메뉴 건너뛰기




Volumn 114, Issue 1, 2010, Pages 160-170

Hypoxic ischemia and proteasome dysfunction alter tau isoform ratio by inhibiting exon 10 splicing

Author keywords

Ischemia; Proteasome; Splicing; Tau; Tra2

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; LACTACYSTIN; PROTEASOME; TAU PROTEIN;

EID: 77953311303     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06732.x     Document Type: Article
Times cited : (11)

References (50)
  • 2
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer C., Acker C. M., Kress Y., Hof P. R., Duff K. Davies P. (2005) Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J. Neurosci. 25, 5446 5454.
    • (2005) J. Neurosci. , vol.25 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 3
    • 2542464892 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics by tau in living cells: Implications for development and neurodegeneration
    • Bunker J. M., Wilson L., Jordan M. A. Feinstein S. C. (2004) Modulation of microtubule dynamics by tau in living cells: implications for development and neurodegeneration. Mol. Biol. Cell 15, 2720 2728.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2720-2728
    • Bunker, J.M.1    Wilson, L.2    Jordan, M.A.3    Feinstein, S.C.4
  • 4
    • 0030806805 scopus 로고    scopus 로고
    • Tau mRNA isoforms following sciatic nerve axotomy with and without regeneration
    • Chambers C. B. Muma N. A. (1997) Tau mRNA isoforms following sciatic nerve axotomy with and without regeneration. Brain Res. Mol. Brain Res. 48, 115 124.
    • (1997) Brain Res. Mol. Brain Res. , vol.48 , pp. 115-124
    • Chambers, C.B.1    Muma, N.A.2
  • 6
    • 0033009241 scopus 로고    scopus 로고
    • Activity-dependent regulation of alternative splicing patterns in the rat brain
    • Daoud R., Da Penha B. M., Siedler F., Hubener M. Stamm S. (1999) Activity-dependent regulation of alternative splicing patterns in the rat brain. Eur. J. Neurosci. 11, 788 802.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 788-802
    • Daoud, R.1    Da Penha, B.M.2    Siedler, F.3    Hubener, M.4    Stamm, S.5
  • 7
    • 0037101633 scopus 로고    scopus 로고
    • Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain
    • Daoud R., Mies G., Smialowska A., Olah L., Hossmann K. A. Stamm S. (2002) Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain. J. Neurosci. 22, 5889 5899.
    • (2002) J. Neurosci. , vol.22 , pp. 5889-5899
    • Daoud, R.1    Mies, G.2    Smialowska, A.3    Olah, L.4    Hossmann, K.A.5    Stamm, S.6
  • 8
    • 33646340445 scopus 로고    scopus 로고
    • Arginine/serine-rich protein interaction domain-dependent modulation of a tau exon 10 splicing enhancer: Altered interactions and mechanisms for functionally antagonistic FTDP-17 mutations Delta280K and N279K
    • D'Souza I. Schellenberg G. D. (2006) Arginine/serine-rich protein interaction domain-dependent modulation of a tau exon 10 splicing enhancer: altered interactions and mechanisms for functionally antagonistic FTDP-17 mutations Delta280K AND N279K. J. Biol. Chem. 281, 2460 2469.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2460-2469
    • D'Souza, I.1    Schellenberg, G.D.2
  • 9
    • 0034016093 scopus 로고    scopus 로고
    • Characterization of pathology in transgenic mice over-expressing human genomic and cDNA tau transgenes
    • Duff K., Knight H., Refolo L. M. et al. (2000) Characterization of pathology in transgenic mice over-expressing human genomic and cDNA tau transgenes. Neurobiol. Dis. 7, 87 98.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 87-98
    • Duff, K.1    Knight, H.2    Refolo, L.M.3
  • 10
    • 0242611535 scopus 로고    scopus 로고
    • Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain
    • Fischer D. F., De Vos R. A., Van D. R. et al. (2003) Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain. FASEB J. 17, 2014 2024.
    • (2003) FASEB J. , vol.17 , pp. 2014-2024
    • Fischer, D.F.1    De Vos, R.A.2    Van D, R.3
  • 11
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillantini M. G., Jakes R., Rutherford D. Crowther R. A. (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519 526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 12
    • 58549119790 scopus 로고    scopus 로고
    • The up-regulation of BACE1 mediated by hypoxia and ischemic injury: Role of oxidative stress and HIF1alpha
    • Guglielmotto M., Aragno M., Autelli R. et al. (2009) The up-regulation of BACE1 mediated by hypoxia and ischemic injury: role of oxidative stress and HIF1alpha. J. Neurochem. 108, 1045 1056.
