ArticleProtein science : a publication of the Protein Society2022
Dockground resource for protein recognition studies.
Article in Protein science : a publication of the Protein Society, 2022. 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.
- Dockground: Expanding the Resource to Protein-DNA Complexes.Journal of molecular biology · 2026Article
- PPIscreenML is a method for structure-based screening of protein-protein interactions using AlphaFold.eLife · 2026Article
- IgPose: a generative data-augmented pipeline for robust immunoglobulin-antigen binding prediction.Bioinformatics (Oxford, England) · 2026Article
- Integrating deep learning with physics based modeling enables high precision antibody antigen interface prediction.Scientific reports · 2026Article
- Global comparative structural analysis of responses to protein phosphorylation.Nature communications · 2025Article
- Dockground: The Resource Expands to Protein-RNA Interactome.Journal of molecular biology · 2025Article
- In silico prediction method for plant Nucleotide-binding leucine-rich repeat- and pathogen effector interactions.The Plant journal : for cell and molecular biology · 2025Article
- TopoQA: a topological deep learning-based approach for protein complex structure interface quality assessment.Briefings in bioinformatics · 2025Article
- Challenges in predicting PROTAC-mediated protein-protein interfaces with AlphaFold reveal a general limitation on small interfaces.Bioinformatics advances · 2025Article
- Unmasking AlphaFold to integrate experiments and predictions in multimeric complexes.Nature communications · 2024Article
- A variational expectation-maximization framework for balanced multi-scale learning of protein and drug interactions.Nature communications · 2024Article
- Prediction of Paratope-Epitope Pairs Using Convolutional Neural Networks.International journal of molecular sciences · 2024Article
- GRAMM Web Server for Protein Docking.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Dockground resource for protein recognition studies.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
6 authors.
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Abstract
Structural information of protein-protein interactions is essential for characterization of life processes at the molecular level. While a small fraction of known protein interactions has experimentally determined structures, computational modeling of protein complexes (protein docking) has to fill the gap. The Dockground resource (http://dockground.compbio.ku.edu) provides a collection of datasets for the development and testing of protein docking techniques. Currently, Dockground contains datasets for the bound and the unbound (experimentally determined and simulated) protein structures, model-model complexes, docking decoys of experimentally determined and modeled proteins, and templates for comparative docking. The Dockground bound proteins dataset is a core set, from which other Dockground datasets are generated. It is devised as a relational PostgreSQL database containing information on experimentally determined protein-protein complexes. This report on the Dockground resource describes current status of the datasets, new automated update procedures and further development of the core datasets. We also present a new Dockground interactive web interface, which allows search by various parameters, such as release date, multimeric state, complex type, structure resolution, and so on, visualization of the search results with a number of customizable parameters, as well as downloadable datasets with predefined levels of sequence and structure redundancy.
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Registered trials
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.