ArticleRSC advances2018
Elucidation of the structural stability and dynamics of heterogeneous intermediate ensembles in unfolding pathway of the N-terminal domain of TDP-43.
Article in RSC advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Stability and Dynamics of the N‑Terminal Domain of TDP-43 and the Effect of Point Mutations.ACS omega · 2026Article
- Targeting the Ubiquitin-conjugating Enzyme for Oral Squamous Cell Carcinoma Therapy: Discovering Natural Inhibitors.Current computer-aided drug design · 2026Article
- Heterogeneous Folding Intermediates Govern the Conformational Pathway of the RNA Recognition Motif Domain of the Ewing Sarcoma Protein.Biomolecules · 2025Article
- Bioinformatics approach for discovery of potential lead compound of NSP6 of SARS-CoV-2 using structure based virtual screening and molecular dynamics simulations.Scientific reports · 2025Article
- A comparative study of computational modeling approaches for evaluating structural dynamics and algorithmic suitability of short length peptides.Scientific reports · 2025Article
- Detection of an Intermediate in the Unfolding Process of the N-Terminal Domain of TDP-43.ACS omega · 2025Article
- Investigation into in silico and in vitro approaches for inhibitors targeting MCM10 in Leishmania donovani: a comprehensive study.Molecular diversity · 2025Article
- Boar Sperm Cryopreservation Improvement Using Semen Extender Modification by Dextran and Pentaisomaltose.Animals : an open access journal from MDPI · 2022Article
- Computational Insights of Unfolding of N-Terminal Domain of TDP-43 Reveal the Conformational Heterogeneity in the Unfolding Pathway.Frontiers in molecular neuroscience · 2022Article
- In Silico Identification and Validation of Organic Triazole Based Ligands as Potential Inhibitory Drug Compounds of SARS-CoV-2 Main Protease.Molecules (Basel, Switzerland) · 2021Article
- Insights into the aggregation mechanism of RNA recognition motif domains in TDP-43: a theoretical exploration.Royal Society open science · 2021Article
- Identifying the natural polyphenol catechin as a multi-targeted agent against SARS-CoV-2 for the plausible therapy of COVID-19: an integrated computational approach.Briefings in bioinformatics · 2021Article
- Discovering Potential RNA Dependent RNA Polymerase Inhibitors as Prospective Drugs Against COVID-19: An in silico Approach.Frontiers in pharmacology · 2021Article
- Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases.iScience · 2020Article
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4 authors.
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Abstract
The N-terminal domain of the RNA binding protein TDP-43 (NTD) is essential to both physiology and proteinopathy; however, elucidation of its folding/unfolding still remains a major quest. In this study, we have investigated the biophysical behavior of intermediate ensembles employing all-atom molecular dynamics simulations in 8 M urea accelerated with high temperatures to achieve unfolded states in a confined computation time. The cumulative results of the 2.75 μs simulations show that unfolding of the NTD at 350 K evolves through different stable and meta-stable intermediate states. The free-energy landscape reveals two meta-stable intermediates (I
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