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Volumn 288, Issue 49, 2013, Pages 35500-35510

Interactome analysis reveals ezrin can adopt multiple conformational states

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; MASS SPECTROMETRY;

EID: 84894339622     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.505669     Document Type: Article
Times cited : (38)

References (75)
  • 1
    • 0037688084 scopus 로고    scopus 로고
    • Finding the intracellular signaling pathways affected by mood disorder treatments
    • Coyle, J. T., and Duman, R. S. (2003) Finding the intracellular signaling pathways affected by mood disorder treatments. Neuron 38, 157-160
    • (2003) Neuron , vol.38 , pp. 157-160
    • Coyle, J.T.1    Duman, R.S.2
  • 2
    • 84858293590 scopus 로고    scopus 로고
    • Lithium. Still a major option in the management of bipolar disorder
    • Licht, R. W. (2012) Lithium. Still a major option in the management of bipolar disorder. CNS Neurosci. Ther. 18, 219-226
    • (2012) CNS Neurosci. Ther. , vol.18 , pp. 219-226
    • Licht, R.W.1
  • 3
    • 0036276050 scopus 로고    scopus 로고
    • Regulation of tau phosphorylation and protection against -amyloid-induced neurodegeneration by lithium. Possible implications for Alzheimer's disease
    • Alvarez, G., Muñoz-Montaño, J. R., Satrústegui, J., Avila, J., Bogónez, E., and Díaz-Nido, J. (2002) Regulation of tau phosphorylation and protection against -amyloid-induced neurodegeneration by lithium. Possible implications for Alzheimer's disease. Bipolar. Disord. 4, 153-165
    • (2002) Bipolar. Disord. , vol.4 , pp. 153-165
    • Alvarez, G.1    Muñoz-Montaño, J.R.2    Satrústegui, J.3    Avila, J.4    Bogónez, E.5    Díaz-Nido, J.6
  • 4
    • 34147210411 scopus 로고    scopus 로고
    • Lithium and risk for Alzheimer's disease in elderly patients with bipolar disorder
    • Nunes, P. V., Forlenza, O. V., and Gattaz, W. F. (2007) Lithium and risk for Alzheimer's disease in elderly patients with bipolar disorder. Br. J. Psychiatry 190, 359-360
    • (2007) Br. J. Psychiatry , vol.190 , pp. 359-360
    • Nunes, P.V.1    Forlenza, O.V.2    Gattaz, W.F.3
  • 6
    • 0022602621 scopus 로고
    • Lithium for painful dystonia in Parkinson's disease
    • Quinn, N., and Marsden, C. D. (1986) Lithium for painful dystonia in Parkinson's disease. Lancet 1, 1377
    • (1986) Lancet , vol.1 , pp. 1377
    • Quinn, N.1    Marsden, C.D.2
  • 9
    • 0035960005 scopus 로고    scopus 로고
    • Lithium suppresses excitotoxicity-induced striatal lesions in a rat model of Huntington's disease
    • Wei, H., Qin, Z. H., Senatorov, V. V., Wei, W., Wang, Y., Qian, Y., and Chuang, D. M. (2001) Lithium suppresses excitotoxicity-induced striatal lesions in a rat model of Huntington's disease. Neuroscience 106, 603-612
    • (2001) Neuroscience , vol.106 , pp. 603-612
    • Wei, H.1    Qin, Z.H.2    Senatorov, V.V.3    Wei, W.4    Wang, Y.5    Qian, Y.6    Chuang, D.M.7
  • 10
    • 0042666901 scopus 로고    scopus 로고
    • Chronic lithium chloride treatment has variable effects on motor behaviour and survival of mice transgenic for the Huntington's disease mutation
    • Wood, N. I., and Morton, A. J. (2003) Chronic lithium chloride treatment has variable effects on motor behaviour and survival of mice transgenic for the Huntington's disease mutation. Brain Res. Bull. 61, 375-383
    • (2003) Brain Res. Bull. , vol.61 , pp. 375-383
    • Wood, N.I.1    Morton, A.J.2
  • 12
    • 2642523803 scopus 로고    scopus 로고
    • Lithium facilitates apoptotic signaling induced by activation of the Fas death domain-containing receptor
    • Song, L., Zhou, T., and Jope, R. S. (2004) Lithium facilitates apoptotic signaling induced by activation of the Fas death domain-containing receptor. BMC Neurosci. 5, 20
