ArticleBioinformatics advances2025
Zepyros: a webserver to evaluate the shape complementarity of protein-protein interfaces.
Article in Bioinformatics advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Exploring neural networks to uncover information-richer features for protein interaction prediction.European biophysics journal : EBJ · 2026Article
- Compact Assessment of Molecular Surface Complementarities Enhances Neural Network-Aided Prediction of Key Binding Residues.Journal of chemical information and modeling · 2025Article
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- High-Throughput Interactome Determination via Sulfur Anomalous Scattering.The journal of physical chemistry letters · 2024Article
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Authors and funding
5 authors.
Funding
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Abstract
Motivation: Shape complementarity of molecular surfaces at the interfaces is a well-known characteristic of protein-protein binding regions, and it is critical in influencing the stability of the complex. Measuring such complementarity is of great importance for a number of theoretical and practical implications; however, only a limited number of tools are currently available to efficiently and rapidly assess it. Results: Here, we introduce Zepyros (ZErnike Polynomials analYsis of pROtein Shapes), a webserver for fast measurement of the shape complementarity between two molecular interfaces of a given protein-protein complex using structural information. Zepyros is implemented as a publicly available tool with a user-friendly interface. Availability and implementation: Our server can be found at the following link (all major browser supported): https://zepyros.bio-groups.com.
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Registered trials
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