Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Mikhail B Shevtsov"'
Autor:
Chao-Sheng Chen, Callum Smits, Guy G Dodson, Mikhail B Shevtsov, Natalie Merlino, Paul Gollnick, Alfred A Antson
Publikováno v:
PLoS ONE, Vol 6, Iss 10, p e25296 (2011)
Many critical cellular functions are performed by multisubunit circular protein oligomers whose internal geometry has evolved to meet functional requirements. The subunit number is arguably the most critical parameter of a circular protein assembly,
Externí odkaz:
https://doaj.org/article/f7801003277d4445899bdce6414be90e
Autor:
Egor Marin, Daniil A. Kornilov, Sergey S. Bukhdruker, Vladimir A. Aleksenko, Valentin A. Manuvera, Egor V. Zinovev, Kirill V. Kovalev, Mikhail B. Shevtsov, Anna A. Talyzina, Pavel A. Bobrovsky, Pavel K. Kuzmichev, Alexey V. Mishin, Ivan Y. Gushchin, Vassili N. Lazarev, Valentin I. Borshchevskiy
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-11 (2023)
Abstract Destabilase from the medical leech Hirudo medicinalis belongs to the family of i-type lysozymes. It has two different enzymatic activities: microbial cell walls destruction (muramidase activity), and dissolution of the stabilized fibrin (iso
Externí odkaz:
https://doaj.org/article/701793d976cd4342b1095bd6c97972f6
Autor:
Pavel V. Natashin, Elena V. Eremeeva, Mikhail B. Shevtsov, Margarita I. Kovaleva, Sergey S. Bukhdruker, Daria A. Dmitrieva, Dmitry V. Gulnov, Elena V. Nemtseva, Valentin I. Gordeliy, Alexey V. Mishin, Valentin I. Borshchevskiy, Eugene S. Vysotski
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-14 (2022)
Abstract Coelenterazine-v (CTZ-v), a synthetic vinylene-bridged π-extended derivative, is able to significantly alter bioluminescence spectra of different CTZ-dependent luciferases and photoproteins by shifting them towards longer wavelengths. Howev
Externí odkaz:
https://doaj.org/article/5e569ca5c75d43e5939327cb2a853179
Autor:
Vladislav A. Lushpa, Marina V. Goncharuk, Cong Lin, Arthur O. Zalevsky, Irina A. Talyzina, Aleksandra P. Luginina, Daniil D. Vakhrameev, Mikhail B. Shevtsov, Sergey A. Goncharuk, Alexander S. Arseniev, Valentin I. Borshchevskiy, Xiaohui Wang, Konstantin S. Mineev
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Lushpa et al report the structure and dynamics of the TLR1 toll-interleukin like (TIR) cytoplasmic domain in both crystal and solution. They demonstrate that the TLR1 TIR domain is capable of specific binding of Zn with nanomolar affinity, which appe
Externí odkaz:
https://doaj.org/article/ba1903b9028f4b788d2c7b76bc761832
Autor:
Daniil Vakhrameev, Xiaohui Wang, Irina A. Talyzina, Arthur O. Zalevsky, Sergey A. Goncharuk, Mikhail B. Shevtsov, Konstantin S. Mineev, Valentin Borshchevskiy, Vladislav A. Lushpa, Alexander S. Arseniev, Marina V. Goncharuk, Aleksandra Luginina, Cong Lin
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Communications biology 4(1), 1003 (2021). doi:10.1038/s42003-021-02532-0
Communications Biology
'Communications Biology ', vol: 4, pages: 1003-1-1003-12 (2021)
Communications biology 4(1), 1003 (2021). doi:10.1038/s42003-021-02532-0
Communications Biology
'Communications Biology ', vol: 4, pages: 1003-1-1003-12 (2021)
Toll-like receptors (TLRs) play an important role in the innate immune response. While a lot is known about the structures of their extracellular parts, many questions are still left unanswered, when the structural basis of TLR activation is analyzed
Autor:
Pavel V. Natashin, Ludmila P. Burakova, Margarita I. Kovaleva, Mikhail B. Shevtsov, Daria A. Dmitrieva, Elena V. Eremeeva, Svetlana V. Markova, Alexey V. Mishin, Valentin I. Borshchevskiy, Eugene S. Vysotski
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 7; Pages: 6869
Hydromedusan photoproteins responsible for the bioluminescence of a variety of marine jellyfish and hydroids are a unique biochemical system recognized as a stable enzyme-substrate complex consisting of apoprotein and preoxygenated coelenterazine, wh
Autor:
