ArticleActa neuropathologica communications2014
Novel monoclonal antibodies to normal and pathologically altered human TDP-43 proteins.
Article in Acta neuropathologica communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.
- TDP-43 as a possible biomarker for frontotemporal lobar degeneration: a systematic review of existing antibodies.Acta neuropathologica communications · 2015Pooled it
- A phosphorylation‑independent monoclonal antibody improves detection of TDP‑43 pathology across frontotemporal lobar degeneration, amyotrophic lateral sclerosis, and limbic predominant age related TDP‑43 encephalopathy neuropathological change.Journal of neuropathology and experimental neurology · 2026Article
- Splicing the narrative: alternative TARDBP splicing and its relation to neurodegeneration in ALS and FTD.The Journal of clinical investigation · 2026Review
- Extracellular vesicles in TDP-43 proteinopathies: pathogenesis and biomarker potential.Molecular neurodegeneration · 2025Review
- Targeting the TDP-43 low complexity domain blocks spreading of pathology in a mouse model of ALS/FTD.Acta neuropathologica communications · 2024Article
- Production and characterization of novel monoclonal antibodies against pathological human TDP-43 proteins.Journal of neuropathology and experimental neurology · 2024Article
- In vivo diagnosis of TDP-43 proteinopathies: in search of biomarkers of clinical use.Translational neurodegeneration · 2024Review
- Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo.Acta neuropathologica communications · 2023Article
- "Endothelial Antibody Factory" at the Blood Brain Barrier: Novel Approach to Therapy of Neurodegenerative Diseases.Pharmaceutics · 2022Article
- Evaluation of blood-based, extracellular vesicles as biomarkers for aging-related TDP-43 pathology.Alzheimer's & dementia (Amsterdam, Netherlands) · 2022Article
- Detection and quantification of novel C-terminal TDP-43 fragments in ALS-TDP.Brain pathology (Zurich, Switzerland) · 2021Article
- Role and therapeutic potential of liquid-liquid phase separation in amyotrophic lateral sclerosis.Journal of molecular cell biology · 2021Review
- Novel monoclonal antibodies targeting the RRM2 domain of human TDP-43 protein.Neuroscience letters · 2020Article
- TDP-43, a protein central to amyotrophic lateral sclerosis, is destabilized by tankyrase-1 and -2.Journal of cell science · 2020Article
- The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD.Frontiers in neuroscience · 2019Review
- Age-related deregulation of TDP-43 after stroke enhances NF-κB-mediated inflammation and neuronal damage.Journal of neuroinflammation · 2018Article
- Aberrant activation of non-coding RNA targets of transcriptional elongation complexes contributes to TDP-43 toxicity.Nature communications · 2018Article
- Towards a TDP-43-Based Biomarker for ALS and FTLD.Molecular neurobiology · 2018Review
- TDP-43 Neuropathologic Associations in the Nun Study and the Honolulu-Asia Aging Study.Journal of Alzheimer's disease : JAD · 2018Article
- Expansion of the classification of FTLD-TDP: distinct pathology associated with rapidly progressive frontotemporal degeneration.Acta neuropathologica · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The RNA/DNA-binding protein, TDP-43, is the key component of ubiquitinated inclusions characteristic of amyotrophic lateral sclerosis (ALS) and the majority of frontotemporal lobar degeneration (FTLD-TDP) referred to collectively as TDP-43 proteinopathies. To further elucidate mechanisms of pathological TDP-43 processing and identify TDP-43 epitopes that could be useful as potential biomarkers of TDP-43 proteinopathies, we developed a panel of novel monoclonal antibodies (MAbs) directed at regions extending across the length of TDP-43. Here, we confirm previous observations that there is no or minimal accumulation of TDP-43 N-terminal domains in neocortical inclusions in human TDP-43 proteinopathy tissues and we identify a subset of these MAbs that are specific for human versus mouse TDP-43. Notably, one of these MAbs recognized an epitope that preferentially detected pathological TDP-43 inclusions with negligible reactivity for normal nuclear TDP-43 resembling anti-phospho-TDP-43 specific antibodies that only bind pathological TDP-43. Hence, we infer that this new MAb recognizes a phosphorylation independent but disease-specific pathologic conformation in abnormal TDP-43. These data suggest that the novel MAbs reported here will be useful for patient-oriented research as well as for studies of animal and cell-based models of TDP-43 proteinopathies including ALS and FTLD-TDP.
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