Associated Papers
From Evasion to Collapse: The Kinetic Cascade of TDP-43 and the Failure of Proteostasis.
Jamerlan A et al.
International Journal of Molecular Sciences, 2026
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
Structural insights and milestones in TDP-43 research: A comprehensive review of its pathological and therapeutic advances.
Dang M et al.
International Journal of Biological Macromolecules, 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
Uncovering Intermolecular Interactions Driving the Liquid-Liquid Phase Separation of the TDP-43 Low-Complexity Domain via Atomistic Dimerization Simulations.
Tang H et al.
Journal of Chemical Information and Modeling, 2024
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
Influence of ALS-linked M337V mutation on the conformational ensembles of TDP-43321-340 peptide monomer and dimer.
Zeng J et al.
Proteins, 2024
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP.
Arseni D et al.
Nature, 2023
Mutations in α-synuclein, TDP-43 and tau prolong protein half-life through diminished degradation by lysosomal proteases.
Sampognaro PJ et al.
Molecular Neurodegeneration, 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
Identification of TARDBP Gly298Ser as a founder mutation for amyotrophic lateral sclerosis in Southern China.
Xu F et al.
Bmc Medical Genomics, 2022
Regulating Phase Transition in Neurodegenerative Diseases by Nuclear Import Receptors.
Girdhar A et al.
Biology, 2022
TDP-43 pathology: From noxious assembly to therapeutic removal.
Keating SS et al.
Progress in Neurobiology, 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
TDP-43 Oligomerization and Phase Separation Properties Are Necessary for Autoregulation.
Koehler LC 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
Specific RNA interactions promote TDP-43 multivalent phase separation and maintain liquid properties.
Grese ZR et al.
Embo Reports, 2021
The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils.
Chien HM 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
A novel mutation in TARDBP segregates with amyotrophic lateral sclerosis in a large family with early onset and fast progression.
Goldstein O et al.
Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration, 2020
TDP-43 α-helical structure tunes liquid-liquid phase separation and function.
Conicella AE et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins.
Fernandopulle M et al.
Human Molecular Genetics, 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
ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.
Conicella AE et al.
Structure (london, England : 1993), 2016
A New Phase in ALS Research.
Chong PA et al.
Structure (london, England : 1993), 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
Oxr1 improves pathogenic cellular features of ALS-associated FUS and TDP-43 mutations.
Finelli MJ et al.
Human Molecular Genetics, 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
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
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