Associated Papers
TDP-43 proteinopathies and neurodegeneration: insights from Caenorhabditis elegans models.
Pir GJ et al.
The Febs Journal, 2026
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
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
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
TAR DNA-binding protein 43 oligomers in physiology and pathology.
Lye YS et al.
Iubmb Life, 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
Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions.
Versluys L et al.
Frontiers in Neuroscience, 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
Destination Amyotrophic Lateral Sclerosis.
Keon M et al.
Frontiers in Neurology, 2021
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
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 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
Structural Insights Into TDP-43 and Effects of Post-translational Modifications.
François-Moutal L et al.
Frontiers in Molecular Neuroscience, 2019
TDP-43 post-translational modifications in health and disease.
Buratti E
Expert Opinion on Therapeutic Targets, 2018
Sequestration of PRMT1 and Nd1-L mRNA into ALS-linked FUS mutant R521C-positive aggregates contributes to neurite degeneration upon oxidative stress.
Jun MH et al.
Scientific Reports, 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
Emerging mechanisms of molecular pathology in ALS.
Peters OM et al.
The Journal of Clinical Investigation, 2015
Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.
Holehouse AS et al.
Plos One, 2015
Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders.
Janssens J et al.
Human Molecular Genetics, 2013
Reducing TDP-43 aggregation does not prevent its cytotoxicity.
Liu R et al.
Acta Neuropathologica Communications, 2013
TARDBP and FUS mutations associated with amyotrophic lateral sclerosis: summary and update.
Lattante S et al.
Human Mutation, 2013
Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function.
Chang CK et al.
Febs Letters, 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
TARDBP gene mutations among Chinese patients with sporadic amyotrophic lateral sclerosis.
Huang R et al.
Neurobiology of Aging, 2012
Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking.
Cohen TJ et al.
The Embo Journal, 2012
[Intracellular seeded aggregation of TDP-43].
Nonaka T et al.
Rinsho Shinkeigaku = Clinical Neurology, 2012
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
An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity.
Guo W et al.
Nature Structural & Molecular Biology, 2011
FUS, TARDBP, and SOD1 mutations in a Taiwanese cohort with familial ALS.
Tsai CP et al.
Neurobiology of Aging, 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
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration.
Lagier-Tourenne C et al.
Human Molecular Genetics, 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