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
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
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
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
Molecular dissection of ALS-linked TDP-43 - involvement of the Gly-rich domain in interaction with G-quadruplex mRNA.
Ishiguro A et al.
Febs Letters, 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
TDP-43 post-translational modifications in health and disease.
Buratti E
Expert Opinion on Therapeutic Targets, 2018
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
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
Role of selected mutations in the Q/N rich region of TDP-43 in EGFP-12xQ/N-induced aggregate formation.
Budini M et al.
Brain Research, 2012
TARDBP gene mutations among Chinese patients with sporadic amyotrophic lateral sclerosis.
Huang R et al.
Neurobiology of Aging, 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
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
Broad clinical phenotypes associated with TAR-DNA binding protein (TARDBP) mutations in amyotrophic lateral sclerosis.
Kirby J et al.
Neurogenetics, 2010
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration.
Lagier-Tourenne C et al.
Human Molecular Genetics, 2010
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
Screening for TARDBP mutations in Japanese familial amyotrophic lateral sclerosis.
Kamada M et al.
Journal of the Neurological Sciences, 2009
Contribution of TARDBP mutations to sporadic amyotrophic lateral sclerosis.
Daoud H et al.
Journal of Medical Genetics, 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
RNA-binding proteins in neurodegenerative disease: TDP-43 and beyond.
Hanson KA et al.
Wiley Interdisciplinary Reviews. Rna, 0