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References from Coevolutive, evolutive and stochastic information in protein-protein interactions. Local targets link to admitted publications; unresolved targets remain external evidence.
Folding simulations of a three-dimensional protein model with a nonspecific hydrophobic energy function
10.1103/physreve.64.011912 · 2001 · External reference
Non-native interactions, effective contact order, and protein folding: A mutational investigation with the energetically frustrated hydrophobic model
10.1002/prot.10166 · 2002 · External reference
Correlated mutations and residue contacts in proteins
10.1002/prot.340180402 · 1994 · External reference
10.1038/nrg3414
10.1038/nrg3414 · External reference
Co-evolution of proteins with their interaction partners
10.1006/jmbi.2000.3732 · 2000 · External reference
Similarity of phylogenetic trees as indicator of protein-protein interaction
10.1093/protein/14.9.609 · 2001 · External reference
Inferring protein interactions from phylogenetic distance matrices
10.1093/bioinformatics/btg278 · 2003 · External reference
10.1073/pnas.96.8.4285
10.1073/pnas.96.8.4285 · External reference
10.1016/s0968-0004(98)01274-2
10.1016/s0968-0004(98)01274-2 · External reference
Predicting functional linkages from gene fusions with confidence
2002 · External reference
10.1002/prot.20948
10.1002/prot.20948 · External reference
10.1002/prot.10074
10.1002/prot.10074 · External reference
Accurate prediction of protein-protein interactions from sequence alignments using a Bayesian method
10.1038/msb4100203 · 2008 · External reference
10.1073/pnas.1607570113
10.1073/pnas.1607570113 · External reference
10.1073/pnas.1606762113
10.1073/pnas.1606762113 · External reference
Improving protein-protein interaction prediction using evolutionary information from low-quality MSAs
10.1371/journal.pone.0169356 · 2017 · External reference
10.1371/journal.pcbi.1006401
10.1371/journal.pcbi.1006401 · External reference
10.1101/254789
10.1101/254789 · External reference
Direct-coupling analysis of residue coevolution captures native contacts across many protein families
10.1073/pnas.1111471108 · 2011 · External reference
PSICOV: precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments
10.1093/bioinformatics/btr638 · 2012 · External reference
10.1093/protein/gzs081
10.1093/protein/gzs081 · External reference
Assessing the utility of coevolution-based residue–residue contact predictions in a sequence- and structure-rich era
10.1073/pnas.1314045110 · 2013 · External reference
10.1371/journal.pcbi.1000633
10.1371/journal.pcbi.1000633 · External reference
10.1016/j.febslet.2008.02.017
10.1016/j.febslet.2008.02.017 · External reference
10.1177/117693430800400003
10.1177/117693430800400003 · External reference
10.7554/elife.02030
10.7554/elife.02030 · External reference
Protein-protein docking using evolutionary information
10.1007/978-1-4939-7759-8_28 · 2018 · External reference
Unresolved reference
External reference
10.1093/bioinformatics/btm604
10.1093/bioinformatics/btm604 · External reference
GRAMM-X public web server for protein–protein docking
10.1093/nar/gkl206 · 2006 · External reference