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Volumn 14, Issue 11, 2008, Pages 479-485

TDP-43: an emerging new player in neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; TAR DNA BINDING PROTEIN 43; TAU PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 54249100481     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2008.09.001     Document Type: Article
Times cited : (96)

References (87)
  • 1
    • 0344256486 scopus 로고    scopus 로고
    • Structural diversity and functional implications of the eukaryotic TDP gene family
    • Wang H.Y., et al. Structural diversity and functional implications of the eukaryotic TDP gene family. Genomics 83 (2004) 130-139
    • (2004) Genomics , vol.83 , pp. 130-139
    • Wang, H.Y.1
  • 2
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou S.H., et al. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol. 69 (1995) 3584-3596
    • (1995) J. Virol. , vol.69 , pp. 3584-3596
    • Ou, S.H.1
  • 3
    • 0037108967 scopus 로고    scopus 로고
    • Higher order arrangement of the eukaryotic nuclear bodies
    • Wang I.F., et al. Higher order arrangement of the eukaryotic nuclear bodies. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 13583-13588
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13583-13588
    • Wang, I.F.1
  • 4
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti E., et al. Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J. 20 (2001) 1774-1784
    • (2001) EMBO J. , vol.20 , pp. 1774-1784
    • Buratti, E.1
  • 5
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • Mercado P.A., et al. Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res. 33 (2005) 6000-6010
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6000-6010
    • Mercado, P.A.1
  • 6
    • 54249117446 scopus 로고    scopus 로고
    • Bose, J.K. et al. TDP-43 overexpression enhances exon-7 inclusion during SMN pre-mRNA splicing. J. Biol. Chem. (in press)
    • Bose, J.K. et al. TDP-43 overexpression enhances exon-7 inclusion during SMN pre-mRNA splicing. J. Biol. Chem. (in press)
  • 7
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T., et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351 (2006) 602-611
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 602-611
    • Arai, T.1
  • 8
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M., et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314 (2006) 130-133
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1
  • 9
    • 35348853257 scopus 로고    scopus 로고
    • TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis
    • Neumann M., et al. TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis. Arch. Neurol. 64 (2007) 1388-1394
    • (2007) Arch. Neurol. , vol.64 , pp. 1388-1394
    • Neumann, M.1
  • 10
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E., and Baralle F.E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276 (2001) 36337-36343
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 11
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti E., et al. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J. Biol. Chem. 280 (2005) 37572-37584
    • (2005) J. Biol. Chem. , vol.280 , pp. 37572-37584
    • Buratti, E.1
  • 12
    • 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., et al. 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
  • 13
    • 34848921202 scopus 로고    scopus 로고
    • Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43
    • Zhang Y.J., et al. Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J. Neurosci. 27 (2007) 10530-10534
    • (2007) J. Neurosci. , vol.27 , pp. 10530-10534
    • Zhang, Y.J.1
  • 14
    • 37549025044 scopus 로고    scopus 로고
    • A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function
    • Abhyankar M.M., et al. A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function. J. Biol. Chem. 282 (2007) 36143-36154
