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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.
Zhe Jin,Liu Yang,Si-Jie Liu,Jian Wang,Shuo Li,Huang-Quan Lin,David Chi Cheong Wan,Chun Hu 대한약학회 2010 Archives of Pharmacal Research Vol.33 No.10
Acetylcholinesterase (AChE) inhibitors played an important role in developing a cure for Alzheimer’ s disease. In order to study on the influence of modifications at different groups and side chains on the AChE inhibitory ability and the active sites of 7H-thiazolo[3,2-b][1,2,4]triazin-7-one derivatives, fourteen 3,6-diaryl-7H-thiazolo[3,2-b][1,2,4]triazin-7-one derivatives were designed and synthesized. The study of AChE inhibitory activity was carried out using the Ellman colorimetric assay with huperzine-A as the positive control drug. Most of the target compounds exhibited more than 50% inhibition at 10 μM. Some target compounds showed strong inhibition against AChE. The molecular fields analysis and preliminary structureactivity relationships are discussed.