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Amino Acyl-tRNA Synthetases

Known as: RNA Synthetase, Transfer, Amino Acyl tRNA Ligases, Amino Acyl tRNA Synthetases 
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
National Institutes of Health

Related topics

Related topics

20 relations
Activation of Amino AcidsIn BloodProcess of secretionTransfer RNA Aminoacylation
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Narrower (8)

Asparagine-tRNA ligaseCysteine-tRNA ligaseFAAP protein, mouseGlutamine-tRNA ligase
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Broader (3)

Carbon-Oxygen LigasesLigaseRNA, Transfer, Amino Acyl

Papers overview

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Highly Cited
2012
Highly Cited
2012
Leucyl-tRNA Synthetase Is an Intracellular Leucine Sensor for the mTORC1-Signaling Pathway
Amino acids are required for activation of the mammalian target of rapamycin (mTOR) kinase, which regulates protein translation… Expand
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Review
2010
Review
2010
Adding new chemistries to the genetic code.
The development of new orthogonal aminoacyl-tRNA synthetase/tRNA pairs has led to the addition of approximately 70 unnatural… Expand
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Highly Cited
2003
Highly Cited
2003
A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity
We report a systematic RNA interference (RNAi) screen of 5,690 Caenorhabditis elegans genes for gene inactivations that increase… Expand
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Highly Cited
2001
Highly Cited
2001
Expanding the Genetic Code of Escherichia coli
A unique transfer RNA (tRNA)/aminoacyl-tRNA synthetase pair has been generated that expands the number of genetically encoded… Expand
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Review
2000
Review
2000
Aminoacyl-tRNA Synthetases, the Genetic Code, and the Evolutionary Process
SUMMARY The aminoacyl-tRNA synthetases (AARSs) and their relationship to the genetic code are examined from the evolutionary… Expand
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Highly Cited
1993
Highly Cited
1993
OB(oligonucleotide/oligosaccharide binding)‐fold: common structural and functional solution for non‐homologous sequences.
  • A. Murzin
  • The EMBO journal
  • 1993
    • Corpus ID: 33853086
A novel folding motif has been observed in four different proteins which bind oligonucleotides or oligosaccharides… Expand
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Highly Cited
1989
Highly Cited
1989
Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution.
The crystal structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) complexed with its cognate glutaminyl transfer RNA… Expand
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Highly Cited
1989
Highly Cited
1989
Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.
In a significant fraction of the Escherichia coli cytosolic proteins, the N-terminal methionine residue incorporated during the… Expand
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Review
1986
Review
1986
Biosynthesis and metabolism of arginine in bacteria.
INTRODUCTION ...................................................... 315 BIOSYNTHESIS OF ARGININE… Expand
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Highly Cited
1985
Highly Cited
1985
Hydrogen bonding and biological specificity analysed by protein engineering
The role of complementary hydrogen bonding as a determinant of biological specificity has been examined by protein engineering of… Expand
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