    • (2007) J. Biol. Chem. , vol.282 , pp. 36143-36154
    • Abhyankar, M.M.1
  • 15
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • Lehner B., and Sanderson C.M. A protein interaction framework for human mRNA degradation. Genome Res. 14 (2004) 1315-1323
    • (2004) Genome Res. , vol.14 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 16
    • 9644310314 scopus 로고    scopus 로고
    • The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II
    • Kim M., et al. The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II. Nature 432 (2004) 517-522
    • (2004) Nature , vol.432 , pp. 517-522
    • Kim, M.1
  • 17
    • 33645844251 scopus 로고    scopus 로고
    • The role of Rat1 in coupling mRNA 3′-end processing to transcription termination: implications for a unified allosteric-torpedo model
    • Luo W., et al. The role of Rat1 in coupling mRNA 3′-end processing to transcription termination: implications for a unified allosteric-torpedo model. Genes Dev. 20 (2006) 954-965
    • (2006) Genes Dev. , vol.20 , pp. 954-965
    • Luo, W.1
  • 18
    • 0037089626 scopus 로고    scopus 로고
    • SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins
    • Schultz D.C., et al. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 16 (2002) 919-932
    • (2002) Genes Dev. , vol.16 , pp. 919-932
    • Schultz, D.C.1
  • 19
    • 0033636517 scopus 로고    scopus 로고
    • The U. S. A. -derived transcriptional coactivator PC2 is a submodule of TRAP/SMCC and acts synergistically with other PCs
    • Malik S., et al. The U. S. A. -derived transcriptional coactivator PC2 is a submodule of TRAP/SMCC and acts synergistically with other PCs. Mol. Cell 5 (2000) 753-760
    • (2000) Mol. Cell , vol.5 , pp. 753-760
    • Malik, S.1
  • 20
    • 0347379968 scopus 로고    scopus 로고
    • A mammalian homolog of Drosophila melanogaster transcriptional coactivator intersex is a subunit of the mammalian Mediator complex
    • Sato S., et al. A mammalian homolog of Drosophila melanogaster transcriptional coactivator intersex is a subunit of the mammalian Mediator complex. J. Biol. Chem. 278 (2003) 49671-49674
    • (2003) J. Biol. Chem. , vol.278 , pp. 49671-49674
    • Sato, S.1
  • 21
    • 0037413713 scopus 로고    scopus 로고
    • Genomic structure and analysis of transcriptional regulation of the mouse zinc-fingers and homeoboxes 1 (ZHX1) gene
    • Shou Z., et al. Genomic structure and analysis of transcriptional regulation of the mouse zinc-fingers and homeoboxes 1 (ZHX1) gene. Gene 302 (2003) 83-94
    • (2003) Gene , vol.302 , pp. 83-94
    • Shou, Z.1
  • 22
    • 9644308046 scopus 로고    scopus 로고
    • Human 5′ → 3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites
    • West S., et al. Human 5′ → 3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites. Nature 432 (2004) 522-525
    • (2004) Nature , vol.432 , pp. 522-525
    • West, S.1
  • 23
    • 35548953842 scopus 로고    scopus 로고
    • Splicing- and cleavage-independent requirement of RNA polymerase II CTD for mRNA release from the transcription site
    • Custodio N., et al. Splicing- and cleavage-independent requirement of RNA polymerase II CTD for mRNA release from the transcription site. J. Cell Biol. 179 (2007) 199-207
    • (2007) J. Cell Biol. , vol.179 , pp. 199-207
    • Custodio, N.1
  • 24
    • 0036160338 scopus 로고    scopus 로고
    • Frontotemporal dementia
    • Snowden J.S., et al. Frontotemporal dementia. Br. J. Psychiatry 180 (2002) 140-143
    • (2002) Br. J. Psychiatry , vol.180 , pp. 140-143
    • Snowden, J.S.1
  • 25
    • 34250627671 scopus 로고    scopus 로고
    • The complex aetiology of frontotemporal lobar degeneration
    • Pickering-Brown S.M. The complex aetiology of frontotemporal lobar degeneration. Exp. Neurol. 206 (2007) 1-10
    • (2007) Exp. Neurol. , vol.206 , pp. 1-10
    • Pickering-Brown, S.M.1
