| Nuclear modifier YARS2 allele correction restored retinal ganglion cells-specific deficiencies in Leber's hereditary optic neuropathy. | Nuclear modifier YARS2 allele correction restored retinal ganglion cells-specific deficiencies in Leber's hereditary optic neuropathy.
Chen JR, Chen C, Chen J, Ji Y, Lian Y, Zhang J, Yu J, Li XY, Qu J, Guan MX. | 04/27/2023 |
| Targeting mitochondrial tyrosyl-tRNA synthetase YARS2 suppresses colorectal cancer progression. | Targeting mitochondrial tyrosyl-tRNA synthetase YARS2 suppresses colorectal cancer progression.
Fang Q, Lin J, Gao L, Pan R, Zheng X., Free PMC Article | 10/8/2022 |
| findings provide molecular-level insights into the pathophysiology of maternally transmitted deafness arising from the synergy between tRNA(Ser(UCN)) and mitochondrial YARS mutations | Contribution of a mitochondrial tyrosyl-tRNA synthetase mutation to the phenotypic expression of the deafness-associated tRNA(Ser(UCN)) 7511A>G mutation.
Fan W, Zheng J, Kong W, Cui L, Aishanjiang M, Yi Q, Wang M, Cang X, Tang X, Chen Y, Mo JQ, Sondheimer N, Ge W, Guan MX., Free PMC Article | 07/18/2020 |
| Data suggest that biallelic tyrosyl-tRNA synthetase 2 (YARS2) variants, including severe loss-of-function alleles should be considered as a cause of isolated congenital sideroblastic anemia, as well as the myopathy, lactic acidosis and sideroblastic anemia 2 (MLASA2) syndromic phenotype. | The phenotypic spectrum of germline YARS2 variants: from isolated sideroblastic anemia to mitochondrial myopathy, lactic acidosis and sideroblastic anemia 2.
Riley LG, Heeney MM, Rudinger-Thirion J, Frugier M, Campagna DR, Zhou R, Hale GA, Hilliard LM, Kaplan JA, Kwiatkowski JL, Sieff CA, Steensma DP, Rennings AJ, Simons A, Schaap N, Roodenburg RJ, Kleefstra T, Arenillas L, Fita-Torró J, Ahmed R, Abboud M, Bechara E, Farah R, Tamminga RYJ, Bottomley SS, Sanchez M, Huls G, Swinkels DW, Christodoulou J, Fleming MD., Free PMC Article | 10/26/2019 |
| tyrosyl-tRNA synthetase 2 tyrosine | Sideroblastic anemia with myopathy secondary to novel, pathogenic missense variants in the YARS2 gene.
Smith F, Hopton S, Dallabona C, Gilberti M, Falkous G, Norwood F, Donnini C, Gorman GS, Clark B, Taylor RW, Kulasekararaj AG., Free PMC Article | 10/26/2019 |
| The p.Leu392Ser variant is likely a newly identified founder YARS2 mutation in mitochondrial myopathy. | Clinical Features, Molecular Heterogeneity, and Prognostic Implications in YARS2-Related Mitochondrial Myopathy.
Sommerville EW, Ng YS, Alston CL, Dallabona C, Gilberti M, He L, Knowles C, Chin SL, Schaefer AM, Falkous G, Murdoch D, Longman C, de Visser M, Bindoff LA, Rawles JM, Dean JCS, Petty RK, Farrugia ME, Haack TB, Prokisch H, McFarland R, Turnbull DM, Donnini C, Taylor RW, Gorman GS., Free PMC Article | 07/22/2017 |
| The mutation in YARS2 gene is a nuclear modifier for the phenotypic manifestation of Leber's hereditary optic neuropathy-associated mitochondrial DNA mutation. | The exome sequencing identified the mutation in YARS2 encoding the mitochondrial tyrosyl-tRNA synthetase as a nuclear modifier for the phenotypic manifestation of Leber's hereditary optic neuropathy-associated mitochondrial DNA mutation.
Jiang P, Jin X, Peng Y, Wang M, Liu H, Liu X, Zhang Z, Ji Y, Zhang J, Liang M, Zhao F, Sun YH, Zhang M, Zhou X, Chen Y, Mo JQ, Huang T, Qu J, Guan MX. | 12/17/2016 |
| Data identified novel YARS2 mutations and noted marked phenotypic variability among YARS2 MLASA patients, with phenotypes ranging from mild to lethal, suggesting that the background mtDNA haplotype may be contributing to the phenotypic variability. | Phenotypic variability and identification of novel YARS2 mutations in YARS2 mitochondrial myopathy, lactic acidosis and sideroblastic anaemia.
Riley LG, Menezes MJ, Rudinger-Thirion J, Duff R, de Lonlay P, Rotig A, Tchan MC, Davis M, Cooper ST, Christodoulou J., Free PMC Article | 07/19/2014 |
| The study confirms mutations in YARS2 as a cause of MLASA and shows that, like some of the cytoplasmic ARSs, mitochondrial ARSs occur in high-molecular-weight complexes. | A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia.
Sasarman F, Nishimura T, Thiffault I, Shoubridge EA. | 12/8/2012 |
| Observational study of gene-disease association. (HuGE Navigator) | Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article | 12/5/2010 |
| first example of a TyrRS lacking specificity toward N1-N72 and thus of a TyrRS disobeying the identity rules | Human mitochondrial TyrRS disobeys the tyrosine identity rules.
Bonnefond L, Frugier M, Giegé R, Rudinger-Thirion J., Free PMC Article | 08/3/2010 |
| The YARS2 mutation reported here is an alternative cause of MLASA. | Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome.
Riley LG, Cooper S, Hickey P, Rudinger-Thirion J, McKenzie M, Compton A, Lim SC, Thorburn D, Ryan MT, Giegé R, Bahlo M, Christodoulou J., Free PMC Article | 08/2/2010 |
| The gene for mitochondrial tyrosyl-tRNA synthetase is described and the initial characterization of the enzyme is reported. Genes for the remaining missing synthetases have also been found with the exception of human glutaminyl-tRNA synthetase. | Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS.
Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M. | 03/1/2010 |
| the structure of a strictly mitochondrial human synthetase, namely tyrosyl-tRNA synthetase (mt-TyrRS), in complex with an adenylate analog at 2.2 A resolution | Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features.
Bonnefond L, Frugier M, Touzé E, Lorber B, Florentz C, Giegé R, Sauter C, Rudinger-Thirion J. | 01/21/2010 |
| the apparent occurrence of an unusual TG 3' splice site in intron 5 is discussed | Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns.
Szafranski K, Schindler S, Taudien S, Hiller M, Huse K, Jahn N, Schreiber S, Backofen R, Platzer M., Free PMC Article | 10/9/2007 |