Associated Papers
Structure, Function, Pathomechanisms and Targeting of TDP-43 in Neurodegeneration.
Zhang X et al.
Brain Research, 2026
TDP-43 proteinopathies and neurodegeneration: insights from Caenorhabditis elegans models.
Pir GJ et al.
The Febs Journal, 2026
Antisense Oligonucleotide Therapy for Amyotrophic Lateral Sclerosis (ALS): An Umbrella Review.
Jeong E et al.
Cureus, 2025
Myopathic aggregation-prone variants in the TDP-43 prion-like domain: genetics paving the way.
Ervilha Pereira P et al.
Brain : a Journal of Neurology, 2025
Exploring Protein Misfolding in Amyotrophic Lateral Sclerosis: Structural and Functional Insights.
Ivantsik O et al.
Biomedicines, 2025
Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective Responses.
Verde EM et al.
Cells, 2025
Comprehensive mapping of mutations in TDP-43 and α-Synuclein that affect stability and binding.
Alamri SH et al.
Journal of Biomolecular Structure & Dynamics, 2025
Genetics screening in an Italian cohort of patients with Amyotrophic Lateral Sclerosis: the importance of early testing and its implication.
Libonati L et al.
Journal of Neurology, 2024
Invertebrate genetic models of amyotrophic lateral sclerosis.
Zhou L et al.
Frontiers in Molecular Neuroscience, 2024
TDP-43 as a therapeutic target in neurodegenerative diseases: Focusing on motor neuron disease and frontotemporal dementia.
Babazadeh A et al.
Ageing Research Reviews, 2023
Variability in Clinical Phenotype in TARDBP Mutations: Amyotrophic Lateral Sclerosis Case Description and Literature Review.
Lombardi M et al.
Genes, 2023
Studies of Genetic and Proteomic Risk Factors of Amyotrophic Lateral Sclerosis Inspire Biomarker Development and Gene Therapy.
Bagyinszky E et al.
Cells, 2023
Characterising the Genetic Landscape of Amyotrophic Lateral Sclerosis: A Catalogue and Assessment of Over 1,000 Published Genetic Variants.
McCann EP et al.
Journal of Neuromuscular Diseases, 2023
Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates.
Horvath A et al.
Biochemistry, 2022
Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLD.
Tamaki Y et al.
International Journal of Molecular Sciences, 2022
Proteostasis impairment and ALS.
Lambert-Smith IA et al.
Progress in Biophysics and Molecular Biology, 2022
Identification of TARDBP Gly298Ser as a founder mutation for amyotrophic lateral sclerosis in Southern China.
Xu F et al.
Bmc Medical Genomics, 2022
Genotype-phenotype association of TARDBP mutations in Chinese patients with amyotrophic lateral sclerosis: a single-center study and systematic review of published literature.
Li J et al.
Journal of Neurology, 2022
Unraveling the toxic effects mediated by the neurodegenerative disease-associated S375G mutation of TDP-43 and its S375E phosphomimetic variant.
Paron F et al.
The Journal of Biological Chemistry, 2022
Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions.
Versluys L et al.
Frontiers in Neuroscience, 2022
Dysregulation of Translation in TDP-43 Proteinopathies: Deficits in the RNA Supply Chain and Local Protein Production.
Bjork RT et al.
Frontiers in Neuroscience, 2022
TDP-43 Pathology in Alzheimer's Disease.
Meneses A et al.
Molecular Neurodegeneration, 2021
Nearly 30 Years of Animal Models to Study Amyotrophic Lateral Sclerosis: A Historical Overview and Future Perspectives.
Bonifacino T et al.
International Journal of Molecular Sciences, 2021
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD.
Wood A et al.
International Journal of Molecular Sciences, 2021
Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation.
Tziortzouda P et al.
Nature Reviews. Neuroscience, 2021
Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43.
Li Q et al.
Nature Communications, 2021
Stress granule subtypes: an emerging link to neurodegeneration.
Advani VM et al.
Cellular and Molecular Life Sciences : Cmls, 2020
Cytoplasmic localization of amyotrophic lateral sclerosis-related TDP-43 proteins modulates stress granule formation.
Besnard-Guérin C
The European Journal of Neuroscience, 2020
The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies.
Jo M et al.
Experimental & Molecular Medicine, 2020
RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy.
Chen HJ et al.
Brain : a Journal of Neurology, 2019
A novel S379A TARDBP mutation associated to late-onset sporadic ALS.
Sprovieri T et al.
Neurological Sciences : Official Journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology, 2019
Structural Transition, Function and Dysfunction of TDP-43 in Neurodegenerative Diseases.
Afroz T et al.
Chimia, 2019
The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?
Hergesheimer RC et al.
Brain : a Journal of Neurology, 2019
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis.
Prasad A et al.
Frontiers in Molecular Neuroscience, 2019
The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD.
Berning BA et al.
Frontiers in Neuroscience, 2019
TDP-43 post-translational modifications in health and disease.
Buratti E
Expert Opinion on Therapeutic Targets, 2018
Transactive response DNA-binding protein 43 (TDP-43) regulates alternative splicing of tau exon 10: Implications for the pathogenesis of tauopathies.
Gu J et al.
The Journal of Biological Chemistry, 2017
Cytoplasmic Relocalization of TAR DNA-Binding Protein 43 Is Not Sufficient to Reproduce Cellular Pathologies Associated with ALS In vitro.
Wobst HJ et al.
Frontiers in Molecular Neuroscience, 2017
Reduced stress granule formation and cell death in fibroblasts with the A382T mutation of TARDBP gene: evidence for loss of TDP-43 nuclear function.
Orrù S et al.
Human Molecular Genetics, 2016
Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation.
Chiang CH et al.
Scientific Reports, 2016
Review: Prion-like mechanisms of transactive response DNA binding protein of 43 kDa (TDP-43) in amyotrophic lateral sclerosis (ALS).
Smethurst P et al.
Neuropathology and Applied Neurobiology, 2015
Emerging mechanisms of molecular pathology in ALS.
Peters OM et al.
The Journal of Clinical Investigation, 2015
Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.
Lauranzano E et al.
Brain : a Journal of Neurology, 2015
UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination.
Hans F et al.
The Journal of Biological Chemistry, 2014
The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.
Sun CS et al.
Plos One, 2014
Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders.
Janssens J et al.
Human Molecular Genetics, 2013
Stress granules in neurodegeneration--lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma.
Bentmann E et al.
The Febs Journal, 2013
Reducing TDP-43 aggregation does not prevent its cytotoxicity.
Liu R et al.
Acta Neuropathologica Communications, 2013