Ontology highlight
ABSTRACT:
SUBMITTER: Blocquel D
PROVIDER: S-EPMC5737801 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Nucleic acids research 20170701 13
While having multiple aminoacyl-tRNA synthetases implicated in Charcot-Marie-Tooth (CMT) disease suggests a common mechanism, a defect in enzymatic activity is not shared among the CMT-causing mutants. Protein misfolding is a common hypothesis underlying the development of many neurological diseases. Its process usually involves an initial reduction in protein stability and then the subsequent oligomerization and aggregation. Here, we study the structural effect of three CMT-causing mutations in ...[more]