ArticleProtein science : a publication of the Protein Society2016
A hybrid method for protein-protein interface prediction.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- PrePPI - Structure-based Prediction of Protein-protein Interactomes and Networks.Journal of molecular biology · 2026Article
- Decoding the blueprint of receptor binding by filoviruses through large-scale binding assays and machine learning.Cell host & microbe · 2025Article
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- Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection.Nature communications · 2023Article
- PrePPI: A Structure Informed Proteome-wide Database of Protein-Protein Interactions.Journal of molecular biology · 2023Article
- BabyBoom: 3-Dimensional Structure-Based Ligand and Protein Interaction Prediction by Molecular Docking.Biomolecules · 2022Article
- Integrated structure-based protein interface prediction.BMC bioinformatics · 2022Article
- Getting to know each other: PPIMem, a novel approach for predicting transmembrane protein-protein complexes.Computational and structural biotechnology journal · 2021Article
- Molecular dynamics of the histamine H3 membrane receptor reveals different mechanisms of GPCR signal transduction.Scientific reports · 2020Article
- Article
- Computational approaches to macromolecular interactions in the cell.Current opinion in structural biology · 2019Review
- BIPSPI: a method for the prediction of partner-specific protein-protein interfaces.Bioinformatics (Oxford, England) · 2019Article
- Structure-based prediction of ligand-protein interactions on a genome-wide scale.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Link prediction based on non-negative matrix factorization.PloS one · 2017Article
- Article
- Integrating 3D structural information into systems biology.The Journal of biological chemistryReview
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3 authors.
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Abstract
The growing structural coverage of proteomes is making structural comparison a powerful tool for function annotation. Such template-based approaches are based on the observation that structural similarity is often sufficient to infer similar function. However, it seems clear that, in addition to structural similarity, the specific characteristics of a given protein should also be taken into account in predicting function. Here we describe PredUs 2.0, a method to predict regions on a protein surface likely to bind other proteins, that is, interfacial residues. PredUs 2.0 is based on the PredUs method that is entirely template-based and uses known binding sites in structurally similar proteins to predict interfacial residues. PredUs 2.0 uses a Bayesian approach to combine the template-based scoring of PredUs with a score that reflects the propensities of individual amino acids to be in interfaces. PredUs 2.0 includes a novel protein size dependent metric to determine the number of residues that should be reported as interfacial. PredUs 2.0 significantly outperforms PredUs as well as other published interface prediction methods.
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