Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing.

@article{Cowper2001SerinearginineP,
  title={Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing.},
  author={Alison E. Cowper and Javier F C{\'a}ceres and Akila Mayeda and Gavin Robert Screaton},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 52},
  pages={48908-14}
}
We have characterized two RNA-binding proteins, of apparent molecular masses of approximately 40 and 35 kDa, which possess a single N-terminal RNA-recognition motif (RRM) followed by a C-terminal domain rich in serine-arginine dipeptides. Their primary structures resemble the single-RRM serine-arginine (SR) protein, SC35; however their functional effects are quite distinctive. The 40-kDa protein cannot complement SR protein-deficient HeLa cell S100 extract and showed a dominant negative effect… CONTINUE READING
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