Zobrazeno 1 - 7
of 7
pro vyhledávání: '"O O, Gnedina"'
Publikováno v:
Cell and Tissue Biology. 16:547-554
Autor:
O. O. Gnedina, M. V. Igotti
Publikováno v:
Cell and Tissue Biology. 15:236-247
To establish the mechanisms of transformed cells resistance to the histone deacetylase inhibitors (HDACi), we compared the changes of the main proliferative signaling cascades activities in cells that are sensitive or resistant to HDACi-induced apopt
Publikováno v:
Cell and Tissue Biology. 11:42-50
Histone deacetylase inhibitors (HDIs) cause an irreversible cell cycle arrest in G1 phase and senescence of E1A + Ras transformed fibroblasts. The modulation of the antiproliferative action of the RNA synthesis inhibitor actinomycin D (AMD) with sodi
Publikováno v:
Tsitologiia. 58(10)
In the present article we have studied the combined effect of actinomycin D (AMD) with HDI sodium butyrate (NaBut) on proliferation of transformed cells. It has been shown that NaBut increased the cytotoxic effect of low concentrations of AMD (8 nM).
Publikováno v:
Cell and Tissue Biology. 9:348-355
Histone deacetylase inhibitors (HDIs) cause irreversible cell cycle arrest and senescence of transformed E1A + Ras cells. The HDI sodium butyrate (NaB) causes a violation of DNA repair and, as a consequence, phosphorylation of DNA breaks marker histo
Autor:
E. A. Filippova, O. O. Gnedina, A.K. Pojidaeva, Valery A. Pospelov, S. B. Svetlikova, M.V. Igotti Abramova
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 51:102-110
HDAC inhibitors (HDIs) induce irreversible cell cycle arrest and senescence in E1A+Ras expressing cells. Furthermore, HDIs activate Gadd45α/NF-κB signaling pathway to suppress apoptosis thereby promoting the cell survival. Here, to clarify the role
Publikováno v:
Tsitologiia. 57(4)
Histone deacetylase inhibitors (HDIs) causes irreversible cell cycle arrest and senescence of E1A+Ras transformed cells. HDI sodium butyrate (NaB) affects the DNA repair and consequently modulates the phosphorylation of DNA breaks marker histone H2AX