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Abstract:
Thanks to rule-based modelling languages, we can assemble
large sets of mechanistic protein-protein interactions within
integrated models. Our goal would be to understand how the behaviour
of these systems emerges from these low-level interactions. Yet this
is a quite long term challenge and it is desirable to offer intermediary levels of abstraction, so as to get a better
understanding of the models and to increase our confidence within our mechanistic assumptions.
In this paper, we propose an abstract interpretation of the behaviour of each protein, in isolation.
Given a model written in Kappa, this abstraction computes for each kind of protein a transition system that describes which conformations this protein can take and how a protein can pass from one conformation to another one. Then, we use simplicial complexes to abstract away the interleaving order of the transformations between conformations that commute. As a result, we get a compact summary of the potential behaviour of each protein of the model.
@InProceedings{feret:CMSB2016, title = "Local traces: an over-approximation of the behaviour of the proteins in rule-based models", booktitle = "Fourteenth Conference on Computational Method in Systems Biology (CMSB'16)", series = "LNCS/LNBI", volume = "9859" publisher = "Springer", year = "2016", editor = "E. Bartocci and P. Lio', and N Paoletti", author = "J{\'e}r{\^o}me Feret and Kim Quy{\^e}n L{\'y}"}