• Asymmetric behavior of archaeal prolyl-tRNA synthetase 

      Ambrogelly, A.; Kamtekar, S.; Stathopoulos, C.; Kennedy, D.; Söll, D. (2005)
      Archaeal prolyl-tRNA synthetases differ from their bacterial counterparts: they contain an additional domain (about 70 amino acids) appended to the carboxy-terminus and lack an editing domain inserted into the class II ...
    • The complex evolutionary history of aminoacyl-tRNA synthetases 

      Chaliotis A., Vlastaridis P., Mossialos D., Ibba M., Becker H.D., Stathopoulos C., Amoutzias G.D. (2017)
      Aminoacyl-tRNA synthetases (AARSs) are a superfamily of enzymes responsible for the faithful translation of the genetic code and have lately become a prominent target for synthetic biologists. Our largescale analysis of > ...