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Yongrui Xiao,Zhengle Zhang,Tiedong Ma 제어·로봇·시스템학회 2023 International Journal of Control, Automation, and Vol.21 No.6
This paper mainly discusses the formation of second-order multi-agent systems with fixed and switching topologies by time-delayed impulsive control. The key issue is how to design an appropriate impulsive control algorithm to maintain a desired geometric formation with input delays and switching topologies between neighboring agents. First, according to the restriction of systems, the impulsive protocol is proposed for the follower agents. Then, by using the stability theory, some conditions are derived to ensure the formation consensus. Finally, the numerical examples illustrate the effectiveness and correctness of the designed impulsive control algorithm.
Adaptive finite element analysis of steel girder deck pavement
Wenhuo Sun,Lixiong Gu,Ronghui Wang,Tiedong Qi 대한기계학회 2018 JOURNAL OF MECHANICAL SCIENCE AND TECHNOLOGY Vol.32 No.2
This paper shows a more exact and practical finite element model of the steel girder deck pavement. Based on Mindlin thick plate theory, a 12-node solid thick plate element was constituted to analyze the pavement. The computation result was compared with that by traditional 4-node and 8-node thick plate finite element, and is satisfactory. A combined plate beam element method is presented to investigate the stiffened plate. A 6-node solid thin plate element was constituted to analyze the top plate based on Kirchhoff thin plate theory. The stiffeners acting as the vertical supporting function mainly are taken as Euler beam elements. A method of using the linear interpolation to realize the longitudinal displacement and the cubic Hermite interpolation to the vertical displacement is presented to analyze the stiffeners. In addition, it is essential to consider the displacement coordination between the top plate and stiffeners. A node-to-node contact scheme, which is applicable for three-dimensional contact analyses involving large deformations, was used to treat the contact problem between pavement and stiffened plate by Lagrange multiplier methods.
Isovitexin, a Potential Candidate Inhibitor of Sortase A of Staphylococcus aureus USA300
( Dan Mu ),( Hua Xiang ),( Haisi Dong ),( Dacheng Wang ),( Tiedong Wang ) 한국미생물생명공학회(구 한국산업미생물학회) 2018 Journal of microbiology and biotechnology Vol.28 No.9
Staphylococcus aureus causes a broad variety of diseases. The spread of multidrug-resistant S. aureus highlights the need to develop new ways to combat S. aureus infections. Sortase A (SrtA) can anchor proteins containing LPXTG binding motifs to the bacteria surface and plays a key role in S. aureus infections, making it a promising antivirulence target. In the present study, we used a SrtA activity inhibition assay to discover that isovitexin, a Chinese herbal product, can inhibit SrtA activity with an IC<sub>50</sub> of 28.98 μg/ml. Using a fibrinogen-binding assay and a biofilm formation assay, we indirectly proved the SrtA inhibitory activity of isovitexin. Additionally, isovitexin treatment decreased the amount of staphylococcal protein A (SpA) on the surface of the cells. These data suggest that isovitexin has the potential to be an anti-infective drug against S. aureus via the inhibition of sortase activity.
Isovitexin Is a Direct Inhibitor of Staphylococcus aureus Coagulase
( Hua Xiang ),( Panpan Yang ),( Li Wang ),( Jiaxin Li ),( Tiedong Wang ),( Junze Xue ),( Dacheng Wang ),( Hongxia Ma ) 한국미생물 · 생명공학회 2021 Journal of microbiology and biotechnology Vol.31 No.10
Staphylococcus aureus (S. aureus) is a major pathogen that causes human pneumonia, leading to significant morbidity and mortality. S. aureus coagulase (Coa) triggers the polymerization of fibrin by activating host prothrombin, which then converts fibrinogen to fibrin and contributes to S. aureus pathogenesis and persistent infection. In our research, we demonstrate that isovitexin, an active traditional Chinese medicine component, can inhibit the coagulase activity of Coa but does not interfere with the growth of S. aureus. Furthermore, we show through thermal shift and fluorescence quenching assays that isovitexin directly binds to Coa. Dynamic simulation and structure-activity relationship analyses suggest that V191 and P268 are key amino acid residues responsible for the binding of isovitexin to Coa. Taken together, these data indicate that isovitexin is a direct Coa inhibitor and a promising candidate for drug development against S. aureus infection.