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• W1644470444 abstract "In view of the increasing interest both in inhibitors of protein-protein interactions and in protein drugs themselves, analysis of the three-dimensional structure of protein-protein complexes is assuming greater relevance in drug design. In the many cases where an experimental structure is not available, protein-protein docking becomes the method of choice for predicting the arrangement of the complex. However, reliably scoring protein-protein docking poses is still an unsolved problem. As a consequence, the screening of many docking models is usually required in the analysis step, to possibly single out the correct ones. Here, making use of exemplary cases, we review our recently introduced methods for the analysis of protein complex structures and for the scoring of protein docking poses, based on the use of inter-residue contacts and their visualization in inter-molecular contact maps. We also show that the ensemble of tools we developed can be used in the context of rational drug design targeting protein-protein interactions." @default.
• W1644470444 created "2016-06-24" @default.
• W1644470444 creator A5029620262 @default.
• W1644470444 creator A5053222658 @default.
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• W1644470444 date "2015-07-01" @default.
• W1644470444 modified "2023-10-12" @default.
• W1644470444 title "Analysis and Ranking of Protein-Protein Docking Models Using Inter-Residue Contacts and Inter-Molecular Contact Maps" @default.
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• W1644470444 doi "https://doi.org/10.3390/molecules200712045" @default.
• W1644470444 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6332208" @default.
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