Zobrazeno 1 - 10
of 748
pro vyhledávání: '"Eugene A Permyakov"'
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
Publikováno v:
Biomolecules, Vol 12, Iss 5, p 656 (2022)
Parvalbumin (PA) is a small, acidic, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily. Structural and physical properties of PA are well studied but recently two highly conserved structural motifs consisting of three amino acids each
Externí odkaz:
https://doaj.org/article/74d3bb12d0864e50a8887ace67dd5428
Autor:
Alexey S. Kazakov, Evgenia I. Deryusheva, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Victoria A. Rastrygina, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Publikováno v:
Biomolecules, Vol 12, Iss 1, p 120 (2022)
Erythropoietin (EPO) is a clinically significant four-helical cytokine, exhibiting erythropoietic, cytoprotective, immunomodulatory, and cancer-promoting activities. Despite vast knowledge on its signaling pathways and physiological effects, extracel
Externí odkaz:
https://doaj.org/article/92540717494740aabcac202bfc623a70
Publikováno v:
Biomolecules, Vol 11, Iss 11, p 1576 (2021)
The extracellular calcium-sensing receptor (CaSR) controls vital bone cell functions such as cell growth, differentiation and apoptosis. The binding of the native agonist (Ca2+) to CaSR activates the receptor, which undergoes structural changes that
Externí odkaz:
https://doaj.org/article/c7a26232e69549ffba8a8a9ce092b027
Autor:
Alisa A. Vologzhannikova, Marina P. Shevelyova, Alexey S. Kazakov, Andrey S. Sokolov, Nadezhda I. Borisova, Eugene A. Permyakov, Nikoleta Kircheva, Valya Nikolova, Todor Dudev, Sergei E. Permyakov
Publikováno v:
Biomolecules, Vol 11, Iss 8, p 1158 (2021)
Strontium salts are used for treatment of osteoporosis and bone cancer, but their impact on calcium-mediated physiological processes remains obscure. To explore Sr2+ interference with Ca2+ binding to proteins of the EF-hand family, we studied Sr2+/Ca
Externí odkaz:
https://doaj.org/article/bd844b9458e14347a9e48bc9f3e29bbd
Autor:
Alisa A. Vologzhannikova, Polina A. Khorn, Marina P. Shevelyova, Alexei S. Kazakov, Victor I. Emelyanenko, Eugene A. Permyakov, Sergei E. Permyakov
Publikováno v:
Biomolecules, Vol 11, Iss 1, p 66 (2021)
Oncomodulin (Ocm), or parvalbumin β, is an 11–12 kDa Ca2+-binding protein found inside and outside of vertebrate cells, which regulates numerous processes via poorly understood mechanisms. Ocm consists of two active Ca2+-specific domains of the EF
Externí odkaz:
https://doaj.org/article/f7cfefda04854669a8f755de7705d82a
Autor:
Eugene A. Permyakov
Publikováno v:
Biomolecules, Vol 10, Iss 9, p 1210 (2020)
α-Lactalbumin (α-LA) is a small (Mr 14,200), acidic (pI 4–5), Ca2+-binding protein. α-LA is a regulatory component of lactose synthase enzyme system functioning in the lactating mammary gland. The protein possesses a single strong Ca2+-binding s
Externí odkaz:
https://doaj.org/article/96ce4f81082b47cf816786c489751bfe
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