Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content

Publication date: June 2016
Source:Data in Brief, Volume 7
Author(s): Vladimir F. Lazarev, Alina D. Nikotina, Pavel I. Semenyuk, Diana B. Evstafyeva, Elena R. Mikhaylova, Vladimir I. Muronetz, Maxim A. Shevtsov, Anastasia V. Tolkacheva, Anatoly V. Dobrodumov, Alexey L. Shavarda, Irina V. Guzhova, Boris A. Margulis
This data is related to our paper "Small molecules preventing GAPDH aggregation are therapeutically applicable in cell and rat models of oxidative stress" (Lazarev et al. [1]) where we explore therapeutic properties of small molecules preventing GAPDH aggregation in cell and rat models of oxidative stress. The present article demonstrates a few of additional properties of the chemicals shown to block GAPDH aggregation such as calculated site for targeting the enzyme, effects on GAPDH glycolytic activity, influence on GAPDH intracellular level and anti-aggregate activity of pure polyglutamine exemplifying a denatured protein.



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