    • (2004) BMC Neurosci. , vol.5 , pp. 20
    • Song, L.1    Zhou, T.2    Jope, R.S.3
  • 13
    • 17644421371 scopus 로고    scopus 로고
    • Early gene response in lithium chloride induced apoptosis
    • Zhang, W. V., Jüllig, M., Connolly, A. R., and Stott, N. S. (2005) Early gene response in lithium chloride induced apoptosis. Apoptosis 10, 75-90
    • (2005) Apoptosis , vol.10 , pp. 75-90
    • Zhang, W.V.1    Jüllig, M.2    Connolly, A.R.3    Stott, N.S.4
  • 15
    • 33749080749 scopus 로고    scopus 로고
    • Lithium stabilizes the polarized lens epithelial phenotype and inhibits proliferation, migration, and epithelial mesenchymal transition
    • Stump, R. J., Lovicu, F. J., Ang, S. L., Pandey, S. K., and McAvoy, J. W. (2006) Lithium stabilizes the polarized lens epithelial phenotype and inhibits proliferation, migration, and epithelial mesenchymal transition. J. Pathol. 210, 249-257
    • (2006) J. Pathol. , vol.210 , pp. 249-257
    • Stump, R.J.1    Lovicu, F.J.2    Ang, S.L.3    Pandey, S.K.4    McAvoy, J.W.5
  • 16
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells
    • Stambolic, V., Ruel, L., and Woodgett, J. R. (1996) Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells. Curr. Biol. 6, 1664-1668
    • (1996) Curr. Biol. , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.R.3
  • 17
    • 0042379932 scopus 로고    scopus 로고
    • Lithium and GSK-3. One inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol
    • Jope, R. S. (2003) Lithium and GSK-3. One inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol. Sci. 24, 441-443
    • (2003) Sci. , vol.24 , pp. 441-443
    • Jope, R.S.1
  • 19
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3- in cellular signaling
    • Grimes, C. A., and Jope, R. S. (2001) The multifaceted roles of glycogen synthase kinase 3- in cellular signaling. Prog. Neurobiol. 65, 391-426
    • (2001) Prog. Neurobiol. , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 20
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini, G., Szebenyi, G., Elluru, R., Ratner, N., and Brady, S. T. (2002) Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 21, 281-293
    • (2002) EMBO J. , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 21
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation. The therapeutic challenge for neurodegenerative disease
    • Hanger, D. P., Anderton, B. H., and Noble, W. (2009) Tau phosphorylation. The therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15, 112-119
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 22
    • 51349089480 scopus 로고    scopus 로고
    • The glycogen synthase kinase (GSK) 3- repressesRNApolymerase i transcription
    • Vincent, T., Kukalev, A., Andäng, M., Pettersson, R., and Percipalle, P. (2008) The glycogen synthase kinase (GSK) 3- repressesRNApolymerase I transcription. Oncogene 27, 5254-5259
    • (2008) Oncogene , vol.27 , pp. 5254-5259
    • Vincent, T.1    Kukalev, A.2    Andäng, M.3    Pettersson, R.4    Percipalle, P.5
  • 23
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy. Molecular machinery for self-eating
    • Yorimitsu, T., and Klionsky, D. J. (2005) Autophagy. Molecular machinery for self-eating. Cell Death Differ. 12, 1542-1552
    • (2005) Cell Death Differ. , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 24
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., Levine, B., Cuervo, A. M., and Klionsky, D. J. (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 26
    • 22344444616 scopus 로고    scopus 로고
    • Does autophagy contribute to cell death
    • Debnath, J., Baehrecke, E. H., and Kroemer, G. (2005) Does autophagy contribute to cell death Autophagy 1, 66-74
