劉東祥，1998年博士畢業於中國科學院上海藥物研究所， 上海藥物研究所研究員。
基本介紹
- 中文名：劉東祥
- 國籍：中國
- 民族：漢族
- 畢業院校：中國科學院上海藥物研究所
- 性別：男
- 政治面貌：民眾
個人簡介,研究方向,專家類別,職務,代表論著,
個人簡介
1998-2005年分別以博士後、研究科學家、研究助理教授在美國托馬斯傑弗遜大學、伊利諾大學、伯翰姆研究所學習和工作，期間設計出第一個Bcl-2小分子抑制劑-HA14-1，該抑制劑發表於PNAS並獲一項美國專利。2005年入選中國科學院百人計畫，受聘於上海藥物研究所，任研究員、課題組長。
研究方向
採用生物化學、結構生物學方法，研究與癌症、神經退行性疾病相關蛋白質的結構與功能。
以這些蛋白質為靶標，設計全新化學結構的抑制劑或激動劑，為藥物研發提供新的先導化合物。
發展蛋白質結構功能研究、藥物分子設計的新方法和新技術。
專家類別
研究員；百人計畫
職務
中科院上海藥物所研究員、博士生導師、課題組長
代表論著
Zhou Y, Jiang C, Zhang Y, Liang Z, Liu W, Wang L, Luo C, Zhong T, Sun Y, Zhao L, Xie X, Jiang H, Zhou N, Liu D*, Liu H*. Structural Optimization and Biological Evaluation of Substituted Bisphenol A Derivatives as -Amyloid Peptide Aggregation Inhibitors. Journal of Medicinal Chemistry.
Feng Y, Ding X, Chen T, Chen L, Liu F, Jia X, Luo X, Shen X, Chen K, Jiang H, Wang H*, Liu H*, Liu D*. Design, Synthesis and Interaction Study of Quinazoline-2(1H)-Thione Derivatives as Novel Potential Bcl-xL Inhibitors. Journal of Medicinal Chemistry
Jiang C, Feng Y, Huang X, Xu Y, Zhang Y, Zhou N, Shen X, Chen K, Jiang H*, Liu D*. An enzyme-linked immunosorbent assay to compare the affinity of chemical compounds for -amyloid peptide as a monomer. Analytical and Bioanalytical Chemistry
Chen L, Feng Y, Zhou Y, Zhu W, Shen X, Chen K, Jiang H, Liu D*. Dual role of Zn2+ in maintaining structural integrity and suppressing deacetylase activity of SIRT1. Journal of Inorganic Biochemistry
Feng Y, Liu D*, Shen X, Chen K, Jiang H. Structure assembly of Bcl-xL through α5-α5 and α6-α6 interhelix interactions in lipid membranes. Biochimica et Biophysica Acta-Biomembranes
Feng Y, Wu J, Chen L, Luo C, Shen X, Chen K, Jiang H, Liu D*. A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide. Analytical Biochemistry
Feng Y, Zhang L, Hu T, Shen X, Ding J, Chen K, Jiang H, Liu D*. A conserved hydrophobic core at Bcl-xL mediates its structural stability and binding affinity with BH3-domain peptide of pro-apoptotic protein. Archives of Biochemistry and Biophysics
Feng Y, Shen X, Chen K, Jiang H, Liu D*. A new assay based on fluorescence resonance energy transfer to determine the binding affinity of Bcl-xL inhibitors. Bioscience Biotechnology and Biochemistry
Feng Y, Lin Z, Shen X, Chen K, Jiang H, Liu D*. Bcl-xL forms two distinct homodimers at non-ionic detergents: implications in the dimerization of Bcl-2 family proteins. Journal of Biochemistry.
Li Y*, Liu D*, Cao R, Kumar S, Dong C, An J, Wilson SR, Gao YG, Huang Z. Crystal structure of chemically synthesized vMIP-II. Proteins: Structure, Function, and Bioinformatics
Liu D, Madani N, Li Y, Cao R, Choi WT, Kawatkar SP, Lim MY, Kumar S, Dong CZ, Wang J, Russell JD, Lefebure CR, An J, Wilson S, Gao YG, Pallansch LA, Sodroski JG, Huang Z. Crystal structure and structural mechanism of a novel anti-human immunodeficiency virus and D-amino acid-containing chemokine. Journal of Virology
Liu D*, Xu Y, Feng Y, Liu H, Shen X, Chen K, Ma J, Jiang H*. Inhibitor discovery targeting the intermediate structure of β-amyloid peptide on the conformational transition pathway: implications in the aggregation mechanism of β-amyloid peptide. Biochemistry
Mori M*, Liu D*, Kumar S, Huang Z. NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II. Biochemical And Biophysical Research Communications
Liu D*, Yang B*, Cao R, Huang Z. A chemical strategy to promote helical peptide-protein interactions involved in apoptosis. Bioorganic & Medicinal Chemistry Letters
Yang B*, Liu D*, Huang Z. Identification of Affinity-Enhancing Motifs on Pro-apoptosis peptides derived from the BH3 domain of Bcl-2 family proteins. Bioorganic & Medicinal Chemistry Letters
Liu D*, Huang Z. Synthetic peptides and non-peptidic molecules as probes of structure and function of Bcl-2 family proteins and modulators of apoptosis. Apoptosis
Wang JL*, Liu D*, Zhang ZJ, Shan S, Han X, Srinivasula SM, Croce CM, Alnemri ES, Huang Z. Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells. Proceedings of The National Academy of Sciences of The United States of America
