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- 저자 : Chun-Chi Lo (검색결과 18 건)
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Chun-Yeung Lo,Sze-Ting Choi,Olive Tin-Wai Li,Jacky Chi-Ki Ngo,David Chi-Cheong Wan,Leo Lit-Man Poon,Pang-Chui Shaw1 한국구조생물학회 2015 Biodesign Vol.3 No.3
Currently, many strains of influenza A virus have developed resistance against anti-influenza drugs, and it is essential to find new chemicals to combat this virus. The viral nucleoprotein (NP) is a major component of the ribonucleoprotein (RNP) complex for the transcription and replication of the virus. In this study, we have employed surface plasmon resonance direct binding screening on the influenza A NP and found a hit compound 16 that can subdue influenza RNP activities. Subsequently, two analogs (compounds 55 & 58) from compound 16 were identified which inhibit RNP activities of various influenza A subtypes and viral growth at micromolar levels. These analogs were also shown to directly interact with NP, with KD 12.0±1.25 and 41.6±1.93 μM respectively by surface plasmon resonance assay.
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Liang, Chi-Te,Lin, Li-Hung,Kuang Yoa, Chen,Lo, Shun-Tsung,Wang, Yi-Ting,Lou, Dong-Sheng,Kim, Gil-Ho,Yuan-Huei, Chang,Ochiai, Yuichi,Aoki, Nobuyuki,Chen, Jeng-Chung,Lin, Yiping,Chun-Feng, Huang,Lin, Sh Springer 2011 Nanoscale research letters Vol.6 No.1
<P>A direct insulator-quantum Hall (I-QH) transition corresponds to a crossover/transition from the insulating regime to a high Landau level filling factor ν > 2 QH state. Such a transition has been attracting a great deal of both experimental and theoretical interests. In this study, we present three different two-dimensional electron systems (2DESs) which are in the vicinity of nanoscaled scatterers. All these three devices exhibit a direct I-QH transition, and the transport properties under different nanaoscaled scatterers are discussed.</P>
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( Huei-fen Lo ),( Meng-chun Chi ),( Min-guan Lin ),( Yuan-gin Lan ),( Tzu-fan Wang ),( Long-liu Lin ) 한국미생물생명공학회(구 한국산업미생물학회) 2018 Journal of microbiology and biotechnology Vol.28 No.9
In the present study, the stabilizing effect of four different biological osmolytes on Bacillus licheniformis γ-glutamyl transpeptidase (BlGGT) was investigated. BlGGT appeared to be stable under temperatures below 40°C, but the enzyme retained less than 10% of its activity at 60°C. The tested osmolytes exhibited different degrees of effectiveness against temperature inactivation of BlGGT, and sucrose was found to be the most effective among these. The use of circular dichroism spectroscopy for studying the secondary structure of BlGGT revealed that the temperature-induced conformational change of the protein molecule could be prevented by the osmolytes. Consistently, the molecular structure of the enzyme was essentially conserved by the osmolytes at elevated temperatures as monitored by fluorescence spectroscopy. Sucrose was further observed to counteract guanidine hydrochloride (GdnHCl)- and urea-induced denaturation of BlGGT. Taken together, we observed evidently that some well-known biological osmolytes, especially sucrose, make a dominant contribution to the structural stabilization of BlGTT.
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