Associated Papers
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
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
Opposing roles of p38α-mediated phosphorylation and PRMT1-mediated arginine methylation in driving TDP-43 proteinopathy.
Aikio M et al.
Cell Reports, 2025
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP.
Arseni D et al.
Nature, 2023
Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates.
Horvath A et al.
Biochemistry, 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
Genotype-phenotype correlations in a chinese population with familial amyotrophic lateral sclerosis.
Liu W et al.
Neurological Research, 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
Genetic and clinical features of Chinese sporadic amyotrophic lateral sclerosis patients with TARDBP mutations.
Feng F et al.
Brain and Behavior, 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
RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy.
Chen HJ et al.
Brain : a Journal of Neurology, 2019
Detection and characterization of TDP-43 in human cells and tissues by multiple reaction monitoring mass spectrometry.
Pobran TD et al.
Clinical Mass Spectrometry (del Mar, Calif.), 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
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
Genotype-phenotype correlations of amyotrophic lateral sclerosis.
Li HF et al.
Translational Neurodegeneration, 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
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
TARDBP and FUS mutations associated with amyotrophic lateral sclerosis: summary and update.
Lattante S et al.
Human Mutation, 2013
Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins.
Watanabe S et al.
The Journal of Biological Chemistry, 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
Screening of the TARDBP gene in familial and sporadic amyotrophic lateral sclerosis patients of Chinese origin.
Zou ZY et al.
Neurobiology of Aging, 2012
Large-scale screening of TARDBP mutation in amyotrophic lateral sclerosis in Japanese.
Iida A et al.
Neurobiology of Aging, 2012
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
Association between novel TARDBP mutations and Chinese patients with amyotrophic lateral sclerosis.
Xiong HL et al.
Bmc Medical Genetics, 2010
[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
Novel TARDBP sequence variant and C9ORF72 repeat expansion in a family with frontotemporal dementia.
Kaivorinne AL et al.
Alzheimer Disease and Associated Disorders, 0