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 as a therapeutic target in neurodegenerative diseases: Focusing on motor neuron disease and frontotemporal dementia.
Babazadeh A et al.
Ageing Research Reviews, 2023
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
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
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
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