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Articles by Yali Li
Total Records ( 2 ) for Yali Li
  Yan Feng , Feng Hou and Yali Li

LiV3O8, synthesized from V2O5 and LiOH, by heating of a suspension of V2O5 in a LiOH solution at a low-temperature (100–200 °C), exhibits a high discharge capacity and excellent cyclic stability at a high current density as a cathode material of lithium-ion battery. The charge-discharge curve shows a maximum discharge capacity of 228.6 mAh g-1 at a current density of 150 mA g-1 (0.5 C rate) and the 100 cycles discharge capacity remains 215 mAh g-1. X-ray diffraction indicates the low degree of crystallinity and expanding of inter-plane distance of the LiV3O8 phase, and scanning electronic microscopy reveals the formation of nano-domain structures in the products, which account for the enhanced electrochemical performance. In contrast, the LiV3O8 phase formed at a higher temperature (300 °C) consists of well-developed crystal phases, and coherently, results in a distinct reduction of discharge capacity with cycle numbers. Thus, an enhanced electrochemical performance has been achieved for LiV3O8 by the soft chemical method via a low-temperature heating process.

  Jerzy Frczek , Tae Whan Kim , Hui Xiao , Jianhong Yao , Qian Wen , Yali Li , Jean-Laurent Casanova , Juliusz Pryjma and Xiaoxia Li
  Two parallel interleukin-1 (IL-1)-mediated signaling pathways have been uncovered for IL-1R-TLR-mediated NFκB activation: TAK1-dependent and MEKK3-dependent pathways, respectively. The TAK1-dependent pathway leads to IKKα/β phosphorylation and IKKβ activation, resulting in classic NFκB activation through IκBα phosphorylation and degradation. The TAK1-independent MEKK3-dependent pathway involves IKKγ phosphorylation and IKKα activation, resulting in NFκB activation through dissociation of phosphorylated IκBα from NFκB without IκBα degradation. IL-1 receptor-associated kinase 4 (IRAK4) belongs to the IRAK family of proteins and plays a critical role in IL-1R/TLR-mediated signaling. IRAK4 kinase-inactive mutant failed to mediate the IL-1R-TLR-induced TAK1-dependent NFκB activation pathway, but mediated IL-1-induced TAK1-independent NFκB activation and retained the ability to activate substantial gene expression, indicating a structural role of IRAK4 in mediating this alternative NFκB activation pathway. Deletion analysis of IRAK4 indicates the essential structural role of the IRAK4 death domain in receptor proximal signaling for mediating IL-1R-TLR-induced NFκB activation.
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