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在庫・価格 : 2024年04月24日 02時53分 現在

商品名 商品コード メーカー 包装 価格 在庫 リスト
Anti-TARDBP, Mouse-Mono(2E2-D3) <Anti-TAR DNA Binding Protein>
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H00023435-M01 ABNアブノヴァ
Abnova Corporation
100 μg ¥72,000
(未発注)
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在庫・価格 : 2024年04月24日 02時53分 現在

Anti-TARDBP, Mouse-Mono(2E2-D3) <Anti-TAR DNA Binding Protein>

  • 商品コード:H00023435-M01
  • メーカー:ABN
  • 包装:100μg
  • 価格: ¥72,000
  • 在庫:無(未発注)
使用文献
No. 文献情報 備考 参照
1 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. 2006 Dec;351(3):602-11
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PubMed
2 Neumann M et al. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J. Neuropathol. Exp. Neurol. 2007 Feb;66(2):152-7
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3 Tan CF et al. TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol. 2007 May;113(5):535-42
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PubMed
4 Neumann M et al. TDP-43-positive white matter pathology in frontotemporal lobar degeneration with ubiquitin-positive inclusions. J. Neuropathol. Exp. Neurol. 2007 Mar;66(3):177-83
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PubMed
5 Fukuda T et al. DEAD-box RNA helicase subunits of the Drosha complex are required for processing of rRNA and a subset of microRNAs. Nat. Cell Biol. 2007 May;9(5):604-11
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PubMed
6 Hasegawa M et al. TDP-43 is deposited in the Guam parkinsonism-dementia complex brains. Brain 2007 May;130(Pt 5):1386-94
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PubMed
7 Mackenzie IR et al. Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann. Neurol. 2007 May;61(5):427-34
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PubMed
8 Amador-Ortiz C et al. TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer&quot;s disease. Ann. Neurol. 2007 May;61(5):435-45
Amador-Ortiz C et al
2007/01/01
PubMed
9 Zhang H et al. TDP-43-immunoreactive neuronal and glial inclusions in the neostriatum in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol. 2008 Jan;115(1):115-22
Zhang H et al
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PubMed
10 Shankaran SS et al. Missense mutations in the progranulin gene linked to frontotemporal lobar degeneration with ubiquitin-immunoreactive inclusions reduce progranulin production and secretion. J. Biol. Chem. 2008 Jan;283(3):1744-53
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PubMed
11 Kovacs GG et al. MAPT S305I mutation: implications for argyrophilic grain disease. Acta Neuropathol. 2008 Jul;116(1):103-18
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PubMed
12 Beck J et al. A distinct clinical, neuropsychological and radiological phenotype is associated with progranulin gene mutations in a large UK series. Brain 2008 Mar;131(Pt 3):706-20
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PubMed
13 Zhang HX et al. Epitope mapping of 2E2-D3, a monoclonal antibody directed against human TDP-43. Neurosci. Lett. 2008 Mar;434(2):170-4
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PubMed
14 Winton MJ et al. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 2008 May;283(19):13302-9
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PubMed
15 Johnson BS 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. 2008 Apr;105(17):6439-44
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PubMed
16 Foulds P et al. TDP-43 protein in plasma may index TDP-43 brain pathology in Alzheimer&quot;s disease and frontotemporal lobar degeneration. Acta Neuropathol. 2008 Aug;116(2):141-6
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2008/01/01
PubMed
17 Igaz LM 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. 2008 Jul;173(1):182-94
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PubMed
18 Sleegers K et al. Molecular pathogenesis of frontotemporal lobar degeneration: basic science seminar in neurology. Arch. Neurol. 2008 Jun;65(6):700-4
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PubMed
19 Mori F et al. Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol. 2008 Aug;116(2):193-203
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PubMed
20 Lin WL et al. Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases. Acta Neuropathol. 2008 Aug;116(2):205-13
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2008/01/01
PubMed
21 Weihl CC et al. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J. Neurol. Neurosurg. Psychiatr. 2008 Oct;79(10):1186-9
