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Volumn 21, Issue 10, 2012, Pages 2245-2262

Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; HUNTINGTIN; TRANSCRIPTION FACTOR FKHR; X BOX BINDING PROTEIN 1;

EID: 84860471873     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds040     Document Type: Article
Times cited : (239)

References (84)
  • 1
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: a glimpse into the ER
    • Matus, S., Glimcher, L. and Hetz, C. (2011) Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr. Opin. Cell Biol., 23, 239-252.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 239-252
    • Matus, S.1    Glimcher, L.2    Hetz, C.3
  • 2
    • 56349163764 scopus 로고    scopus 로고
    • Mutant huntingtin and mitochondrial dysfunction
    • Bossy-Wetzel, E., Petrilli, A. and Knott, A.B. (2008) Mutant huntingtin and mitochondrial dysfunction. Trends Neurosci., 31, 609-616.
    • (2008) Trends Neurosci , vol.31 , pp. 609-616
    • Bossy-Wetzel, E.1    Petrilli, A.2    Knott, A.B.3
  • 3
    • 78650827764 scopus 로고    scopus 로고
    • Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease
    • Vidal, R., Caballero, B., Couve, A. and Hetz, C. (2011) Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease. Curr. Mol. Med., 11, 1-12.
    • (2011) Curr. Mol. Med. , vol.11 , pp. 1-12
    • Vidal, R.1    Caballero, B.2    Couve, A.3    Hetz, C.4
  • 4
    • 0036533795 scopus 로고    scopus 로고
    • Lessons from animal models of Huntington's disease
    • Rubinsztein, D.C. (2002) Lessons from animal models of Huntington's disease. Trends Genet., 18, 202-209.
    • (2002) Trends Genet , vol.18 , pp. 202-209
    • Rubinsztein, D.C.1
  • 5
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: protein misfolding revisited
    • Williams, A.J. and Paulson, H.L. (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci., 31, 521-528.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 6
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D. and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol., 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 7
    • 79958033194 scopus 로고    scopus 로고
    • Modulating stress responses by the UPRosome: a matter of life and death
    • Woehlbier, U. and Hetz, C. (2011) Modulating stress responses by the UPRosome: a matter of life and death. Trends Biochem. Sci., 36, 329-337.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 329-337
    • Woehlbier, U.1    Hetz, C.2
  • 8
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz, C. (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol., 13, 89-102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 9
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome
    • Hetz, C. and Glimcher, L.H. (2009) Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome. Mol. Cell, 35, 551-561.
    • (2009) Mol. Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 10
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M., Zeng, H., Urano, F., Till, J.H., Hubbard, S.R., Harding, H.P., Clark, S.G. and Ron, D. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature, 415, 92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 11
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T. and Mori, K. (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell, 107, 881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 12
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A.H., Iwakoshi, N.N. and Glimcher, L.H. (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol., 23, 7448-7459.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 14
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H.P., Novoa, I., Zhang, Y., Zeng, H., Wek, R., Schapira, M. and Ron, D. (2000) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell, 6, 1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 16
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R.T., Remotti, H., Stevens, J.L. and Ron, D. (1998) CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev., 12, 982-995.
    • (1998) Genes Dev , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5    Remotti, H.6    Stevens, J.L.7    Ron, D.8
  • 17
    • 79952705597 scopus 로고    scopus 로고
    • Integrating stress signals at the endoplasmic reticulum: the BCL-2 protein family rheostat
    • Rodriguez, D., Rojas-Rivera, D. and Hetz, C. (2011) Integrating stress signals at the endoplasmic reticulum: the BCL-2 protein family rheostat. Biochim. Biophys. Acta, 1813, 564-574.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 564-574
    • Rodriguez, D.1    Rojas-Rivera, D.2    Hetz, C.3
  • 19
    • 76249091683 scopus 로고    scopus 로고
    • Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear huntingtin fragments in a mouse model of Huntington disease
    • Cho, K.J., Lee, B.I., Cheon, S.Y., Kim, H.W., Kim, H.J. and Kim, G.W. (2009) Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear huntingtin fragments in a mouse model of Huntington disease. Neuroscience, 163, 1128-1134.
    • (2009) Neuroscience , vol.163 , pp. 1128-1134
    • Cho, K.J.1    Lee, B.I.2    Cheon, S.Y.3    Kim, H.W.4    Kim, H.J.5    Kim, G.W.6
  • 22
    • 27744483960 scopus 로고    scopus 로고
    • siRNA-mediated inhibition of endogenous Huntington disease gene expression induces an aberrant configuration of the ER network in vitro
    • Omi, K., Hachiya, N.S., Tokunaga, K. and Kaneko, K. (2005) siRNA-mediated inhibition of endogenous Huntington disease gene expression induces an aberrant configuration of the ER network in vitro. Biochem. Biophys. Res. Commun., 338, 1229-1235.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1229-1235
    • Omi, K.1    Hachiya, N.S.2    Tokunaga, K.3    Kaneko, K.4
  • 24
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald, M.L. and Lindquist, S. (2008) Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev., 22, 3308-3319.
    • (2008) Genes Dev , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 25
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A. and Ichijo, H. (2002) ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev., 16, 1345-1355.
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 26
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai, Y.C., Fishman, P.S., Thakor, N.V. and Oyler, G.A. (2003) Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem., 278, 22044-22055.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 27
    • 33846211417 scopus 로고    scopus 로고
    • ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation
    • Kouroku, Y., Fujita, E., Tanida, I., Ueno, T., Isoai, A., Kumagai, H., Ogawa, S., Kaufman, R.J., Kominami, E. and Momoi, T. (2007) ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ., 14, 230-239.
    • (2007) Cell Death Differ , vol.14 , pp. 230-239
    • Kouroku, Y.1    Fujita, E.2    Tanida, I.3    Ueno, T.4    Isoai, A.5    Kumagai, H.6    Ogawa, S.7    Kaufman, R.J.8    Kominami, E.9    Momoi, T.10
  • 28
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • Reijonen, S., Putkonen, N., Norremolle, A., Lindholm, D. and Korhonen, L. (2008) Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp. Cell Res., 314, 950-960.
    • (2008) Exp. Cell Res. , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhonen, L.5
  • 30
    • 80054037000 scopus 로고    scopus 로고
    • Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin
    • Lajoie, P. and Snapp, E.L. (2011) Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin. J. Cell Sci., 124, 3332-3343.
    • (2011) J. Cell Sci. , vol.124 , pp. 3332-3343
    • Lajoie, P.1    Snapp, E.L.2
  • 31
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang, H., Liu, C., Zhong, Y., Luo, S., Monteiro, M.J. and Fang, S. (2010) Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One, 5, e8905.
    • (2010) PLoS One , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 32
    • 78349312360 scopus 로고    scopus 로고
    • Impaired ATF6alpha processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease
    • Fernandez-Fernandez, M.R., Ferrer, I. and Lucas, J.J. (2011) Impaired ATF6alpha processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease. Neurobiol. Dis., 41, 23-32.
    • (2011) Neurobiol. Dis. , vol.41 , pp. 23-32
    • Fernandez-Fernandez, M.R.1    Ferrer, I.2    Lucas, J.J.3
  • 34
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D.C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature, 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 35
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar, B., Vacher, C., Berger, Z., Davies, J.E., Luo, S., Oroz, L.G., Scaravilli, F., Easton, D.F., Duden, R., O'Kane, C.J. et al. (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat. Genet., 36, 585-595.
    • (2004) Nat. Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6    Scaravilli, F.7    Easton, D.F.8    Duden, R.9    O'Kane, C.J.10
  • 37
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • Atwal, R.S., Xia, J., Pinchev, D., Taylor, J., Epand, R.M. and Truant, R. (2007) Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum. Mol. Genet., 16, 2600-2615.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 38
    • 38049053467 scopus 로고    scopus 로고
    • A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy
    • Atwal, R.S. and Truant, R. (2008) A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy, 4, 91-93.
    • (2008) Autophagy , vol.4 , pp. 91-93
    • Atwal, R.S.1    Truant, R.2
  • 44
    • 0035170536 scopus 로고    scopus 로고
    • Activation of EGFP expression by Cre-mediated excision in a new ROSA26 reporter mouse strain
    • Mao, X., Fujiwara, Y., Chapdelaine, A., Yang, H. and Orkin, S.H. (2001) Activation of EGFP expression by Cre-mediated excision in a new ROSA26 reporter mouse strain. Blood, 97, 324-326.
    • (2001) Blood , vol.97 , pp. 324-326
    • Mao, X.1    Fujiwara, Y.2    Chapdelaine, A.3    Yang, H.4    Orkin, S.H.5
  • 45
    • 78049342155 scopus 로고    scopus 로고
    • Phosphorylation of huntingtin at Ser421 in YAC128 neurons is associated with protection of YAC128 neurons from NMDA-mediated excitotoxicity and is modulated by PP1 and PP2A
    • Metzler, M., Gan, L., Mazarei, G., Graham, R.K., Liu, L., Bissada, N., Lu, G., Leavitt, B.R. and Hayden, M.R. (2010) Phosphorylation of huntingtin at Ser421 in YAC128 neurons is associated with protection of YAC128 neurons from NMDA-mediated excitotoxicity and is modulated by PP1 and PP2A. J. Neurosci., 30, 14318-14329.
    • (2010) J. Neurosci. , vol.30 , pp. 14318-14329
    • Metzler, M.1    Gan, L.2    Mazarei, G.3    Graham, R.K.4    Liu, L.5    Bissada, N.6    Lu, G.7    Leavitt, B.R.8    Hayden, M.R.9
  • 46
    • 0034163497 scopus 로고    scopus 로고
    • Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice
    • Wheeler, V.C., White, J.K., Gutekunst, C.A., Vrbanac, V., Weaver, M., Li, X.J., Li, S.H., Yi, H., Vonsattel, J.P., Gusella, J.F. et al. (2000) Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice. Hum. Mol. Genet., 9, 503-513.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 503-513
    • Wheeler, V.C.1    White, J.K.2    Gutekunst, C.A.3    Vrbanac, V.4    Weaver, M.5    Li, X.J.6    Li, S.H.7    Yi, H.8    Vonsattel, J.P.9    Gusella, J.F.10
  • 47
    • 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
  • 48
    • 67650649726 scopus 로고    scopus 로고
    • A genetic screen in Drosophila reveals novel cytoprotective functions of the autophagy-lysosome pathway
    • Arsham, A.M. and Neufeld, T.P. (2009) A genetic screen in Drosophila reveals novel cytoprotective functions of the autophagy-lysosome pathway. PLoS One, 4, e6068.
    • (2009) PLoS One , vol.4
    • Arsham, A.M.1    Neufeld, T.P.2
  • 50
    • 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
  • 52
    • 77950853379 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis
    • Sasaki, S. (2010) Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol., 69, 346-355.
    • (2010) J. Neuropathol. Exp. Neurol. , vol.69 , pp. 346-355
    • Sasaki, S.1
  • 54
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • Lee, A.H., Scapa, E.F., Cohen, D.E. and Glimcher, L.H. (2008) Regulation of hepatic lipogenesis by the transcription factor XBP1. Science, 320, 1492-1496.
    • (2008) Science , vol.320 , pp. 1492-1496
    • Lee, A.H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 55
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski, D.T. and Hegde, R.S. (2010) Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell Biol., 189, 783-794.
    • (2010) J. Cell Biol. , vol.189 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 57
    • 70350500068 scopus 로고    scopus 로고
    • FoxO transcription factors promote autophagy in cardiomyocytes
    • Sengupta, A., Molkentin, J.D. and Yutzey, K.E. (2009) FoxO transcription factors promote autophagy in cardiomyocytes. J. Biol. Chem., 284, 28319-28331.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28319-28331
    • Sengupta, A.1    Molkentin, J.D.2    Yutzey, K.E.3
  • 58
    • 41549135942 scopus 로고    scopus 로고
    • FoxO transcription factors in the maintenance of cellular homeostasis during aging
    • Salih, D.A. and Brunet, A. (2008) FoxO transcription factors in the maintenance of cellular homeostasis during aging. Curr. Opin. Cell Biol., 20, 126-136.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 126-136
    • Salih, D.A.1    Brunet, A.2
  • 60
    • 79951720176 scopus 로고    scopus 로고
    • JNK regulates FoxO-dependent autophagy in neurons
    • Xu, P., Das, M., Reilly, J. and Davis, R.J. (2011) JNK regulates FoxO-dependent autophagy in neurons. Genes Dev., 25, 310-322.
    • (2011) Genes Dev , vol.25 , pp. 310-322
    • Xu, P.1    Das, M.2    Reilly, J.3    Davis, R.J.4
  • 61
    • 77951290227 scopus 로고    scopus 로고
    • TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages
    • Martinon, F., Chen, X., Lee, A.H. and Glimcher, L.H. (2011) TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat. Immunol., 11, 411-418.