    • (2009) J. Neurochem. , vol.108 , pp. 1045-1056
    • Guglielmotto, M.1    Aragno, M.2    Autelli, R.3
  • 13
    • 34249292315 scopus 로고    scopus 로고
    • Marked prevention of ischemic brain injury by Neu2000, an NMDA antagonist and antioxidant derived from aspirin and sulfasalazine
    • Gwag B. J., Lee Y. A., Ko S. Y. et al. (2007) Marked prevention of ischemic brain injury by Neu2000, an NMDA antagonist and antioxidant derived from aspirin and sulfasalazine. J. Cereb. Blood Flow Metab. 27, 1142 1151.
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 1142-1151
    • Gwag, B.J.1    Lee, Y.A.2    Ko, S.Y.3
  • 14
    • 67649388412 scopus 로고    scopus 로고
    • Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in vitro
    • Han D., Qureshi H. Y., Lu Y. Paudel H. K. (2009) Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in vitro. J. Biol. Chem. 284, 13422 13433.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13422-13433
    • Han, D.1    Qureshi, H.Y.2    Lu, Y.3    Paudel, H.K.4
  • 15
    • 0001020243 scopus 로고
    • Neurofilament and tubulin expression recapitulates the developmental program during axonal regeneration: Induction of a specific beta-tubulin isotype
    • Hoffman P. N. Cleveland D. W. (1988) Neurofilament and tubulin expression recapitulates the developmental program during axonal regeneration: induction of a specific beta-tubulin isotype. Proc. Natl Acad. Sci. USA 85, 4530 4533.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4530-4533
    • Hoffman, P.N.1    Cleveland, D.W.2
  • 16
    • 0038155122 scopus 로고    scopus 로고
    • Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression
    • Hope A. D., de S. R., Fischer D. F., Hol E. M., van Leeuwen F. W. Lees A. J. (2003) Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression. J. Neurochem. 86, 394 404.
    • (2003) J. Neurochem. , vol.86 , pp. 394-404
    • Hope, A.D.1    De S, R.2    Fischer, D.F.3    Hol, E.M.4    Van Leeuwen, F.W.5    Lees, A.J.6
  • 17
    • 0034192398 scopus 로고    scopus 로고
    • Protein aggregation after transient cerebral ischemia
    • Hu B. R., Martone M. E., Jones Y. Z. Liu C. L. (2000) Protein aggregation after transient cerebral ischemia. J. Neurosci. 20, 3191 3199.
    • (2000) J. Neurosci. , vol.20 , pp. 3191-3199
    • Hu, B.R.1    Martone, M.E.2    Jones, Y.Z.3    Liu, C.L.4
  • 18
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M., Lendon C. L., Rizzu P. et al. (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702 705.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 19
    • 33749152589 scopus 로고    scopus 로고
    • No alteration in tau exon 10 alternative splicing in tangle-bearing neurons of the Alzheimer's disease brain
    • Ingelsson M., Ramasamy K., Cantuti-Castelvetri I. et al. (2006) No alteration in tau exon 10 alternative splicing in tangle-bearing neurons of the Alzheimer's disease brain. Acta Neuropathol. (Berl) 112, 439 449.
    • (2006) Acta Neuropathol. (Berl) , vol.112 , pp. 439-449
    • Ingelsson, M.1    Ramasamy, K.2    Cantuti-Castelvetri, I.3
  • 20
    • 0038819945 scopus 로고    scopus 로고
    • Mutations in tau gene exon 10 associated with FTDP-17 alter the activity of an exonic splicing enhancer to interact with Tra2 beta
    • Jiang Z., Tang H., Havlioglu N., Zhang X., Stamm S., Yan R. Wu J. Y. (2003) Mutations in tau gene exon 10 associated with FTDP-17 alter the activity of an exonic splicing enhancer to interact with Tra2 beta. J. Biol. Chem. 278, 18997 19007.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18997-19007
    • Jiang, Z.1    Tang, H.2    Havlioglu, N.3    Zhang, X.4    Stamm, S.5    Yan, R.6    Wu, J.Y.7
  • 21
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J. N., Hanni K. B. Markesbery W. R. (2000) Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75, 436 439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 22
    • 1542330117 scopus 로고    scopus 로고
    • Tra2 beta, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA
    • Kondo S., Yamamoto N., Murakami T., Okumura M., Mayeda A. Imaizumi K. (2004) Tra2 beta, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA. Genes Cells 9, 121 130.