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PubMed
22 Miklossy J et al. Enduring involvement of tau, beta-amyloid, alpha-synuclein, ubiquitin and TDP-43 pathology in the amyotrophic lateral sclerosis/parkinsonism-dementia complex of Guam (ALS/PDC). Acta Neuropathol. 2008 Dec;116(6):625-37
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PubMed
23 Skoglund L et al. Frontotemporal dementia in a large Swedish family is caused by a progranulin null mutation. Neurogenetics 2009 Feb;10(1):27-34
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PubMed
24 Nishihira Y et al. Sporadic amyotrophic lateral sclerosis of long duration is associated with relatively mild TDP-43 pathology. Acta Neuropathol. 2009 Jan;117(1):45-53
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2009/01/01
PubMed
25 Kasai T et al. Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis. Acta Neuropathol. 2009 Jan;117(1):55-62
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2009/01/01
PubMed
26 Sepp辰nen A et al. Expression of collagen XVII and ubiquitin-binding protein p62 in motor neuron disease. Brain Res. 2009 Jan;1247:171-7
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2009/01/01
PubMed
27 Steinacker P et al. TDP-43 in cerebrospinal fluid of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Arch. Neurol. 2008 Nov;65(11):1481-7
Steinacker P et al
2008/01/01
PubMed
28 Moisse K et al. 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. 2009 Jan;1249:202-11
Moisse K et al
2009/01/01
PubMed
29 Igaz LM et al. Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies. J. Biol. Chem. 2009 Mar;284(13):8516-24
Igaz LM et al
2009/01/01
PubMed
30 Rollinson S et al. Ubiquitin associated protein 1 is a risk factor for frontotemporal lobar degeneration. Neurobiol. Aging 2009 Apr;30(4):656-65
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2009/01/01
PubMed
31 Velakoulis D et al. Frontotemporal dementia presenting as schizophrenia-like psychosis in young people: clinicopathological series and review of cases. Br J Psychiatry 2009 Apr;194(4):298-305
Velakoulis D et al
2009/01/01
PubMed
32 Oliv辿 M et al. TAR DNA-Binding protein 43 accumulation in protein aggregate myopathies. J. Neuropathol. Exp. Neurol. 2009 Mar;68(3):262-73
Oliv辿 M et al
2009/01/01
PubMed
33 Schwab C et al. Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease. J. Neuropathol. Exp. Neurol. 2008 Dec;67(12):1159-65
Schwab C et al
2008/01/01
PubMed
34 Sanelli T et al. Evidence that TDP-43 is not the major ubiquitinated target within the pathological inclusions of amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 2007 Dec;66(12):1147-53
Sanelli T et al
2007/01/01
PubMed
35 Clarim坦n J et al. Early-onset familial lewy body dementia with extensive tauopathy: a clinical, genetic, and neuropathological study. J. Neuropathol. Exp. Neurol. 2009 Jan;68(1):73-82
Clarim坦n J et al
2009/01/01
PubMed
36 Kovacs GG et al. White matter tauopathy with globular glial inclusions: a distinct sporadic frontotemporal lobar degeneration. J. Neuropathol. Exp. Neurol. 2008 Oct;67(10):963-75
Kovacs GG et al
2008/01/01
PubMed
37 Humayun S et al. The complement factor C5a receptor is upregulated in NFL-/- mouse motor neurons. J. Neuroimmunol. 2009 May;210(1-2):52-62
Humayun S et al
2009/01/01
PubMed
38 Gitcho MA et al. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J. Biol. Chem. 2009 May;284(18):12384-98
Gitcho MA et al
2009/01/01
PubMed
39 Moisse K et al. Cytosolic TDP-43 expression following axotomy is associated with caspase 3 activation in NFL-/- mice: support for a role for TDP-43 in the physiological response to neuronal injury. Brain Res. 2009 Nov;1296:176-86
Moisse K et al
2009/01/01
PubMed
40 Foulds PG et al. Plasma phosphorylated-TDP-43 protein levels correlate with brain pathology in frontotemporal lobar degeneration. Acta Neuropathol. 2009 Nov;118(5):647-58
Foulds PG et al
2009/01/01
PubMed
41 Velakoulis D et al. Abnormal hippocampal distribution of TDP-43 in patients with-late onset psychosis. Aust N Z J Psychiatry 2009 Aug;43(8):739-45
Velakoulis D et al
2009/01/01
PubMed
42 Nishimoto Y et al. Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43. J. Biol. Chem. 2010 Jan;285(1):608-19
Nishimoto Y et al
2010/01/01
PubMed
43 Fiesel FC et al. Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6. EMBO J. 2010 Jan;29(1):209-21
Fiesel FC et al
2010/01/01
PubMed
44 Zhang HX et al. Alteration of biochemical and pathological properties of TDP-43 protein by a lipid mediator, 15-deoxy-Delta(12,14)-prostaglandin J(2). Exp. Neurol. 2010 Apr;222(2):296-303
Zhang HX et al
2010/01/01
PubMed
45 Ilieva EV et al. Depletion of oxidative and endoplasmic reticulum stress regulators in Pick disease. Free Radic. Biol. Med. 2010 May;48(10):1302-10
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46 Wils H et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. U.S.A. 2010 Feb;107(8):3858-63
Wils H et al
2010/01/01
PubMed
47 Braak H et al. Amyotrophic lateral sclerosis: dash-like accumulation of phosphorylated TDP-43 in somatodendritic and axonal compartments of somatomotor neurons of the lower brainstem and spinal cord. Acta Neuropathol. 2010 Jul;120(1):67-74
Braak H et al
2010/01/01
PubMed
48 Ling SC et al. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS. Proc. Natl. Acad. Sci. U.S.A. 2010 Jul;107(30):13318-23
Ling SC et al
2010/01/01
PubMed
49 Jansen C et al. The first case of protease-sensitive prionopathy (PSPr) in The Netherlands: a patient with an unusual GSS-like clinical phenotype. J. Neurol. Neurosurg. Psychiatr. 2010 Sep;81(9):1052-5
Jansen C et al
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PubMed
50 Ash PE et al. Neurotoxic effects of TDP-43 overexpression in C. elegans. Hum. Mol. Genet. 2010 Aug;19(16):3206-18
Ash PE et al
2010/01/01
PubMed
51 Xu YF et al. Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J. Neurosci. 2010 Aug;30(32):10851-9
Xu YF et al
2010/01/01
PubMed
52 Higashi S et al. TDP-43 physically interacts with amyotrophic lateral sclerosis-linked mutant CuZn superoxide dismutase. Neurochem. Int. 2010 Dec;57(8):906-13
Higashi S et al
2010/01/01
PubMed
53 H旦ftberger R et al. Tubulin polymerization promoting protein (TPPP/p25) as a marker for oligodendroglial changes in multiple sclerosis. Glia 2010 Nov;58(15):1847-57
H旦ftberger R et al
2010/01/01
PubMed
54 De Marco G et al. Cytoplasmic accumulation of TDP-43 in circulating lymphomonocytes of ALS patients with and without TARDBP mutations. Acta Neuropathol. 2011 May;121(5):611-22
De Marco G et al
2011/01/01
PubMed
55 Wang DB et al. Expansive gene transfer in the rat CNS rapidly produces amyotrophic lateral sclerosis relevant sequelae when TDP-43 is overexpressed. Mol. Ther. 2010 Dec;18(12):2064-74
Wang DB et al
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PubMed
56 Rauramaa T et al. TAR-DNA binding protein-43 and alterations in the hippocampus. J Neural Transm 2011 May;118(5):683-9
Rauramaa T et al
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PubMed
57 Herman AM et al. &#x3B2;-amyloid triggers ALS-associated TDP-43 pathology in AD models. Brain Res. 2011 Apr;1386:191-9
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PubMed
58 Lashley T et al. TDP-43 pathology may occur in the BRI2 gene-related dementias. Acta Neuropathol. 2011 Apr;121(4):559-60
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PubMed
59 Hartikainen PH et al. Unusual clinical presentation and neuropathology in two subjects with fused-in sarcoma (FUS) positive inclusions. Neuropathology 2012 Feb;32(1):60-8
Hartikainen PH et al
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60 Pikkarainen M et al. Distribution and pattern of pathology in subjects with familial or sporadic late-onset cerebellar ataxia as assessed by p62/sequestosome immunohistochemistry. Cerebellum 2011 Dec;10(4):720-31
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61 Mundi単ano IC et al. Increased dopaminergic cells and protein aggregates in the olfactory bulb of patients with neurodegenerative disorders. Acta Neuropathol. 2011 Jul;122(1):61-74
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62 Tian T et al. TDP-43 potentiates alpha-synuclein toxicity to dopaminergic neurons in transgenic mice. Int. J. Biol. Sci. 2011;7(2):234-43
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63 Che MX et al. Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing. FASEB J. 2011 Jul;25(7):2344-53
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64 Rusina R et al. FTLD-TDP with motor neuron disease, visuospatial impairment and a progressive supranuclear palsy-like syndrome: broadening the clinical phenotype of TDP-43 proteinopathies. A report of three cases. BMC Neurol 2011;11:50
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65 Azizi AA et al. Identification of c-myc-dependent proteins in the medulloblastoma cell line D425Med. Amino Acids 2011 Jun;
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66 L坦pez-Hern叩ndez T et al. Molecular mechanisms of MLC1 and GLIALCAM mutations in megalencephalic leukoencephalopathy with subcortical cysts. Hum. Mol. Genet. 2011 Aug;20(16):3266-77