  • 26
    • 34547663747 scopus 로고    scopus 로고
    • TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions
    • Cairns N.J., et al. TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions. Am. J. Pathol. 171 (2007) 227-240
    • (2007) Am. J. Pathol. , vol.171 , pp. 227-240
    • Cairns, N.J.1
  • 27
    • 0037044240 scopus 로고    scopus 로고
    • The overlap of amyotrophic lateral sclerosis and frontotemporal dementia
    • Lomen-Hoerth C., et al. The overlap of amyotrophic lateral sclerosis and frontotemporal dementia. Neurology 59 (2002) 1077-1079
    • (2002) Neurology , vol.59 , pp. 1077-1079
    • Lomen-Hoerth, C.1
  • 28
    • 33947259313 scopus 로고    scopus 로고
    • Establishing subtypes of the continuum of frontal lobe impairment in amyotrophic lateral sclerosis
    • Murphy J., et al. Establishing subtypes of the continuum of frontal lobe impairment in amyotrophic lateral sclerosis. Arch. Neurol. 64 (2007) 330-334
    • (2007) Arch. Neurol. , vol.64 , pp. 330-334
    • Murphy, J.1
  • 29
    • 34247147601 scopus 로고    scopus 로고
    • Continuum of frontal lobe impairment in amyotrophic lateral sclerosis
    • Murphy J.M., et al. Continuum of frontal lobe impairment in amyotrophic lateral sclerosis. Arch. Neurol. 64 (2007) 530-534
    • (2007) Arch. Neurol. , vol.64 , pp. 530-534
    • Murphy, J.M.1
  • 30
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie I.R., et al. Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann. Neurol. 61 (2007) 427-434
    • (2007) Ann. Neurol. , vol.61 , pp. 427-434
    • Mackenzie, I.R.1
  • 31
    • 34249949338 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
    • Amador-Ortiz C., et al. TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease. Ann. Neurol. 61 (2007) 435-445
    • (2007) Ann. Neurol. , vol.61 , pp. 435-445
    • Amador-Ortiz, C.1
  • 32
    • 44649137415 scopus 로고    scopus 로고
    • Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies
    • Uryu K., et al. Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies. J. Neuropathol. Exp. Neurol. 67 (2008) 555-564
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 555-564
    • Uryu, K.1
  • 33
    • 36348972414 scopus 로고    scopus 로고
    • Concurrence of TDP-43, tau and α-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies
    • Higashi S., et al. Concurrence of TDP-43, tau and α-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies. Brain Res. 1184 (2007) 284-294
    • (2007) Brain Res. , vol.1184 , pp. 284-294
    • Higashi, S.1
  • 34
    • 34547733547 scopus 로고    scopus 로고
    • Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases
    • Nakashima-Yasuda H., et al. Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases. Acta Neuropathol. 114 (2007) 221-229
    • (2007) Acta Neuropathol. , vol.114 , pp. 221-229
    • Nakashima-Yasuda, H.1
  • 35
    • 34249709931 scopus 로고    scopus 로고
    • TDP-43 is deposited in the Guam parkinsonism-dementia complex brains
    • Hasegawa M., et al. TDP-43 is deposited in the Guam parkinsonism-dementia complex brains. Brain 130 (2007) 1386-1394
    • (2007) Brain , vol.130 , pp. 1386-1394
    • Hasegawa, M.1
  • 36
    • 36949036676 scopus 로고    scopus 로고
    • Pathological TDP-43 in parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam
    • Geser F., et al. Pathological TDP-43 in parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam. Acta Neuropathol 115 (2008) 133-145
    • (2008) Acta Neuropathol , vol.115 , pp. 133-145
    • Geser, F.1
  • 37
    • 34848856633 scopus 로고    scopus 로고
    • Hippocampal sclerosis dementia: a reappraisal
    • Probst A., et al. Hippocampal sclerosis dementia: a reappraisal. Acta Neuropathol. 114 (2007) 335-345
    • (2007) Acta Neuropathol. , vol.114 , pp. 335-345
    • Probst, A.1
  • 38
    • 37549012160 scopus 로고    scopus 로고
