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- W4387314907 abstract "Cells are susceptible of oxidative stress and have intracellular signaling pathways able to sense it and activate an appropriate response. In between these, we identified Thioredoxin (TRX), a major antioxidant protein, and its endogenous inhibitor TXNIP. TXNIP bonds TRX by means of a disulfide bridge that saturates its active site. Such an interaction is redox-dependent as ROS can dissociate it resulting in a Thiol-Disulfide Interchange Reaction. Following a growing interest in finding subcellular targets and mechanisms linked to a possible cytoprotective effect of electromagnetic (EM) fields, we studied the influence of electric field over this system through a hybrid QM/MM approach. Results show a strong catalytic effect of the static electric field over the TRX-TXNIP complex dissociation reaction and a consistent products’ stabilization. A preliminary study on nanopulses also shows the effect to be significant in the transient period, making time a relevant variable only if the field amplitude is increased. These results are promising for a further characterization of this interaction mechanism, which could be the way (or one of many) in which EM fields might directly influence intracellular signaling pathways." @default.
- W4387314907 created "2023-10-04" @default.
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- W4387314907 date "2023-08-19" @default.
- W4387314907 modified "2023-10-16" @default.
- W4387314907 title "Electric Field Effect on Protein Dissociation: a Computational Evaluation of the Energy Barrier over Thiol-Disulfide Interchange Reaction in TRX-TXNIP Complex as an Interaction Model for Biological Antioxidant Response" @default.
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- W4387314907 doi "https://doi.org/10.23919/ursigass57860.2023.10265479" @default.
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