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- W2097160075 abstract "Cardioviruses of the Encephalomyocarditis virus (EMCV) and Theilovirus species encode small, amino-terminal proteins called Leaders (L). Phosphorylation of the EMCV L (LE) at two distinct sites by CK2 and Syk kinases is important for virus-induced Nup phosphorylation and nucleocytoplasmic trafficking inhibition. Despite similar biological activities, the LE phosphorylation sites are not conserved in the Theiloviruses, Saffold virus (LS, SafV) or Theiler׳s murine encephalitis virus (LT, TMEV) sequences even though these proteins also become phosphorylated in cells and cell-free extracts. Site prediction algorithms, combined with panels of site-specific protein mutations now identify analogous, but not homologous phosphorylation sites in the Ser/Thr and Theilo protein domains of LT and LS, respectively. In both cases, recombinant AMP-activated kinase (AMPK) was reactive with the proteins at these sites, and also with LE, modifying the same residue recognized by CK2." @default.
- W2097160075 created "2016-06-24" @default.
- W2097160075 creator A5021257425 @default.
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- W2097160075 date "2014-08-01" @default.
- W2097160075 modified "2023-09-29" @default.
- W2097160075 title "AMP-activated protein kinase phosphorylates EMCV, TMEV and SafV leader proteins at different sites" @default.
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- W2097160075 doi "https://doi.org/10.1016/j.virol.2014.06.026" @default.
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