The proposals in our study, albeit motivated by excellent theoretical considerations, are currently speculative. This is an important limitation of our study; one that we hope will be addressed by epidemiological studies in the future. The technique we present can potentially aid in easing some of the complexity of personal therapy design. We stress, however, that therapy design is a complex process that involves multiple considerations. In other words, oxidative NDMC101 stress profiling can only be one of the tools �C however crucial �C in the clinician��s repertoire. It would be interesting to study further nuances of our technique; such as how might factors like duration of the disease IR or ER stress be incorporated into the analysis. Another aspect is accounting for antioxidant capacity being influenced by factors Clonixin unrelated to diabetes, co-existing infections for example. Finally, we note that oxidative stress is related not only to glucose but also several other molecules that are linked to diabetes, lipids for instance. While we have not found a significant variation of GSH with BMI in this study, in principle such dependence could exist, perhaps in other population groups. Future research will determine the extent to which the current method will be found effective, and what modifications will follow. Nevertheless, our method of oxidative stress profiling is readily amenable to clinical practice in its current form. Based on sequence homology, eight Shaker-related subfamilies of voltage-gated potassium channels have been identified: Kv1- Kv6 and Kv8-Kv9. Each a-subunit consists of six transmembrane segments and cytoplasmic N- and C-termini. Four a-subunits assemble into a Kv channel in which S5-S6 form the K + selective pore while S1-S4 constitute the voltage sensing domain. Members of the Kv1-Kv4 subfamilies form electrically functional channels at the plasma membrane in both homo- and heterotetrameric configurations within each subfamily.This subfamily-specific channel assembly is controlled by the N-terminal tetramerization domain T1 that facilitates the assembly of compatible a-subunits into possible homo- and heterotetrameric channels and prevents subunits belonging to different subfamilies from assembling.