A disease-associated polymorphism alters splicing of the human CD45 phosphatase gene by disrupting combinatorial repression by heterogeneous nuclear ribonucleoproteins (hnRNPs).

@article{MottaMena2011ADP,
  title={A disease-associated polymorphism alters splicing of the human CD45 phosphatase gene by disrupting combinatorial repression by heterogeneous nuclear ribonucleoproteins (hnRNPs).},
  author={Laura B. Motta-Mena and Sarah A. Smith and Michael J. Mallory and Jason K. Jackson and Jiarong Wang and Kristen W. Lynch},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 22},
  pages={20043-53}
}
Alternative splicing is typically controlled by complexes of regulatory proteins that bind to sequences within or flanking variable exons. The identification of regulatory sequence motifs and the characterization of sequence motifs bound by splicing regulatory proteins have been essential to predicting splicing regulation. The activation-responsive sequence (ARS) motif has previously been identified in several exons that undergo changes in splicing upon T cell activation. hnRNP L binds to this… CONTINUE READING
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unpublished results. C77G Mutation Disrupts hnRNP Control of CD45

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