    • (2005) Autophagy , vol.1 , pp. 66-74
    • Debnath, J.1    Baehrecke, E.H.2    Kroemer, G.3
  • 27
    • 2442482810 scopus 로고    scopus 로고
    • Autophagy as a cell death and tumor suppressor mechanism
    • Gozuacik, D., and Kimchi, A. (2004) Autophagy as a cell death and tumor suppressor mechanism. Oncogene 23, 2891-2906
    • (2004) Oncogene , vol.23 , pp. 2891-2906
    • Gozuacik, D.1    Kimchi, A.2
  • 28
    • 25444440875 scopus 로고    scopus 로고
    • The role of autophagy in cancer development and response to therapy
    • Kondo, Y., Kanzawa, T., Sawaya, R., and Kondo, S. (2005) The role of autophagy in cancer development and response to therapy. Nat. Rev. Cancer 5, 726-734
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 726-734
    • Kondo, Y.1    Kanzawa, T.2    Sawaya, R.3    Kondo, S.4
  • 29
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B., and Kroemer, G. (2008) Autophagy in the pathogenesis of disease. Cell 132, 27-42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 31
    • 61849102412 scopus 로고    scopus 로고
    • Lithium induces clearance of protease resistant prion protein in prioninfected cells by induction of autophagy
    • Heiseke, A., Aguib, Y., Riemer, C., Baier, M., and Schätzl, H. M. (2009) Lithium induces clearance of protease resistant prion protein in prioninfected cells by induction of autophagy. J. Neurochem. 109, 25-34
    • (2009) J. Neurochem. , vol.109 , pp. 25-34
    • Heiseke, A.1    Aguib, Y.2    Riemer, C.3    Baier, M.4    Schätzl, H.M.5
  • 33
    • 33644946604 scopus 로고    scopus 로고
    • HATs and HDACs in neurodegeneration. A tale of disconcerted acetylation homeostasis
    • Saha, R. N., and Pahan, K. (2006) HATs and HDACs in neurodegeneration. A tale of disconcerted acetylation homeostasis. Cell Death Differ. 13, 539-550
    • (2006) Cell Death Differ. , vol.13 , pp. 539-550
    • Saha, R.N.1    Pahan, K.2
  • 34
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci, S., and Pelicci, P. G. (2006) Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 6, 38-51
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 36
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak, M. A., and Seto, E. (2007) Histone deacetylases and cancer. Oncogene 26, 5420-5432
    • (2007) Oncogene , vol.26 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 39
    • 0347624644 scopus 로고    scopus 로고
    • Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
    • Rouaux, C., Jokic, N., Mbebi, C., Boutillier, S., Loeffler, J. P., and Boutillier, A. L. (2003) Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration. EMBO J. 22, 6537-6549
    • (2003) EMBO J. , vol.22 , pp. 6537-6549
    • Rouaux, C.1    Jokic, N.2    Mbebi, C.3    Boutillier, S.4    Loeffler, J.P.5    Boutillier, A.L.6
  • 40
    • 69449086451 scopus 로고    scopus 로고
    • DNA methylation of Alzheimer disease and tauopathy-related genes in postmortem brain
    • Barrachina, M., and Ferrer, I. (2009) DNA methylation of Alzheimer disease and tauopathy-related genes in postmortem brain. J. Neuropathol. Exp. Neurol. 68, 880-891
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 880-891
    • Barrachina, M.1    Ferrer, I.2
  • 42
    • 79960114652 scopus 로고    scopus 로고
    • Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA)
    • Jiang, Y. J., Che, M. X., Yuan, J. Q., Xie, Y. Y., Yan, X. Z., and Hu, H. Y. (2011) Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA). J. Biol. Chem. 286, 25236-25245
    • (2011) J. Biol. Chem. , vol.286 , pp. 25236-25245
    • Jiang, Y.J.1    Che, M.X.2    Yuan, J.Q.3    Xie, Y.Y.4    Yan, X.Z.5    Hu, H.Y.6
  • 44
    • 0842277812 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1
