Associated Papers
Computational Exploration of the Molecular Mechanism of Epigallocatechin Gallate against TDP-43 Aggregation.
Yi W et al.
Journal of Chemical Information and Modeling, 2026
TDP-43 proteinopathies and neurodegeneration: insights from Caenorhabditis elegans models.
Pir GJ et al.
The Febs Journal, 2026
On the potential roles of TDP-43 in the formation of membraneless organelles and their transformation into toxic aggregates.
Sergeeva OS et al.
Biochemical and Biophysical Research Communications, 2025
Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates.
Yan X et al.
Cell, 2025
Cognitive Decline in Parkinsonism: From Clinical Phenotypes to the Genetic Background.
Koros C et al.
Biomedicines, 2025
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
Deciphering the Inhibitory Mechanism of ALS-Associated N352S and S352p Variants against TDP-43 Aggregation and Its Destabilization Effect on TDP-43 Protofibrils.
Xu Z et al.
Acs Chemical Neuroscience, 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
Conformational switches in human RNA binding proteins involved in neurodegeneration.
Chatterjee S et al.
Biochimica Et Biophysica Acta. General Subjects, 2025
A systematic review and functional in-silico analysis of genes and variants associated with amyotrophic lateral sclerosis.
Arreola-Aldape CA et al.
Frontiers in Neuroscience, 2025
Mutations in human prion-like domains: pathogenic but not always amyloidogenic.
Bartolomé-Nafría A et al.
Prion, 2024
Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin α1/β Signaling.
Ko YH et al.
Journal of Molecular Biology, 2024
TDP-43 Amyloid Fibril Formation via Phase Separation-Related and -Unrelated Pathways.
Lin PH et al.
Acs Chemical Neuroscience, 2024
Molecular Mechanisms of Phase Separation and Amyloidosis of ALS/FTD-linked FUS and TDP-43.
Song J
Aging and Disease, 2024
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
Dissecting the effect of ALS mutation S375G on the conformational properties and aggregation dynamics of TDP-43370-375 fragment.
Xu Z et al.
Biophysical Chemistry, 2024
Cryo-EM structures of functional and pathological amyloid ribonucleoprotein assemblies.
Garcia-Pardo J et al.
Trends in Biochemical Sciences, 2024
Slow disease progression and characteristic TDP-43 inclusions in a patient with familial amyotrophic lateral sclerosis carrying a TARDBP G357S variant.
Sainouchi M et al.
Neuropathology and Applied Neurobiology, 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
Dissecting the Effect of ALS Mutation G335D on the Early Aggregation of the TDP-43 Amyloidogenic Core Peptide: Helix-to-β-Sheet Transition and Conformational Shift.
Li F et al.
Journal of Chemical Information and Modeling, 2023
ALS-Linked A315T and A315E Mutations Enhance β-Barrel Formation of the TDP-43307-319 Hexamer: A REST2 Simulation Study.
Liu X et al.
Acs Chemical Neuroscience, 2023
14-3-3ζ Participates in the Phase Separation of Phosphorylated and Glycated Tau and Modulates the Physiological and Pathological Functions of Tau.
Liu YQ et al.
Acs Chemical Neuroscience, 2023
Role of Triggers on the Structural and Functional Facets of TAR DNA-binding Protein 43.
Camilus N et al.
Neuroscience, 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
Distinct neurotoxic TDP-43 fibril polymorphs are generated by heterotypic interactions with α-Synuclein.
Dhakal S et al.
The Journal of Biological Chemistry, 2022
Atomistic Insights into A315E Mutation-Enhanced Pathogenicity of TDP-43 Core Fibrils.
Li F et al.
Acs Chemical Neuroscience, 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
ALS-associated A315E and A315pT variants exhibit distinct mechanisms in inducing irreversible aggregation of TDP-43312-317 peptides.
Liu X et al.
Physical Chemistry Chemical Physics : Pccp, 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
Dysregulation of Translation in TDP-43 Proteinopathies: Deficits in the RNA Supply Chain and Local Protein Production.
Bjork RT et al.
Frontiers in Neuroscience, 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
Zn2+ modulates in vitro phase separation of TDP-432C and mutant TDP-432C-A315T C-terminal fragments of TDP-43 protein implicated in ALS and FTLD-TDP diseases.
Preethi S et al.
International Journal of Biological Macromolecules, 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
Computational insights into mechanism of AIM4-mediated inhibition of aggregation of TDP-43 protein implicated in ALS and evidence for in vitro inhibition of liquid-liquid phase separation (LLPS) of TDP-432C-A315T by AIM4.
Girdhar A et al.
International Journal of Biological Macromolecules, 2020
RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy.
Chen HJ et al.
Brain : a Journal of Neurology, 2019
TDP-43 and FUS-structural insights into RNA recognition and self-association.
Loughlin FE et al.
Current Opinion in Structural Biology, 2019
Lysosomal Dysfunction at the Centre of Parkinson's Disease and Frontotemporal Dementia/Amyotrophic Lateral Sclerosis.
Wallings RL et al.
Trends in Neurosciences, 2019