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67 Martinez-Saez E et al. Hirano body-rich subtypes of Creutzfeldt-Jakob disease. Neuropathol Appl Neurobiol 2012 Apr;38(2):153-161
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68 Swarup V et al. Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain 2011 Sep;134(Pt 9):2610-26
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69 Thom M et al. Neurofibrillary tangle pathology and Braak staging in chronic epilepsy in relation to traumatic brain injury and hippocampal sclerosis: a post-mortem study. Brain 2011 Oct;134(Pt 10):2969-81
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70 Wang JW et al. The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span. J. Clin. Invest. 2011 Oct;121(10):4118-26
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71 Antonell A et al. Breakpoint sequence analysis of an A&#x3B2;PP locus duplication associated with autosomal dominant Alzheimer&quot;s disease and severe cerebral amyloid angiopathy. J. Alzheimers Dis. 2012;28(2):303-8
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72 Tsuji H et al. Epitope mapping of antibodies against TDP-43 and detection of protease-resistant fragments of pathological TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Biochem. Biophys. Res. Commun. 2012 Jan;417(1):116-21
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73 Dayton RD et al. Frontotemporal lobar degeneration-related proteins induce only subtle memory-related deficits when bilaterally overexpressed in the dorsal hippocampus. Exp. Neurol. 2012 Feb;233(2):807-14
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74 Huang C et al. Mutant TDP-43 in motor neurons promotes the onset and progression of ALS in rats. J. Clin. Invest. 2012 Jan;122(1):107-18
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75 Fiesel FC et al. TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR. Nucleic Acids Res. 2012 Mar;40(6):2668-82
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76 Troakes C et al. An MND/ALS phenotype associated with C9orf72 repeat expansion: Abundant p62-positive, TDP-43-negative inclusions in cerebral cortex, hippocampus and cerebellum but without associated cognitive decline. Neuropathology 2011 Dec;
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77 Herman AM et al. Wild type TDP-43 induces neuro-inflammation and alters APP metabolism in lentiviral gene transfer models. Exp. Neurol. 2012 May;235(1):297-305
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78 Ech叩varri C et al. Co-occurrence of different pathologies in dementia: implications for dementia diagnosis. J. Alzheimers Dis. 2012;30(4):909-17
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79 Vilas D et al. Pick&quot;s pathology in Parkinson&quot;s disease with dementia. Neuropathol. Appl. Neurobiol. 2012 Dec;38(7):737-43
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80 Gelpi E et al. Atypical neuropathological sCJD-MM phenotype with abundant white matter Kuru-type plaques sparing the cerebellar cortex. Neuropathology 2012 Aug;
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81 Colom-Cadena M et al. MAPT H1 haplotype is associated with enhanced &#x3B1;-synuclein deposition in dementia with Lewy bodies. Neurobiol. Aging 2013 Mar;34(3):936-42
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82 L坦pez-Gonz叩lez I et al. Characterization of Thorn-Shaped Astrocytes in White Matter of Temporal Lobe in Alzheimer&quot;s Disease Brains. Brain Pathol. 2012 Aug;
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83 Verstraete E et al. TDP-43 plasma levels are higher in amyotrophic lateral sclerosis. Amyotroph Lateral Scler 2012 Sep;13(5):446-51
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84 Tong J et al. XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats. J. Neurochem. 2012 Nov;123(3):406-16
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85 Swarup V et al. Abnormal regenerative responses and impaired axonal outgrowth after nerve crush in TDP-43 transgenic mouse models of amyotrophic lateral sclerosis. J. Neurosci. 2012 Dec;32(50):18186-95
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86 Watanabe S et al. Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins. J. Biol. Chem. 2013 Feb;288(5):3641-54
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88 Hebron ML et al. Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6). J. Biol. Chem. 2013 Feb;288(6):4103-15
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89 Iyer A et al. Cell injury and Premature Neurodegeneration in Focal Malformations of Cortical Development. Brain Pathol. 2013 Apr;
