메뉴 건너뛰기




Volumn 1533, Issue , 2013, Pages 131-140

Chronic cerebral ischemia induces redistribution and abnormal phosphorylation of transactivation-responsive DNA-binding protein-43 in mice

Author keywords

Chronic cerebral ischemia; Hippocampal sclerosis; Phosphorylation; TAR DNA binding protein 43

Indexed keywords

KARYOPHERIN BETA; TAR DNA BINDING PROTEIN;

EID: 84884592251     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2013.08.007     Document Type: Article
Times cited : (10)

References (30)
  • 5
    • 80855138138 scopus 로고    scopus 로고
    • Rodent models of TDP-43 proteinopathy: Investigating the mechanisms of TDP-43-mediated neurodegeneration
    • T.F. Gendron, and L. Petrucelli Rodent models of TDP-43 proteinopathy: investigating the mechanisms of TDP-43-mediated neurodegeneration J. Mol. Neurosci. 45 2011 486 499
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 486-499
    • Gendron, T.F.1    Petrucelli, L.2
  • 8
    • 8644262258 scopus 로고    scopus 로고
    • Importin β: Conducting a much larger cellular symphony
    • A. Harel, and D.J. Forbes Importin β: conducting a much larger cellular symphony Mol. Cell 16 2004 319 330
    • (2004) Mol. Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 11
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • P.H. Kuo, L.G. Doudeva, Y.T. Wang, C.K. Shen, and H.S. Yuan Structural insights into TDP-43 in nucleic-acid binding and domain interactions Nucleic Acids Res. 37 2009 1799 1808
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 12
    • 39749083266 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system
    • E.B. Lee, V.M. Lee, J.Q. Trojanowski, and M. Neumann TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system Acta Neuropathol. 115 2008 305 311
    • (2008) Acta Neuropathol. , vol.115 , pp. 305-311
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3    Neumann, M.4
  • 13
    • 58049221032 scopus 로고    scopus 로고
    • Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: Implications for TDP-43 in the physiological response to neuronal injury
    • K. Moisse, K. Volkening, C. Leystra-Lantz, I. Welch, T. Hill, and M.J. Strong Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: implications for TDP-43 in the physiological response to neuronal injury Brain. Res. 1249 2009 202 211
    • (2009) Brain. Res. , vol.1249 , pp. 202-211
    • Moisse, K.1    Volkening, K.2    Leystra-Lantz, C.3    Welch, I.4    Hill, T.5    Strong, M.J.6
  • 16
    • 77953019135 scopus 로고    scopus 로고
    • Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration
    • A.L. Nishimura, V. Zupunski, C. Troakes, C. Kathe, P. Fratta, M. Howell, J.M. Gallo, T. Hortobágyi, C.E. Shaw, and B. Rogelj Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration Brain 133 2010 1763 1771
    • (2010) Brain , vol.133 , pp. 1763-1771
    • Nishimura, A.L.1    Zupunski, V.2    Troakes, C.3    Kathe, C.4    Fratta, P.5    Howell, M.6    Gallo, J.M.7    Hortobágyi, T.8    Shaw, C.E.9    Rogelj, B.10
  • 18
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • T. Nonaka, T. Arai, E. Buratti, F.E. Baralle, H. Akiyama, and M. Hasegawa Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells FEBS Lett. 583 2009 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
  • 19
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • T. Nonaka, F. Kametani, T. Arai, H. Akiyama, and M. Hasegawa Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43 Hum. Mol. Genet. 18 2009 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
  • 22
    • 7644244605 scopus 로고    scopus 로고
    • White matter lesions and glial activation in a novel mouse model of chronic cerebral hypoperfusion
    • M. Shibata, R. Ohtani, M. Ihara, and H. Tomimoto White matter lesions and glial activation in a novel mouse model of chronic cerebral hypoperfusion Stroke 35 2004 2598 2603
    • (2004) Stroke , vol.35 , pp. 2598-2603
    • Shibata, M.1    Ohtani, R.2    Ihara, M.3    Tomimoto, H.4
  • 24
    • 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
    • H. Suzuki, K. Lee, and M. Matsuoka 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 2011 13171 13183
    • (2011) J. Biol. Chem. , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 26
    • 0028223151 scopus 로고
    • Glial activation and white matter changes in the rat brain induced by chronic cerebral hypoperfusion: An immunohistochemical study
    • H. Wakita, H. Tomimoto, I. Akiguchi, and J. Kimura Glial activation and white matter changes in the rat brain induced by chronic cerebral hypoperfusion: an immunohistochemical study Acta Neuropathol. 87 1994 484 492
    • (1994) Acta Neuropathol. , vol.87 , pp. 484-492
    • Wakita, H.1    Tomimoto, H.2    Akiguchi, I.3    Kimura, J.4
  • 27
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic Tar DNA binding protein (TDP-43) induces disease-like redistribution, sequestration and aggregate formation
    • M.J. Winton, L.M. Igaz, M.M. Wong, L.K. Kwong, J.Q. Trojanowski, and V.M. Lee Disturbance of nuclear and cytoplasmic Tar DNA binding protein (TDP-43) induces disease-like redistribution, sequestration and aggregate formation J. Biol. Chem. 283 2008 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
  • 28
    • 54049110088 scopus 로고    scopus 로고
    • Understanding hippocampal sclerosis in the elderly: Epidemiology, characterization, and diagnostic issues
    • C. Zarow, T.E. Sitzer, and H.C. Chui Understanding hippocampal sclerosis in the elderly: epidemiology, characterization, and diagnostic issues Curr. Neurol. Neurosci. Rep. 8 2008 363 370
    • (2008) Curr. Neurol. Neurosci. Rep. , vol.8 , pp. 363-370
    • Zarow, C.1    Sitzer, T.E.2    Chui, H.C.3
  • 29
    • 79955433159 scopus 로고    scopus 로고
    • TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin/IGF-1 signaling
    • T. Zhang, P.C. Mullane, G. Periz, and J. Wang TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin/IGF-1 signaling Hum. Mol. Genet. 20 2011 1952 1965
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1952-1965
    • Zhang, T.1    Mullane, P.C.2    Periz, G.3    Wang, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.