Chen, K.; Cohen, S. Peroxovanadate induces tyrosine phosphorylation of multiple signaling proteins in mouse liver and kidney J. Biol. Chem. 1997, 272, 1263-7
    • (1997) J. Biol. Chem. , vol.272 , pp. 1263-1267
    • Ruff, S.J.1    Chen, K.2    Cohen, S.3
  • 67
    • 27544451272 scopus 로고    scopus 로고
    • Phosphorylation inhibits DNA-binding of alternatively spliced aryl hydrocarbon receptor nuclear translocator
    • Kewley, R. J.; Whitelaw, M. L. Phosphorylation inhibits DNA-binding of alternatively spliced aryl hydrocarbon receptor nuclear translocator Biochem. Biophys. Res. Commun. 2005, 338, 660-7
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 660-667
    • Kewley, R.J.1    Whitelaw, M.L.2
  • 69
    • 0035798677 scopus 로고    scopus 로고
    • The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically
    • Huffman, J. L.; Mokashi, A.; Bächinger, H. P.; Brennan, R. G. The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically J. Biol. Chem. 2001, 276, 40537-44
    • (2001) J. Biol. Chem. , vol.276 , pp. 40537-40544
    • Huffman, J.L.1    Mokashi, A.2    Bächinger, H.P.3    Brennan, R.G.4
  • 70
    • 0027403810 scopus 로고
    • Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor
    • Whitelaw, M.; Pongratz, I.; Wilhelmsson, A.; Gustafsson, J. A.; Poellinger, L. Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor Mol. Cell. Biol. 1993, 13, 2504-14
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2504-2514
    • Whitelaw, M.1    Pongratz, I.2    Wilhelmsson, A.3    Gustafsson, J.A.4    Poellinger, L.5
  • 71
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy
    • Xue, Y.; Ren, J.; Gao, X.; Jin, C.; Wen, L.; Yao, X. GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy Mol. Cell. Proteomics 2008, 7, 1598-1608
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1598-1608
    • Xue, Y.1    Ren, J.2    Gao, X.3    Jin, C.4    Wen, L.5    Yao, X.6
  • 73
    • 23944453389 scopus 로고    scopus 로고
    • Global phosphoproteome of HT-29 human colon adenocarcinoma cells
    • Kim, J.-E.; Tannenbaum, S. R.; White, F. M. Global phosphoproteome of HT-29 human colon adenocarcinoma cells J. Proteome Res. 2005, 4, 1339-46
    • (2005) J. Proteome Res. , vol.4 , pp. 1339-1346
    • Kim, J.-E.1    Tannenbaum, S.R.2    White, F.M.3
  • 74
    • 36348937958 scopus 로고    scopus 로고
    • Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra
    • Yu, L.-R.; Zhu, Z.; Chan, K. C.; Issaq, H. J.; Dimitrov, D. S.; Veenstra, T. D. Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra J. Proteome Res. 2007, 6, 4150-62
    • (2007) J. Proteome Res. , vol.6 , pp. 4150-4162
    • Yu, L.-R.1    Zhu, Z.2    Chan, K.C.3    Issaq, H.J.4    Dimitrov, D.S.5    Veenstra, T.D.6
  • 75
    • 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. U.S.A. 2007, 104, 2199-204
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 77
    • 66349106471 scopus 로고    scopus 로고
    • Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach
    • Gauci, S.; Helbig, A. O.; Slijper, M.; Krijgsveld, J.; Heck, A. J. R.; Mohammed, S. Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach Anal. Chem. 2009, 81, 4493-501
    • (2009) Anal. Chem. , vol.81 , pp. 4493-4501
    • Gauci, S.1    Helbig, A.O.2    Slijper, M.3    Krijgsveld, J.4    Heck, A.J.R.5    Mohammed, S.6
  • 78
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • Mayya, V.; Lundgren, D. H.; Hwang, S.-I.; Rezaul, K.; Wu, L.; Eng, J. K.; Rodionov, V.; Han, D. K. Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions Sci. Signal. 2009, 2, ra46
    • (2009) Sci. Signal. , vol.2 , pp. 46
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.-I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 79
  • 80
    • 47749150659 scopus 로고    scopus 로고
    • Phosphorylation at Ser473 regulates heterochromatin protein 1 binding and corepressor function of TIF1beta/KAP1
