Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Dmitriy S. Blokhin"'
Autor:
Daria A. Osetrina, Aleksandra M. Kusova, Aydar G. Bikmullin, Evelina A. Klochkova, Aydar R. Yulmetov, Evgenia A. Semenova, Timur A. Mukhametzyanov, Konstantin S. Usachev, Vladimir V. Klochkov, Dmitriy S. Blokhin
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 10, p 8949 (2023)
It is known that four peptide fragments of predominant protein in human semen Semenogelin 1 (SEM1) (SEM1(86–107), SEM1(68–107), SEM1(49–107) and SEM1(45–107)) are involved in fertilization and amyloid formation processes. In this work, the st
Externí odkaz:
https://doaj.org/article/8e41e79393aa4eca85af4ab07ef22491
Autor:
Rezeda A. Ishkaeva, Ilyas S. Nizamov, Dmitriy S. Blokhin, Elizaveta A. Urakova, Vladimir V. Klochkov, Ilnar D. Nizamov, Bulat I. Gareev, Diana V. Salakhieva, Timur I. Abdullin
Publikováno v:
Molecules, Vol 26, Iss 10, p 2973 (2021)
Phosphorus species are potent modulators of physicochemical and bioactive properties of peptide compounds. O,O-diorganyl dithiophoshoric acids (DTP) form bioactive salts with nitrogen-containing biomolecules; however, their potential as a peptide mod
Externí odkaz:
https://doaj.org/article/b55695d2231549c688a9d3a3e22acb04
Publikováno v:
Biochemistry.
Autor:
Aleksandra M. Kusova, Dmitriy S. Blokhin, Daria Sanchugova, Vladimir V. Klochkov, Aydar Bikmullin
Publikováno v:
BioNanoScience. 11:182-188
SEM1(86-107) peptide is a cleavage product of semenogelin 1 (SEM1) expressed in seminal vesicles. SEM1(86-107) forms amyloid fibrils in semen increasing HIV infectivity by up to 3–5 orders of magnitude. The study of fibrillation process includes pe
Autor:
Thomas Friedrich, Gennady Yu. Laptev, Chi-Fon Chang, Nikolai N. Sluchanko, Eugene G. Maksimov, Vladimir I. Polshakov, Dmitriy S. Blokhin, Vladimir V. Klochkov, Yury B. Slonimskiy
Publikováno v:
Biomolecular NMR Assignments. 15:17-23
Photoprotection in cyanobacteria is mediated by the Orange Carotenoid Protein (OCP), a two-domain photoswitch which has multiple natural homologs of its N- and C-terminal domains. Recently, it was demonstrated that C-terminal domain homologs (CTDHs)
Autor:
I. S. Nizamov, Elizaveta A Urakova, B. I. Gareev, Timur I. Abdullin, Rezeda A. Ishkaeva, Dmitriy S. Blokhin, Ilnar D. Nizamov, Diana V. Salakhieva, Vladimir V. Klochkov
Publikováno v:
Molecules
Volume 26
Issue 10
Molecules, Vol 26, Iss 2973, p 2973 (2021)
Volume 26
Issue 10
Molecules, Vol 26, Iss 2973, p 2973 (2021)
Phosphorus species are potent modulators of physicochemical and bioactive properties of peptide compounds. O,O-diorganyl dithiophoshoric acids (DTP) form bioactive salts with nitrogen-containing biomolecules
however, their potential as a peptide
however, their potential as a peptide
Publikováno v:
MethodsX, Vol 8, Iss, Pp 101512-(2021)
The semenogelin 1 protein is secreted in the seminal vesicles. After ejaculation it is split into small peptide fragments using internal proteases. It was shown that the fragments SEM1(45-107), SEM1(49-107), SEM1(68-107) (SEM1(86-107) form amyloid fi
Autor:
Eugene G, Maksimov, Gennady Yu, Laptev, Dmitriy S, Blokhin, Vladimir V, Klochkov, Yury B, Slonimskiy, Nikolai N, Sluchanko, Thomas, Friedrich, Chi-Fon, Chang, Vladimir I, Polshakov
Publikováno v:
Biomolecular NMR assignments. 15(1)
Photoprotection in cyanobacteria is mediated by the Orange Carotenoid Protein (OCP), a two-domain photoswitch which has multiple natural homologs of its N- and C-terminal domains. Recently, it was demonstrated that C-terminal domain homologs (CTDHs)
Autor:
I. Khusainov, Albert V. Aganov, Konstantin S. Usachev, Liliya I. Nurullina, Shamil Validov, Marat Yusupov, Natalia Garaeva, Aydar Bikmullin, Dmitriy S. Blokhin, Vladimir V. Klochkov
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2019, 13 (1), pp.27-30. ⟨10.1007/s12104-018-9845-0⟩
Biomolecular NMR Assignments, Springer, 2019, 13 (1), pp.27-30. ⟨10.1007/s12104-018-9845-0⟩
Ribosome binding factor A (RbfA) is a 14.9 kDa adaptive protein of cold shock, which is important for bacterial growth at low temperatures. RbfA can bind to the free 30S ribosomal subunit and interacts with the 5'-terminal helix (helix I) of 16S rRNA
Publikováno v:
BioNanoScience. 8:423-427
Alzheimer’s disease is a fatal neurodegenerative disorder involving the abnormal accumulation and deposition of peptides (amyloid-β, Aβ) derived from the amyloid precursor protein. Various factors that cause pathology data are revealed, but, at t