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Articles by Rong Zhu
Total Records ( 2 ) for Rong Zhu
  Yan Xiao , Caifeng Bi , Yuhua Fan , Shanbing Liu , Xia Zhang , Dongmei Zhang , Yilong Wang and Rong Zhu
  To investigate the structure-activity relationship of L-glutamine and L-asparagine Schiff base copper complexes in applications, L-glutamine and L-asparagine Schiff bases (GV and AV) and their copper complexes [Cu3(GV)2(CH3COO)2(H2O)] · 2H2O (GVC) and [CuAV(H2O)3] (AVC) have been synthesized and characterized by molar conductance, elemental analysis, UV-Vis, IR, 1H-NMR, and TG-DTG. We examined the geometries of GV, AV, GVC, and AVC through Hartree-Fock method and electronic absorption spectra. We also tested their antibacterial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Bacillus subtilis bacteria and antiproliferation activity on human breast cancer MDA-MB-231 cells. The side chain difference between L-glutamine and L-asparagine results in different geometry of GV and AV, which leads to different geometry of GVC and AVC. GVC, a trinuclear Cu(II) complex, shows the highest antibacterial activity and the highest growth inhibition activity on MDA-MB-231 cells. Our results suggest that GVC has potential as an antibacterial and anticancer agent.
  Rong Zhu , Yi-Bing Zhang , Qi-Ya Zhang and Jian-Fang Gui
  The double-stranded RNA (dsRNA)-dependent protein kinase PKR is thought to mediate a conserved antiviral pathway by inhibiting viral protein synthesis via the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2α). However, little is known about the data related to the lower vertebrates, including fish. Recently, the identification of PKR-like, or PKZ, has addressed the question of whether there is an orthologous PKR in fish. Here, we identify the first fish PKR gene from the Japanese flounder Paralichthys olivaceus (PoPKR). PoPKR encodes a protein that shows a conserved structure that is characteristic of mammalian PKRs, having both the N-terminal region for dsRNA binding and the C-terminal region for the inhibition of protein translation. The catalytic activity of PoPKR is further evidence that it is required for protein translation inhibition in vitro. PoPKR is constitutively transcribed at low levels and is highly induced after virus infection. Strikingly, PoPKR overexpression increases eIF2α phosphorylation and inhibits the replication of Scophthalmus maximus rhabdovirus (SMRV) in flounder embryonic cells, whereas phosphorylation and antiviral effects are impaired in transfected cells expressing the catalytically inactive PKR-K421R variant, indicating that PoPKR inhibits virus replication by phosphorylating substrate eIF2α. The interaction between PoPKR and eIF2α is demonstrated by coimmunoprecipitation assays, and the transfection of PoPKR-specific short interfering RNA further reveals that the enhanced eIF2α phosphorylation is catalyzed by PoPKR during SMRV infection. The current data provide significant evidence for the existence of a PKR-mediated antiviral pathway in fish and reveal considerable conservation in the functional domains and the antiviral effect of PKR proteins between fish and mammals.
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