ArticleNucleic acids research2012
IBIS (Inferred Biomolecular Interaction Server) reports, predicts and integrates multiple types of conserved interactions for proteins.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
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- BioLiP2: an updated structure database for biologically relevant ligand-protein interactions.Nucleic acids research · 2024Article
- ScanNet: an interpretable geometric deep learning model for structure-based protein binding site prediction.Nature methods · 2022Article
- CATH functional families predict functional sites in proteins.Bioinformatics (Oxford, England) · 2021Article
- Biological impact of mutually exclusive exon switching.PLoS computational biology · 2021Article
- MutaBind2: Predicting the Impacts of Single and Multiple Mutations on Protein-Protein Interactions.iScience · 2020Article
- ProtCID: a data resource for structural information on protein interactions.Nature communications · 2020Article
- Exploring the functional impact of alternative splicing on human protein isoforms using available annotation sources.Briefings in bioinformatics · 2019Review
- Evolutionary coupling analysis identifies the impact of disease-associated variants at less-conserved sites.Nucleic acids research · 2019Article
- Pathogenicity and functional impact of non-frameshifting insertion/deletion variation in the human genome.PLoS computational biology · 2019Article
- In Silico Analysis of Homologous Heterodimers of Cruzipain-Chagasin from Structural Models Built by Homology.International journal of molecular sciences · 2019Article
- A CATH domain functional family based approach to identify putative cancer driver genes and driver mutations.Scientific reports · 2019Article
- Article
- PremPDI estimates and interprets the effects of missense mutations on protein-DNA interactions.PLoS computational biology · 2018Article
- Computational Approaches to Prioritize Cancer Driver Missense Mutations.International journal of molecular sciences · 2018Review
- Article
- PDB-wide identification of biological assemblies from conserved quaternary structure geometry.Nature methods · 2018Article
- Structural and Functional View of Polypharmacology.Scientific reports · 2017Article
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Authors and funding
9 authors.
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Abstract
We have recently developed the Inferred Biomolecular Interaction Server (IBIS) and database, which reports, predicts and integrates different types of interaction partners and locations of binding sites in proteins based on the analysis of homologous structural complexes. Here, we highlight several new IBIS features and options. The server's webpage is now redesigned to allow users easier access to data for different interaction types. An entry page is added to give a quick summary of available results and to now accept protein sequence accessions. To elucidate the formation of protein complexes, not just binary interactions, IBIS currently presents an expandable interaction network. Previously, IBIS provided annotations for four different types of binding partners: proteins, small molecules, nucleic acids and peptides; in the current version a new protein-ion interaction type has been added. Several options provide easy downloads of IBIS data for all Protein Data Bank (PDB) protein chains and the results for each query. In this study, we show that about one-third of all RefSeq sequences can be annotated with IBIS interaction partners and binding sites. The IBIS server is available at http://www.ncbi.nlm.nih.gov/Structure/ibis/ibis.cgi and updated biweekly.
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