CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit similar pattern of toxicity and share common genetic modifiers in Drosophila.

@article{Ermanoska2014CMTassociatedMI,
  title={CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit similar pattern of toxicity and share common genetic modifiers in Drosophila.},
  author={Biljana Ermanoska and William W. Motley and Ricardo Leit{\~a}o-Gonçalves and Bob Asselbergh and LaTasha H Lee and Peter De Rijk and Kristel Sleegers and Tinne Ooms and Tanja A Godenschwege and Vincent Timmerman and Kenneth H. Fischbeck and Albena Jordanova},
  journal={Neurobiology of disease},
  year={2014},
  volume={68},
  pages={180-9}
}
Aminoacyl-tRNA synthetases are ubiquitously expressed proteins that charge tRNAs with their cognate amino acids. By ensuring the fidelity of protein synthesis, these enzymes are essential for the viability of every cell. Yet, mutations in six tRNA synthetases specifically affect the peripheral nerves and cause Charcot-Marie-Tooth (CMT) disease. The CMT-causing mutations in tyrosyl- and glycyl-tRNA synthetases (YARS and GARS, respectively) alter the activity of the proteins in a range of ways… CONTINUE READING
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