Evidence map›Paper›PMID 21127034›Full record

ArticleBioinformatics (Oxford, England)2011

A regression framework incorporating quantitative and negative interaction data improves quantitative prediction of PDZ domain-peptide interaction from primary sequence.

Xiaojian Shao, Chris S H Tan, Courtney Voss, Shawn S C Li, Naiyang Deng, Gary D Bader

Abstract read
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Article in Bioinformatics (Oxford, England), 2011. 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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0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Learning sequence determinants of protein:protein interaction specificity with sparse graphical models.Journal of computational biology : a journal of computational molecular cell biology · 2015
    Article
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  9. Learning Sequence Determinants of Protein:protein Interaction Specificity with Sparse Graphical Models.Research in computational molecular biology : ... Annual International Conference, RECOMB ... : proceedings. RECOMB (Conference : 2005- ) · 2014
    Article
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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Xiaojian ShaoDepartment of Applied Mathematics, College of Science, China Agricultural University, Beijing, 100083, China.
Chris S H Tan
Courtney Voss
Shawn S C Li
Naiyang Deng
Gary D Bader

Funding

Canadian Institutes of Health Research MOP-84324
6 · The paper itself

Abstract

motivationPredicting protein interactions involving peptide recognition domains is essential for understanding the many important biological processes they mediate. It is important to consider the binding strength of these interactions to help us construct more biologically relevant protein interaction networks that consider cellular context and competition between potential binders.

resultsWe developed a novel regression framework that considers both positive (quantitative) and negative (qualitative) interaction data available for mouse PDZ domains to quantitatively predict interactions between PDZ domains, a large peptide recognition domain family, and their peptide ligands using primary sequence information. First, we show that it is possible to learn from existing quantitative and negative interaction data to infer the relative binding strength of interactions involving previously unseen PDZ domains and/or peptides given their primary sequence. Performance was measured using cross-validated hold out testing and testing with previously unseen PDZ domain-peptide interactions. Second, we find that incorporating negative data improves quantitative interaction prediction. Third, we show that sequence similarity is an important prediction performance determinant, which suggests that experimentally collecting additional quantitative interaction data for underrepresented PDZ domain subfamilies will improve prediction. AVAILABILITY AND IMPLEMENTATION: The Matlab code for our SemiSVR predictor and all data used here are available at http://baderlab.org/Data/PDZAffinity.

Indexed as

Models, MolecularPDZ DomainsPeptidesAnimalsComputational BiologyLigandsMiceMutationProtein BindingProteinsProtein Structure, TertiaryRegression AnalysisReproducibility of ResultsLigandsPeptidesProteins

Identifiers

PMID21127034
PMCPMC3031032

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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.