Aberrations in redox potential are associated with cancerous phenotypes, resulting in a resistance towards chemotherapeutic drugs. Reactive oxygen species (ROS) such as hydrogen peroxide and superoxide are generated by ligation events across a diverse range of receptor families; redox couples provide a means of translating the presence of ROS into useful signals in the cell. Thioredoxin and glutathione-mediated post-translational modifications of proteins (thiolation and glutathionylation, respectively) have been shown to functionally alter the activity of certain proteins. However, few proteins have been investigated in depth to understand this relationship. More broadly, an in-depth quantitative analysis of how redox-related effects systemically influence the regulation of a receptor signaling pathway has never been undertaken. Challenges in quantifying post-translational events and discerning the effects of one redox couple from another have compounded the difficulties in understanding the role of redox-potential in cellular signaling, mandating a modeling-based approach for gaining insight into these biological processes.