ArticleScientific reports2017
Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 70 citations in OpenAlex.
- Investigating the effect of progressive truncations at the ALS-linked protein TDP-43 RRM2 on its aggregation mechanism.Frontiers in molecular biosciences · 2026Article
- The plasma nanoDSF denaturation profiles predict the presence of breast cancer.Journal of translational medicine · 2025Article
- Natural L-Hexapeptides with Therapeutic Potential for Alzheimer's Disease and Tauopathies.ACS omega · 2025Article
- Identifying interactions between TDP-43's N-terminal and RNA-binding domains.Protein science : a publication of the Protein Society · 2025Article
- Divalent and Trivalent Metallic Ions Differentially Affect Alpha-Synuclein Aggregation.ACS chemical neuroscience · 2025Article
- Metal-Induced Genotoxic Events: Possible Distinction Between Sporadic and Familial ALS.Toxics · 2025Review
- Potential Correlation Between Molecular Biomarkers and Oxidative Stress in Traumatic Brain Injury.International journal of molecular sciences · 2025Review
- Homeostasis and metabolism of iron and other metal ions in neurodegenerative diseases.Signal transduction and targeted therapy · 2025Review
- Molecular Mechanisms of Phase Separation and Amyloidosis of ALS/FTD-linked FUS and TDP-43.Aging and disease · 2024Review
- Review
- Which Environmental Pollutants Are Toxic to Our Ears?-Evidence of the Ototoxicity of Common Substances.Toxics · 2024Review
- Preparation and Characterization of Zn(II)-Stabilized AβACS chemical neuroscience · 2024Article
- Exploring the Influence of Zinc Ions on the Conformational Stability and Activity of Protein Disulfide Isomerase.International journal of molecular sciences · 2024Article
- Copper toxicity and deficiency: the vicious cycle at the core of protein aggregation in ALS.Frontiers in molecular neuroscience · 2024Review
- Zinc Modulation of Neuronal Calcium Sensor Proteins: Three Modes of Interaction with Different Structural Outcomes.Biomolecules · 2022Article
- Mechanism of ZnBiomolecules · 2021Article
- Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling.International journal of molecular sciences · 2021Article
- Metals in ALS TDP-43 Pathology.International journal of molecular sciences · 2021Review
- Insights into the aggregation mechanism of RNA recognition motif domains in TDP-43: a theoretical exploration.Royal Society open science · 2021Article
- TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of TDP-43 (transactive response DNA binding protein 43 kDa) is a hallmark of certain forms of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Moreover, intracellular TDP-43-positive inclusions are often found in other neurodegenerative diseases. Recently it was shown that zinc ions can provoke the aggregation of endogenous TDP-43 in cells, allowing to assume a direct interaction of TDP-43 with zinc ions. In this work, we investigated zinc binding to the 102-269 TDP-43 fragment, which comprise the two RNA recognition motifs. Using isothermal titration calorimetry, mass spectrometry, and differential scanning fluorimetry, we showed that zinc binds to this TDP-43 domain with a dissociation constant in the micromolar range and modifies its tertiary structure leading to a decrease of its thermostability. Moreover, the study by dynamic light scattering and negative stain electron microscopy demonstrated that zinc ions induce auto-association process of this TDP-43 fragment into rope-like structures. These structures are thioflavin-T-positive allowing to hypothesize the direct implication of zinc ions in pathological aggregation of TDP-43.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.