V
Vladimir I. Muronetz
Researcher at Moscow State University
Publications - 179
Citations - 2699
Vladimir I. Muronetz is an academic researcher from Moscow State University. The author has contributed to research in topics: Glyceraldehyde 3-phosphate dehydrogenase & Dehydrogenase. The author has an hindex of 26, co-authored 161 publications receiving 2313 citations. Previous affiliations of Vladimir I. Muronetz include Laboratory of Molecular Biology & Institut national de la recherche agronomique.
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Journal ArticleDOI
Oxidation of glyceraldehyde-3-phosphate dehydrogenase enhances its binding to nucleic acids.
TL;DR: It is shown that the oxidation of SH-groups of the active site of GAPDH enhanced its binding with total transfer RNA or with total DNA, though NAD was much less effective than NADH in the case of oxidized GAPDh.
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Influence of Complexing Polyanions on the Thermostability of Basic Proteins
Olga N. Ivinova,Olga N. Ivinova,Vladimir A. Izumrudov,Vladimir I. Muronetz,Igor Yu. Galaev,Bo Mattiasson +5 more
TL;DR: The data obtained strongly suggest that the protein-polyelectrolyte interactions in solution, while leaving the thermostability and activity of the proteins practically unaffected over a rather wide temperature range, result in the effective denaturation of proteins once a certain critical temperature is achieved.
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Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of huntington disease
Irina V. Guzhova,Vladimir F. Lazarev,Anastasia V. Kaznacheeva,Maria V. Ippolitova,Vladimir I. Muronetz,Alexander V. Kinev,Boris A. Margulis +6 more
TL;DR: It is concluded that Hsp70 protects cells in HD by removing/sequestering two intrinsic components of protein aggregates: the polyQ itself and GAPDH, which is an important target for pharmacological treatment of HD and other polyglutamine expansion-related diseases.
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Mechanism of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase.
Kira A. Markossian,Helen A. Khanova,Sergey Yu. Kleimenov,Dmitrii I. Levitsky,Natalia A. Chebotareva,R.A. Asryants,Vladimir I. Muronetz,Luciano Saso,I. K. Yudin,Boris I. Kurganov +9 more
TL;DR: A strict correlation between thermal aggregation of GAPDH registered by the increase in the light scattering intensity and protein denaturation characterized by DSC has been proved.
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Binding Constants and Stoichiometries of Glyceraldehyde 3-Phosphate Dehydrogenase-Tubulin Complexes
TL;DR: The catalytic activity of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) decreased (almost linearly) as a function of increasing concentrations of tubulin; the total loss in activity was attained at a ratio of 1.2 to 1.8 tubulin dimer to GAPDH tetramer.