Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions

@inproceedings{Fantini2010CriticalLR,
  title={Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions},
  author={Damiano Fantini and Carlo Vascotto and Daniela Marasco and Chiara D’Ambrosio and Milena Romanello and Luigi Vitagliano and Carlo Pedone and Mattia Poletto and Laura Cesaratto and Franco Quadrifoglio and Andrea Scaloni and J. Pablo Radicella and Gianluca Tell},
  booktitle={Nucleic acids research},
  year={2010}
}
Apurinic/apyrimidinic endonuclease 1 (APE1), an essential protein in mammals, is involved in base excision DNA repair (BER) and in regulation of gene expression, acting as a redox co-activator of several transcription factors. Recent findings highlight a novel role for APE1 in RNA metabolism, which is modulated by nucleophosmin (NPM1). The results reported in this article show that five lysine residues (K24, K25, K27, K31 and K32), located in the APE1 N-terminal unstructured domain, are… CONTINUE READING

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Intrusion of a DNA repair protein in the RNome world: is this the beginning of a new era

  • G. Tell, D. M. Wilson
  • Mol. Cell. Biol.,
  • 2010
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