Variant: rs137852643 

    present in Gene: GARS1
    present in Chromosome: 7
    Position on Chromosome: 30609729
    Alleles of this Variant: G/C

rs137852643 in GARS1 gene and Charcot-Marie-Tooth disease, Type 2D PMID 26244500 2015 Two Novel De Novo GARS Mutations Cause Early-Onset Axonal Charcot-Marie-Tooth Disease.

PMID 20169446 2010 Charcot-Marie-Tooth disease type 2D with a novel glycyl-tRNA synthetase gene (GARS) mutation.

PMID 25168514 2014 Impaired function is a common feature of neuropathy-associated glycyl-tRNA synthetase mutations.

PMID 24604904 2014 Application of whole exome sequencing in undiagnosed inherited polyneuropathies.

PMID 17035524 2006 Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons.

PMID 26503042 2015 CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-tRNA synthetase.

PMID 17101916 2006 Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene.

PMID 17663003 2007 Further evidence for genetic heterogeneity of distal HMN type V, CMT2 with predominant hand involvement and Silver syndrome.

PMID 12690580 2003 Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.

rs137852643 in GARS1 gene and Hereditary Motor and Sensory-Neuropathy Type II PMID 26503042 2015 CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-tRNA synthetase.

PMID 17595294 2007 Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect.

PMID 27008886 2016 Dimerization is required for GARS-mediated neurotoxicity in dominant CMT disease.

PMID 26138142 2015 Impaired protein translation in Drosophila models for Charcot-Marie-Tooth neuropathy caused by mutant tRNA synthetases.

PMID 21737751 2011 Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening.

PMID 17035524 2006 Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons.