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Volumn 127, Issue 14, 2014, Pages 3024-3038

Metabolism and mis-metabolism of the neuropathological signature protein TDP-43

Author keywords

Chaperone mediated autophagy; Protein degradation; Proteolytic cleavage; TDP 43; TDP 43 proteinopathies; TDP 43 positive aggregate

Indexed keywords

HEAT SHOCK COGNATE PROTEIN 70; PROTEASOME; TAR DNA BINDING PROTEIN; UBIQUITIN; DNA BINDING PROTEIN; PROTEIN TDP-43;

EID: 84904314590     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.136150     Document Type: Article
Times cited : (84)

References (83)
  • 2
    • 84864762305 scopus 로고    scopus 로고
    • Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection
    • Avendaño-Vázquez, S. E., Dhir, A., Bembich, S., Buratti, E., Proudfoot, N. and Baralle, F. E. (2012). Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection. Genes Dev. 26, 1679-1684.
    • (2012) Genes Dev. , vol.26 , pp. 1679-1684
    • Avendaño-Vázquez, S.E.1    Dhir, A.2    Bembich, S.3    Buratti, E.4    Proudfoot, N.5    Baralle, F.E.6
  • 5
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Baloh, R. H. (2011). TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. FEBS J. 278, 3539-3549.
    • (2011) FEBS J. , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 6
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates, G. (2003). Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361, 1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 7
  • 8
    • 80855143681 scopus 로고    scopus 로고
    • TDP-43 variants of frontotemporal lobar degeneration
    • Bigio, E. H. (2011). TDP-43 variants of frontotemporal lobar degeneration. J. Mol. Neurosci. 45, 390-401.
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 390-401
    • Bigio, E.H.1
  • 9
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtininduced cell death
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H. and Johansen, T. (2005). p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtininduced cell death. J. Cell Biol. 171, 603-614.
    • (2005) J. Cell Biol , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 10
    • 33749056809 scopus 로고    scopus 로고
    • ALS: a disease of motor neurons and their nonneuronal neighbors
    • Boillée, S., Vande Velde, C. and Cleveland, D. W. (2006). ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron 52, 39-59.
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillée, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 11
    • 79957583304 scopus 로고    scopus 로고
    • Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast
    • Braun, R. J., Sommer, C., Carmona-Gutierrez, D., Khoury, C. M., Ring, J., Büttner, S. and Madeo, F. (2011). Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast. J. Biol. Chem. 286, 19958-19972.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19958-19972
    • Braun, R.J.1    Sommer, C.2    Carmona-Gutierrez, D.3    Khoury, C.M.4    Ring, J.5    Büttner, S.6    Madeo, F.7
  • 12
    • 70350454798 scopus 로고    scopus 로고
    • Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability
    • Caccamo, A., Majumder, S., Deng, J. J., Bai, Y., Thornton, F. B. and Oddo, S. (2009). Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability. J. Biol. Chem. 284, 27416-27424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27416-27424
    • Caccamo, A.1    Majumder, S.2    Deng, J.J.3    Bai, Y.4    Thornton, F.B.5    Oddo, S.6
  • 13
    • 79960160835 scopus 로고    scopus 로고
    • Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing
    • Che, M. X., Jiang, Y. J., Xie, Y. Y., Jiang, L. L. and Hu, H. Y. (2011). Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing. FASEB J. 25, 2344-2353.
    • (2011) FASEB J. , vol.25 , pp. 2344-2353
    • Che, M.X.1    Jiang, Y.J.2    Xie, Y.Y.3    Jiang, L.L.4    Hu, H.Y.5
  • 15
    • 77950867149 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 in neurodegenerative disease
    • Chen-Plotkin, A. S., Lee, V. M. and Trojanowski, J. Q. (2010). TAR DNA-binding protein 43 in neurodegenerative disease. Nat. Rev. Neurol. 6, 211-220.
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 211-220
    • Chen-Plotkin, A.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 17
    • 80755153025 scopus 로고    scopus 로고
    • TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
    • Cohen, T. J., Lee, V. M. and Trojanowski, J. Q. (2011). TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends Mol. Med. 17, 659-667.
    • (2011) Trends Mol. Med. , vol.17 , pp. 659-667
    • Cohen, T.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 18
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo, A. M. and Dice, J. F. (2000). Regulation of lamp2a levels in the lysosomal membrane. Traffic 1, 570-583.
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 19
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T. and Sulzer, D. (2004). Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305, 1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 20
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: enzymes with therapeutic potential in Alzheimer disease
    • De Strooper, B., Vassar, R. and Golde, T. (2010). The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat. Rev. Neurol. 6, 99-107.
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 21
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino, G. N. and Slaughter, C. A. (1999). The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274, 22123-22126.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 23
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice, J. F. (2007). Chaperone-mediated autophagy. Autophagy 3, 295-299.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 24
    • 67650432367 scopus 로고    scopus 로고
    • Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin
    • Dormann, D., Capell, A., Carlson, A. M., Shankaran, S. S., Rodde, R., Neumann, M., Kremmer, E., Matsuwaki, T., Yamanouchi, K., Nishihara, M. et al. (2009). Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J. Neurochem. 110, 1082-1094.
    • (2009) J. Neurochem. , vol.110 , pp. 1082-1094
    • Dormann, D.1    Capell, A.2    Carlson, A.M.3    Shankaran, S.S.4    Rodde, R.5    Neumann, M.6    Kremmer, E.7    Matsuwaki, T.8    Yamanouchi, K.9    Nishihara, M.10
  • 26
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions
    • Furukawa, Y., Kaneko, K., Watanabe, S., Yamanaka, K. and Nukina, N. (2011). A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions. J. Biol. Chem. 286, 18664-18672.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 27
    • 77951236534 scopus 로고    scopus 로고
    • Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS)
    • Hanson, K. A., Kim, S. H., Wassarman, D. A. and Tibbetts, R. S. (2010). Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS). J. Biol. Chem. 285, 11068-11072.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11068-11072
    • Hanson, K.A.1    Kim, S.H.2    Wassarman, D.A.3    Tibbetts, R.S.4
  • 29
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases
    • Hashimoto, M., Rockenstein, E., Crews, L. and Masliah, E. (2003). Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases. Neuromolecular Med. 4, 21-36.
    • (2003) Neuromolecular Med. , vol.4 , pp. 21-36
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 30
    • 0029047863 scopus 로고
    • Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2, resulting in alternative transmembrane and cytoplasmic domains
    • Hatem, C. L., Gough, N. R. and Fambrough, D. M. (1995). Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2, resulting in alternative transmembrane and cytoplasmic domains. J. Cell Sci. 108, 2093-2100.
    • (1995) J. Cell Sci. , vol.108 , pp. 2093-2100
    • Hatem, C.L.1    Gough, N.R.2    Fambrough, D.M.3
  • 31
    • 84859385707 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy promotes tumor cell survival and adaptation to antiangiogenic treatment in glioblastoma
    • Hu, Y. L., DeLay, M., Jahangiri, A., Molinaro, A. M., Rose, S. D., Carbonell,W. S. and Aghi, M. K. (2012). Hypoxia-induced autophagy promotes tumor cell survival and adaptation to antiangiogenic treatment in glioblastoma. Cancer Res. 72, 1773-1783.
    • (2012) Cancer Res. , vol.72 , pp. 1773-1783
    • Hu, Y.L.1    DeLay, M.2    Jahangiri, A.3    Molinaro, A.M.4    Rose, S.D.5    Carbonell, W.S.6    Aghi, M.K.7
  • 32
    • 46749138739 scopus 로고    scopus 로고
    • Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Igaz, L. M., Kwong, L. K., Xu, Y., Truax, A. C., Uryu, K., Neumann, M., Clark, C. M., Elman, L. B., Miller, B. L., Grossman, M. et al. (2008). Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am. J. Pathol. 173, 182-194.
    • (2008) Am. J. Pathol. , vol.173 , pp. 182-194
    • Igaz, L.M.1    Kwong, L.K.2    Xu, Y.3    Truax, A.C.4    Uryu, K.5    Neumann, M.6    Clark, C.M.7    Elman, L.B.8    Miller, B.L.9    Grossman, M.10
  • 34
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata, A., Riley, B. E., Johnston, J. A. and Kopito, R. R. (2005). HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J. Biol. Chem. 280, 40282-40292.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 35
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson, B. S., McCaffery, J. M., Lindquist, S. and Gitler, A. D. (2008). A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc. Natl. Acad. Sci. USA 105, 6439-6444.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, J.M.2    Lindquist, S.3    Gitler, A.D.4
  • 39
    • 65549084887 scopus 로고    scopus 로고
    • Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1
    • Kim, S. H., Shi, Y., Hanson, K. A., Williams, L. M., Sakasai, R., Bowler, M. J. and Tibbetts, R. S. (2009). Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1. J. Biol. Chem. 284, 8083-8092.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8083-8092
    • Kim, S.H.1    Shi, Y.2    Hanson, K.A.3    Williams, L.M.4    Sakasai, R.5    Bowler, M.J.6    Tibbetts, R.S.7
  • 40
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I. and Dikic, I. (2009). A role for ubiquitin in selective autophagy. Mol. Cell 34, 259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 42
    • 0034805395 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells
    • Kuusisto, E., Suuronen, T. and Salminen, A. (2001). Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. Biochem. Biophys. Res. Commun. 280, 223-228.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 43
    • 34447103093 scopus 로고    scopus 로고
    • TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease
    • Kwong, L. K., Neumann, M., Sampathu, D. M., Lee, V. M. and Trojanowski, J. Q. (2007). TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease. Acta Neuropathol. 114, 63-70.
    • (2007) Acta Neuropathol. , vol.114 , pp. 63-70
    • Kwong, L.K.1    Neumann, M.2    Sampathu, D.M.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 44
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne, C., Polymenidou, M. and Cleveland, D. W. (2010). TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 19 R1, R46-R64.
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.R1
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 45
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury, P. T. and Lashuel, H. A. (2006). A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443, 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 46
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee, E. B., Lee, V. M. and Trojanowski, J. Q. (2012). Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat. Rev. Neurosci. 13, 38-50.
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 47
    • 79957801387 scopus 로고    scopus 로고
    • Neuronal function and dysfunction of Drosophila dTDP
    • Lin, M. J., Cheng, C. W. and Shen, C. K. (2011). Neuronal function and dysfunction of Drosophila dTDP. PLoS ONE 6, e20371.
    • (2011) PLoS ONE , vol.6
    • Lin, M.J.1    Cheng, C.W.2    Shen, C.K.3
  • 48
    • 70349666552 scopus 로고    scopus 로고
    • Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways
    • Liu, H., Wang, P., Song, W. and Sun, X. (2009). Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways. FASEB J. 23, 3383-3392.
    • (2009) FASEB J. , vol.23 , pp. 3383-3392
    • Liu, H.1    Wang, P.2    Song, W.3    Sun, X.4
  • 51
    • 34447099071 scopus 로고    scopus 로고
    • Gene expression analysis of frontotemporal lobar degeneration of the motor neuron disease type with ubiquitinated inclusions
    • Mishra, M., Paunesku, T., Woloschak, G. E., Siddique, T., Zhu, L. J., Lin, S., Greco, K. and Bigio, E. H. (2007). Gene expression analysis of frontotemporal lobar degeneration of the motor neuron disease type with ubiquitinated inclusions. Acta Neuropathol. 114, 81-94.
    • (2007) Acta Neuropathol. , vol.114 , pp. 81-94
    • Mishra, M.1    Paunesku, T.2    Woloschak, G.E.3    Siddique, T.4    Zhu, L.J.5    Lin, S.6    Greco, K.7    Bigio, E.H.8
  • 52
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima, N., Yoshimori, T. and Levine, B. (2010). Methods in mammalian autophagy research. Cell 140, 313-326.
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 53
    • 59649086176 scopus 로고    scopus 로고
    • Molecular neuropathology of TDP-43 proteinopathies
    • Neumann, M. (2009). Molecular neuropathology of TDP-43 proteinopathies. Int. J. Mol. Sci. 10, 232-246.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 232-246
    • Neumann, M.1
  • 56
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • Nonaka, T., Arai, T., Buratti, E., Baralle, F. E., Akiyama, H. and Hasegawa, M. (2009a). Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett. 583, 394-400.
    • (2009) FEBS Lett. , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5    Hasegawa, M.6
  • 57
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • Nonaka, T., Kametani, F., Arai, T., Akiyama, H. and Hasegawa, M. (2009b). Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum. Mol. Genet. 18, 3353-3364.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 58
    • 79956304001 scopus 로고    scopus 로고
    • A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport
    • Pesiridis, G. S., Tripathy, K., Tanik, S., Trojanowski, J. Q. and Lee, V. M. (2011). A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport. J. Biol. Chem. 286, 18845-18855.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18845-18855
    • Pesiridis, G.S.1    Tripathy, K.2    Tanik, S.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 61
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A. and Poirier, M. A. (2004). Protein aggregation and neurodegenerative disease. Nat. Med. 10 Suppl, S10-S17.
    • (2004) Nat. Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 62
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration? Nat
    • Ross, C. A. and Poirier, M. A. (2005). Opinion: What is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6, 891-898.
    • (2005) Rev. Mol. Cell Biol. , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 64
    • 84857410934 scopus 로고    scopus 로고
    • Delineation of the core aggregation sequences of TDP-43 C-terminal fragment
    • Saini, A. and Chauhan, V. S. (2011). Delineation of the core aggregation sequences of TDP-43 C-terminal fragment. ChemBioChem 12, 2495-2501.
    • (2011) ChemBioChem , vol.12 , pp. 2495-2501
    • Saini, A.1    Chauhan, V.S.2
  • 65
  • 67
    • 79953855830 scopus 로고    scopus 로고
    • TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage
    • Suzuki, H., Lee, K. and Matsuoka, M. (2011). TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage. J. Biol. Chem. 286, 13171-13183.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 69
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida, I., Minematsu-Ikeguchi, N., Ueno, T. and Kominami, E. (2005). Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 1, 84-91.
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 70
    • 77955395385 scopus 로고    scopus 로고
    • Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U
    • Tsai, K.J., Yang,C.H.,Fang, Y. H.,Cho,K.H.,Chien,W. L.,Wang,W.T.,Wu, T.W., Lin, C. P., Fu,W. M. and Shen, C. K. (2010). Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U. J. Exp. Med. 207, 1661-1673.
    • (2010) J. Exp. Med. , vol.207 , pp. 1661-1673
    • Tsai, K.J.1    Yang, C.H.2    Fang, Y.H.3    Cho, K.H.4    Chien, W.L.5    Wang, W.T.6    Wu, T.W.7    Lin, C.P.8    Fu, W.M.9    Shen, C.K.10
  • 71
    • 76549101965 scopus 로고    scopus 로고
    • Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43
    • Urushitani, M., Sato, T., Bamba, H., Hisa, Y. and Tooyama, I. (2010). Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43. J. Neurosci. Res. 88, 784-797.
    • (2010) J. Neurosci. Res. , vol.88 , pp. 784-797
    • Urushitani, M.1    Sato, T.2    Bamba, H.3    Hisa, Y.4    Tooyama, I.5
  • 72
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang, I. F., Wu, L. S., Chang, H. Y. and Shen, C. K. (2008). TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem. 105, 797-806.
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.4
  • 73
    • 72649087184 scopus 로고    scopus 로고
    • Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
    • Wang, X., Fan, H., Ying, Z., Li, B., Wang, H. and Wang, G. (2010). Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci. Lett. 469, 112-116.
    • (2010) Neurosci. Lett. , vol.469 , pp. 112-116
    • Wang, X.1    Fan, H.2    Ying, Z.3    Li, B.4    Wang, H.5    Wang, G.6
  • 74
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • Wang, I. F., Guo, B. S., Liu, Y. C., Wu, C. C., Yang, C. C., Tsai, K. J. and Shen, C. K. J. (2012). Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc. Natl. Acad. Sci. USA 109, 15024-15029.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15024-15029
    • Wang, I.F.1    Guo, B.S.2    Liu, Y.C.3    Wu, C.C.4    Yang, C.C.5    Tsai, K.J.6    Shen, C.K.J.7
  • 75
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M. and Baloh, R. H. (2009). TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. USA 106, 18809-18814.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 77
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman, R. L., Gordon, C. and Mayer, R. J. (2005). Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat. Rev. Mol. Cell Biol. 6, 599-609.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 79
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton, M. J., Igaz, L. M., Wong, M. M., Kwong, L. K., Trojanowski, J. Q. and Lee, V. M. (2008). Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283, 13302-13309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 80
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong, J., Zhang, J., Si, X., Gao, G., Mao, I., McManus, B. M. and Luo, H. (2008). Autophagosome supports coxsackievirus B3 replication in host cells. J. Virol. 82, 9143-9153.
    • (2008) J. Virol. , vol.82 , pp. 9143-9153
    • Wong, J.1    Zhang, J.2    Si, X.3    Gao, G.4    Mao, I.5    McManus, B.M.6    Luo, H.7


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