ArticlePLoS computational biology2007
Structure-templated predictions of novel protein interactions from sequence information.
Article in PLoS computational biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
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- ProteinPrompt: a webserver for predicting protein-protein interactions.Bioinformatics advances · 2022Article
- Computational identification of protein-protein interactions in model plant proteomes.Scientific reports · 2019Article
- Prediction of Protein-Protein Interaction Sites with Machine-Learning-Based Data-Cleaning and Post-Filtering Procedures.The Journal of membrane biology · 2016Article
- MSCA: a spectral comparison algorithm between time series to identify protein-protein interactions.BMC bioinformatics · 2015Article
- A computational framework for boosting confidence in high-throughput protein-protein interaction datasets.Genome biology · 2012Article
- The identification of short linear motif-mediated interfaces within the human interactome.Bioinformatics (Oxford, England) · 2012Article
- Prediction and characterization of protein-protein interaction networks in swine.Proteome science · 2012Article
- SPPS: a sequence-based method for predicting probability of protein-protein interaction partners.PloS one · 2012Article
- Short Co-occurring Polypeptide Regions Can Predict Global Protein Interaction Maps.Scientific reports · 2012Article
- iWRAP: An interface threading approach with application to prediction of cancer-related protein-protein interactions.Journal of molecular biology · 2011Article
- A strategy for interaction site prediction between phospho-binding modules and their partners identified from proteomic data.Molecular & cellular proteomics : MCP · 2010Article
- Critical assessment of sequence-based protein-protein interaction prediction methods that do not require homologous protein sequences.BMC bioinformatics · 2009Article
- Accurate prediction of peptide binding sites on protein surfaces.PLoS computational biology · 2009Article
- Genomic landscape of developing male germ cells.Birth defects research. Part C, Embryo today : reviews · 2009Review
- Predicting PDZ domain-peptide interactions from primary sequences.Nature biotechnology · 2008Article
- Global investigation of protein-protein interactions in yeast Saccharomyces cerevisiae using re-occurring short polypeptide sequences.Nucleic acids research · 2008Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The multitude of functions performed in the cell are largely controlled by a set of carefully orchestrated protein interactions often facilitated by specific binding of conserved domains in the interacting proteins. Interacting domains commonly exhibit distinct binding specificity to short and conserved recognition peptides called binding profiles. Although many conserved domains are known in nature, only a few have well-characterized binding profiles. Here, we describe a novel predictive method known as domain-motif interactions from structural topology (D-MIST) for elucidating the binding profiles of interacting domains. A set of domains and their corresponding binding profiles were derived from extant protein structures and protein interaction data and then used to predict novel protein interactions in yeast. A number of the predicted interactions were verified experimentally, including new interactions of the mitotic exit network, RNA polymerases, nucleotide metabolism enzymes, and the chaperone complex. These results demonstrate that new protein interactions can be predicted exclusively from sequence information.
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