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( Indrani Datta ),( Subrata Sau ),( Alok Kumar Sil ),( Nitai C. Mandal ) 생화학분자생물학회 2005 BMB Reports Vol.38 No.1
Under the condition of expression of λP protein at lethal level, the oriC DNA-binding activity is significantly affected in wild-type E. coli but not in the rpl mutant. In purified system, the λP protein inhibits the binding of both oriC DNA and ATP to the wild-type DnaA protein but not to the rpl DnaA protein. We conclude that the λ P protein inhibits the binding of oriC DNA and ATP to the wild-type DnaA protein, which causes the inhibition of host DNA synthesis initiation that ultimately leads to bacterial death. A possible beneficial effect of this interaction of λ P protein with E. call DNA initiator protein DnaA for phage DNA replication has been proposed.
SINGHLAXMAN,U. S. Rai,Alok Kumar Rai,K. D. Mandal,이선영 대한금속·재료학회 2013 ELECTRONIC MATERIALS LETTERS Vol.9 No.1
CaCu2.90Zn0.10Ti4O12 ceramic was synthesized by a novel semi-wet route and calcined at 800°C in air for 8 h. The obtained powder was divided into three parts and sintered in air at 950°C for 6 h, 8 h, and 12 h,separately. XRD results confirmed the single phase formation of all the sintered samples with similar cubic structure of CaCu3Ti4O12 (CCTO). Scanning electron micrographs of the CaCu2.9Zn0.1Ti4O12 ceramic sintered for 6 h shows bimodal grain size distribution. Increasing the sintering time significantly promotes the grain growth and microstructural densification. The sintering duration was found to have tremendous influence on microstructure and dielectric properties of CaCu2.90Zn0.10Ti4O12 ceramic. The CaCu2.9Zn0.1Ti4O12 ceramic sintered for 12 h exhibited high dielectric constant εr ~ 5971 at 1 kHz and room temperature. It is found that εr is independent at high frequency and weakly dependent on temperature.
Datta, Indrani,Sau, Subrata,Sil, Alok Kumar,Mandal, Mitai C. Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.1
Under the condition of expression of $\lambda$ P protein at lethal level, the oriC DNA-binding activity is significantly affected in wild-type E. coli but not in the rpl mutant. In purified system, the $\lambda$ P protein inhibits the binding of both oriC DNA and ATP to the wild-type DnaA protein but not to the rpl DnaA protein. We conclude that the $\lambda$ P protein inhibits the binding of oriC DNA and ATP to the wild-type DnaA protein, which causes the inhibition of host DNA synthesis initiation that ultimately leads to bacterial death. A possible beneficial effect of this interaction of $\lambda$ P protein with E. coli DNA initiator protein DnaA for phage DNA replication has been proposed.