Phosphorylation-induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain.

@article{Mari2000PhosphorylationinducedDO,
  title={Phosphorylation-induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain.},
  author={Isabelle J. Mari{\'e} and Eric J. Smith and Arun J. Prakash and David E. Levy},
  journal={Molecular and cellular biology},
  year={2000},
  volume={20 23},
  pages={8803-14}
}
Interferon regulatory factor 7 (IRF7) is an interferon (IFN)-inducible transcription factor required for activation of a subset of IFN-alpha genes that are expressed with delayed kinetics following viral infection. IRF7 is synthesized as a latent protein and is posttranslationally modified by protein phosphorylation in infected cells. Phosphorylation required a carboxyl-terminal regulatory domain that controlled the retention of the active protein exclusively in the nucleus, as well as its… CONTINUE READING

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Phosphorylation-dependent Dimerization of Irf7

  • Y. Fujii, T. Shimizu, M. Kusumoto, Y. Kyogoku, T. Taniguchi
  • VOL. 20,
  • 2000

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