Associated Papers
Cryptic Splicing of GAP43 mRNA is a Novel Hallmark of TDP-43-Associated ALS and AD.
Yang M et al.
Advanced Science (weinheim, Baden-wurttemberg, Germany), 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
Pathogenic TDP-43 in amyotrophic lateral sclerosis.
Chong ZZ et al.
Drug Discovery Today, 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
Variability in Clinical Phenotype in TARDBP Mutations: Amyotrophic Lateral Sclerosis Case Description and Literature Review.
Lombardi M et al.
Genes, 2023
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP.
Arseni D et al.
Nature, 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
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
Structure of pathological TDP-43 filaments from ALS with FTLD.
Arseni D et al.
Nature, 2022
Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions.
Versluys L et al.
Frontiers in Neuroscience, 2022
Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons.
Vishal SS et al.
Frontiers in Cell and Developmental Biology, 2022
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
A novel mutation in the cleavage site N291 of TDP-43 protein in a familial case of amyotrophic lateral sclerosis.
Chami AA et al.
Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration, 2020
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
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
Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation.
Guenther EL et al.
Nature Structural & Molecular Biology, 2018
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
TDP-43 suppresses tau expression via promoting its mRNA instability.
Gu J et al.
Nucleic Acids Research, 2017
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
Identification of rare protein disulfide isomerase gene variants in amyotrophic lateral sclerosis patients.
Gonzalez-Perez P et al.
Gene, 2015
Emerging mechanisms of molecular pathology in ALS.
Peters OM et al.
The Journal of Clinical Investigation, 2015
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
TARDBP and FUS mutations associated with amyotrophic lateral sclerosis: summary and update.
Lattante S et al.
Human Mutation, 2013
Absence of mutations in exon 6 of the TARDBP gene in 207 Chinese patients with sporadic amyotrohic lateral sclerosis.
Ye CH et al.
Plos One, 2013
[Intracellular seeded aggregation of TDP-43].
Nonaka T et al.
Rinsho Shinkeigaku = Clinical Neurology, 2012
Mutational analysis of TARDBP in neurodegenerative diseases.
Ticozzi N et al.
Neurobiology of Aging, 2011
TDP-43 and FUS/TLS: cellular functions and implications for neurodegeneration.
Fiesel FC et al.
The Febs Journal, 2011
The role of mutant TAR DNA-binding protein 43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.
Janssens J et al.
Biochemical Society Transactions, 2011
Protein misdirection inside and outside motor neurons in Amyotrophic Lateral Sclerosis (ALS): a possible clue for therapeutic strategies.
Ido A et al.
International Journal of Molecular Sciences, 2011
TAR DNA-binding protein 43 in neurodegenerative disease.
Chen-Plotkin AS et al.
Nature Reviews. Neurology, 2010
Pathogenic TARDBP mutations in amyotrophic lateral sclerosis and frontotemporal dementia: disease-associated pathways.
Barmada SJ et al.
Reviews in the Neurosciences, 2010
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.
Pesiridis GS et al.
Human Molecular Genetics, 2009
Identification of casein kinase-1 phosphorylation sites on TDP-43.
Kametani F et al.
Biochemical and Biophysical Research Communications, 2009
High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis.
Corrado L et al.
Human Mutation, 2009
[Study of mutations in 5'-noncoding region of BCL-6 gene in B-cell non-Hodgkin's lymphomas].
Min DL et al.
Zhonghua Bing Li Xue Za Zhi = Chinese Journal of Pathology, 2004