    • TDP-43: a novel neurodegenerative proteinopathy
    • Forman M.S., et al. TDP-43: a novel neurodegenerative proteinopathy. Curr. Opin. Neurobiol. 17 (2007) 548-555
    • (2007) Curr. Opin. Neurobiol. , vol.17 , pp. 548-555
    • Forman, M.S.1
  • 39
    • 34447099564 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: clinical and pathological relationships
    • Snowden J., et al. Frontotemporal lobar degeneration: clinical and pathological relationships. Acta Neuropathol. 114 (2007) 31-38
    • (2007) Acta Neuropathol. , vol.114 , pp. 31-38
    • Snowden, J.1
  • 40
    • 49249118746 scopus 로고    scopus 로고
    • TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander
    • Banks G.T., et al. TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander. Mamm. Genome 19 (2008) 299-305
    • (2008) Mamm. Genome , vol.19 , pp. 299-305
    • Banks, G.T.1
  • 41
    • 54249097175 scopus 로고    scopus 로고
    • ALS and FTLD: two faces of TDP-43 proteinopathy
    • Liscic R.M., et al. ALS and FTLD: two faces of TDP-43 proteinopathy. Eur. J. Neurol. 15 (2008) 772-780
    • (2008) Eur. J. Neurol. , vol.15 , pp. 772-780
    • Liscic, R.M.1
  • 42
    • 34447098604 scopus 로고    scopus 로고
    • Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy
    • Guinto J.B., et al. Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy. Acta Neuropathol. 114 (2007) 55-61
    • (2007) Acta Neuropathol. , vol.114 , pp. 55-61
    • Guinto, J.B.1
  • 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., et al. TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease. Acta Neuropathol. 114 (2007) 63-70
    • (2007) Acta Neuropathol. , vol.114 , pp. 63-70
    • Kwong, L.K.1
  • 44
    • 34447097449 scopus 로고    scopus 로고
    • The neuropathology and clinical phenotype of FTD with progranulin mutations
    • Mackenzie I.R. The neuropathology and clinical phenotype of FTD with progranulin mutations. Acta Neuropathol. 114 (2007) 49-54
    • (2007) Acta Neuropathol. , vol.114 , pp. 49-54
    • Mackenzie, I.R.1
  • 45
    • 35448970651 scopus 로고    scopus 로고
    • The molecular genetics and neuropathology of frontotemporal lobar degeneration: recent developments
    • Mackenzie I.R., and Rademakers R. The molecular genetics and neuropathology of frontotemporal lobar degeneration: recent developments. Neurogenetics 8 (2007) 237-248
    • (2007) Neurogenetics , vol.8 , pp. 237-248
    • Mackenzie, I.R.1    Rademakers, R.2
  • 46
    • 37349039461 scopus 로고    scopus 로고
    • TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis
    • Kwong L.K., et al. TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis. Neurosignals 16 (2008) 41-51
    • (2008) Neurosignals , vol.16 , pp. 41-51
    • Kwong, L.K.1
  • 47
    • 34447108549 scopus 로고    scopus 로고
    • Progranulin and frontotemporal lobar degeneration
    • Pickering-Brown S.M. Progranulin and frontotemporal lobar degeneration. Acta Neuropathol. 114 (2007) 39-47
    • (2007) Acta Neuropathol. , vol.114 , pp. 39-47
    • Pickering-Brown, S.M.1
  • 48
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration
    • Cairns N.J., et al. Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol. 114 (2007) 5-22
    • (2007) Acta Neuropathol. , vol.114 , pp. 5-22
    • Cairns, N.J.1
  • 49
    • 34247625005 scopus 로고    scopus 로고
    • Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43
    • Davidson Y., et al. Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43. Acta Neuropathol. 113 (2007) 521-533
    • (2007) Acta Neuropathol. , vol.113 , pp. 521-533
    • Davidson, Y.1
  • 50
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang I.F., et al. TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem. 105 (2008) 797-806
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1
  • 51
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • Filimonenko M., et al. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J. Cell Biol. 179 (2007) 485-500
