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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Zusätzlich bieten wir Ihnen Tyrosyl-tRNA Synthetase Antikörper (67) und Tyrosyl-tRNA Synthetase Proteine (13) und viele weitere Produktgruppen zu diesem Protein an.
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.
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 (zeige FGFR2 ELISA Kits)) 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 (zeige E2F1 ELISA Kits) to upregulate the expression of DNA damage repair genes such as BRCA1 and RAD51 (zeige RAD51 ELISA Kits).
A major difference between the first- and second-generation tRNA synthetases (RSs (zeige GRB10 ELISA Kits)) is that the second-generation RSs (zeige GRB10 ELISA Kits) 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.
Naturally occurring fragments of the two proteins involved in translation, TyrRS and TrpRS (zeige WARS ELISA Kits), have opposing activities on angiogenesis.
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