Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Dmitry A. Suplatov"'
Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.
Autor:
Ekaterina Yu Bezsudnova, Alena Yu Nikolaeva, Alina K Bakunova, Tatiana V Rakitina, Dmitry A Suplatov, Vladimir O Popov, Konstantin M Boyko
Publikováno v:
PLoS ONE, Vol 16, Iss 7, p e0255098 (2021)
Creating biocatalysts for (R)-selective amination effectively is highly desirable in organic synthesis. Despite noticeable progress in the engineering of (R)-amine activity in pyridoxal-5'-phosphate-dependent transaminases of fold type IV, the specia
Externí odkaz:
https://doaj.org/article/8d9e7e54227c47c895f595f8bffbc68c
Publikováno v:
Bioinformatics. 38:985-989
Motivation With the increasing availability of 3D-data, the focus of comparative bioinformatic analysis is shifting from protein sequence alignments toward more content-rich 3D-alignments. This raises the need for new ways to improve the accuracy of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7803c7c18001a79f18b83628eb658374
https://doi.org/10.1093/bioinformatics/btab798
https://doi.org/10.1093/bioinformatics/btab798
Autor:
Vladimir V. Voevodin, Ivan Timokhin, Yana A. Sharapova, Dmitry A. Suplatov, Nina Popova, Maksim V. Shegay, Vytas K. Švedas
Publikováno v:
The Journal of Supercomputing. 77:12382-12398
The field of biology is producing data faster than ever before. To approach its analysis efficiently, one can take advantage of a systematic symbiosis between the power of huge distributed-memory systems and the flexibility of locally managed shared-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::381ca5954842b18ea12085113d3df782
https://doi.org/10.1007/s11227-021-03691-x
https://doi.org/10.1007/s11227-021-03691-x
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 1302-1311 (2021)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal
Graphical abstract
Local 3D-structural differences in homologous proteins contribute to functional diversity observed in a superfamily, but so far received little attention as bioinformatic analysis was usually carried out at the level of amino
Local 3D-structural differences in homologous proteins contribute to functional diversity observed in a superfamily, but so far received little attention as bioinformatic analysis was usually carried out at the level of amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44a82cf2b81c2a1335bd8f8bba128bd6
http://www.sciencedirect.com/science/article/pii/S2001037021000568
http://www.sciencedirect.com/science/article/pii/S2001037021000568
Publikováno v:
Journal of Chemical Information and Modeling. 60:3692-3696
The ability of ligands to form crucial interactions with a protein target, characteristic for the substrate and/or inhibitors, could be considered a structural criterion for identifying potent binders among docked compounds. Structural filtration of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f311a8890e5d62528b0ab600386118e8
https://doi.org/10.1021/acs.jcim.0c00303
https://doi.org/10.1021/acs.jcim.0c00303
Publikováno v:
Nucleic Acids Research
Zebra2 is a highly automated web-tool to search for subfamily-specific and conserved positions (i.e. the determinants of functional diversity as well as the key catalytic and structural residues) in protein superfamilies. The bioinformatic analysis i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9403a2a9af5e09d4dc1bd0102230746
http://europepmc.org/articles/PMC7319439
http://europepmc.org/articles/PMC7319439
Autor:
Ekaterina Yu. Bezsudnova, Konstantin M. Boyko, Alena Yu. Nikolaeva, Yulia S. Zeifman, Tatiana V. Rakitina, Dmitry A. Suplatov, Vladimir O. Popov
Publikováno v:
Biochimie. 158:130-138
The high catalytic efficiency of enzymes under reaction conditions is one of the main goals in biocatalysis. Despite the dramatic progress in the development of more efficient biocatalysts by protein design, the search for natural enzymes with useful
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bac9590d135a5c671f214a060c0da508
https://doi.org/10.1016/j.biochi.2018.12.017
https://doi.org/10.1016/j.biochi.2018.12.017
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 37:2049-2060
Doramapimod (BIRB-796) is widely recognized as one of the most potent and selective type II inhibitors of human p38α mitogen-activated protein kinase (MAPK); however, the understanding of its binding mechanism remains incomplete. Previous studies in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fce31d4433e190f612678d4a05ae7ad
https://doi.org/10.1080/07391102.2018.1475260
https://doi.org/10.1080/07391102.2018.1475260
Autor:
Garri Manasaryan, D. K. Nilov, Vytas K. Švedas, Sergey Pushkarev, A. N. Kuimov, Dmitry A. Suplatov, Viktor Drobot
Publikováno v:
Cancers, Vol 13, Iss 1201, p 1201 (2021)
Cancers
Volume 13
Issue 6
Cancers
Volume 13
Issue 6
Simple Summary The PARP family consists of 17 proteins, and some of them are responsible for cancer cells’ viability. Much attention is therefore given to the search for chemical compounds with the ability to suppress distinct PARP family members (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df21e4be9bed3b8c32c3a715197a0148
https://www.mdpi.com/2072-6694/13/6/1201
https://www.mdpi.com/2072-6694/13/6/1201
Publikováno v:
Methods in Molecular Biology ISBN: 9781071610350
Bioinformatic analysis of functionally diverse superfamilies can help to study the structure-function relationship in proteins, but represents a methodological challenge. The Mustguseal web-server can build large structure-guided sequence alignments
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56175bc65a2b5f6c574b4ff144a5385f
https://doi.org/10.1007/978-1-0716-1036-7_12
https://doi.org/10.1007/978-1-0716-1036-7_12