    • (2004) Genes Cells , vol.9 , pp. 121-130
    • Kondo, S.1    Yamamoto, N.2    Murakami, T.3    Okumura, M.4    Mayeda, A.5    Imaizumi, K.6
  • 23
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik K. S., Orecchio L. D., Bakalis S. Neve R. L. (1989) Developmentally regulated expression of specific tau sequences. Neuron 2, 1389 1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 24
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • van Leeuwen F. W., de Kleijn D. P., van den Hurk H. H. et al. (1998) Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279, 242 247.
    • (1998) Science , vol.279 , pp. 242-247
    • Van Leeuwen, F.W.1    De Kleijn, D.P.2    Van Den Hurk, H.H.3
  • 25
    • 48249148310 scopus 로고    scopus 로고
    • Tau exon 10 alternative splicing and tauopathies
    • Liu F. Gong C. X. (2008) Tau exon 10 alternative splicing and tauopathies. Mol. Neurodegener. 3, 8.
    • (2008) Mol. Neurodegener. , vol.3 , pp. 8
    • Liu, F.1    Gong, C.X.2
  • 26
    • 0034789533 scopus 로고    scopus 로고
    • Relationship of the extended tau haplotype to tau biochemistry and neuropathology in progressive supranuclear palsy
    • DOI 10.1002/ana.1159
    • Liu W. K., Le T. V., Adamson J., Baker M., Cookson N., Hardy J., Hutton M., Yen S. H. Dickson D. W. (2001) Relationship of the extended tau haplotype to tau biochemistry and neuropathology in progressive supranuclear palsy. Ann. Neurol. 50, 494 502. (Pubitemid 32938894)
    • (2001) Annals of Neurology , vol.50 , Issue.4 , pp. 494-502
    • Liu, W.-K.1    Le, T.V.2    Adamson, J.3    Baker, M.4    Cookson, N.5    Hardy, J.6    Hutton, M.7    Yen, S.-H.8    Dickson, D.W.9
  • 27
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow E. M., Stamer K., Vogel R., Thies E. Mandelkow E. (2003) Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol. Aging 24, 1079 1085.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 29
    • 0031214452 scopus 로고    scopus 로고
    • Attenuation of oxidative neuronal necrosis by a dopamine D1 agonist in mouse cortical cell cultures
    • Noh J. S. Gwag B. J. (1997) Attenuation of oxidative neuronal necrosis by a dopamine D1 agonist in mouse cortical cell cultures. Exp. Neurol. 146, 604 608.
    • (1997) Exp. Neurol. , vol.146 , pp. 604-608
    • Noh, J.S.1    Gwag, B.J.2
  • 30
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S., Billings L., Kesslak J. P., Cribbs D. H. LaFerla F. M. (2004) Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43, 321 332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    Laferla, F.M.5
  • 31
    • 0000991680 scopus 로고    scopus 로고
    • Proteasome inhibitors induce cytochrome c-caspase-3-like protease-mediated apoptosis in cultured cortical neurons
    • Qiu J. H., Asai A., Chi S., Saito N., Hamada H. Kirino T. (2000) Proteasome inhibitors induce cytochrome c-caspase-3-like protease-mediated apoptosis in cultured cortical neurons. J. Neurosci. 20, 259 265.
    • (2000) J. Neurosci. , vol.20 , pp. 259-265
    • Qiu, J.H.1    Asai, A.2    Chi, S.3    Saito, N.4    Hamada, H.5    Kirino, T.6
  • 32
    • 25144460507 scopus 로고    scopus 로고
    • A new mutation of the tau gene, G303V, in early-onset familial progressive supranuclear palsy
    • Ros R., Thobois S., Streichenberger N. et al. (2005) A new mutation of the tau gene, G303V, in early-onset familial progressive supranuclear palsy. Arch. Neurol. 62, 1444 1450.
