Varaico: Literature-Extracted Genetic Variants

Gene:TARDBP
Variant:p.Q343R
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TARDBP

NM_007375.4:p.Q343R

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

Neurodegenerative disease and autophagy in iPSC-based models.

Odonchimed S et al.

Neuroscience Research, 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

Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective Responses.

Verde EM et al.

Cells, 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

Pathogenic TDP-43 in amyotrophic lateral sclerosis.

Chong ZZ et al.

Drug Discovery Today, 2025

Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy.

Balendra R et al.

The Lancet. Neurology, 2025

40252666 (PubMed )
Supplement: EMS205435-supplement-Supplementary_table_1.pdf

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

38126188 (PubMed )
Supplement: supplement_1.xlsx › Table_S8

Enhanced secretion of the amyotrophic lateral sclerosis ALS-associated misfolded TDP-43 mediated by the ER-ubiquitin specific peptidase USP19.

Picard F et al.

Cellular and Molecular Life Sciences : Cmls, 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

40589786 (PubMed )
Supplement: Table_4.xlsx › ClinVar_filtered_variants

Computational Insights Into the Mechanism of EGCG's Binding and Inhibition of the TDP-43 Aggregation.

Meshram VD et al.

Chemical Biology & Drug Design, 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

Elevated nuclear TDP-43 induces constitutive exon skipping.

Carmen-Orozco RP et al.

Molecular Neurodegeneration, 2024

38853250 (PubMed )
Supplement: 13024_2024_732_MOESM1_ESM.pdf

The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosis.

Zibold J et al.

Brain : a Journal of Neurology, 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

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

Invertebrate genetic models of amyotrophic lateral sclerosis.

Zhou L et al.

Frontiers in Molecular Neuroscience, 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

Multiscale simulations reveal TDP-43 molecular-level interactions driving condensation.

Ingólfsson HI et al.

Biophysical Journal, 2023

37853696 (PubMed )
Supplement: mmc3.pdf

Mitochondria, a Key Target in Amyotrophic Lateral Sclerosis Pathogenesis.

Genin EC et al.

Genes, 2023

Genetic variability in sporadic amyotrophic lateral sclerosis.

Van Daele SH et al.

Brain : a Journal of Neurology, 2023

37043475 (PubMed )
Supplement: awad120_supplementary_data.zip › brain-2022-02191-File008.xlsx › suppl_table_6_P_LP

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP.

Arseni D et al.

Nature, 2023

37532939 (PubMed )
Supplement: 41586_2023_6405_MOESM1_ESM.pdf

Studies of Genetic and Proteomic Risk Factors of Amyotrophic Lateral Sclerosis Inspire Biomarker Development and Gene Therapy.

Bagyinszky E et al.

Cells, 2023

Specific vulnerability of iPSC-derived motor neurons with TDP-43 gene mutation to oxidative stress.

Onda-Ohto A et al.

Molecular Brain, 2023

Integrated Omic Analysis Delineates Pathways Modulating Toxic TDP-43 Protein Aggregates in Amyotrophic Lateral Sclerosis.

Rajaratnam S et al.

Cells, 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

37638449 (PubMed )
Supplement: jnd-10-jnd230148-s001.xlsx › variant_list

Loss of TDP-43 function contributes to genomic instability in amyotrophic lateral sclerosis.

Fang M et al.

Frontiers in Neuroscience, 2023

Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates.

Horvath A et al.

Biochemistry, 2022

36341999 (PubMed )
Supplement: bi2c00499_si_005.xlsx › Single_mutations

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

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

Altered TDP-43 Structure and Function: Key Insights into Aberrant RNA, Mitochondrial, and Cellular and Systemic Metabolism in Amyotrophic Lateral Sclerosis.

Jiang L et al.

Metabolites, 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

Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons.

Vishal SS et al.

Frontiers in Cell and Developmental Biology, 2022

TDP-43 Pathology in Alzheimer's Disease.

Meneses A et al.

Molecular Neurodegeneration, 2021

Nearly 30 Years of Animal Models to Study Amyotrophic Lateral Sclerosis: A Historical Overview and Future Perspectives.

Bonifacino T et al.

International Journal of Molecular Sciences, 2021

Reduced PHOX2B stability causes axonal growth impairment in motor neurons with TARDBP mutations.

Mitsuzawa S et al.

Stem Cell Reports, 2021

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."