Associated Papers
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
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
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
Cross-Interaction with Amyloid-β Drives Pathogenic Structural Transformation within the Amyloidogenic Core Region of TDP-43.
Gatch AJ et al.
Acs Chemical Neuroscience, 2025
Single-point mutations in disordered proteins: Linking sequence, ensemble, and function.
Flores E et al.
Current Opinion in Structural Biology, 2025
The Regulation of TDP-43 Structure and Phase Transitions: A Review.
Liu Y et al.
The Protein Journal, 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
Pathological Mutations D169G and P112H Electrostatically Aggravate the Amyloidogenicity of the Functional Domain of TDP-43.
Pillai M et al.
Acs Chemical Neuroscience, 2024
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
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
The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.
Fakim H et al.
Seminars in Cell & Developmental Biology, 2024
Phosphomimetic substitutions in TDP-43's transiently α-helical region suppress phase separation.
Haider R et al.
Biophysical Journal, 2024
Cell phenotypes can be predicted from propensities of protein conformations.
Nussinov R et al.
Current Opinion in Structural Biology, 2023
Multiscale simulations reveal TDP-43 molecular-level interactions driving condensation.
Ingólfsson HI et al.
Biophysical Journal, 2023
Variability in Clinical Phenotype in TARDBP Mutations: Amyotrophic Lateral Sclerosis Case Description and Literature Review.
Lombardi M et al.
Genes, 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
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
An Atypical Presentation of Upper Motor Neuron Predominant Juvenile Amyotrophic Lateral Sclerosis Associated with TARDBP Gene: A Case Report and Review of the Literature.
Sánchez-Tejerina D et al.
Genes, 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
Protein synthesis modulation as a therapeutic approach for amyotrophic lateral sclerosis and frontotemporal dementia.
Charif SE et al.
Neural Regeneration 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
Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons.
Vishal SS et al.
Frontiers in Cell and Developmental Biology, 2022
Functional implication of ubiquitinating and deubiquitinating mechanisms in TDP-43 proteinopathies.
Tran NN et al.
Frontiers in Cell and Developmental Biology, 2022
Translational regulation in the brain by TDP-43 phase separation.
Gao J et al.
The Journal of Cell Biology, 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
HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells.
Yu H et al.
Science (new York, N.y.), 2021
TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance in ALS.
Zuo X et al.
Nature Structural & Molecular Biology, 2021
Destination Amyotrophic Lateral Sclerosis.
Keon M et al.
Frontiers in Neurology, 2021
Stress granule subtypes: an emerging link to neurodegeneration.
Advani VM et al.
Cellular and Molecular Life Sciences : Cmls, 2020
A Systematic and Comprehensive Review on Disease-Causing Genes in Amyotrophic Lateral Sclerosis.
Srinivasan E et al.
Journal of Molecular Neuroscience : Mn, 2020
Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases.
Wright GSA et al.
Iscience, 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
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
Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration.
Vivoli Vega M et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2019
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 2019
Structural Transition, Function and Dysfunction of TDP-43 in Neurodegenerative Diseases.
Afroz T et al.
Chimia, 2019