ArticleActa neuropathologica2013
Robust cytoplasmic accumulation of phosphorylated TDP-43 in transgenic models of tauopathy.
Article in Acta neuropathologica, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Direct interaction between TDP-43 and Tau promotes their co-condensation, while suppressing Tau fibril formation and seeding.The EMBO journal · 2025Article
- TDP-43 promotes tau accumulation and selective neurotoxicity in bigenic Caenorhabditis elegans.Disease models & mechanisms · 2022Article
- Mechanistic Insights of Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis: An Update on a Lasting Relationship.Metabolites · 2022Review
- Single-synapse analyses of Alzheimer's disease implicate pathologic tau, DJ1, CD47, and ApoE.Science advances · 2021Article
- Hexanucleotide Repeat Expansions in c9FTD/ALS and SCA36 Confer Selective Patterns of Neurodegeneration In Vivo.Cell reports · 2020Article
- Aberrant deposition of stress granule-resident proteins linked to C9orf72-associated TDP-43 proteinopathy.Molecular neurodegeneration · 2019Article
- Changes in proteome solubility indicate widespread proteostatic disruption in mouse models of neurodegenerative disease.Acta neuropathologica · 2018Article
- Differential induction of mutant SOD1 misfolding and aggregation by tau and α-synuclein pathology.Molecular neurodegeneration · 2018Article
- A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing.The EMBO journal · 2018Article
- TDP-43 expression influences amyloidβ plaque deposition and tau aggregation.Neurobiology of disease · 2017Article
- Frontotemporal Lobar Degeneration: Mechanisms and Therapeutic Strategies.Molecular neurobiology · 2016Review
- Lentiviral vector-mediated overexpression of mutant ataxin-7 recapitulates SCA7 pathology and promotes accumulation of the FUS/TLS and MBNL1 RNA-binding proteins.Molecular neurodegeneration · 2016Article
- What we can learn from animal models about cerebral multi-morbidity.Alzheimer's research & therapy · 2015Article
- Increased tau phosphorylation and aggregation in the hippocampus of mice overexpressing corticotropin-releasing factor.Journal of Alzheimer's disease : JAD · 2015Article
- Hippocampal and mesial temporal sclerosis in early-onset frontotemporal lobar degeneration versus Alzheimer's disease.American journal of Alzheimer's disease and other dementias · 2014Article
- Effects of the C57BL/6 strain background on tauopathy progression in the rTg4510 mouse model.Molecular neurodegeneration · 2014Article
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Authors and funding
20 authors at 3 institutions in 1 country.
Funding
Abstract
Frontotemporal lobar degeneration (FTLD) has been subdivided based on the main pathology found in the brains of affected individuals. When the primary pathology is aggregated, hyperphosphorylated tau, the pathological diagnosis is FTLD-tau. When the primary pathology is cytoplasmic and/or nuclear aggregates of phosphorylated TAR-DNA-binding protein (TDP-43), the pathological diagnosis is FTLD-TDP. Notably, TDP-43 pathology can also occur in conjunction with a number of neurodegenerative disorders; however, unknown environmental and genetic factors may regulate this TDP-43 pathology. Using transgenic mouse models of several diseases of the central nervous system, we explored whether a primary proteinopathy might secondarily drive TDP-43 proteinopathy. We found abnormal, cytoplasmic accumulation of phosphorylated TDP-43 specifically in two tau transgenic models, but TDP-43 pathology was absent in mouse models of Aβ deposition, α-synucleinopathy or Huntington's disease. Though tau pathology showed considerable overlap with cytoplasmic, phosphorylated TDP-43, tau pathology generally preceded TDP-43 pathology. Biochemical analysis confirmed the presence of TDP-43 abnormalities in the tau mice, which showed increased levels of high molecular weight, soluble TDP-43 and insoluble full-length and ~35 kD TDP-43. These data demonstrate that the neurodegenerative cascade associated with a primary tauopathy in tau transgenic mice can also promote TDP-43 abnormalities. These findings provide the first in vivo models to understand how TDP-43 pathology may arise as a secondary consequence of a primary proteinopathy.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.