换一批
换一批Highly Selective Activation of Heat Shock Protein 70 by Allosteric Regulation Provides an Insight into Efficient Neuroinflammation Inhibition.
第一作者：
Li-Chao,Wang
第一单位：
State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100191, China; State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
作者：
主题词
别构调节(Allosteric Regulation);别构部位(Allosteric Site);动物(Animals);结合部位(Binding Sites);秀丽新小杆线虫(Caenorhabditis elegans);细胞系(Cell Line);半胱氨酸(Cysteine);细胞因子类(Cytokines);酶激活(Enzyme Activation);HSP70热休克蛋白质类(HSP70 Heat-Shock Proteins);人类(Humans);炎症(Inflammation);炎症介导素类(Inflammation Mediators);配体(Ligands);男(雄)性(Male);小鼠(Mice);模型, 生物学(Models, Biological);模型, 分子(Models, Molecular);分子构象(Molecular Conformation);分子结构(Molecular Structure);突变(Mutation);NF-κB(NF-kappa B);神经系统疾病(Nervous System Diseases);蛋白质结合(Protein Binding);量化构效关系(Quantitative Structure-Activity Relationship);TNF受体相关因子6(TNF Receptor-Associated Factor 6);萜类(Terpenes);泛素化(Ubiquitination);斑马鱼(Zebrafish)
DOI
10.1016/j.ebiom.2017.08.011
PMID
28807514
发布时间
2018-11-13
- 浏览7
EBioMedicine
2017年23卷
160-172页
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