    • (2005) Arch. Neurol. , vol.62 , pp. 1444-1450
    • Ros, R.1    Thobois, S.2    Streichenberger, N.3
  • 33
    • 0033009603 scopus 로고    scopus 로고
    • Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: Tau pathologies with exclusively "exon 10" isoforms
    • Sergeant N., Wattez A. Delacourte A. (1999) Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: tau pathologies with exclusively "exon 10" isoforms. J. Neurochem. 72, 1243 1249.
    • (1999) J. Neurochem. , vol.72 , pp. 1243-1249
    • Sergeant, N.1    Wattez, A.2    Delacourte, A.3
  • 34
    • 0031859745 scopus 로고    scopus 로고
    • Neuronal death in cultured murine cortical cells is induced by inhibition of GAPDH and triosephosphate isomerase
    • Sheline C. T. Choi D. W. (1998) Neuronal death in cultured murine cortical cells is induced by inhibition of GAPDH and triosephosphate isomerase. Neurobiol. Dis. 5, 47 54.
    • (1998) Neurobiol. Dis. , vol.5 , pp. 47-54
    • Sheline, C.T.1    Choi, D.W.2
  • 35
    • 0038170494 scopus 로고    scopus 로고
    • Pathological inclusion bodies in tauopathies contain distinct complements of tau with three or four microtubule-binding repeat domains as demonstrated by new specific monoclonal antibodies
    • de Silva R., Lashley T., Gibb G. et al. (2003) Pathological inclusion bodies in tauopathies contain distinct complements of tau with three or four microtubule-binding repeat domains as demonstrated by new specific monoclonal antibodies. Neuropathol. Appl. Neurobiol. 29, 288 302.
    • (2003) Neuropathol. Appl. Neurobiol. , vol.29 , pp. 288-302
    • De Silva, R.1    Lashley, T.2    Gibb, G.3
  • 36
    • 33645766284 scopus 로고    scopus 로고
    • An immunohistochemical study of cases of sporadic and inherited frontotemporal lobar degeneration using 3R- and 4R-specific tau monoclonal antibodies
    • de Silva R., Lashley T., Strand C. et al. (2006) An immunohistochemical study of cases of sporadic and inherited frontotemporal lobar degeneration using 3R- and 4R-specific tau monoclonal antibodies. Acta Neuropathol. (Berl) 111, 329 340.
    • (2006) Acta Neuropathol. (Berl) , vol.111 , pp. 329-340
    • De Silva, R.1    Lashley, T.2    Strand, C.3
  • 38
    • 0036607704 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor-dependent inhibition of AP-1 activity by 2,3,7,8-tetrachlorodibenzo-p-dioxin in activated B cells
    • Suh J., Jeon Y. J., Kim H. M., Kang J. S., Kaminski N. E. Yang K. H. (2002) Aryl hydrocarbon receptor-dependent inhibition of AP-1 activity by 2,3,7,8-tetrachlorodibenzo-p-dioxin in activated B cells. Toxicol. Appl. Pharmacol. 181, 116 123.
    • (2002) Toxicol. Appl. Pharmacol. , vol.181 , pp. 116-123
    • Suh, J.1    Jeon, Y.J.2    Kim, H.M.3    Kang, J.S.4    Kaminski, N.E.5    Yang, K.H.6
  • 39
    • 27644484454 scopus 로고    scopus 로고
    • Induction and attenuation of neuronal apoptosis by proteasome inhibitors in murine cortical cell cultures
    • Suh J., Lee Y. A. Gwag B. J. (2005) Induction and attenuation of neuronal apoptosis by proteasome inhibitors in murine cortical cell cultures. J. Neurochem. 95, 684 694.
    • (2005) J. Neurochem. , vol.95 , pp. 684-694
    • Suh, J.1    Lee, Y.A.2    Gwag, B.J.3
  • 40
    • 0038292060 scopus 로고    scopus 로고
    • Isoforms changes of tau protein during development in various species
    • Takuma H., Arawaka S. Mori H. (2003) Isoforms changes of tau protein during development in various species. Brain Res. Dev. Brain Res. 142, 121 127.
