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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Additionally we are shipping and many more products for this protein.
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This study showed that show that apoptotic loser cells secrete Tyrosyl-tRNA synthetase, which is best known as a core component of the translational machinery.
Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy.
Platelet replenishment by YRS(ACT) is independent of thrombopoietin (TPO (show THPO Proteins)), as evidenced by expansion of the megakaryocytes from induced pluripotent stem cell-derived hematopoietic stem cells from a patient deficient in TPO (show THPO Proteins) signaling.
These YARS variants occur in the catalytic domain and the C-terminal domain, respectively. Mutations in YARS have been previously associated with an autosomal dominant form of Charcot-Marie-Tooth (CMT); our findings suggest the disease spectrum associated with YARS dysregulation is broader than peripheral neuropathy.
Studied the structural effect of three Charcot-Marie-Tooth disease-causing mutations in tyrosyl-tRNA synthetase. The mutations do not induce changes in protein secondary structures, or shared effects on oligomerization state and stability. However, all mutations provide access to a surface masked in the wild-type enzyme, and that access correlates with protein misinteraction.
Data show that the internal deletion of tyrosyl-tRNA synthetase TyrRSDeltaE2-4 splice variants (SVs (show FGFR2 Proteins)) gave an alternative, neomorphic dimer interface 'orthogonal' to that of native TyrRS.
Expression of CMT-mutant tyrosyl-tRNA synthetase in Drosophila impairs protein translation.
Computational modeling of molecular dynamics of G41R mutant form of human tyrosyl-tRNA synthetase, assosiated with Charcot-Marie-Tooth neuropathy has been presented.
the association of rare YARS variant with late-onset autosomal dominant Charcot-Marie-Tooth neuropathy
nuclear-localized TyrRS activates transcription factor E2F1 (show E2F1 Proteins) to upregulate the expression of DNA damage repair genes such as BRCA1 and RAD51 (show RAD51 Proteins).
A major difference between the first- and second-generation tRNA synthetases (RSs (show GRB10 Proteins)) is that the second-generation RSs (show GRB10 Proteins) have an active site more compatible with tyrosine binding.
The full length tyrosyl-tRNA synthetase lacks its cytokine activity because of the interactions between N-terminal and the C-terminal modules, which protect the ELR cytokine motif.
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.
tyrosine--tRNA ligase, cytoplasmic
, tyrosyl--tRNA ligase
, tyrosyl-tRNA synthetase, cytoplasmic
, tyrosyl-tRNA synthetase
, Tyrosyl-tRNA synthetase, cytoplasmic
, tyrosine tRNA ligase 1, cytoplasmic