Varaico: Literature-Extracted Genetic Variants

Gene:TARDBP
Variant:p.M359V
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TARDBP

NM_007375.4:p.M359V

Associated Papers

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

Semantic behavioral variant frontotemporal dementia and semantic dementia associated with TARDBP mutations.

Piga G et al.

Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration, 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

Structural Integrity of Nucleolin Is Required to Suppress TDP-43-Mediated Cytotoxicity in Yeast and Human Cell Models.

Peggion C et al.

International Journal of Molecular Sciences, 2023

Variability in Clinical Phenotype in TARDBP Mutations: Amyotrophic Lateral Sclerosis Case Description and Literature Review.

Lombardi M 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_7_VUS

Identification of TARDBP Gly298Ser as a founder mutation for amyotrophic lateral sclerosis in Southern China.

Xu F et al.

Bmc Medical Genomics, 2022

35932023 (PubMed )
Supplement: 12920_2022_1327_MOESM1_ESM.docx

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

Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation.

Tziortzouda P et al.

Nature Reviews. Neuroscience, 2021

Frontotemporal dementia-linked P112H mutation of TDP-43 induces protein structural change and impairs its RNA binding function.

Agrawal S et al.

Protein Science : a Publication of the Protein Society, 2021

RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy.

Chen HJ et al.

Brain : a Journal of Neurology, 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

30938443 (PubMed )
Supplement: awz078_supplementary_data.pdf

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

Phase to Phase with TDP-43.

Sun Y et al.

Biochemistry, 2017

Decreased Levels of Foldase and Chaperone Proteins Are Associated with an Early-Onset Amyotrophic Lateral Sclerosis.

Filareti M et al.

Frontiers in Molecular Neuroscience, 2017

Defining the spectrum of frontotemporal dementias associated with TARDBP mutations.

Caroppo P et al.

Neurology. Genetics, 2016

Clinical phenotypes and radiological findings in frontotemporal dementia related to TARDBP mutations.

Floris G et al.

Journal of Neurology, 2015

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

Mutational analysis of TARDBP in Parkinson's disease.

van Blitterswijk M et al.

Neurobiology of Aging, 2013

Role of selected mutations in the Q/N rich region of TDP-43 in EGFP-12xQ/N-induced aggregate formation.

Budini M et al.

Brain Research, 2012

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

TARDBP mutations in frontotemporal lobar degeneration: frequency, clinical features, and disease course.

Borroni B et al.

Rejuvenation Research, 2010

Novel TARDBP sequence variant and C9ORF72 repeat expansion in a family with frontotemporal dementia.

Kaivorinne AL et al.

Alzheimer Disease and Associated Disorders, 0

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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."