    • Chang, C.-W.; Chou, H.-Y.; Lin, Y.-S.; Huang, K.-H.; Chang, C.-J.; Hsu, T.-C.; Lee, S.-C. Phosphorylation at Ser473 regulates heterochromatin protein 1 binding and corepressor function of TIF1beta/KAP1 BMC Mol. Biol. 2008, 9, 61
    • (2008) BMC Mol. Biol. , vol.9 , pp. 61
    • Chang, C.-W.1    Chou, H.-Y.2    Lin, Y.-S.3    Huang, K.-H.4    Chang, C.-J.5    Hsu, T.-C.6    Lee, S.-C.7
  • 82
    • 0036404933 scopus 로고    scopus 로고
    • 2,3,7,8-tetrachlorodibenzo-p-dioxin-dependent release from contact inhibition in WB-F344 cells: Involvement of cyclin A
    • Dietrich, C.; Faust, D.; Budt, S.; Moskwa, M.; Kunz, A.; Bock, K.-W.; Oesch, F. 2,3,7,8-tetrachlorodibenzo-p-dioxin-dependent release from contact inhibition in WB-F344 cells: Involvement of cyclin A Toxicol. Appl. Pharmacol. 2002, 183, 117-26
    • (2002) Toxicol. Appl. Pharmacol. , vol.183 , pp. 117-126
    • Dietrich, C.1    Faust, D.2    Budt, S.3    Moskwa, M.4    Kunz, A.5    Bock, K.-W.6    Oesch, F.7
  • 83
    • 0026021837 scopus 로고
    • Toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin in vitro: H4IIEC3-derived 5L hepatoma cells as a model system
    • Wiebel, F. J.; Klose, U.; Kiefer, F. Toxicity of 2,3,7,8- tetrachlorodibenzo-p-dioxin in vitro: H4IIEC3-derived 5L hepatoma cells as a model system Toxicol. Lett. 1991, 55, 161-9
    • (1991) Toxicol. Lett. , vol.55 , pp. 161-169
    • Wiebel, F.J.1    Klose, U.2    Kiefer, F.3
  • 84
    • 33646252021 scopus 로고    scopus 로고
    • Quantitative analysis of 2,3,7,8-tetrachlorodibenzo- p -dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels
    • Sarioglu, H.; Brandner, S.; Jacobsen, C.; Meindl, T.; Schmidt, A.; Kellermann, J.; Lottspeich, F.; Andrae, U. Quantitative analysis of 2,3,7,8-tetrachlorodibenzo- p -dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels Proteomics 2006, 6, 2407-21
    • (2006) Proteomics , vol.6 , pp. 2407-2421
    • Sarioglu, H.1    Brandner, S.2    Jacobsen, C.3    Meindl, T.4    Schmidt, A.5    Kellermann, J.6    Lottspeich, F.7    Andrae, U.8
  • 85
    • 0034704078 scopus 로고    scopus 로고
    • A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1
    • Underhill, C.; Qutob, M. S.; Yee, S. P.; Torchia, J. A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1 J. Biol. Chem. 2000, 275, 40463-70
    • (2000) J. Biol. Chem. , vol.275 , pp. 40463-40470
    • Underhill, C.1    Qutob, M.S.2    Yee, S.P.3    Torchia, J.4
  • 87
    • 42949170563 scopus 로고    scopus 로고
    • Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column
    • Imami, K.; Sugiyama, N.; Kyono, Y.; Tomita, M.; Ishihama, Y. Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column Anal. Sci. 2008, 24, 161-6
    • (2008) Anal. Sci. , vol.24 , pp. 161-166
    • Imami, K.1    Sugiyama, N.2    Kyono, Y.3    Tomita, M.4    Ishihama, Y.5
  • 88
    • 33746403681 scopus 로고    scopus 로고
    • Controlling the elongation phase of transcription with P-TEFb
    • Peterlin, B. M.; Price, D. H. Controlling the elongation phase of transcription with P-TEFb Mol. Cell 2006, 23, 297-305
    • (2006) Mol. Cell , vol.23 , pp. 297-305
    • Peterlin, B.M.1    Price, D.H.2
  • 89
    • 34247552158 scopus 로고    scopus 로고
    • NELF interacts with CBC and participates in 3′ end processing of replication-dependent histone mRNAs
    • Narita, T.; Yung, T. M. C.; Yamamoto, J.; Tsuboi, Y.; Tanabe, H.; Tanaka, K.; Yamaguchi, Y.; Handa, H. NELF interacts with CBC and participates in 3′ end processing of replication-dependent histone mRNAs Mol. Cell 2007, 26, 349-65
    • (2007) Mol. Cell , vol.26 , pp. 349-365
    • Narita, T.1    Yung, T.M.C.2    Yamamoto, J.3    Tsuboi, Y.4    Tanabe, H.5    Tanaka, K.6    Yamaguchi, Y.7    Handa, H.8
  • 90
    • 0242498382 scopus 로고    scopus 로고
    • Interactions between the aryl hydrocarbon receptor and P-TEFb. Sequential recruitment of transcription factors and differential phosphorylation of C-terminal domain of RNA polymerase II at cyp1a1 promoter
