Zobrazeno 1 - 10
of 174
pro vyhledávání: '"Eugene A Permyakov"'
Autor:
Anna V Lomonosova, Andrei B Ulitin, Alexei S Kazakov, Tajib A Mirzabekov, Eugene A Permyakov, Sergei E Permyakov
Publikováno v:
PLoS ONE, Vol 12, Iss 1, p e0170349 (2017)
Small antibody mimetics, or alternative binding proteins (ABPs), extend and complement antibody functionality with numerous applications in research, diagnostics and therapeutics. Given the superiority of ABPs, the last two decades have witnessed dev
Externí odkaz:
https://doaj.org/article/b2cb9c993d7741e0838077d0271c1463
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
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:
Alexey S. Kazakov, Evgenia I. Deryusheva, Victoria A. Rastrygina, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Publikováno v:
Biomolecules, Vol 13, Iss 9, p 1345 (2023)
S100 is a family of over 20 structurally homologous, but functionally diverse regulatory (calcium/zinc)-binding proteins of vertebrates. The involvement of S100 proteins in numerous vital (patho)physiological processes is mediated by their interactio
Externí odkaz:
https://doaj.org/article/dfaff76adb454f5a9fb997fcb3c02783
Autor:
Alisa A. Vologzhannikova, Victor I. Emelyanenko, Alexey S. Kazakov, Nadezhda I. Borisova, Eugene A. Permyakov
Publikováno v:
Protein & Peptide Letters. 30:108-115
Background: Small Ca2+-binding protein parvalbumin possesses two strong Ca2+/Mg2+- binding sites located within two EF-hand domains. Most parvalbumins have no tryptophan residues, while cod protein contains a single tryptophan residue, which fluoresc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4914dd87ece79bf59da438cca585edc7
https://doi.org/10.2174/0929866530666230109123224
https://doi.org/10.2174/0929866530666230109123224
Autor:
Alexey S. Kazakov, Marina Y. Zemskova, Gleb K. Rystsov, Alisa A. Vologzhannikova, Evgenia I. Deryusheva, Victoria A. Rastrygina, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 24; Pages: 15956
Tumor necrosis factor (TNF) inhibitors (anti-TNFs) represent a cornerstone of the treatment of various immune-mediated inflammatory diseases and are among the most commercially successful therapeutic agents. Knowledge of TNF binding partners is criti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9234c2b9075f8e441d5382a9bc5ba0b0
Autor:
Alexey S. Kazakov, Marina Y. Zemskova, Gleb K. Rystsov, Alisa A. Vologzhannikova, Evgenia I. Deryusheva, Victoria A. Rastrygina, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Tumor necrosis factor (TNF) inhibitors (anti-TNFs) represent a cornerstone of the treatment of various immune-mediated inflammatory diseases and are among the most commercially successful therapeutic agents. Knowledge of TNF binding partners is criti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29a7ddc574a054bb2d57d1b2bf00a122
Autor:
Alexey S. Kazakov, Evgenia I. Deryusheva, Maria E. Permyakova, Andrey S. Sokolov, Victoria A. Rastrygina, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 19; Pages: 12000
S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0805c57d948c74b4a2218c07929514dd
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:
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