Alexander S. Apt, R. Astashkin, Konstantin B. Majorov, Vladimir I. Dolgopalets, Aleksandra Luginina, Ivan Maslov, Natallia Strushkevich, Sviatlana Smolskaya, Valentin Gordeliy, Raisa P. Litvinovskaya, Boris Nikonenko, Andrei A. Gilep, Darrell E. Hurt, Anna Kavaleuskaya, Anton Kavaleuski, Polina Shabunya, Tatsiana Varaksa, A. V. Rogachev, Egor Marin, Alex Rosenthal, Yury Charnou, Mikhail B. Shevtsov, Anastasiia Gusach, Valentin Borshchevskiy, Evgeny Shevchenko, Alaksiej L. Hurski, Kirill Kovalev, Sergey Bukhdruker, Dmitrii Zabelskii, Alexander V. Baranovsky, Aleh Savachka, Alexey Mishin, Andrei Gabrielian, Irina Grabovec
Publikováno v:
Journal of molecular biology 433(4), 166763-(2021). doi:10.1016/j.jmb.2020.166763
Mycobacterium tuberculosis (Mtb) infection is among top ten causes of death worldwide, and the number of drug-resistant strains is increasing. The direct interception of human immune signaling molecules by Mtb remains elusive, limiting drug discovery
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f5941fde8889634dd0a0610b952e0f6
https://hdl.handle.net/2128/29692
https://hdl.handle.net/2128/29692
Autor:
Philippe Sarret, Kirill Kovalev, Alexey Mishin, Toru Maruyama, Aleksandra Luginina, Gye Won Han, Margarita Ergasheva, Egor Marin, Vadim Cherezov, Anastasiia Gusach, Anastasiia Stepko, Nilkanth Patel, Valentin Borshchevskiy, Benjamin Stauch, Élie Besserer-Offroy, Petr Popov, Andrii Ishchenko, Mikhail B. Shevtsov, Taku Fujimoto, Jean-Michel Longpré, Rebecca L. Brouillette, Daria Romanovskaia, Vsevolod Katritch, Valentin Gordeliy
Publikováno v:
Nature Communications 10, 5573 (2019). doi:10.1038/s41467-019-13348-2
Nature Communications
'Nature Communications ', vol: 10, pages: 5573-1-5573-9 (2019)
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Nature Communications
'Nature Communications ', vol: 10, pages: 5573-1-5573-9 (2019)
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Cysteinyl leukotriene G protein-coupled receptors CysLT1 and CysLT2 regulate pro-inflammatory responses associated with allergic disorders. While selective inhibition of CysLT1R has been used for treating asthma and associated diseases for over two d
Autor:
Anna Swiderska, S.J. Thresh, Mikhail B. Shevtsov, Simon Streeter, John McGeehan, Geoff Kneale
Publikováno v:
'Acta Crystallographica D ', vol: 71, pages: 398-407 (2015)
Shevtsov, M B, Streeter, S D, Thresh, S-J, Swiderska, A, Mcgeehan, J E & Kneale, G G 2015, ' Structural analysis of DNA binding by C.Csp231I, a member of a novel class of R-M controller proteins regulating gene expression ', Acta Crystallographica Section D, vol. 71, no. 2, pp. 398-407 . https://doi.org/10.1107/S139900471402690X
Acta Crystallographica Section D: Biological Crystallography
Shevtsov, M B, Streeter, S D, Thresh, S-J, Swiderska, A, Mcgeehan, J E & Kneale, G G 2015, ' Structural analysis of DNA binding by C.Csp231I, a member of a novel class of R-M controller proteins regulating gene expression ', Acta Crystallographica Section D, vol. 71, no. 2, pp. 398-407 . https://doi.org/10.1107/S139900471402690X
Acta Crystallographica Section D: Biological Crystallography
The structure of the new class of controller proteins (exemplified by C.Csp231I) in complex with its 21 bp DNA-recognition sequence is presented, and the molecular basis of sequence recognition in this class of proteins is discussed. An unusual exten
Autor:
Alexander Popov, Vadim Cherezov, Alexey Mishin, Valentin Borshchevskiy, Alexey Alekseev, Ivan Gushchin, Valentin Gordeliy, Mikhail B. Shevtsov, Vitaly Shevchenko, Vitaly Polovinkin, Igor Melnikov, Francisco Rodriguez-Valera, Gordon A. Leonard, Kirill Kovalev
Publikováno v:
Science advances 3(5), e1602952 (2017). doi:10.1126/sciadv.1602952
ResearcherID
'Science Advances ', vol: 3, pages: e1602952-1-e1602952-13 (2017)
Science Advances
ResearcherID
'Science Advances ', vol: 3, pages: e1602952-1-e1602952-13 (2017)
Science Advances
A potentially universal method for the de novo solution of the crystal structures of membrane proteins is described.
We describe a fast, easy, and potentially universal method for the de novo solution of the crystal structures of membrane protei
We describe a fast, easy, and potentially universal method for the de novo solution of the crystal structures of membrane protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d46713fb224ad6aafe5eae91174a355