    • Tian, Y.; Ke, S.; Chen, M.; Sheng, T. Interactions between the aryl hydrocarbon receptor and P-TEFb. Sequential recruitment of transcription factors and differential phosphorylation of C-terminal domain of RNA polymerase II at cyp1a1 promoter J. Biol. Chem. 2003, 278, 44041-8
    • (2003) J. Biol. Chem. , vol.278 , pp. 44041-44048
    • Tian, Y.1    Ke, S.2    Chen, M.3    Sheng, T.4
  • 91
    • 0031452275 scopus 로고    scopus 로고
    • GEFs, GAPs, GDIs, and effectors: Taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins
    • Geyer, M.; Wittinghofer, A. GEFs, GAPs, GDIs, and effectors: Taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins Curr. Opin. Struct. Biol. 1997, 7, 786-92
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 786-792
    • Geyer, M.1    Wittinghofer, A.2
  • 92
    • 39749127706 scopus 로고    scopus 로고
    • Analysis of 2,3,7,8-tetrachlorodibenzo- p -dioxin-induced proteome changes in 5L rat hepatoma cells reveals novel targets of dioxin action including the mitochondrial apoptosis regulator VDAC2
    • Sarioglu, H.; Brandner, S.; Haberger, M.; Jacobsen, C.; Lichtmannegger, J.; Wormke, M.; Andrae, U. Analysis of 2,3,7,8-tetrachlorodibenzo- p -dioxin-induced proteome changes in 5L rat hepatoma cells reveals novel targets of dioxin action including the mitochondrial apoptosis regulator VDAC2 Mol. Cell. Proteomics 2008, 7, 394-410
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 394-410
    • Sarioglu, H.1    Brandner, S.2    Haberger, M.3    Jacobsen, C.4    Lichtmannegger, J.5    Wormke, M.6    Andrae, U.7
  • 93
    • 0038071660 scopus 로고    scopus 로고
    • Isolation of the novel human guanine nucleotide exchange factor Src homology 3 domain-containing guanine nucleotide exchange factor (SGEF) and of C-terminal SGEF, an N-terminally truncated form of SGEF, the expression of which is regulated by androgen in prostate cancer cells
    • Qi, H.; Fournier, A.; Grenier, J.; Fillion, C.; Labrie, Y.; Labrie, C. Isolation of the novel human guanine nucleotide exchange factor Src homology 3 domain-containing guanine nucleotide exchange factor (SGEF) and of C-terminal SGEF, an N-terminally truncated form of SGEF, the expression of which is regulated by androgen in prostate cancer cells Endocrinology 2003, 144, 1742-52
    • (2003) Endocrinology , vol.144 , pp. 1742-1752
    • Qi, H.1    Fournier, A.2    Grenier, J.3    Fillion, C.4    Labrie, Y.5    Labrie, C.6
  • 96
    • 33645779696 scopus 로고    scopus 로고
    • Beyond linker histones and high mobility group proteins: Global profiling of perchloric acid soluble proteins
    • Zougman, A.; Wiśniewski, J. R. Beyond linker histones and high mobility group proteins: global profiling of perchloric acid soluble proteins J. Proteome Res. 2006, 5, 925-34
    • (2006) J. Proteome Res. , vol.5 , pp. 925-934
    • Zougman, A.1    Wiśniewski, J.R.2
  • 97
    • 67649390779 scopus 로고    scopus 로고
    • Hematopoietic- and neurologic-expressed sequence 1 (Hn1) depletion in B16.F10 melanoma cells promotes a differentiated phenotype that includes increased melanogenesis and cell cycle arrest
    • Laughlin, K. M.; Luo, D.; Liu, C.; Shaw, G.; Warrington, J.; Kenneth, H.; Law, B. K.; Harrison, J. K. Hematopoietic- and neurologic-expressed sequence 1 (Hn1) depletion in B16.F10 melanoma cells promotes a differentiated phenotype that includes increased melanogenesis and cell cycle arrest Differentiation 2009, 78, 35-44
    • (2009) Differentiation , vol.78 , pp. 35-44
    • Laughlin, K.M.1    Luo, D.2    Liu, C.3    Shaw, G.4    Warrington, J.5    Kenneth, H.6    Law, B.K.7    Harrison, J.K.8
  • 102
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru, G.; Graumann, J.; Smith, G. T.; Kolawa, N. J.; Fang, R.; Deshaies, R. J. UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover Cell 2008, 134, 804-16
