Chaotification of a continuous stable complex network via impulsive control

2015 ◽  
Vol 28 (6) ◽  
pp. 1271-1278 ◽  
Author(s):  
Na Liu ◽  
Zhihong Guan
2015 ◽  
Vol 83 (3) ◽  
pp. 1437-1451 ◽  
Author(s):  
Hui Zhao ◽  
Lixiang Li ◽  
Haipeng Peng ◽  
Jinghua Xiao ◽  
Yixian Yang ◽  
...  

2017 ◽  
Vol 31 (02) ◽  
pp. 1750008 ◽  
Author(s):  
Hui Zhao ◽  
Lixiang Li ◽  
Haipeng Peng ◽  
Jinghua Xiao ◽  
Yixian Yang ◽  
...  

In the paper, the fixed-time and finite-time synchronizations of multi-links complex network are investigated. Compared with finite-time synchronization, the settling time of fixed-time synchronization is independent of initial conditions. For uncertain multi-links complex networks, this paper further analyzes synchronization mechanism and unknown parameters based on the drive-response concept and finite-time stability theory. Novel synchronization control criteria and the result of parameters identification are, respectively, obtained in a finite time by utilizing Lyapunov function and linear matrix inequality (LMI). Besides, we give other two versions of finite-time synchronization and parameters identification for uncertain multi-links complex network with impulsive control input. Finally, numerical examples are given to illustrate the effectiveness of our theoretical results.


2001 ◽  
Vol 114 (10) ◽  
pp. 1959-1965 ◽  
Author(s):  
I.G. Mills ◽  
S. Urbe ◽  
M.J. Clague

Homotypic fusion between early endosomes requires the phosphatidylinositol 3-phosphate (PI3P)-binding protein, Early Endosomal Autoantigen 1 (EEA1). We have investigated the role of other proteins that interact with EEA1 in the fusion of early endosomes derived from Baby Hamster Kidney (BHK) cells. We confirm a requirement for syntaxin 13, but additionally show that the assay is equally sensitive to reagents specifically targeted against syntaxin 6. Binding of EEA1 to immobilised GST-syntaxin 6 and 13 was directly compared; only syntaxin 6 formed a stable complex with EEA1. Early endosome fusion requires the release of intravesicular calcium, and calmodulin plays a vital role in the fusion pathway, as judged by sensitivity to antagonists. We demonstrate that both EEA1 and syntaxin 13 interact with calmodulin. In the case of EEA1, binding to calmodulin requires an IQ domain, which is adjacent to a C-terminal FYVE domain that specifically binds to PI3P. We have assessed the influence of protein binding partners on EEA1 interaction with PI3P and find that both calmodulin and rab5-GTP are antagonistic to PI3P binding, whilst syntaxins 6 and 13 have no effect. These studies reveal a complex network of interactions between the proteins required for endosome fusion.


2014 ◽  
Vol 24 (1) ◽  
pp. 013141 ◽  
Author(s):  
Wen Sun ◽  
Jinhu Lü ◽  
Shihua Chen ◽  
Xinghuo Yu

1983 ◽  
Vol 22 (05) ◽  
pp. 246-250 ◽  
Author(s):  
M. Al-Hilli ◽  
H. M. A. Karim ◽  
M. H. S. Al-Hissoni ◽  
M. N. Jassim ◽  
N. H. Agha

Gelchromatography column scanning has been used to study the fractions of reduced hydrolyzed 99mTc, 99mTc-pertechnetate and 99mTc-chelate in a 99mTc-glucoheptonate (GH) preparation. A stable high labelling yield of 99mTc-GH complex in the radiopharmaceutical has been obtained with a concentration of 40-50 mg of glucoheptonic acid-calcium salt and not less than 0.45 mg of SnCl2 2 H2O at an optimal pH between 6.5 and 7.0. The stability of the complex has been found significantly affected when sodium hydroxide solution was used for the pH adjustment. However, an alternative procedure for final pH adjustment of the preparation has been investigated providing a stable complex for the usual period of time prior to the injection. The organ distribution and the blood clearance data of 99mTc-GH in rabbits were relatively similar to those reported earlier. The mean concentration of the radiopharmaceutical in both kidneys has been studied in normal subjects for one hour with a scintillation camera and the results were satisfactory.


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