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RISS 인기검색어
- 검색키워드
- 저자 : (Takeshi Tokuhisa) (검색결과 3 건)
- 무료
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- 유료
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Gao, Shuyan,Koshizaki, Naoto,Tokuhisa, Hideo,Koyama, Emiko,Sasaki, Takeshi,Kim, Jae-Kwan,Ryu, Joonghyun,Kim, Deok-Soo,Shimizu, Yoshiki WILEY-VCH Verlag 2010 Advanced Functional Materials Vol.20 No.1
<P>Colloidal Au-amplified surface plasmon resonance (SPR), like traditional SPR, is typically used to detect binding events on a thin noble metal film. The two major concerns in developing colloidal Au-amplified SPR lie in 1) the instability, manifested as a change in morphology following immersion in organic solvents and aqueous solutions, and 2) the uncontrollable interparticle distance, determining probe spacing and inducing steric hindrance between neighboring probe molecules. This may introduce uncertainties into such detecting techniques, degrade the sensitivity, and become the barricade hampering colloidal Au-based transducers from applications in sensing. In this paper, colloidal Au-amplified SPR transducers are produced by using ultrathin Au/Al<SUB>2</SUB>O<SUB>3</SUB> nanocomposite films via a radio frequency magnetron co-sputtering method. Deposited Au/Al<SUB>2</SUB>O<SUB>3</SUB> nanocomposite films exhibit superior stability, and average interparticle distances between Au nanoparticles with similar average sizes can be tuned by changing surface coverage. These characteristics are ascribed to the spacer function and rim confinement of dielectric Al<SUB>2</SUB>O<SUB>3</SUB> and highlight their advantages for application in optimal nanoparticle-amplified SPR, especially when the probe size is smaller than the target molecule size. This importance is demonstrated here for the binding of protein (streptavidin) targets to the probe (biotin) surface. In this case, the dielectric matrix Al<SUB>2</SUB>O<SUB>3</SUB> is a main contributor, behaving as a spacer, tuning the concentration of Au nanoparticles, and manipulating the average interparticle distance, and thus guaranteeing an appropriate number of biotin molecules and expected near-field coupling to obtain optimal sensing performance.</P> <B>Graphic Abstract</B> <P>An innovative colloidal Au-amplified surface plasmon resonance (SPR) transducer is achieved by a using remarkably stable and space-tunable Au/Al<SUB>2</SUB>O<SUB>3</SUB> nanocomposite film. This study indicates that the Au/Al<SUB>2</SUB>O<SUB>3</SUB> nanocomposite film is very promising; it simultaneously overcomes the instability and uncontrollable interparticle distance, which are the current bottlenecks hampering the application of SPR sensors. <img src='wiley_img/1616301X-2010-20-1-ADFM200901232-content.gif' alt='wiley_img/1616301X-2010-20-1-ADFM200901232-content'> </P>
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Downregulation of bcl - xL Is Relevant to UV - induced Apoptosis in Fibroblasts
(Yuki Nakagawa),(Seiji Okada),(Masahiko Hatano),(Masaaki Ebara),(Hiromitsu Saisho),(Takeshi Tokuhisa) 생화학분자생물학회 2002 BMB Reports Vol.35 No.5
Exposure to ultraviolet light (UV) induces apoptosis in mammalian cells. The caspase group of proteases is required for the apoptosis. This pathway is initiated by a release of cytochrome c from the mitochondria into the cytosol. Several Bcl-2 family proteins can regulate the release of cytochrome c by stabilizing the mitochondrial membrane. Here we show that expression of the endogenous bcl-xL was strongly downregulated in NIH3T3 cells within 2 h after UV-C irradiation, and that of bax was upregulated from 8 h after irradiation. Apoptosis was induced in more than 50% of the NIH3T3 cells 48 h after irradiation. Constitutive overexpression of bcl-xL in NIH3T3 cells protected the UV-induced apoptosis by preventing the loss of mitochondrial membrane potential and the activation of caspase 9. These results suggest that downregulation of Bcl-xL is relevant to UV-induced apoptosis of fibroblasts.
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Downregulation of bcl-xL Is Relevant to UV-induced Apoptosis in Fibroblasts
Nakagawa, Yuki,Okada, Seiji,Hatano, Masahiko,Ebara, Masaaki,Saisho, Hiromitsu,Tokuhisa, Takeshi Korean Society for Biochemistry and Molecular Biol 2002 Journal of biochemistry and molecular biology Vol.35 No.5
Exposure to ultraviolet light (UV) induces apoptosis in mammalian cells, The caspase group of proteases is required for the appotosis. This pathway is initiated by a release of cytochrome c from the mitochondria into the cytosol. Several Bcl-2 family proteins can regulate the release of cytochrome c by stabilizing the mitochondrial membrane. Here we show that expression of the endogenous bcl-xL was strongly downregulated in NIH3T3 cells within 2 h after UV-C irradiation, and that of bax was upregulated from 8 h after irradiation. Apoptosis was induced in more than 50% of the NIH3T3 cells 48 h after irradiation. Constitutive overexpression of bcl-xL in NIH3T3 cells protected the UV-induced apoptosis by preventing the loss of mitochondrial membrane potential and the activation of caspase 9. There results suggest that downregulation of Bcl-xL is relevant to UV-induced apoptosis of tibroblasts.
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