ReviewJournal of molecular neuroscience : MN2011
TDP-43 autoregulation: implications for disease.
Review in Journal of molecular neuroscience : MN, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 66 citations in OpenAlex.
- Caspase-4 transgenic mice exhibit cytoplasmic TDP-43 accumulation and age-dependent neuropathology.Nature communications · 2026Article
- Broad brain biodistribution conferred by an AAV to restore TDP-43 function mitigates Frontotemporal Demenia-like deficits.bioRxiv : the preprint server for biology · 2025Article
- RNA-binding deficient TDP-43 drives cognitive decline in a mouse model of TDP-43 proteinopathy.eLife · 2023Article
- TDP-43 Epigenetic Facets and Their Neurodegenerative Implications.International journal of molecular sciences · 2023Review
- RNA methylation influences TDP43 binding and disease pathogenesis in models of amyotrophic lateral sclerosis and frontotemporal dementia.Molecular cell · 2023Article
- Cell environment shapes TDP-43 function with implications in neuronal and muscle disease.Communications biology · 2022Article
- Low-level overexpression of wild type TDP-43 causes late-onset, progressive neurodegeneration and paralysis in mice.PloS one · 2022Article
- TDP-43 and amyloid precursor protein processing: implications for Alzheimer's disease.Neural regeneration research · 2021Article
- Review
- Amyotrophic lateral sclerosis: Correlations between fluid biomarkers of NfL, TDP-43, and tau, and clinical characteristics.PloS one · 2021Article
- Trends in Understanding the Pathological Roles of TDP-43 and FUS Proteins.Advances in experimental medicine and biology · 2021Article
- Integrative transcriptomic analysis suggests new autoregulatory splicing events coupled with nonsense-mediated mRNA decay.Nucleic acids research · 2019Article
- Reduction of matrix metalloproteinase 9 (MMP-9) protects motor neurons from TDP-43-triggered death in rNLS8 mice.Neurobiology of disease · 2019Article
- Structural Insights Into TDP-43 and Effects of Post-translational Modifications.Frontiers in molecular neuroscience · 2019Review
- Autoregulation of RBM10 and cross-regulation of RBM10/RBM5 via alternative splicing-coupled nonsense-mediated decay.Nucleic acids research · 2017Article
- Retrotransposon activation contributes to neurodegeneration in a Drosophila TDP-43 model of ALS.PLoS genetics · 2017Article
- Stress granules at the intersection of autophagy and ALS.Brain research · 2016Review
- Inside out: the role of nucleocytoplasmic transport in ALS and FTLD.Acta neuropathologica · 2016Review
- Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43.Nucleic acids research · 2016Article
- Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses.Nature communications · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TDP-43 is a nuclear protein that has been shown to play a central role in RNA metabolism. In recent years, this protein has become very important in the study of neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal lobar degeneration (FTLD). These diseases share, as common feature, the presence of abnormally aggregated, posttranslationally modified, and mislocalized TDP-43 in the cell cytoplasm of both neurons and glial cells. A major question in TDP-43 research is represented by the investigation of the mechanism(s) that trigger this process and its potential consequences. Regarding the first issue, it is likely that relative protein expression levels might play an important role as has been demonstrated for many protein aggregation processes. In fact, the eventual misregulation of TDP-43 expression leading to enhanced protein production might well correlate with enhanced aggregation, and thus results in increasingly harmful gain- or loss-of-function effects on cellular metabolism. For this reason, it is important to determine the mechanisms that act to regulate TDP-43 levels within the cell. In normal conditions, it is now clear that TDP-43 can modulate its own protein levels through a negative feedback loop triggered by binding to its own RNA in the 3'UTR region leading to mRNA degradation. This work discusses how an eventual disruption of this mechanism might affect TDP-43 pathology, focusing in particular on its association with stress granules and intrinsic aggregation properties.
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Registered trials
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.