Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation.

@article{Henderson2010DiseasecausingMM,
  title={Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation.},
  author={Davin M Henderson and Ann Lee and James M. Ervasti},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 21},
  pages={9632-7}
}
Mutations in the dystrophin gene cause Duchenne muscular dystrophy (DMD) most commonly through loss of protein expression. In a small subpopulation of patients, missense mutations can cause DMD, Becker muscular dystrophy, or X-linked cardiomyopathy. Nearly one-half of disease-causing missense mutations are located in actin-binding domain 1 (ABD1) of dystrophin. To test the hypothesis that ABD1 missense mutations cause disease by impairing actin-binding activity, we engineered the K18N, L54R… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 24 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 42 references

Protein misfolding, aggregation, and conformational diseases part B: molecular mechanisms of conformational diseases, eds

  • A Vrabie, HH Goebel
  • VN Uversky and AL Fink (Springer, New York),
  • 2007

Similar Papers

Loading similar papers…