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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Asparaginyl-tRNA synthetase

Asparaginyl-tRNA synthetase
Top mentioned proteins: ACID, CAN, Aspartate-tRNA Ligase, V1a, HAD
Papers on Asparaginyl-tRNA synthetase
Brugia malayi Asparaginyl - tRNA Synthetase Stimulates Endothelial Cell Proliferation, Vasodilation and Angiogenesis.
Dhanasekaran et al., Chennai, India. In Plos One, Dec 2015
Prior work showed that the asparaginyl-tRNA synthetase (BmAsnRS) of Brugia malayi, an etiological agent of lymphatic filariasis, acts as a physiocrine that binds specifically to interleukin-8 (IL-8) chemokine receptors.
Flow Analysis of Amino Acids by Using a Newly Developed Aminoacyl-tRNA Synthetase-Immobilized, Small Reactor Column-Based Assay.
Fukada et al., Hiroshima, Japan. In Appl Biochem Biotechnol, Dec 2015
For the recognition of asparagine and lysine, asparaginyl-tRNA synthetase and lysyl-tRNA synthase were immobilized onto microparticles, respectively, and coupled with coloration reagents for spectrophotometric detection.
Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh syndrome.
Riazuddin et al., Lahore, Pakistan. In Plos Genet, Mar 2015
Here we demonstrate association of variants in the mitochondrial asparaginyl-tRNA synthetase NARS2 with human hearing loss and Leigh syndrome.
Two siblings with homozygous pathogenic splice-site variant in mitochondrial asparaginyl-tRNA synthetase (NARS2).
Van Coster et al., Gent, Belgium. In Hum Mutat, Feb 2015
A homozygous missense mutation (c.822G>C) was found in the gene encoding the mitochondrial asparaginyl-tRNA synthetase (NARS2) in two siblings born to consanguineous parents.
Whole exome sequencing reveals mutations in NARS2 and PARS2, encoding the mitochondrial asparaginyl-tRNA synthetase and prolyl-tRNA synthetase, in patients with Alpers syndrome.
Asin-Cayuela et al., Göteborg, Sweden. In Mol Genet Genomic Med, 2015
Alpers syndrome is a progressive neurodegenerative disorder that presents in infancy or early childhood and is characterized by diffuse degeneration of cerebral gray matter.
Virtual screening of traditional Chinese medicine (TCM) database: identification of fragment-like lead molecules for filariasis target asparaginyl-tRNA synthetase.
Coumar et al., Pondicherry, India. In J Mol Model, 2014
In this study, asparaginyl-tRNA synthetase (AsnRS; PDB ID: 2XGT) essential for the protein bio-synthesis in the filarial nematode was used to carry out virtual screening (VS) of plant constituents from traditional Chinese medicine (TCM) database.
Relaxed tRNA specificity of the Staphylococcus aureus aspartyl-tRNA synthetase enables RNA-dependent asparagine biosynthesis.
Sheppard et al., Saratoga Springs, United States. In Febs Lett, 2014
S. aureus does use an asparaginyl-tRNA synthetase (AsnRS) to directly ligate asparagine to tRNA(Asn).
Genetic validation of aminoacyl-tRNA synthetases as drug targets in Trypanosoma brucei.
Phillips et al., Dallas, United States. In Eukaryot Cell, 2014
Here we survey the essentiality of eight Trypanosoma brucei aaRSs by RNA interference (RNAi) gene expression knockdown, covering an enzyme from each major aaRS class: valyl-tRNA synthetase (ValRS) (class Ia), tryptophanyl-tRNA synthetase (TrpRS-1) (class Ib), arginyl-tRNA synthetase (ArgRS) (class Ic), glutamyl-tRNA synthetase (GluRS) (class 1c), threonyl-tRNA synthetase (ThrRS) (class IIa), asparaginyl-tRNA synthetase (AsnRS) (class IIb), and phenylalanyl-tRNA synthetase (α and β) (PheRS) (class IIc).
Aminoacylation of Plasmodium falciparum tRNA(Asn) and insights in the synthesis of asparagine repeats.
Frugier et al., Strasbourg, France. In J Biol Chem, 2014
Here, we studied tRNA(Asn) accumulation as well as the catalytic capacities of the asparaginyl-tRNA synthetase of the parasite in vitro.
The predatory bacterium Bdellovibrio bacteriovorus aspartyl-tRNA synthetase recognizes tRNAAsn as a substrate.
Sheppard et al., Saratoga Springs, United States. In Plos One, 2013
However, despite encoding asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, B. bacteriovorus also contains the amidotransferase GatCAB.
Overproduction of the N-terminal anticodon-binding domain of the non-discriminating aspartyl-tRNA synthetase from Helicobacter pylori for crystallization and NMR measurements.
Songsiriritthigul et al., Bangkok, Thailand. In Protein Expr Purif, 2013
For the human pathogenic bacterium Helicobacter pylori, a gene encoding asparaginyl-tRNA synthetase (AsnRS) is absent whilst an aspartyl-tRNA synthetase (AspRS) aminoacylates both tRNA(Asp) and tRNA(Asn) with aspartate.
Autoantigens act as tissue-specific chemoattractants.
Howard et al., Frederick, United States. In J Leukoc Biol, 2005
Our initial observation that myositis-associated autoantigens, histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, were chemotactic for CC chemokine receptor 5 (CCR5)- and CCR3-expressing leukocytes, while other nonautoantigenic aminoacyl-tRNA synthesases were not, suggested that only self-antigens capable of interacting with receptors on antigen-presenting cells were immunogenic.
Update on myositis-specific and myositis-associated autoantibodies.
Targoff, Oklahoma City, United States. In Curr Opin Rheumatol, 2000
Among the more important developments were identification of a new antisynthetase, reacting with asparaginyl-tRNA synthetase; the detection of antibodies to the tRNA(his) in a over a third of anti-Jo-1 sera; and the description of distinctive features of the histopathology of patients with anti-Jo-1.
Domain-specific recruitment of amide amino acids for protein synthesis.
Söll et al., New Haven, United States. In Nature, 2000
These amide aminoacyl-tRNAs can be formed by the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, respectively.
Anomalous X-ray diffraction with soft X-ray synchrotron radiation.
Kahn et al., Grenoble, France. In Cell Mol Biol Incl Cyto Enzymol, 2000
The anomalous dispersion of an uranium derivative of asparaginyl-tRNA synthetase (hexagonal unit cell; a = 123.4
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