Z
Zhenshan Zhang
Researcher at Chinese Academy of Sciences
Publications - 8
Citations - 178
Zhenshan Zhang is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Quantitative structure–activity relationship & Binding site. The author has an hindex of 7, co-authored 8 publications receiving 166 citations.
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Journal ArticleDOI
The Dipeptide H-Trp-Glu-OH Shows Highly Antagonistic Activity against PPARγ: Bioassay with Molecular Modeling Simulation
Fei Ye,Zhenshan Zhang,Haibin Luo,Jianhua Shen,Kaixian Chen,Xu Shen,Xu Shen,Hualiang Jiang,Hualiang Jiang +8 more
TL;DR: The dipeptide H‐Trp‐Glu‐OH (G3335) was discovered to be a novel PPARγ antagonist and the results suggested that residues Cys285, Arg288, Ser289, and His449 in PParγ play vital roles inPPARγ‐LBD–G33 35 binding.
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Binding Investigation of Human 5-Lipoxygenase with Its Inhibitors by SPR Technology Correlating with Molecular Docking Simulation
TL;DR: The surface plasmon resonance biosensor results showed that the equilibrium dissociation constant (KD) values evaluated by Biacore 3000 for the inhibitors showed a good correlation with its reported IC50, suggesting that SPR technology might be applicable as a direct assay method in screening new 5-LOX inhibitors at an early stage.
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Essential structural profile of a dual functional inhibitor against cyclooxygenase-2 (COX-2) and 5-lipoxygenase (5-LOX): Molecular docking and 3D-QSAR analyses on DHDMBF analogues
TL;DR: Both the docking simulations and QSAR analyses suggest that new potent dual inhibitors should share a structural feature with a moderately bulky group at R2 position and a rather negatively charged group around the position of the carbonyl group of DHDMBFs.
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3D-QSAR study of 20 (S)-camptothecin analogs.
TL;DR: The CoMFA model indicated that bulky negative-charged group at position 9, 10 and 11 of CPT would increase activity, but excessively increasing bulky group at Position 10 is adverse to inhibitory activity; substituents that occupy position 7 with the bulky positive group will enhance the inhibitive activity.
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Inhibitory mode of indole-2-carboxamide derivatives against HLGPa: molecular docking and 3D-QSAR analyses.
Guixia Liu,Zhenshan Zhang,Xiaomin Luo,Jianhua Shen,Hong Liu,Xu Shen,Kaixian Chen,Hualiang Jiang +7 more
TL;DR: In this paper, a series of indole-2-carboxamide compounds with human liver glycogen phosphorylase a (HLGPa) have been studied employing molecular docking and 3D-QSAR approaches.