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 103
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
    • Ye, Y. Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase J. Struct. Biol. 2006, 156, 29-40
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 105
    • 41649108038 scopus 로고    scopus 로고
    • Significance of prolyl hydroxylase 2 in the interference of aryl hydrocarbon receptor and hypoxia-inducible factor-1 alpha signaling
    • Seifert, A.; Katschinski, D. M.; Tonack, S.; Fischer, B.; Navarrete Santos, A. Significance of prolyl hydroxylase 2 in the interference of aryl hydrocarbon receptor and hypoxia-inducible factor-1 alpha signaling Chem. Res. Toxicol. 2008, 21, 341-8
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 341-348
    • Seifert, A.1    Katschinski, D.M.2    Tonack, S.3    Fischer, B.4    Navarrete Santos, A.5
  • 107
    • 70349148185 scopus 로고    scopus 로고
    • Roles of Ca(v) channels and AHNAK1 in T cells: The beauty and the beast
    • Matza, D.; Flavell, R. A. Roles of Ca(v) channels and AHNAK1 in T cells: the beauty and the beast Immunol. Rev. 2009, 231, 257-64
    • (2009) Immunol. Rev. , vol.231 , pp. 257-264
    • Matza, D.1    Flavell, R.A.2
  • 109
    • 0347753248 scopus 로고    scopus 로고
    • AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture
    • Benaud, C.; Gentil, B. J.; Assard, N.; Court, M.; Garin, J.; Delphin, C.; Baudier, J. AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture J. Cell Biol. 2004, 164, 133-44
    • (2004) J. Cell Biol. , vol.164 , pp. 133-144
    • Benaud, C.1    Gentil, B.J.2    Assard, N.3    Court, M.4    Garin, J.5    Delphin, C.6    Baudier, J.7
  • 110
    • 1642488945 scopus 로고    scopus 로고
    • The AHNAKs are a class of giant propeller-like proteins that associate with calcium channel proteins of cardiomyocytes and other cells
    • Komuro, A.; Masuda, Y.; Kobayashi, K.; Babbitt, R.; Gunel, M.; Flavell, R. A.; Marchesi, V. T. The AHNAKs are a class of giant propeller-like proteins that associate with calcium channel proteins of cardiomyocytes and other cells Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 4053-8
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 4053-4058
    • Komuro, A.1    Masuda, Y.2    Kobayashi, K.3    Babbitt, R.4    Gunel, M.5    Flavell, R.A.6    Marchesi, V.T.7
  • 111
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim, E.; Sheng, M. PDZ domain proteins of synapses Nat. Rev. Neurosci. 2004, 5, 771-81
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 113
    • 72249101914 scopus 로고    scopus 로고
    • Astrocyte elevated gene-1: Far more than just a gene regulated in astrocytes
    • Sarkar, D.; Emdad, L.; Lee, S.-G.; Yoo, B. K.; Su, Z.-Z.; Fisher, P. B. Astrocyte elevated gene-1: far more than just a gene regulated in astrocytes Cancer Res. 2009, 69, 8529-35
    • (2009) Cancer Res. , vol.69 , pp. 8529-8535
    • Sarkar, D.1    Emdad, L.2    Lee, S.-G.3    Yoo, B.K.4    Su, Z.-Z.5    Fisher, P.B.6
  • 115
    • 55249104113 scopus 로고    scopus 로고
    • Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis
    • Zhou, H.; Ye, M.; Dong, J.; Han, G.; Jiang, X.; Wu, R.; Zou, H. Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis J. Proteome Res. 2008, 7, 3957-67
    • (2008) J. Proteome Res. , vol.7 , pp. 3957-3967
    • Zhou, H.1    Ye, M.2    Dong, J.3    Han, G.4    Jiang, X.5    Wu, R.6    Zou, H.7
  • 117
    • 70349459893 scopus 로고    scopus 로고
    • The multifaceted role of MTDH/AEG-1 in cancer progression
    • Hu, G.; Wei, Y.; Kang, Y. The multifaceted role of MTDH/AEG-1 in cancer progression Clin. Cancer Res. 2009, 15, 5615-20
    • (2009) Clin. Cancer Res. , vol.15 , pp. 5615-5620
    • Hu, G.1    Wei, Y.2    Kang, Y.3


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