Community‐wide evaluation of methods for predicting the effect of mutations on protein–protein interactions
By Rocco Moretti, Sarel Jacob Fleishman, R. Agius, Mieczyslaw Torchala, Paul A. Bates, Panagiotis L. Kastritis, João P. G. L. M. Rodrigues, Mikael E. Trellet, Alexandre M. J. J. Bonvin, Meng Cui and 60 more. 2013
102 citations recorded by the source corpus.
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- Iain H. Moal
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- Alexandre M. J. J. Bonvin
Citations in the corpus
- The scoring of poses in protein-protein docking: current capabilities and future directions (2013, background): “The 3D structures of a protein-protein complex can be used to estimate the effect of mutations [16-21], and thus for protein design [22-29] and determining the functional consequences of mutations associated with diseases (for instance [30]).”
- Score_set: A CAPRI benchmark for scoring protein complexes (2014, background): “44,45 Developing improved function for scoring protein-protein complexes therefore remains a very important research goal.”
- Prediction of homo- and hetero-protein complexes by protein docking and template-based modeling: a CASP-CAPRI experiment (2016, unknown): “With a majority of the targets being offered by structural genomics consortia before their coordinates were deposited in the PDB, author-assigned oligomeric states were available to predictors only for a subset ( (cid:2) 15) of the targets, and those were often tentative.”
- The targets of CAPRI rounds 20–27 (2013, methodology): “22 The general conclusion was that, whilst the correlation to the experiment remained medi-ocre, the best procedures were those that took into account the mutation effects on stability, packing, electrostatic and solvation, and performed explicit side chain sampling and backbone relaxation.”
- SKEMPI 2.0: an updated benchmark of changes in protein–protein binding energy, kinetics and thermodynamics upon mutation (2018, methodology): “Moretti,R. et al. (2013) Community-wide evaluation of methods for predicting the effect of mutations on protein-protein interactions.”