Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ekaterina M, Sogorina"'
Autor:
Irina A, Eliseeva, Ekaterina M, Sogorina, Egor A, Smolin, Ivan V, Kulakovskiy, Dmitry N, Lyabin
Publikováno v:
Biochemistry (Moscow). 87:S48-S70
YB proteins are DNA/RNA binding proteins, members of the family of proteins with cold shock domain. Role of YB proteins in the life of cells, tissues, and whole organisms is extremely important. They are involved in transcription regulation, pre-mRNA
Autor:
Daria Mordovkina, Dmitry N. Lyabin, Egor A. Smolin, Ekaterina M. Sogorina, Lev P. Ovchinnikov, Irina Eliseeva
Publikováno v:
Biomolecules, Vol 10, Iss 4, p 591 (2020)
Y-box binding proteins (YB proteins) are DNA/RNA-binding proteins belonging to a large family of proteins with the cold shock domain. Functionally, these proteins are known to be the most diverse, although the literature hardly offers any molecular m
Externí odkaz:
https://doaj.org/article/307e504e3b15478e8655c5518aaabfa8
Autor:
Ekaterina M. Sogorina, Ekaterina R. Kim, Alexey V. Sorokin, Dmitry N. Lyabin, Lev P. Ovchinnikov, Daria A. Mordovkina, Irina A. Eliseeva
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences; Volume 23; Issue 1; Pages: 428
International Journal of Molecular Sciences, Vol 23, Iss 428, p 428 (2022)
International Journal of Molecular Sciences; Volume 23; Issue 1; Pages: 428
International Journal of Molecular Sciences, Vol 23, Iss 428, p 428 (2022)
YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress
Autor:
Lev P. Ovchinnikov, Daria A. Mordovkina, Egor A. Smolin, Dmitry N. Lyabin, Irina A. Eliseeva, Ekaterina M Sogorina
Publikováno v:
Biomolecules
Biomolecules, Vol 10, Iss 591, p 591 (2020)
Biomolecules, Vol 10, Iss 591, p 591 (2020)
Y-box binding proteins (YB proteins) are DNA/RNA-binding proteins belonging to a large family of proteins with the cold shock domain. Functionally, these proteins are known to be the most diverse, although the literature hardly offers any molecular m