ArticleNucleic acids research2010
Inferred Biomolecular Interaction Server--a web server to analyze and predict protein interacting partners and binding sites.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
54 citing papers in PubMed.
- Pathogen-driven cancers from a structural perspective: Targeting host-pathogen protein-protein interactions.Frontiers in oncology · 2023Review
- A Deep Learning and XGBoost-Based Method for Predicting Protein-Protein Interaction Sites.Frontiers in genetics · 2021Article
- Review
- Principles and characteristics of biological assemblies in experimentally determined protein structures.Current opinion in structural biology · 2019Review
- In Silico Analysis of Homologous Heterodimers of Cruzipain-Chagasin from Structural Models Built by Homology.International journal of molecular sciences · 2019Article
- Article
- Ranking Enzyme Structures in the PDB by Bound Ligand Similarity to Biological Substrates.Structure (London, England : 1993) · 2018Article
- Exploring the potential of 3D Zernike descriptors and SVM for protein-protein interface prediction.BMC bioinformatics · 2018Article
- Annotating Mutational Effects on Proteins and Protein Interactions: Designing Novel and Revisiting Existing Protocols.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Exploring Protein-Protein Interactions as Drug Targets for Anti-cancer Therapy with In Silico Workflows.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Elucidating the druggable interface of protein-protein interactions using fragment docking and coevolutionary analysis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Understanding the fabric of protein crystals: computational classification of biological interfaces and crystal contacts.Bioinformatics (Oxford, England) · 2016Review
- Large-Scale Analysis Exploring Evolution of Catalytic Machineries and Mechanisms in Enzyme Superfamilies.Journal of molecular biology · 2016Article
- Progress and challenges in predicting protein interfaces.Briefings in bioinformatics · 2016Review
- Review
- Mutations in the KDM5C ARID Domain and Their Plausible Association with Syndromic Claes-Jensen-Type Disease.International journal of molecular sciences · 2015Article
- Improving protein-ligand docking with flexible interfacial water molecules using SWRosettaLigand.Journal of molecular modeling · 2015Article
- A Pan-Cancer Catalogue of Cancer Driver Protein Interaction Interfaces.PLoS computational biology · 2015Article
- Structural Perspectives on the Evolutionary Expansion of Unique Protein-Protein Binding Sites.Biophysical journal · 2015Article
- Surfing the Protein-Protein Interaction Surface Using Docking Methods: Application to the Design of PPI Inhibitors.Molecules (Basel, Switzerland) · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
IBIS is the NCBI Inferred Biomolecular Interaction Server. This server organizes, analyzes and predicts interaction partners and locations of binding sites in proteins. IBIS provides annotations for different types of binding partners (protein, chemical, nucleic acid and peptides), and facilitates the mapping of a comprehensive biomolecular interaction network for a given protein query. IBIS reports interactions observed in experimentally determined structural complexes of a given protein, and at the same time IBIS infers binding sites/interacting partners by inspecting protein complexes formed by homologous proteins. Similar binding sites are clustered together based on their sequence and structure conservation. To emphasize biologically relevant binding sites, several algorithms are used for verification in terms of evolutionary conservation, biological importance of binding partners, size and stability of interfaces, as well as evidence from the published literature. IBIS is updated regularly and is freely accessible via http://www.ncbi.nlm.nih.gov/Structure/ibis/ibis.html.
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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.