PMC:1764415 / 46723-47829 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/1764415","sourcedb":"PMC","sourceid":"1764415","source_url":"https://www.ncbi.nlm.nih.gov/pmc/1764415","text":"Overwhelming performance of our approach has been demonstrated in several criteria including visual inspection. STM generated bigger size clusters with arbitrary shape, and those identified clusters are more biologically enriched, i.e., higher P-value, even though they have low density. There are more than 5% of unannotated proteins in the identified clusters. The function of those unannotated proteins can be predicted according to their assigned main functions by our method. Completeness of our clustering method is another distinct strength compared to the other methods. Our method discarded only about 7.8% of proteins which is tremendously lower than the other approaches did, 59% in average. In conclusion, STM has strong pharmacodynamics-based underpinnings and is an effective, versatile approach for analyzing protein-protein interactions. The STM approach contains a framework for rationally incorporating reaction rates, protein concentrations and interaction stoichiometry should these become available. It could therefore have potential applications in the drug discovery and development.","tracks":[]}