Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Alexander I Denesyuk"'
Autor:
Anna V Lomonosova, Elena V Ovchinnikova, Alexei S Kazakov, Alexander I Denesyuk, Alexander D Sofin, Roman V Mikhailov, Andrei B Ulitin, Tajib A Mirzabekov, Eugene A Permyakov, Sergei E Permyakov
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0134906 (2015)
Due to their remarkably high structural stability, proteins from extremophiles are particularly useful in numerous biological applications. Their utility as alternative protein scaffolds could be especially valuable in small antibody mimetic engineer
Externí odkaz:
https://doaj.org/article/69dc8a9ab4a84808b4790602bfa4e9e2
Publikováno v:
Molecules, Vol 29, Iss 15, p 3451 (2024)
The superfamily of acid proteases has two catalytic aspartates for proteolysis of their peptide substrates. Here, we show a minimal structural scaffold, the structural catalytic core (SCC), which is conserved within each family of acid proteases, but
Externí odkaz:
https://doaj.org/article/b3fce8cb48fe43c9bc9fd0860cbdfa5c
Autor:
Konstantin Denessiouk, Alexander I. Denesyuk, Sergei E. Permyakov, Eugene A. Permyakov, Mark S. Johnson, Vladimir N. Uversky
Publikováno v:
Current Research in Structural Biology, Vol 7, Iss , Pp 100123- (2024)
SGNH hydrolase-like fold proteins are serine proteases with the default Asp-His-Ser catalytic triad. Here, we show that these proteins share two unique conserved structural organizations around the active site: (1) the Nuc-Oxy Zone around the catalyt
Externí odkaz:
https://doaj.org/article/1098fa70563b46f4be0235157daee249
Autor:
Alexander I. Denesyuk, Sergei E. Permyakov, Mark S. Johnson, Konstantin Denessiouk, Eugene A. Permyakov
Publikováno v:
Biomolecules, Vol 10, Iss 4, p 588 (2020)
We introduce five new local metal cation (first of all, Ca2+) recognition units in proteins: Clampn,(n−2), Clampn,(n−1), Clampn,n, Clampn,(n+1) and Clampn,(n+2). In these units, the backbone oxygen atom of a residue in position “n” of an amin
Externí odkaz:
https://doaj.org/article/a060c782615942bfaaaf8340e7a76e3f
Autor:
Alexander I. Denesyuk, Sergei E. Permyakov, Eugene A. Permyakov, Mark S. Johnson, Konstantin Denessiouk, Vladimir N. Uversky
Publikováno v:
Journal of biomolecular structuredynamics.
Intracellular calcium sensor protein calmodulin (CaM) belongs to the large EF-hand protein superfamily. CaM shows a unique and not fully understood ability to bind to multiple targets, allows them to participate in a variety of regulatory processes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c90d5b39903053a8dc4bc212c7022862
https://pubmed.ncbi.nlm.nih.gov/36106955
https://pubmed.ncbi.nlm.nih.gov/36106955
Autor:
Sergey E. Permyakov, Alisa S. Vologzhannikova, Ekaterina L. Nemashkalova, Alexei S. Kazakov, Alexander I. Denesyuk, Konstantin Denessiouk, Viktoriia E. Baksheeva, Andrey A. Zamyatnin, Evgeni Yu. Zernii, Vladimir N. Uversky, Eugene A. Permyakov
Publikováno v:
Molecules, Vol 24, Iss 13, p 2494 (2019)
Recently, we have found that calcium binding proteins of the EF-hand superfamily (i.e., a large family of proteins containing helix-loop-helix calcium binding motif or EF-hand) contain two types of conserved clusters called cluster I (‘black’ clu
Externí odkaz:
https://doaj.org/article/aebbd46b5c74438f8292075676a5a1c4
Autor:
Sergei E. Permyakov, Vladimir N. Uversky, Alexander I. Denesyuk, Konstantin Denessiouk, Mark S. Johnson, Eugene A. Permyakov
Publikováno v:
International Journal of Biological Macromolecules
There are several families of cysteine proteinases with different folds – for example the (chymo)trypsin fold family and papain-like fold family – but in both families the hydrolase activity of cysteine proteinases requires a cysteine residue as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::242f83aeb62d2bc1a9f0af2a344a9798
https://doi.org/10.1016/j.ijbiomac.2020.10.022
https://doi.org/10.1016/j.ijbiomac.2020.10.022
Autor:
Outi M. H. Salo-Ahen, Vladimir N. Uversky, Konstantin Denessiouk, Mark S. Johnson, Alexander I. Denesyuk
Publikováno v:
International Journal of Biological Macromolecules
(Chymo)trypsin-like serine fold proteases belong to the serine/cysteine proteases found in eukaryotes, prokaryotes, and viruses. Their catalytic activity is carried out using a triad of amino acids, a nucleophile, a base, and an acid. For this superf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed0888fdf85d1dbe93cab4d2a870b18c
https://doi.org/10.1016/j.ijbiomac.2020.03.025
https://doi.org/10.1016/j.ijbiomac.2020.03.025
Autor:
Konstantin Denessiouk, Sergei E. Permyakov, Vladimir N. Uversky, Eugene A. Permyakov, Alexander I. Denesyuk, Mark S. Johnson
Publikováno v:
International Journal of Biological Macromolecules
Three dimensional structures of (chymo)trypsin-like proteinase (3CLpro) from SARS-CoV-2 and SARS-CoV differ at 8 positions. We previously found that the Val86Leu, Lys88Arg, Phe134His, and Asn180Lys mutations in these enzymes can change the orientatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83e7194b9c1197c925adc76b3b80b953
http://europepmc.org/articles/PMC8580570
http://europepmc.org/articles/PMC8580570
Autor:
Eugene A. Permyakov, Sergei E. Permyakov, Mark S. Johnson, Konstantin Denessiouk, Vladimir N. Uversky, Alexander I. Denesyuk
Publikováno v:
International journal of biological macromolecules. 179
Proteinases with the (chymo)trypsin-like serine/cysteine fold comprise a large superfamily performing their function through the Acid – Base – Nucleophile catalytic triad. In our previous work (Denesyuk AI, Johnson MS, Salo-Ahen OMH, Uversky VN,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ebbed71ef2ad8f6b6479848eb811fa4
https://pubmed.ncbi.nlm.nih.gov/33713772
https://pubmed.ncbi.nlm.nih.gov/33713772