    • (2011) Nat. Immunol. , vol.11 , pp. 411-418
    • Martinon, F.1    Chen, X.2    Lee, A.H.3    Glimcher, L.H.4
  • 65
    • 80054722420 scopus 로고    scopus 로고
    • The unfolded protein response: integrating stress signals through the stress sensor IRE1alpha
    • Hetz, C., Martinon, F., Rodriguez, D. and Glimcher, L.H. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1alpha. Physiol. Rev., 91, 1219-1243.
    • (2011) Physiol. Rev. , vol.91 , pp. 1219-1243
    • Hetz, C.1    Martinon, F.2    Rodriguez, D.3    Glimcher, L.H.4
  • 66
    • 83455169115 scopus 로고    scopus 로고
    • IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux
    • Lee, H., Noh, J.Y., Oh, Y., Kim, Y., Chang, J.W., Chung, C.W., Lee, S.T., Kim, M., Ryu, H. and Jung, Y.K. (2011) IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux. Hum. Mol. Genet., 21, 101-114.
    • (2011) Hum. Mol. Genet. , vol.21 , pp. 101-114
    • Lee, H.1    Noh, J.Y.2    Oh, Y.3    Kim, Y.4    Chang, J.W.5    Chung, C.W.6    Lee, S.T.7    Kim, M.8    Ryu, H.9    Jung, Y.K.10
  • 67
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili, D. and Arden, K.C. (2004) FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell, 117, 421-426.
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 68
    • 42749086593 scopus 로고    scopus 로고
    • OutFOXOing disease and disability: the therapeutic potential of targeting FoxO proteins
    • Maiese, K., Chong, Z.Z. and Shang, Y.C. (2008) OutFOXOing disease and disability: the therapeutic potential of targeting FoxO proteins. Trends Mol. Med., 14, 219-227.
    • (2008) Trends Mol. Med. , vol.14 , pp. 219-227
    • Maiese, K.1    Chong, Z.Z.2    Shang, Y.C.3
  • 71
    • 84857852395 scopus 로고    scopus 로고
    • Activation of the Unfolded Protein Response enhances motor recovery after spinal cord injury
    • doi:10.1038/cddis.2012.8, eK
    • Valenzuela, V., Collyer, E., Armentano, D., Parsons, G., Court, F. and Hetz, C. (2012) Activation of the Unfolded Protein Response enhances motor recovery after spinal cord injury. Cell Death Dis., 3, eK. doi:10.1038/cddis.2012.8.
    • (2012) Cell Death Dis. , vol.3
    • Valenzuela, V.1    Collyer, E.2    Armentano, D.3    Parsons, G.4    Court, F.5    Hetz, C.6
  • 75
    • 79953665568 scopus 로고    scopus 로고
    • Targeting autophagy in ALS: a complex mission
    • Nassif, M. and Hetz, C. (2011) Targeting autophagy in ALS: a complex mission. Autophagy, 7, 450-453.
    • (2011) Autophagy , vol.7 , pp. 450-453
    • Nassif, M.1    Hetz, C.2
  • 76
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong, E. and Cuervo, A.M. (2010) Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci., 13, 805-811.
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 79
    • 79954417611 scopus 로고    scopus 로고
    • Autophagy for tissue homeostasis and neuroprotection
    • Marino, G., Madeo, F. and Kroemer, G. (2011) Autophagy for tissue homeostasis and neuroprotection. Curr. Opin. Cell Biol., 23, 198-206.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 198-206
    • Marino, G.1    Madeo, F.2    Kroemer, G.3
  • 80
    • 84934438243 scopus 로고    scopus 로고
    • Fine structure of the autophagosome
    • Eskelinen, E.L. (2008) Fine structure of the autophagosome. Methods Mol. Biol., 445, 11-28.
    • (2008) Methods Mol. Biol. , vol.445 , pp. 11-28
    • Eskelinen, E.L.1
  • 82
    • 0020085949 scopus 로고
    • Isolation of autophagic vacuoles from rat liver: morphological and biochemical characterization
    • Marzella, L., Ahlberg, J. and Glaumann, H. (1982) Isolation of autophagic vacuoles from rat liver: morphological and biochemical characterization. J. Cell Biol., 93, 144-154.
    • (1982) J. Cell Biol. , vol.93 , pp. 144-154
    • Marzella, L.1    Ahlberg, J.2    Glaumann, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.