Several variants of this approach exist: correcting for the underlying speciation signal has been reported to improve accuracy [ 25, 26], incorporation of phylogenetic information in addition to distance matrices has been used to aid supervised learning for prediction of protein-protein interactions [ 27] and multiple interacting partners have been included [ 28].
A plethora of potential interacting partners have been identified, particularly for the secreted form of NS1, with many being implicated in immune evasion strategies.
However, while many physiological and putative PrP interacting partners have been described (reviewed in [15]), very little is known about Dpl-interacting proteins.
Since, our understanding how NCPs interact with multiple partners has been extending from single chromatin-binding domains recognizing post-translational modifications (PTMs) in histone tails towards the recognition of higher-order chromatin structure by multi-subunit chromatin remodeling complexes.
Since several binding partners have been reported to interact with the C-terminus of FLNa molecule, these mutations may perturb their interaction as well [1], [26].
Similarly, PTB is also known to interact with mRNAs that encode proteins with a diverse range of functions and some of its binding partners have been identified.
Due to the vast size and volume of interacting partners, Titin has been studied on a modular basis.
Although we demonstrated the importance of the cytoplasmic domain of CD248, a structure that is highly conserved, with a PDZ binding motif and potential sites for phosphorylation, no intracellular interacting partners have yet been identified.
This suggests that the main selective pressure towards gene clustering could be the co-localization of the synthesis of interacting partners, as it has been previously proposed on a limited number of genomes [ 18, 52, 53].
SF-1 also interacts with Ku70, which has been identified as a binding partner of cyclin A in the centrosome [ 17].
