doi: 10.1016/j.expneurol.2007.11.016
Here we determined the rate constants for the individual redox reactions between the two redox-sensitive cysteinyl residues of roGFP2 and the active-site cysteinyl residues of the model class I glutaredoxin PfGrx from the malaria parasite Plasmodium falciparum using stopped-flow kinetic measurements in combination with redox mobility shift assays
Impurities, such as bacterial endotoxins, can provoke inflammatory responses that may skew experimental results
We can change the conformation and function of mutant p53 via pharmacological intervention in specific posttranslational modification pathways
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