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Articles by YanPing Li
Total Records ( 3 ) for YanPing Li
  Yanping Li and Liyong Zhang
  ML algorithm has low computational complexity but its timing estimation is not good. In order to improve the problem, combination of stochastic approximation and ML algorithm is proposed. Using ML algorithm as timing coarse estimation and stochastic approximation algorithm as timing fine estimation, the simulation results show that the proposed algorithm can realize more accurate symbol timing than ML algorithm.
  YanPing Li
  Cyclic prefix is a copy of the last samples of OFDM symbol. The OFDM synchronization estimation algorithm based on cyclic prefix has low complexity and can save the bandwidth resource of the OFDM systems, so the synchronization method proposed in this study is based on cyclic prefix. Novel symbol timing metric is presented in the proposed method and the timing metric has a peak plateau. The proposed method does not need to seek for the peak value of the timing metric to realize the synchronization estimation. It just needs to find the edge of the peak plateau. In the proposed method we need to set a threshold to process symbol timing metric, after which it is easy to find the edge of the peak plateau, so the proposed method has low complexity. The simulation results show that the proposed method has low mean error and MSE.
  Chang Liu , Maho Takahashi , Yanping Li , Shuang Song , Tara J. Dillon , Ujwal Shinde and Philip J. S. Stork
  Exchange proteins activated by cAMP (cyclic AMP) 2 (Epac2) is a guanine nucleotide exchange factor for Rap1, a small G protein involved in many cellular functions, including cell adhesion, differentiation, and exocytosis. Epac2 interacts with Ras-GTP via a Ras association (RA) domain. Previous studies have suggested that the RA domain was dispensable for Epac2 function. Here we show for the first time that Ras and cAMP regulate Epac2 function in a parallel fashion and the Ras-Epac2 interaction is required for the cAMP-dependent activation of endogenous Rap1 by Epac2. The mechanism for this requirement is not allosteric activation of Epac2 by Ras but the compartmentalization of Epac2 on the Ras-containing membranes. A computational modeling is consistent with this compartmentalization being a function of both the level of Ras activation and the affinity between Ras and Epac2. In PC12 cells, a well-established model for sympathetic neurons, the Epac2 signaling is coupled to activation of mitogen-activated protein kinases and contributes to neurite outgrowth. Taken together, the evidence shows that Epac2 is not only a cAMP sensor but also a bona fide Ras effector. Coincident detection of both cAMP and Ras signals is essential for Epac2 to activate Rap1 in a temporally and spatially controlled manner.
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