An intermediate step in the recognition of tRNA Asp by aspartyl-tRNA synthetase 1 1Edited by J. Doudna

This publication has 28 references indexed in Scilit:

• Crystals of Thermus thermophilus tRNA^Asp Complexed with its Cognate Aspartyl-tRNA Synthetase Have a Solvent Content of 75%. Comparison with Other Aminoacylation Systems
  Acta Crystallographica Section D-Biological Crystallography, 1998
• Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
  Acta Crystallographica Section D-Biological Crystallography, 1998
• Existence of Two Distinct Aspartyl-tRNA Synthetases in Thermus thermophilus. Structural and Biochemical Properties of the Two Enzymes^†
  Biochemistry, 1997
• Structural and functional considerations of the aminoacylation reaction
  Trends in Biochemical Sciences, 1997
• New applications of simulated annealing in X-ray crystallography and solution NMR
  Structure, 1997
• Identity of Prokaryotic and Eukaryotic tRNA^Asp for Aminoacylation by Aspartyl-tRNA Synthetase from Thermus thermophilus
  Biochemistry, 1996
• The 2.9 Å Crystal Structure of T. thermophilus Seryl-tRNA Synthetase Complexed with tRNA ^Ser
  Science, 1994
• The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.
  The EMBO Journal, 1994
• Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase
  Nature, 1993
• Recognition of tRNAs by aminoacyl-tRNA synthetases.
  The FASEB Journal, 1993