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37 results on '"Baranova, Ancha V."'

16. Functional implications of calcium permeability of the channel formed by pannexin 1

Author

Abeele, Fabien Vanden, Bidaux, Gabriel, Gordienko, Dmitri, Beck, Benjamin, Panchin, Yuri V., Baranova, Ancha V., Ivanov, Dmitry V., Skryma, Roman, and Prevarskaya, Natalia

Subjects
Calcium-binding proteins -- Physiological aspects, Calcium channels -- Research, Cells -- Permeability, Cells -- Research, Biological sciences
Abstract

Although human pannexins (PanX) are homologous to gap junction molecules, their physiological function in vertebrates remains poorly understood. Our results demonstrate that overexpression of PanX1 results in the formation of [Ca.sup.2+]-permeable gap junction channels between adjacent cells, thus, allowing direct intercellular [Ca.sup.2+] diffusion and facilitating intercellular [Ca.sup.2+] wave propagation. More intriguingly, our results strongly suggest that PanX1 may also form [Ca.sup.2+]-permeable channels in the endoplasmic reticulum (ER). These channels contribute to the ER [Ca.sup.2+] leak and thereby affect the ER [Ca.sup.2+] load. Because leakage remains the most enigmatic of those processes involved in intracellular calcium homeostasis, and the molecular nature of the leak channels is as yet unknown, the results of this work provide new insight into calcium signaling mechanisms. These results imply that for vertebrates, a new protein family, referred to as pannexins, may not simply duplicate the connexin function but may also provide additional pathways for intra- and intercellular calcium signaling and homeostasis.

Published
2006

20. The N-terminal domain of Aliivibrio fischeri LuxR Is a target of the GroEL chaperonin

Author

Manukhov, Ilya V., Melkina, Olga E., Goryanin, Ignatii I., Baranova, Ancha V., and Zavilgelsky, Gennadii B.

Subjects
Protein binding -- Research, Bacterial proteins -- Properties, Genetic transcription -- Research, Escherichia coli -- Physiological aspects, Escherichia coli -- Genetic aspects, Biological sciences
Abstract

Here we show that the C-terminal domain of LuxR activates the transcription of Aliivibrio fischeri luxICDABEG in Escherichia coli SKB178 [gro.sup.+] and E. coli OFBllll groEL673 strains to the same level. Using affinity chromatography, we showed that GroEL binds to the N-terminal domain of LuxR, pointing to a GroEL/GroES requirement for the folding of the N-terminal domain of LuxR. doi: 10.1128/JB.00754-10

Published
2010

21. Correction to: selected articles from Belyaev Conference 2017: structural biology

Author

Orlov, Yuriy L and Baranova, Ancha V

Subjects
Evolution, Molecular, Models, Molecular, Superoxide Dismutase-1, Protein Conformation, Amyotrophic Lateral Sclerosis, Mutation, Correction, Humans, Hydrogen Bonding, Amino Acids, Survival Analysis, Conserved Sequence, Protein Structure, Secondary
Abstract

So far, little is known about the molecular mechanisms of amyotrophic lateral sclerosis onset and progression caused by SOD1 mutations. One of the hypotheses is based on SOD1 misfolding resulting from mutations and subsequent deposition of its cytotoxic aggregates. This hypothesis is complicated by the fact that known SOD1 mutations of similar clinical effect could be distributed over the whole protein structure.In this work, a measure of hydrogen bond stability in conformational states was studied with elastic network analysis of 35 SOD1 mutants. Twenty-eight hydrogen bonds were detected in nine of 35 mutants with their stability being significantly different from that with the wild-type. These hydrogen bonds were formed by the amino acid residues known from the literature to be located in contact between SOD1 aggregates. Additionally, residues disposed between copper binding sites of both protein subunits were found from the models to form a stiff core, which can be involved in mechanical impulse transduction between these active centres.The modelling highlights that both stability of the copper binding site and stability of the dimer can play an important role in ALS progression.

Published
2018

22. Evolutionarily new sequences expressed in tumors

Author

Baranova Ancha V, Samusik Nickolai A, Dukhovlinov Ilya V, Galachyants Yuri P, Kozlov Andrei P, Polev Dmitry E, and Krukovskaya Larisa L

Subjects
Neoplasms. Tumors. Oncology. Including cancer and carcinogens, RC254-282, Infectious and parasitic diseases, RC109-216
Abstract

Abstract Background Earlier we suggested the concept of the positive evolutionary role of tumors. According to this concept, tumors provide conditions for the expression of evolutionarily new and/or sleeping genes in their cells. Thus, tumors are considered as evolutionary proving ground or reservoir of expression. To support this concept we have previously characterized in silico and experimentally a new class of human tumor-related transcribed sequences. Results In this article we describe results of further studies of previously described tumor-related sequences. The results of molecular phylogeny studies, Southern hybridization experiments and computational comparison with genomes of other species are presented. Conclusion These results suggest that these previously described tumor-related human transcripts are also relatively evolutionarily new.

Published
2006
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34. Functional implications of calcium permeability of the channel formed by pannexin 1.

Author

Vanden Abeele, Fabien, Bidaux, Gabriel, Gordienko, Dmitri, Beck, Benjamin, Panchin, Yuri, Baranova, Ancha V, Ivanov, Dimitri, Skryma, Roman, Prevarskaya, Natalia, Vanden Abeele, Fabien, Bidaux, Gabriel, Gordienko, Dmitri, Beck, Benjamin, Panchin, Yuri, Baranova, Ancha V, Ivanov, Dimitri, Skryma, Roman, and Prevarskaya, Natalia

Abstract

Although human pannexins (PanX) are homologous to gap junction molecules, their physiological function in vertebrates remains poorly understood. Our results demonstrate that overexpression of PanX1 results in the formation of Ca(2+)-permeable gap junction channels between adjacent cells, thus, allowing direct intercellular Ca(2+) diffusion and facilitating intercellular Ca(2+) wave propagation. More intriguingly, our results strongly suggest that PanX1 may also form Ca(2+)-permeable channels in the endoplasmic reticulum (ER). These channels contribute to the ER Ca(2+) leak and thereby affect the ER Ca(2+) load. Because leakage remains the most enigmatic of those processes involved in intracellular calcium homeostasis, and the molecular nature of the leak channels is as yet unknown, the results of this work provide new insight into calcium signaling mechanisms. These results imply that for vertebrates, a new protein family, referred to as pannexins, may not simply duplicate the connexin function but may also provide additional pathways for intra- and intercellular calcium signaling and homeostasis., Journal Article, Research Support, Non-U.S. Gov't, info:eu-repo/semantics/published

Published
2006

36. Evolutionarily new sequences expressed in tumors

Author

Kozlov, Andrei P, primary, Galachyants, Yuri P, additional, Dukhovlinov, Ilya V, additional, Samusik, Nickolai A, additional, Baranova, Ancha V, additional, Polev, Dmitry E, additional, and Krukovskaya, Larisa L, additional

Published
2006
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