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At the active site, a glycyl-AMP (show APRT ELISA Kits) molecule is synthesized and is waiting for the transfer of the glycyl moiety to occur.
GlyRS functions as a chaperone that critically supports neddylation.
Data indicate that dimerization is required for the dominant neurotoxicity of disease-associated GARS mutations and provide a rapid, tractable model for studying newly identified GARS variants for a role in human disease.
one of the mRNAs isoforms tightly controls expression and localization of human GARS.
This study reports two crystal structures of human GlyRS variants, in the free form and in complex with tRNA(Gly) respectively, and reveal new aspects of the glycylation mechanism.
GARS mutations are an uncommon cause of Charcot-Marie-Tooth Disease (CMT) in Taiwan. The p.Asp146Tyr and p.Met238Arg mutations are associated with early-onset axonal CMT.
Our findings suggest that mutant GlyRS gains access to ectopic sub-compartments of the motor neuron, providing a possible explanation for the selective neuropathology caused by mutations in a widely expressed gene.
Expression of three CMT-mutant GARS proteins in Drosophila induces defects in motor performance and motor and sensory neuron morphology, and shortens lifespan.
The c.999G>T mutation is a novel mutation of the glycyl-tRNA synthetase gene that has not been previously reported. The phenotype of this family is Charcot-Marie-Tooth disease type 2D, which is first reported in Chinese population.
we propose that the disease-causing L129P mutant of glycyl-tRNA synthetase is linked to a distribution defect in peripheral nerves in vivo.
findings link the selective pathology of Charcot-Marie-Tooth disease type 2D to the neomorphic binding activity of GlyRS(CMT2D) that antagonizes the VEGF (show VEGFA ELISA Kits)-Nrp1 (show NRP1 ELISA Kits) interaction, meaning the VEGF (show VEGFA ELISA Kits)-Nrp1 (show NRP1 ELISA Kits) signalling axis is an actionable target for treating CMT2D
Results indicate that Charcot-Marie-Tooth peripheral neuropathies, type 2D (CMT2D) phenotype is caused by novel pathogenic roles for the mutant GARS that specifically affect peripheral neurons.
a glycyl-tRNA synthetase (GARS) mutation causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy
Gars(C201R) mutation significantly delayed disease onset in the SOD1 (show SOD1 ELISA Kits)(G93A);Gars(C201R/+) double heterozygous mutant mice and increased lifespan by 29% on the genetic background investigated
Expression levels of ADSL, GARS-AIRS-GART, and DGAT1 were higher in longissimus lumborum muscle than in heart or liver tissues
This gene encodes glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. The encoded enzyme is an (alpha)2 dimer which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
, Charcot-Marie-Tooth neuropathy 2D
, Charcot-Marie-Tooth neuropathy, neuronal type, D
, diadenosine tetraphosphate synthetase
, glycine tRNA ligase
, glycine--tRNA ligase
, glycyl-tRNA synthetase
, storage granule protein 23
, glycyl-tran synthetase