王鹏
教授
所属大学: 安徽师范大学
所属学院: 生命科学学院
个人简介
学习工作经历 2012年7月获安徽师范大学博士学位 2012年7月至今在安徽师范大学生命科学学院工作,历任讲师、副教授、教授 2014年12月至2017年2月在美国阿拉巴马大学伯明翰分校从事博士后研究工作 2021年3月至今任生命科学学院副院长 社会兼职 安徽省生物工程学会 常务理事 安徽省生物化学与分子生物学学会 理事
研究领域
主要从事蛋白质生物化学研究,重点关注主要代谢酶的结构、功能及进化
近期论文
Tian C, Wen B, Bian M, Jin M, Wang P*, Xu L*, Zhu G* (2021) From a dimer to a monomer: Construction of a chimeric monomeric isocitrate dehydrogenase. Protein Science 30(12):2396-2407. (*correspondence author) Tang W, Wu M, Qin N, Liu L, Meng R, Wang C, Wang P*, Zang J*, Zhu G* (2021) Crystal structures of NAD+-linked isocitrate dehydrogenase from the green alga Ostreococcus tauri and its evolutionary relationship with eukaryotic NADP+-linked homologs. Archives of Biochemistry and Biophysics 708:108898. (*correspondence author) Song P, Wang ML, Zheng QY, Wang P*, Zhu G* (2021) Isocitrate dehydrogenase 1 from Acinetobacter baummanii (AbIDH1) enzymatic characterization and its regulation by phosphorylation. Biochimie 181:77-85. (*correspondence author) Wang P#, Wang Y#, Guo X, Huang S, Zhu G. (2020) Biochemical and phylogenetic characterization of a monomeric isocitrate dehydrogenase from a marine methanogenic archaeon Methanococcoides methylutens. Extremophiles 24: 319-328. (#co-first author) Wang P#, Chen X#, Yang J, Pei Y, Bian M, Zhu G. (2019) Characterization of the nicotinamide adenine dinucleotides (NAD and NADP) binding sites of the monomeric isocitrate dehydrogenases from Campylobacter species. Biochimie 160, 148-155. (#co-first author) Wang P, Liu T, Zhou X, Zhu G. (2019) Evaluation of the potential phosphorylation effect on isocitrate dehydrogenases from Saccharomyces cerevisiae and Yarrowia lipolytica. Applied Biochemistry and Biotechnology 187: 1131-1142. Zhu Y#, Wang P#, Zhang L, Bai G, Yang C, Wang Y, He J, Zhang Z, Zhu G, Zou D (2019) Superhero Rictor promotes cellular differentiation of mouse embryonic stem cells. Cell Death and Differentiation 26(5): 958-968. (#co-first author) Wang P#, Li J#, Tao J, Sha B (2018) The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. Journal of Biological Chemistry 293(11): 4110-4121. (#co-first author) Wang P, Li J, Weaver C, Lucius A, Sha B (2017) Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for Hsp104 functions to dissolve prions. Acta Crystallographica Section D 73, 365-372. Wang P, Li J, Sha B (2016) The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins. Acta Crystallographica Section D 72, 1290-1297.