Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Vitaly Polovinkin"'
Autor:
Dmitrii Zabelskii, Natalia Dmitrieva, Oleksandr Volkov, Vitaly Shevchenko, Kirill Kovalev, Taras Balandin, Dmytro Soloviov, Roman Astashkin, Egor Zinovev, Alexey Alekseev, Ekaterina Round, Vitaly Polovinkin, Igor Chizhov, Andrey Rogachev, Ivan Okhrimenko, Valentin Borshchevskiy, Vladimir Chupin, Georg Büldt, Natalia Yutin, Ernst Bamberg, Eugene Koonin, Valentin Gordeliy
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Zabelskii et al. present a structural and functional analysis of the lightdriven proton pump LR (Mac) from the fungus Leptosphaeria maculans. Their findings indicate that the archaeal ancestry of eukaryotic type 1 rhodopsins, and that the archaeal ho
Externí odkaz:
https://doaj.org/article/ffd8f8139a3d4a9c8b6afe6dc044007f
Autor:
Dmitry Bratanov, Kirill Kovalev, Jan-Philipp Machtens, Roman Astashkin, Igor Chizhov, Dmytro Soloviov, Dmytro Volkov, Vitaly Polovinkin, Dmitrii Zabelskii, Thomas Mager, Ivan Gushchin, Tatyana Rokitskaya, Yuri Antonenko, Alexey Alekseev, Vitaly Shevchenko, Natalya Yutin, Riccardo Rosselli, Christian Baeken, Valentin Borshchevskiy, Gleb Bourenkov, Alexander Popov, Taras Balandin, Georg Büldt, Dietmar J. Manstein, Francisco Rodriguez-Valera, Christoph Fahlke, Ernst Bamberg, Eugene Koonin, Valentin Gordeliy
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Rhodopsin genes have been identified in some large double-stranded DNA viruses, but the structure and functions of viral rhodopsins remain unknown. Here authors present crystal structure and characterization of an Organic Lake Phycodnavirus rhodopsin
Externí odkaz:
https://doaj.org/article/20ce96168fbe41fdba6908ad7848aa9e
Autor:
Krishna P. Khakurel, Shirly Espinoza, Martin Savko, Vitaly Polovinkin, Jan Dohnalek, William Shepard, Angelina Angelova, Janos Hajdu, Jakob Andreasson, Borislav Angelov
Publikováno v:
Crystals, Vol 10, Iss 12, p 1146 (2020)
Time-resolved in-house macromolecular crystallography is primarily limited by the capabilities of the in-house X-ray sources. These sources can only provide a time-averaged structure of the macromolecules. A significant effort has been made in the de
Externí odkaz:
https://doaj.org/article/72eb84e2a21545119f84dfd322e38a4a
Autor:
Egor Marin, Aleksandra Luginina, Anastasiia Gusach, Kirill Kovalev, Sergey Bukhdruker, Polina Khorn, Vitaly Polovinkin, Elizaveta Lyapina, Andrey Rogachev, Valentin Gordeliy, Alexey Mishin, Vadim Cherezov, Valentin Borshchevskiy
Publikováno v:
Scientific Data, Vol 7, Iss 1, Pp 1-1 (2020)
A Correction to this paper has been published: https://doi.org/10.1038/s41597-020-00759-w
Externí odkaz:
https://doaj.org/article/2cc6e5f2b9104fa693fb6ef368ca0642
Autor:
Ivan Gushchin, Philipp Orekhov, Igor Melnikov, Vitaly Polovinkin, Anastasia Yuzhakova, Valentin Gordeliy
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 9, p 3110 (2020)
Membrane-embedded sensor histidine kinases (HKs) and chemoreceptors are used ubiquitously by bacteria and archaea to percept the environment, and are often crucial for their survival and pathogenicity. The proteins can transmit the signal from the se
Externí odkaz:
https://doaj.org/article/bff2b31de11c4e2bb4ed151e945611e7
Publikováno v:
Crystals, Vol 10, Iss 3, p 149 (2020)
Two-component signaling systems (TCSs) are a large and important class of sensory systems in bacteria, archaea, and some eukaryotes, yet their mechanism of action is still not fully understood from the structural point of view. Many TCS receptors are
Externí odkaz:
https://doaj.org/article/7c847446b637418ba1900fedc9c7663d
Autor:
Dmitry Bratanov, Taras Balandin, Ekaterina Round, Vitaly Shevchenko, Ivan Gushchin, Vitaly Polovinkin, Valentin Borshchevskiy, Valentin Gordeliy
Publikováno v:
PLoS ONE, Vol 10, Iss 6, p e0128390 (2015)
Heterologous overexpression of functional membrane proteins is a major bottleneck of structural biology. Bacteriorhodopsin from Halobium salinarum (bR) is a striking example of the difficulties in membrane protein overexpression. We suggest a general
Externí odkaz:
https://doaj.org/article/8e322458e268483fa2d3b018ad8164b1
Autor:
Valentin Borshchevskiy, Ekaterina Round, Yulia Bertsova, Vitaly Polovinkin, Ivan Gushchin, Andrii Ishchenko, Kirill Kovalev, Alexey Mishin, Galina Kachalova, Alexander Popov, Alexander Bogachev, Valentin Gordeliy
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0118548 (2015)
Na+-translocating NADH:quinone oxidoreductase (NQR) is a redox-driven sodium pump operating in the respiratory chain of various bacteria, including pathogenic species. The enzyme has a unique set of redox active prosthetic groups, which includes two
Externí odkaz:
https://doaj.org/article/f352ddcc21aa4a39b3d46f7f3ac5c67b
Autor:
Vitaly Shevchenko, Ivan Gushchin, Vitaly Polovinkin, Ekaterina Round, Valentin Borshchevskiy, Petr Utrobin, Alexander Popov, Taras Balandin, Georg Büldt, Valentin Gordeliy
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e112873 (2014)
Bacteriorhodopsins are a large family of seven-helical transmembrane proteins that function as light-driven proton pumps. Here, we present the crystal structure of a new member of the family, Haloarcula marismortui bacteriorhodopsin I (HmBRI) D94N mu
Externí odkaz:
https://doaj.org/article/94b754aa625b4cd29d657acb08d19290
Autor:
Borislav Angelov, Vitaly Polovinkin, William Shepard, Shirly Espinoza, Janos Hajdu, Jan Dohnálek, Krishna P. Khakurel, Angelina Angelova, Martin Savko, Jakob Andreasson
Publikováno v:
Crystals
Crystals, MDPI, 2020, 10 (12), pp.1146. ⟨10.3390/cryst10121146⟩
Crystals, Vol 10, Iss 1146, p 1146 (2020)
Volume 10
Issue 12
Crystals, MDPI, 2020, 10 (12), pp.1146. ⟨10.3390/cryst10121146⟩
Crystals, Vol 10, Iss 1146, p 1146 (2020)
Volume 10
Issue 12
International audience; Time-resolved in-house macromolecular crystallography is primarily limited by the capabilities of the in-house X-ray sources. These sources can only provide a time-averaged structure of the macromolecules. A significant effort
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb8ee986e05f9ba567c9d48c4f5a3e2a
https://hal.archives-ouvertes.fr/hal-03093546
https://hal.archives-ouvertes.fr/hal-03093546