    • Gui, C. Y., Ngo, L., Xu, W. S., Richon, V. M., and Marks, P. A. (2004) Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1. Proc. Natl. Acad. Sci. U.S.A. 101, 1241-1246
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1241-1246
    • Gui, C.Y.1    Ngo, L.2    Xu, W.S.3    Richon, V.M.4    Marks, P.A.5
  • 46
    • 13544271667 scopus 로고    scopus 로고
    • ICI182,780 induces p21Waf1 gene transcription through releasing histone deacetylase 1 and estrogen receptor- from Sp1 sites to induce cell cycle arrest in MCF-7 breast cancer cell line
    • Varshochi, R., Halim, F., Sunters, A., Alao, J. P., Madureira, P. A., Hart, S. M., Ali, S., Vigushin, D. M., Coombes, R. C., and Lam, E. W. (2005) ICI182,780 induces p21Waf1 gene transcription through releasing histone deacetylase 1 and estrogen receptor- from Sp1 sites to induce cell cycle arrest in MCF-7 breast cancer cell line. J. Biol. Chem. 280, 3185-3196
    • (2005) J. Biol. Chem. , vol.280 , pp. 3185-3196
    • Varshochi, R.1    Halim, F.2    Sunters, A.3    Alao, J.P.4    Madureira, P.A.5    Hart, S.M.6    Ali, S.7    Vigushin, D.M.8    Coombes, R.C.9    Lam, E.W.10
  • 47
    • 54449086844 scopus 로고    scopus 로고
    • HDAC1 cooperates with C/EBP- in the inhibition of liver proliferation in old mice
    • Wang, G. L., Salisbury, E., Shi, X., Timchenko, L., Medrano, E. E., and Timchenko, N. A. (2008) HDAC1 cooperates with C/EBP- in the inhibition of liver proliferation in old mice. J. Biol. Chem. 283, 26169-26178
    • (2008) J. Biol. Chem. , vol.283 , pp. 26169-26178
    • Wang, G.L.1    Salisbury, E.2    Shi, X.3    Timchenko, L.4    Medrano, E.E.5    Timchenko, N.A.6
  • 49
    • 38349053826 scopus 로고    scopus 로고
    • Dual localization of the RNA binding protein CUGBP-1 to stress granule and perinucleolar compartment
    • Fujimura, K., Kano, F., and Murata, M. (2008) Dual localization of the RNA binding protein CUGBP-1 to stress granule and perinucleolar compartment. Exp. Cell Res. 314, 543-553
    • (2008) Exp. Cell Res. , vol.314 , pp. 543-553
    • Fujimura, K.1    Kano, F.2    Murata, M.3
  • 50
    • 79957547144 scopus 로고    scopus 로고
    • P21(WAF1/CIP1) upregulation through the stress granule-associated protein CUGBP1 confers resistance to bortezomibmediated apoptosis
    • Gareau, C., Fournier, M. J., Filion, C., Coudert, L., Martel, D., Labelle, Y., and Mazroui, R. (2011) p21(WAF1/CIP1) upregulation through the stress granule-associated protein CUGBP1 confers resistance to bortezomibmediated apoptosis. PLoS ONE 6, e20254
    • (2011) PLoS ONE , vol.6
    • Gareau, C.1    Fournier, M.J.2    Filion, C.3    Coudert, L.4    Martel, D.5    Labelle, Y.6    Mazroui, R.7
  • 51
    • 69749113137 scopus 로고    scopus 로고
    • MicroRNA expression changes in lymphoblastoid cell lines in response to lithium treatment. Int
    • Chen, H., Wang, N., Burmeister, M., and McInnis, M. G. (2009) MicroRNA expression changes in lymphoblastoid cell lines in response to lithium treatment. Int. J. Neuropsychopharmacol. 12, 975-981
    • (2009) J. Neuropsychopharmacol. , vol.12 , pp. 975-981
    • Chen, H.1    Wang, N.2    Burmeister, M.3    McInnis, M.G.4
  • 53
    • 78650837680 scopus 로고    scopus 로고
    • Expression profile of microRNAs in rat hippocampus following lithiumpilocarpine- induced status epilepticus
    • Hu, K., Zhang, C., Long, L., Long, X., Feng, L., Li, Y., and Xiao, B. (2011) Expression profile of microRNAs in rat hippocampus following lithiumpilocarpine- induced status epilepticus. Neurosci. Lett. 488, 252-257
    • (2011) Neurosci. Lett. , vol.488 , pp. 252-257
    • Hu, K.1    Zhang, C.2    Long, L.3    Long, X.4    Feng, L.5    Li, Y.6    Xiao, B.7
  • 54
    • 71049179047 scopus 로고    scopus 로고
