Article
CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit similar pattern of toxicity and share common genetic modifiers in Drosophila.
Neurobiology of disease - 1 Aug 2014
Ermanoska Biljana, Motley William W, Leitão-Gonçalves Ricardo, Asselbergh Bob, Lee LaTasha H, De Rijk Peter, Sleegers Kristel, Ooms Tinne, Godenschwege Tanja A, Timmerman Vincent, Fischbeck Kenneth H, Jordanova Albena
Abstract excerpt
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...
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