Selected article for: "current study and sequence homology"

Author: Yang, Darong; Li, Nan L.; Wei, Dahai; Liu, Baoming; Guo, Fang; Elbahesh, Husni; Zhang, Yunzhi; Zhou, Zhi; Chen, Guo-Yun; Li, Kui
Title: The E3 ligase TRIM56 is a host restriction factor of Zika virus and depends on its RNA-binding activity but not miRNA regulation, for antiviral function
  • Document date: 2019_6_28
  • ID: 1nr0hggt_42
    Snippet: Data from the current study on ZIKV as well as from several others on BVDV, YFV, DENV2 and influenza viruses, all underscore the importance of the C-terminal portion of TRIM56 for restricting RNA viruses [24] [25] [26] . While TRIM56 is classified within the subgroup C-V that consists of TRIM proteins without known functional domains in their C-terminal regions, the C-terminal portion of TRIM56 exhibits sequence homology with the NHL repeat of se.....
    Document: Data from the current study on ZIKV as well as from several others on BVDV, YFV, DENV2 and influenza viruses, all underscore the importance of the C-terminal portion of TRIM56 for restricting RNA viruses [24] [25] [26] . While TRIM56 is classified within the subgroup C-V that consists of TRIM proteins without known functional domains in their C-terminal regions, the C-terminal portion of TRIM56 exhibits sequence homology with the NHL repeat of several TRIM-NHL proteins including TRIM2, TRIM3, TRIM32 and TRIM71 [26] . Of these, TRIM71 and TRIM32 were reported to bind to miRNAs and/or mRNAs and regulate their function or metabolism [27] [28] [29] . Thus, we tested the possibility that the NHL-like repeat in the C-terminal portion of TRIM56 may contribute to antiviral activity via a miRNA-dependent mechanism.

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