    • Expression levels of histone deacetylases determine the cell fate of hematopoietic progenitors
    • Wada, T., Kikuchi, J., Nishimura, N., Shimizu, R., Kitamura, T., and Furukawa, Y. (2009) Expression levels of histone deacetylases determine the cell fate of hematopoietic progenitors. J. Biol. Chem. 284, 30673-30683
    • (2009) J. Biol. Chem. , vol.284 , pp. 30673-30683
    • Wada, T.1    Kikuchi, J.2    Nishimura, N.3    Shimizu, R.4    Kitamura, T.5    Furukawa, Y.6
  • 55
    • 3142692649 scopus 로고    scopus 로고
    • Valproic acid inhibits proliferation and induces apoptosis in acute myeloid leukemia cells expressing P-gp and MRP1
    • Tang, R., Faussat, A. M., Majdak, P., Perrot, J. Y., Chaoui, D., Legrand, O., and Marie, J. P. (2004) Valproic acid inhibits proliferation and induces apoptosis in acute myeloid leukemia cells expressing P-gp and MRP1. Leukemia 18, 1246-1251
    • (2004) Leukemia , vol.18 , pp. 1246-1251
    • Tang, R.1    Faussat, A.M.2    Majdak, P.3    Perrot, J.Y.4    Chaoui, D.5    Legrand, O.6    Marie, J.P.7
  • 58
    • 3042635178 scopus 로고    scopus 로고
    • GSK3 inhibitors. Development and therapeutic potential
    • Cohen, P., and Goedert, M. (2004) GSK3 inhibitors. Development and therapeutic potential. Nat. Rev. Drug Discov. 3, 479-487
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 479-487
    • Cohen, P.1    Goedert, M.2
  • 60
    • 0038143284 scopus 로고    scopus 로고
    • ERK and p38 inhibit the expression of 4E-BP1 repressor of translation through induction of Egr-1
    • Rolli-Derkinderen, M., Machavoine, F., Baraban, J. M., Grolleau, A., Beretta, L., and Dy, M. (2003) ERK and p38 inhibit the expression of 4E-BP1 repressor of translation through induction of Egr-1. J. Biol. Chem. 278, 18859-18867
    • (2003) J. Biol. Chem. , vol.278 , pp. 18859-18867
    • Rolli-Derkinderen, M.1    Machavoine, F.2    Baraban, J.M.3    Grolleau, A.4    Beretta, L.5    Dy, M.6
  • 61
    • 35648962915 scopus 로고    scopus 로고
    • Inhibition of mammalian target of rapamycin induces phosphatidylinositol 3-kinasedependent and Mnk-mediated eukaryotic translation initiation factor 4E phosphorylation
    • Wang, X., Yue, P., Chan, C. B., Ye, K., Ueda, T., Watanabe-Fukunaga, R., Fukunaga, R., Fu, H., Khuri, F. R., and Sun, S. Y. (2007) Inhibition of mammalian target of rapamycin induces phosphatidylinositol 3-kinasedependent and Mnk-mediated eukaryotic translation initiation factor 4E phosphorylation. Mol. Cell Biol. 27, 7405-7413
    • (2007) Mol. Cell Biol. , vol.27 , pp. 7405-7413
    • Wang, X.1    Yue, P.2    Chan, C.B.3    Ye, K.4    Ueda, T.5    Watanabe-Fukunaga, R.6    Fukunaga, R.7    Fu, H.8    Khuri, F.R.9    Sun, S.Y.10
  • 62
    • 77949653043 scopus 로고    scopus 로고
    • Glycolysis inhibition sensitizes tumor cells to death receptors-induced apoptosis by AMP kinase activation leading to Mcl-1 block in translation
    • Pradelli, L. A., Bénéteau, M., Chauvin, C., Jacquin, M. A., Marchetti, S., Muñoz-Pinedo, C., Auberger, P., Pende, M., and Ricci, J. E. (2010) Glycolysis inhibition sensitizes tumor cells to death receptors-induced apoptosis by AMP kinase activation leading to Mcl-1 block in translation. Oncogene 29, 1641-1652
    • (2010) Oncogene , vol.29 , pp. 1641-1652
    • Pradelli, L.A.1    Bénéteau, M.2    Chauvin, C.3    Jacquin, M.A.4    Marchetti, S.5    Muñoz-Pinedo, C.6    Auberger, P.7    Pende, M.8    Ricci, J.E.9
  • 63
    • 75549089982 scopus 로고    scopus 로고
    • HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage
    • Kim, J. Y., Shen, S., Dietz, K., He, Y., Howell, O., Reynolds, R., and Casaccia, P. (2010) HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage. Nat. Neurosci. 13, 180-189
