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Publikováno v:
IOP Conference Series: Earth and Environmental Science. 240:022061
Publikováno v:
Journal of Biological Chemistry. 268:18431-18434
To analyze the mechanism by which histone H3 phosphorylation occurs specifically during mitosis, the effect of H1 on mitosis-specific H3 phosphorylation (Ser-10) was investigated in nucleosomes. H1 interaction with H1-depleted nucleosomes suppressed
Autor:
Yoshio Nishimoto, Kimiko Nishizawa, Masaki Inagaki, Takayasu Date, M Kusagawa, Akio Matsukage, R Yatani, K Ajiro, Toshiya Tokui
Publikováno v:
Journal of Biological Chemistry. 266:10820-10824
The Mr = 38,300 polypeptide of the purified recombinant rat DNA polymerase beta served as an excellent substrate for protein kinase C (PKC) in vitro but not for the catalytic subunit of cAMP-dependent protein kinase. The phosphorylation by PKC result
Publikováno v:
Journal of Biological Chemistry. 265:6494-6500
At the initial phase of cell differentiation in mouse neuroblastoma (N18) induced by dibutyrylcyclic AMP (dbcAMP), an additional site of histone H1 was extensively phosphorylated. Forskolin and various phosphodiesterase inhibitors also induced both c
Autor:
K, Ajiro
Publikováno v:
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme. 45(5)
Autor:
K, Ajiro
Publikováno v:
The Journal of biological chemistry. 275(1)
Histone phosphorylation was investigated in several mammalian cells undergoing apoptosis (human HL-60 and HeLa, mouse FM3A and N18 cells, and rat thymocytes). Among the four nucleosomal core histones (H2A, H2B, H3, and H4), H2B, which is not usually
Autor:
K, Ajiro
Publikováno v:
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme. 42(9)
Publikováno v:
The Journal of biological chemistry. 271(22)
Effects of okadaic acid (OA), a protein phosphatase inhibitor, on chromatin structure and phosphorylation of histones were examined using HeLa and N18 cells. The chromatin condensation in HeLa cells was mild and resemble prometaphase nuclei, while th
Autor:
T, Tokui, M, Inagaki, K, Nishizawa, R, Yatani, M, Kusagawa, K, Ajiro, Y, Nishimoto, T, Date, A, Matsukage
Publikováno v:
The Journal of biological chemistry. 266(17)
The Mr = 38,300 polypeptide of the purified recombinant rat DNA polymerase beta served as an excellent substrate for protein kinase C (PKC) in vitro but not for the catalytic subunit of cAMP-dependent protein kinase. The phosphorylation by PKC result