Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content
Autor: | Elena R. Mikhaylova, Irina V. Guzhova, Vladimir F. Lazarev, Diana B. Evstafyeva, Maxim Shevtsov, A. Dobrodumov, Boris A. Margulis, Alexey L. Shavarda, Alina D. Nikotina, Pavel I. Semenyuk, Vladimir I. Muronetz, Anastasia V. Tolkacheva |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
chemistry.chemical_classification Multidisciplinary biology Chemistry Rat model lcsh:Computer applications to medicine. Medical informatics Bioinformatics medicine.disease_cause Small molecule 03 medical and health sciences 030104 developmental biology Enzyme Biochemistry stomatognathic system biology.protein medicine lcsh:R858-859.7 Glycolysis lcsh:Science (General) Glyceraldehyde 3-phosphate dehydrogenase Oxidative stress Intracellular lcsh:Q1-390 Data Article |
Zdroj: | Data in Brief Data in Brief, Vol 7, Iss, Pp 524-528 (2016) |
ISSN: | 2352-3409 |
DOI: | 10.1016/j.dib.2016.02.054 |
Popis: | 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. |
Databáze: | OpenAIRE |
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