    • (2003) Brain Res. Dev. Brain Res. , vol.142 , pp. 121-127
    • Takuma, H.1    Arawaka, S.2    Mori, H.3
  • 41
    • 0019868418 scopus 로고
    • Focal cerebral ischaemia in the rat: I. Description of technique and early neuropathological consequences following middle cerebral artery occlusion
    • Tamura A., Graham D. I., McCulloch J. Teasdale G. M. (1981) Focal cerebral ischaemia in the rat: 1. Description of technique and early neuropathological consequences following middle cerebral artery occlusion. J. Cereb. Blood Flow Metab. 1, 53 60. (Pubitemid 12230166)
    • (1981) Journal of Cerebral Blood Flow and Metabolism , vol.1 , Issue.1 , pp. 53-60
    • Tamura, A.1    Graham, D.I.2    McCulloch, J.3    Teasdale, G.M.4
  • 42
    • 0026719357 scopus 로고
    • Dementia after stroke: Baseline frequency, risks, and clinical features in a hospitalized cohort
    • Tatemichi T. K., Desmond D. W., Mayeux R. et al. (1992) Dementia after stroke: baseline frequency, risks, and clinical features in a hospitalized cohort. Neurology 42, 1185 1193.
    • (1992) Neurology , vol.42 , pp. 1185-1193
    • Tatemichi, T.K.1    Desmond, D.W.2    Mayeux, R.3
  • 43
    • 33645874205 scopus 로고    scopus 로고
    • Stroke-induced neurogenesis: Physiopathology and mechanisms
    • Taupin P. (2006) Stroke-induced neurogenesis: physiopathology and mechanisms. Curr. Neurovasc. Res. 3, 67 72.
    • (2006) Curr. Neurovasc. Res. , vol.3 , pp. 67-72
    • Taupin, P.1
  • 44
    • 0035823577 scopus 로고    scopus 로고
    • Functional differences of tau isoforms containing 3 or 4 C-terminal repeat regions and the influence of oxidative stress
    • Utton M. A., Gibb G. M., Burdett I. D., Anderton B. H. Vandecandelaere A. (2001) Functional differences of tau isoforms containing 3 or 4 C-terminal repeat regions and the influence of oxidative stress. J. Biol. Chem. 276, 34288 34297.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34288-34297
    • Utton, M.A.1    Gibb, G.M.2    Burdett, I.D.3    Anderton, B.H.4    Vandecandelaere, A.5
  • 45
    • 2542428253 scopus 로고    scopus 로고
    • Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats
    • Wen Y., Yang S., Liu R., Brun-Zinkernagel A. M., Koulen P. Simpkins J. W. (2004) Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats. J. Biol. Chem. 279, 22684 22692.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22684-22692
    • Wen, Y.1    Yang, S.2    Liu, R.3    Brun-Zinkernagel, A.M.4    Koulen, P.5    Simpkins, J.W.6
  • 47
    • 0037203544 scopus 로고    scopus 로고
    • Cellular and molecular pathways of ischemic neuronal death
    • Won S. J., Kim D. Y. Gwag B. J. (2002) Cellular and molecular pathways of ischemic neuronal death. J. Biochem. Mol. Biol. 35, 67 86.
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 67-86
    • Won, S.J.1    Kim, D.Y.2    Gwag, B.J.3
  • 48
    • 34249883587 scopus 로고    scopus 로고
    • Induction and selective accumulation of mutant ubiquitin in CA1 pyramidal neurons after transient global ischemia
    • Yamashiro K., Liu R., Maeda M., Hattori N. Urabe T. (2007) Induction and selective accumulation of mutant ubiquitin in CA1 pyramidal neurons after transient global ischemia. Neuroscience 147, 71 79.
    • (2007) Neuroscience , vol.147 , pp. 71-79
    • Yamashiro, K.1    Liu, R.2    Maeda, M.3    Hattori, N.4    Urabe, T.5
  • 49
    • 33748996792 scopus 로고    scopus 로고
    • Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies
    • Yoshida M. (2006) Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies. Neuropathology 26, 457 470.
    • (2006) Neuropathology , vol.26 , pp. 457-470
    • Yoshida, M.1
  • 50
    • 77649273643 scopus 로고    scopus 로고
    • Mutant ubiquitin-mediated beta-secretase stability via activation of caspase-3 is related to beta-amyloid accumulation in ischemic striatum in rats
    • Zhang Y., Xiong M., Yan R. Q. Sun F. Y. (2010) Mutant ubiquitin-mediated beta-secretase stability via activation of caspase-3 is related to beta-amyloid accumulation in ischemic striatum in rats. J. Cereb. Blood Flow Metab. 30, 566 575.
    • (2010) J. Cereb. Blood Flow Metab. , vol.30 , pp. 566-575
    • Zhang, Y.1    Xiong, M.2    Yan, R.Q.3    Sun, F.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.