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Ashley Cannon et al.
ACTA NEUROPATHOLOGICA (2012)
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Mutant TDP-43 in motor neurons promotes the onset and progression of ALS in rats
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Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
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TDP-43 regulates its mRNA levels through a negative feedback loop
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Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
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Expression of mutant TDP-43 induces neuronal dysfunction in transgenic mice
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Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis
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Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43
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Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
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Aberrant alternative splicing and extracellular matrix gene expression in mouse models of myotonic dystrophy
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TDP-43-Mediated Neuron Loss In Vivo Requires RNA-Binding Activity
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Deletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism
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Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
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TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
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Transgenic Rat Model of Neurodegeneration Caused by Mutation in the TDP Gene
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Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
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Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies
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TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity
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Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
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TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
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Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
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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
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GluR2 deficiency accelerates motor neuron degeneration in a mouse model of amyotrophic lateral sclerosis
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