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90 Tong J et al. Expression of ALS-linked TDP-43 mutant in astrocytes causes non-cell-autonomous motor neuron death in rats. EMBO J. 2013 Jul;32(13):1917-26
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93 Nishimoto Y et al. The long non-coding RNA nuclear-enriched abundant transcript 1_2 induces paraspeckle formation in the motor neuron during the early phase of amyotrophic lateral sclerosis. Mol Brain 2013;6:31
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94 Gelpi E et al. Globular glial-like inclusions in a patient with advanced Alzheimer&quot;s disease. Acta Neuropathol. 2013 Jul;126(1):155-7
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95 Mundi単ano IC et al. Reduced cholinergic olfactory centrifugal inputs in patients with neurodegenerative disorders and MPTP-treated monkeys. Acta Neuropathol. 2013 Sep;126(3):411-25
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96 Dayton RD et al. Selective forelimb impairment in rats expressing a pathological TDP-43 25&#x2009;kDa C-terminal fragment to mimic amyotrophic lateral sclerosis. Mol. Ther. 2013 Jul;21(7):1324-34
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97 Finsterer J et al. Asymptomatic hyper-creatine-kinase-emia as sole manifestation of inclusion body myositis. Neurol Int 2013 Jun;5(2):34-6
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99 Hebron M et al. Parkin reverses TDP-43-induced cell death and failure of amino acid homeostasis. J. Neurochem. 2013 Dec;
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100 De Marco G et al. Reduced cellular Ca(2+) availability enhances TDP-43 cleavage by apoptotic caspases. Biochim. Biophys. Acta 2014 Apr;1843(4):725-34
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101 Su叩rez-Calvet M et al. Plasma phosphorylated TDP-43 levels are elevated in patients with frontotemporal dementia carrying a C9orf72 repeat expansion or a GRN mutation. J. Neurol. Neurosurg. Psychiatr. 2013 Dec;
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102 Yan S et al. TDP-43 causes differential pathology in neuronal versus glial cells in the mouse brain. Hum. Mol. Genet. 2014 Jan;
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103 Iovino M et al. The novel MAPT mutation K298E: mechanisms of mutant tau toxicity, brain pathology and tau expression in induced fibroblast-derived neurons. Acta Neuropathol. 2014 Feb;127(2):283-95
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104 Cortese A et al. Widespread RNA metabolism impairment in sporadic inclusion body myositis TDP43-proteinopathy. Neurobiol. Aging 2014 Jun;35(6):1491-8
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105 Ohta Y et al. Interaction of transactive response DNA binding protein 43 with nuclear factor &#x3BA;B in mild cognitive impairment with episodic memory deficits. Acta Neuropathol Commun 2014;2(1):37
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PubMed
106 Carlomagno Y et al. Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins. PLoS ONE 2014;9(3):e90452
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107 Araki W et al. Disease-Associated Mutations of TDP-43 Promote Turnover of the Protein Through the Proteasomal Pathway. Mol. Neurobiol. 2014 Jan;
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108 Kara E et al. A 6.4 Mb Duplication of the &#x3B1;-Synuclein Locus Causing Frontotemporal Dementia and Parkinsonism: Phenotype-Genotype Correlations. JAMA Neurol 2014 Sep;71(9):1162-71
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109 Hans F et al. UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination. J. Biol. Chem. 2014 Jul;289(27):19164-79
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110 Gelpi E et al. Multiple organ involvement by alpha-synuclein pathology in Lewy body disorders. Mov. Disord. 2014 Jul;29(8):1010-8
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111 Alafuzoff I et al. Neuropathological assessments of the pathology in frontotemporal lobar degeneration with TDP43-positive inclusions: an inter-laboratory study by the BrainNet Europe consortium. J Neural Transm 2014 Sep;
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112 Balasa M et al. Clinical and neuropathological variability in clinically isolated central nervous system Whipple&quot;s disease. Brain Pathol. 2014 Apr;24(3):230-8
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113 Walker AK et al. ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS ONE 2013;8(11):e81170
Walker AK et al
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