ArticleBiophysics (Nagoya-shi, Japan)2007
Prediction of interacting proteins from homology-modeled complex structures using sequence and structure scores.
Article in Biophysics (Nagoya-shi, Japan), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Blood Flow Restriction Training for Rehabilitation and Readiness in Tactical Populations: A Scoping Review.Healthcare (Basel, Switzerland) · 2026Review
- Article
- HOMCOS: an updated server to search and model complex 3D structures.Journal of structural and functional genomics · 2016Article
- Template-based structure modeling of protein-protein interactions.Current opinion in structural biology · 2014Review
- A computational framework for boosting confidence in high-throughput protein-protein interaction datasets.Genome biology · 2012Article
- iWRAP: An interface threading approach with application to prediction of cancer-related protein-protein interactions.Journal of molecular biology · 2011Article
- Struct2Net: a web service to predict protein-protein interactions using a structure-based approach.Nucleic acids research · 2010Article
- HOMCOS: a server to predict interacting protein pairs and interacting sites by homology modeling of complex structures.Nucleic acids research · 2008Article
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Authors and funding
3 authors.
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Abstract
Protein-protein interactions support most biological processes, and it is important to find specifically interacting partner proteins among homologous proteins in order to elucidate cellular functions such as signal transduction systems. Various high-throughput experimental methods for identifying these interactions have been invented, and used to generate a huge amount of data. Because these experiments have been applied to only a few organisms, and their accuracy is believed to be limited, it would be valuable to develop computational methods for predicting protein-protein interactions from their amino acid sequences or tertiary structural information. In this study, we describe a prediction method of interacting proteins based on homology-modeled complex structures. We employed the statistical residue-residue contact energy used in a previous study, and two types of new scores, simple electrostatic energy and sequence similarity between target sequences and template structures. The validity of each protein-protein complex model was measured using their single and combined scores. We applied our method to all the protein heterodimers of
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