    • (2007) J. Cell Biol. , vol.179 , pp. 485-500
    • Filimonenko, M.1
  • 52
    • 23044471011 scopus 로고    scopus 로고
    • Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
    • Skibinski G., et al. Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia. Nat. Genet. 37 (2005) 806-808
    • (2005) Nat. Genet. , vol.37 , pp. 806-808
    • Skibinski, G.1
  • 53
    • 33749006845 scopus 로고    scopus 로고
    • ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B)
    • Parkinson N., et al. ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B). Neurology 67 (2006) 1074-1077
    • (2006) Neurology , vol.67 , pp. 1074-1077
    • Parkinson, N.1
  • 54
    • 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., et al. A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 6439-6444
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6439-6444
    • Johnson, B.S.1
  • 55
    • 0037452563 scopus 로고    scopus 로고
    • The staufen/pumilio pathway is involved in Drosophila long-term memory
    • Dubnau J., et al. The staufen/pumilio pathway is involved in Drosophila long-term memory. Curr. Biol. 13 (2003) 286-296
    • (2003) Curr. Biol. , vol.13 , pp. 286-296
    • Dubnau, J.1
  • 56
    • 0033730999 scopus 로고    scopus 로고
    • Local protein synthesis and its role in synapse-specific plasticity
    • Martin K.C., et al. Local protein synthesis and its role in synapse-specific plasticity. Curr. Opin. Neurobiol. 10 (2000) 587-592
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 587-592
    • Martin, K.C.1
  • 57
    • 33749077101 scopus 로고    scopus 로고
    • Dendritic protein synthesis, synaptic plasticity, and memory
    • Sutton M.A., and Schuman E.M. Dendritic protein synthesis, synaptic plasticity, and memory. Cell 127 (2006) 49-58
    • (2006) Cell , vol.127 , pp. 49-58
    • Sutton, M.A.1    Schuman, E.M.2
  • 58
    • 32344440041 scopus 로고    scopus 로고
    • RNA binding proteins and the regulation of neuronal synaptic plasticity
    • Ule J., and Darnell R.B. RNA binding proteins and the regulation of neuronal synaptic plasticity. Curr. Opin. Neurobiol. 16 (2006) 102-110
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 102-110
    • Ule, J.1    Darnell, R.B.2
  • 59
    • 33745597062 scopus 로고    scopus 로고
    • A clustered plasticity model of long-term memory engrams
    • Govindarajan A., et al. A clustered plasticity model of long-term memory engrams. Nat. Rev. Neurosci. 7 (2006) 575-583
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 575-583
    • Govindarajan, A.1
  • 60
    • 33846252240 scopus 로고    scopus 로고
    • Genome-wide atlas of gene expression in the adult mouse brain
    • Lein E.S., et al. Genome-wide atlas of gene expression in the adult mouse brain. Nature 445 (2007) 168-176
    • (2007) Nature , vol.445 , pp. 168-176
    • Lein, E.S.1
  • 61
    • 33847283381 scopus 로고    scopus 로고
    • The fragile X mental retardation protein-RNP granules show an mGluR-dependent localization in the post-synaptic spines
    • Ferrari F., et al. The fragile X mental retardation protein-RNP granules show an mGluR-dependent localization in the post-synaptic spines. Mol. Cell. Neurosci. 34 (2007) 343-354
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 343-354
    • Ferrari, F.1
  • 62
    • 2342487399 scopus 로고    scopus 로고
    • The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs
    • Villace P., et al. The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 (2004) 2411-2420
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2411-2420
    • Villace, P.1
  • 63
    • 33645727310 scopus 로고    scopus 로고
    • Characterization of an RNA granule from developing brain
    • Elvira G., et al. Characterization of an RNA granule from developing brain. Mol. Cell. Proteomics 5 (2006) 635-651
