Phosphorylation site analysis of Semliki forest virus nonstructural protein 3.

@article{Vihinen2000PhosphorylationSA,
  title={Phosphorylation site analysis of Semliki forest virus nonstructural protein 3.},
  author={Helena Vihinen and Juhani O. Saarinen},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 36},
  pages={27775-83}
}
Nonstructural protein 3 (Nsp3) is an essential subunit of the alphavirus RNA replication complex, although its specific function(s) has yet to be well defined. Previously, it has been shown that Semliki Forest virus Nsp3 (482 amino acids) is a phosphoprotein, and, in the present study, we have mapped its major phosphorylation sites. Mass spectrometric methods utilized included precursor ion scanning, matrix-assisted laser desorption/ionization mass spectrometry used in conjunction with on… CONTINUE READING