    • (2010) Nat. Neurosci. , vol.13 , pp. 180-189
    • Kim, J.Y.1    Shen, S.2    Dietz, K.3    He, Y.4    Howell, O.5    Reynolds, R.6    Casaccia, P.7
  • 65
    • 1942422305 scopus 로고    scopus 로고
    • Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBP-LIP in mammary epithelial cells
    • Baldwin, B. R., Timchenko, N. A., and Zahnow, C. A. (2004) Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBP-LIP in mammary epithelial cells. Mol. Cell Biol. 24, 3682-3691
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3682-3691
    • Baldwin, B.R.1    Timchenko, N.A.2    Zahnow, C.A.3
  • 66
    • 1842529234 scopus 로고    scopus 로고
    • Overexpression of CUG triplet repeat-binding protein, CUGBP1, in mice inhibits myogenesis
    • Timchenko, N. A., Patel, R., Iakova, P., Cai, Z. J., Quan, L., and Timchenko, L. T. (2004) Overexpression of CUG triplet repeat-binding protein, CUGBP1, in mice inhibits myogenesis. J. Biol. Chem. 279, 13129-13139
    • (2004) J. Biol. Chem. , vol.279 , pp. 13129-13139
    • Timchenko, N.A.1    Patel, R.2    Iakova, P.3    Cai, Z.J.4    Quan, L.5    Timchenko, L.T.6
  • 68
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos, J., Bodai, L., Lukacsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., and Marsh, J. L. (2008) Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17, 3767-3775
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6    Marsh, J.L.7
  • 69
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach, A., Sauvageot, O., Carmichael, J., Diaz-Latoud, C., Arrigo, A. P., and Rubinsztein, D. C. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 11, 1137-1151
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 70
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., and Finkbeiner, S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 71
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • Sarkar, S., Krishna, G., Imarisio, S., Saiki, S., O'Kane, C. J., and Rubinsztein, D. C. (2008) A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum. Mol. Genet. 17, 170-178
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5    Rubinsztein, D.C.6
  • 72
    • 34347394714 scopus 로고    scopus 로고
    • Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance
    • Carew, J. S., Nawrocki, S. T., Kahue, C. N., Zhang, H., Yang, C., Chung, L., Houghton, J. A., Huang, P., Giles, F. J., and Cleveland, J. L. (2007) Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance. Blood 110, 313-322
    • (2007) Blood , vol.110 , pp. 313-322
    • Carew, J.S.1    Nawrocki, S.T.2    Kahue, C.N.3    Zhang, H.4    Yang, C.5    Chung, L.6    Houghton, J.A.7    Huang, P.8    Giles, F.J.9    Cleveland, J.L.10
  • 73
    • 41249099242 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase1 induces autophagy
    • Oh, M., Choi, I. K., and Kwon, H. J. (2008) Inhibition of histone deacetylase1 induces autophagy. Biochem. Biophys. Res. Commun. 369, 1179-1183
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 1179-1183
    • Oh, M.1    Choi, I.K.2    Kwon, H.J.3
  • 75
    • 34547697173 scopus 로고    scopus 로고
    • RNA-binding proteins hnRNP A2/B1 and CUGBP1 suppress fragile X CGG premutation repeat-induced neurodegeneration in a Drosophila model of FXTAS
    • Sofola, O. A., Jin, P., Qin, Y., Duan, R., Liu, H., de Haro, M., Nelson, D. L., and Botas, J. (2007) RNA-binding proteins hnRNP A2/B1 and CUGBP1 suppress fragile X CGG premutation repeat-induced neurodegeneration in a Drosophila model of FXTAS. Neuron 55, 565-571
    • (2007) Neuron , vol.55 , pp. 565-571
    • Sofola, O.A.1    Jin, P.2    Qin, Y.3    Duan, R.4    Liu, H.5    De Haro, M.6    Nelson, D.L.7    Botas, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.