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 635-651
    • Elvira, G.1
  • 64
    • 33845445765 scopus 로고    scopus 로고
    • Staufen- and FMRP-containing neuronal RNPs are structurally and functionally related to somatic P bodies
    • Barbee S.A., et al. Staufen- and FMRP-containing neuronal RNPs are structurally and functionally related to somatic P bodies. Neuron 52 (2006) 997-1009
    • (2006) Neuron , vol.52 , pp. 997-1009
    • Barbee, S.A.1
  • 65
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R., and Sheth U. P bodies and the control of mRNA translation and degradation. Mol. Cell 25 (2007) 635-646
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 66
    • 9144225636 scopus 로고    scopus 로고
    • The Microprocessor complex mediates the genesis of microRNAs
    • Gregory R.I., et al. The Microprocessor complex mediates the genesis of microRNAs. Nature 432 (2004) 235-240
    • (2004) Nature , vol.432 , pp. 235-240
    • Gregory, R.I.1
  • 67
    • 0035140593 scopus 로고    scopus 로고
    • Spaced stimuli stabilize MAPK pathway activation and its effects on dendritic morphology
    • Wu G.Y., et al. Spaced stimuli stabilize MAPK pathway activation and its effects on dendritic morphology. Nat. Neurosci. 4 (2001) 151-158
    • (2001) Nat. Neurosci. , vol.4 , pp. 151-158
    • Wu, G.Y.1
  • 68
    • 0037168109 scopus 로고    scopus 로고
    • Disruption of dendritic translation of CaMKIIα impairs stabilization of synaptic plasticity and memory consolidation
    • Miller S., et al. Disruption of dendritic translation of CaMKIIα impairs stabilization of synaptic plasticity and memory consolidation. Neuron 36 (2002) 507-519
    • (2002) Neuron , vol.36 , pp. 507-519
    • Miller, S.1
  • 69
    • 67349161628 scopus 로고    scopus 로고
    • Neuronal inclusion protein TDP-43 has no primary genetic role in FTD and ALS
    • 10.1016/j.neurobiolaging.2007.11.002
    • Gijselinck I., et al. Neuronal inclusion protein TDP-43 has no primary genetic role in FTD and ALS. Neurobiol. Aging (2007). http://www.sciencedirect.com/science/journal/01974580 10.1016/j.neurobiolaging.2007.11.002
    • (2007) Neurobiol. Aging
    • Gijselinck, I.1
  • 70
    • 34247868841 scopus 로고    scopus 로고
    • TDP-43 gene analysis in frontotemporal lobar degeneration
    • Rollinson S., et al. TDP-43 gene analysis in frontotemporal lobar degeneration. Neurosci. Lett. 419 (2007) 1-4
    • (2007) Neurosci. Lett. , vol.419 , pp. 1-4
    • Rollinson, S.1
  • 71
    • 56049111858 scopus 로고    scopus 로고
    • No association of TDP-43 with sporadic frontotemporal dementia
    • 10.1016/j.neurobiolaging.2007.05.022
    • Schumacher A., et al. No association of TDP-43 with sporadic frontotemporal dementia. Neurobiol. Aging (2007). http://www.sciencedirect.com/science/journal/01974580 10.1016/j.neurobiolaging.2007.05.022
    • (2007) Neurobiol. Aging
    • Schumacher, A.1
  • 72
    • 41949119043 scopus 로고    scopus 로고
    • TDP-43 A315T mutation in familial motor neuron disease
    • Gitcho M.A., et al. TDP-43 A315T mutation in familial motor neuron disease. Ann. Neurol. 63 (2008) 535-538
    • (2008) Ann. Neurol. , vol.63 , pp. 535-538
    • Gitcho, M.A.1
  • 73
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E., et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 40 (2008) 572-574
    • (2008) Nat. Genet. , vol.40 , pp. 572-574
    • Kabashi, E.1
  • 74
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J., et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319 (2008) 1668-1672
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1
  • 75
    • 41949100148 scopus 로고    scopus 로고
    • TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis
    • Van Deerlin V.M., et al. TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis. Lancet Neurol. 7 (2008) 409-416
    • (2008) Lancet Neurol. , vol.7 , pp. 409-416
