ArticleBiomolecules2025
Evaluating the Topological Features of Monomeric and Trimeric TRAF2-C: A Multi-Disciplinary Approach.
Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Allantopyrone A promotes cross-linking of ubiquitin-specific protease 5 (USP5) and inhibits its deubiquitinase activity by targeting distinct domains.The Journal of antibiotics · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
This study investigates the structural dynamics of the TRAF2 C-terminal domain (TRAF2-C), a key adaptor protein in TNF receptor signaling. TRAF2 usually forms trimers, but its ability to dissociate into monomers is critical for regulating apoptosis, inflammation, and cell survival. Using Fluorescence Fluctuation Spectroscopy, dynamic light scattering, circular dichroism, and Small Angle Neutron Scattering, we analyzed TRAF2-C over a wide concentration range. At nanomolar levels, the protein dissociates easily, with trimers representing only a minor fraction, while micromolar concentrations strongly favor trimerization. Dissociation also reduces α-helical content without disrupting the overall fold. Molecular dynamics simulations and protein contact network analysis support this analysis, identifying interfacial residues and hydrogen bonds as key factors stabilizing oligomers and enabling dynamic asymmetry. Overall, these findings highlight TRAF2-C's capacity to switch between monomeric and trimeric states as a crucial regulatory mechanism, offering insights into TRAF-mediated signaling and potential therapeutic strategies.
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Registered trials
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