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
From TDP-43/RNA complex formation to disease-linked TDP-43 aggregation through a structural and cellular approach.
Feng Y et al.
Nature Communications, 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
Identifying interactions between TDP-43's N-terminal and RNA-binding domains.
Scott DD et al.
Protein Science : a Publication of the Protein Society, 2025
Antisense Oligonucleotide Therapy for Amyotrophic Lateral Sclerosis (ALS): An Umbrella Review.
Jeong E et al.
Cureus, 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
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
The Regulation of TDP-43 Structure and Phase Transitions: A Review.
Liu Y et al.
The Protein Journal, 2025
TDP-43 as a potential retinal biomarker for neurodegenerative diseases.
Glashutter M et al.
Frontiers in Neuroscience, 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
Pathological Mutations D169G and P112H Electrostatically Aggravate the Amyloidogenicity of the Functional Domain of TDP-43.
Pillai M et al.
Acs Chemical Neuroscience, 2024
Targeting Protein Misfolding and Aggregation as a Therapeutic Perspective in Neurodegenerative Disorders.
Sidoryk-Węgrzynowicz M et al.
International Journal of Molecular Sciences, 2024
Molecular Mechanisms of Phase Separation and Amyloidosis of ALS/FTD-linked FUS and TDP-43.
Song J
Aging and Disease, 2024
Conformational Enigma of TDP-43 Misfolding in Neurodegenerative Disorders.
Pillai M et al.
Acs Omega, 2024
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
N-Terminal Fragments of TDP-43-In Vitro Analysis and Implication in the Pathophysiology of Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration.
Chami AA et al.
Genes, 2024
Stress-induced TDP-43 nuclear condensation causes splicing loss of function and STMN2 depletion.
Huang WP et al.
Cell Reports, 2024
Halogen doped graphene quantum dots modulate TDP-43 phase separation and aggregation in the nucleus.
Zhang H et al.
Nature Communications, 2024
The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.
Fakim H et al.
Seminars in Cell & Developmental Biology, 2024
Drug Screening and Validation Targeting TDP-43 Proteinopathy for Amyotrophic Lateral Sclerosis.
Xin J et al.
Aging and Disease, 2024
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.
Khalil B et al.
Molecular Neurodegeneration, 2024
Proteomics elucidating physiological and pathological functions of TDP-43.
García Morato J et al.
Proteomics, 2023
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
Variability in Clinical Phenotype in TARDBP Mutations: Amyotrophic Lateral Sclerosis Case Description and Literature Review.
Lombardi M et al.
Genes, 2023
TDP-43 protein interactome informs about perturbed canonical pathways and may help develop personalized medicine approaches for patients with TDP-43 pathology.
Helmold BR et al.
Drug Discovery Today, 2023
Mitochondria, a Key Target in Amyotrophic Lateral Sclerosis Pathogenesis.
Genin EC et al.
Genes, 2023
TDP-43 Epigenetic Facets and Their Neurodegenerative Implications.
Gimenez J et al.
International Journal of Molecular Sciences, 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
Identifying the molecular drivers of ALS-implicated missense mutations.
Portelli S et al.
Journal of Medical Genetics, 2023
Integrated Omic Analysis Delineates Pathways Modulating Toxic TDP-43 Protein Aggregates in Amyotrophic Lateral Sclerosis.
Rajaratnam S et al.
Cells, 2023
Shapeshifter TDP-43: Molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators.
Doke AA et al.
Biophysical Chemistry, 2023
Proteostasis and Ribostasis Impairment as Common Cell Death Mechanisms in Neurodegenerative Diseases.
Lim SM et al.
Journal of Clinical Neurology (seoul, Korea), 2023
Aggregation of Disordered Proteins Associated with Neurodegeneration.
Tsoi PS et al.
International Journal of Molecular Sciences, 2023
Potential roles of the endoplasmic reticulum stress pathway in amyotrophic lateral sclerosis.
Jeon YM et al.
Frontiers in Aging Neuroscience, 2023
Codon-optimized TDP-43 mediates neurodegeneration in a Drosophila model of ALS/FTLD.
Yusuff T et al.
Frontiers in Genetics, 2023
Amyotrophic lateral sclerosis.
Younger DS et al.
Handbook of Clinical Neurology, 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
TDP-43 dysregulation and neuromuscular junction disruption in amyotrophic lateral sclerosis.
Lépine S et al.
Translational Neurodegeneration, 2022
Importin α/β and the tug of war to keep TDP-43 in solution: quo vadis?
Doll SG et al.
Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology, 2022
Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLD.
Tamaki Y et al.
International Journal of Molecular Sciences, 2022
Proteostasis impairment and ALS.
Lambert-Smith IA et al.
Progress in Biophysics and Molecular Biology, 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