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Articles by Cheng Luo
Total Records ( 2 ) for Cheng Luo
  Chang-Fan Zhang , Min Yan , Jing He , Cheng Luo and Yuan-Yuan Xiao
  Aiming at the improvement of operation reliability, the study present a sensor fault diagnosis method for the doubly-fed wind generator control system. Firstly, a double-fed wind generator modeling method on consideration of unknown input disturbance is presented. The designs of Luenberger observer and sliding mode observer are following. The former is in order to change the nonlinear system into a linear time-invariant one and the latter for the elimination of the influence of unknown input disturbance in fault diagnosis. Finally, an observers-based sensor fault diagnosis method is proposed and its effectiveness is verified through experiments with different types of sensor faults.
  Liang Zhang , Weizhi Liu , Tiancen Hu , Li Du , Cheng Luo , Kaixian Chen , Xu Shen and Hualiang Jiang
  β-Hydroxyacyl-acyl carrier protein dehydratase (FabZ) is an important enzyme for the elongation cycles of both saturated and unsaturated fatty acids biosyntheses in the type II fatty acid biosynthesis system (FAS II) pathway. FabZ has been an essential target for the discovery of compounds effective against pathogenic microbes. In this work, to characterize the catalytic and inhibitory mechanisms of FabZ, the crystal structures of the FabZ of Helicobacter pylori (HpFabZ) and its complexes with two newly discovered inhibitors have been solved. Different from the structures of other bacterial FabZs, HpFabZ contains an extra short two-turn α-helix (α4) between α3 and β3, which plays an important role in shaping the substrate-binding tunnel. Residue Tyr-100 at the entrance of the tunnel adopts either an open or closed conformation in the crystal structure. The crystal structural characterization, the binding affinity determination, and the enzymatic activity assay of the HpFabZ mutant (Y100A) confirm the importance of Tyr-100 in catalytic activity and substrate binding. Residue Phe-83 at the exit tunnel was also refined in two alternative conformations, leading the tunnel to form an L-shape and U-shape. All these data thus contributed much to understanding the catalytic mechanism of HpFabZ. In addition, the co-crystal structures of HpFabZ with its inhibitors have suggested that the enzymatic activity of HpFabZ could be inhibited either by occupying the entrance of the tunnel or plugging the tunnel to prevent the substrate from accessing the active site. Our study has provided some insights into the catalytic and inhibitory mechanisms of FabZ, thus facilitating antibacterial agent development.
 
 
 
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