Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content
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
Affiliations
Vladimir F. Lazarev
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia; Correspondence to: Institute of Cytology of Russian Academy of Sciences, Tikhoretsky pr., 4, 194064 St. Petersburg, Russia.
Alina D. Nikotina
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia
Pavel I. Semenyuk
Belozersky Institute of Physico-Chemical Biology of Moscow State University, 119992 Moscow, Russia
Diana B. Evstafyeva
Belozersky Institute of Physico-Chemical Biology of Moscow State University, 119992 Moscow, Russia
Elena R. Mikhaylova
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia
Vladimir I. Muronetz
Belozersky Institute of Physico-Chemical Biology of Moscow State University, 119992 Moscow, Russia
Maxim A. Shevtsov
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia
Anastasia V. Tolkacheva
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia
Anatoly V. Dobrodumov
Institute of Macromolecular Compounds Russian Academy of Sciences, 199004 St. Petersburg, Russia
Alexey L. Shavarda
Komarov Botanical Institute Russian Academy of Sciences, 197376 St. Petersburg, Russia
Irina V. Guzhova
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia
Boris A. Margulis
Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia
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.