    • Van Deerlin, V.M.1
  • 76
    • 42949094584 scopus 로고    scopus 로고
    • TDP-43 mutation in familial amyotrophic lateral sclerosis
    • Yokoseki A., et al. TDP-43 mutation in familial amyotrophic lateral sclerosis. Ann. Neurol. 63 (2008) 538-542
    • (2008) Ann. Neurol. , vol.63 , pp. 538-542
    • Yokoseki, A.1
  • 77
    • 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., et al. 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 (2008) 182-194
    • (2008) Am. J. Pathol. , vol.173 , pp. 182-194
    • Igaz, L.M.1
  • 78
    • 9444279617 scopus 로고    scopus 로고
    • Stress granule assembly is mediated by prion-like aggregation of TIA-1
    • Gilks N., et al. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol. Biol. Cell 15 (2004) 5383-5398
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5383-5398
    • Gilks, N.1
  • 79
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li S.H., and Li X.J. Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet. 20 (2004) 146-154
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 80
    • 2942575993 scopus 로고    scopus 로고
    • A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology
    • Sato S., et al. A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology. Mol. Cell 14 (2004) 685-691
    • (2004) Mol. Cell , vol.14 , pp. 685-691
    • Sato, S.1
  • 81
    • 25144498379 scopus 로고    scopus 로고
    • A human protein-protein interaction network: a resource for annotating the proteome
    • Stelzl U., et al. A human protein-protein interaction network: a resource for annotating the proteome. Cell 122 (2005) 957-968
    • (2005) Cell , vol.122 , pp. 957-968
    • Stelzl, U.1
  • 82
    • 34247123666 scopus 로고    scopus 로고
    • TDP-43-positive white matter pathology in frontotemporal lobar degeneration with ubiquitin-positive inclusions
    • Neumann M., et al. TDP-43-positive white matter pathology in frontotemporal lobar degeneration with ubiquitin-positive inclusions. J. Neuropathol. Exp. Neurol. 66 (2007) 177-183
    • (2007) J. Neuropathol. Exp. Neurol. , vol.66 , pp. 177-183
    • Neumann, M.1
  • 83
    • 33846815066 scopus 로고    scopus 로고
    • TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations
    • Neumann M., et al. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J. Neuropathol. Exp. Neurol. 66 (2007) 152-157
    • (2007) J. Neuropathol. Exp. Neurol. , vol.66 , pp. 152-157
    • Neumann, M.1
  • 84
    • 36949008994 scopus 로고    scopus 로고
    • TDP-43-immunoreactive neuronal and glial inclusions in the neostriatum in amyotrophic lateral sclerosis with and without dementia
    • Zhang H., et al. TDP-43-immunoreactive neuronal and glial inclusions in the neostriatum in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol. 115 (2008) 115-122
    • (2008) Acta Neuropathol. , vol.115 , pp. 115-122
    • Zhang, H.1
  • 85
    • 44949162153 scopus 로고    scopus 로고
    • Atypical frontotemporal lobar degeneration with ubiquitin-positive, TDP-43-negative neuronal inclusions
    • Mackenzie I.R., et al. Atypical frontotemporal lobar degeneration with ubiquitin-positive, TDP-43-negative neuronal inclusions. Brain 131 (2008) 1282-1293
    • (2008) Brain , vol.131 , pp. 1282-1293
    • Mackenzie, I.R.1
  • 86
    • 47949123961 scopus 로고    scopus 로고
    • TDP-43-negative FTLD-U is a significant new clinico-pathological subtype of FTLD
    • Roeber S., et al. TDP-43-negative FTLD-U is a significant new clinico-pathological subtype of FTLD. Acta Neuropathol. 116 (2008) 147-157
    • (2008) Acta Neuropathol. , vol.116 , pp. 147-157
    • Roeber, S.1
  • 87
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M., et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann. Neurol. 64 (2008) 60-70
    • (2008) Ann. Neurol. , vol.64 , pp. 60-70
    • Hasegawa, M.1


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