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Gene Review

WARS  -  tryptophanyl-tRNA synthetase

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Disease relevance of WARS


Psychiatry related information on WARS

  • Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease [2].

High impact information on WARS


Biological context of WARS


Anatomical context of WARS


Associations of WARS with chemical compounds


Physical interactions of WARS


Other interactions of WARS


Analytical, diagnostic and therapeutic context of WARS


  1. A mammalian tryptophanyl-tRNA synthetase shows little homology to prokaryotic synthetases but near identity with mammalian peptide chain release factor. Garret, M., Pajot, B., Trézéguet, V., Labouesse, J., Merle, M., Gandar, J.C., Benedetto, J.P., Sallafranque, M.L., Alterio, J., Gueguen, M. Biochemistry (1991) [Pubmed]
  2. Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease. Paley, E.L., Smelyanski, L., Malinovskii, V., Subbarayan, P.R., Berdichevsky, Y., Posternak, N., Gershoni, J.M., Sokolova, O., Denisova, G. Mol. Immunol. (2007) [Pubmed]
  3. VE-cadherin links tRNA synthetase cytokine to anti-angiogenic function. Tzima, E., Reader, J.S., Irani-Tehrani, M., Ewalt, K.L., Schwartz, M.A., Schimmel, P. J. Biol. Chem. (2005) [Pubmed]
  4. Structure-activity relationships in tryptophanyl transfer ribonucleic acid synthetase from beef pancreas. Influence of the alkylation of the sulfhydryl groups on the dimer-monomer equilibrium. Iborra, F., Labouesse, B., Labouesse, J. J. Biol. Chem. (1975) [Pubmed]
  5. Molecular aspects of the inactivation of tryptophanyl transfer ribonucleic acid synthetase by N-ethylmaleimide. Iborra, F., Gros, C., Labouesse, B., Labouesse, J. J. Biol. Chem. (1975) [Pubmed]
  6. Effects of the ligands of beef tryptophanyl-tRNA synthetase on the elementary steps of the tRNA(Trp) aminoacylation. Merle, M., Trezeguet, V., Gandar, J.C., Labouesse, B. Biochemistry (1988) [Pubmed]
  7. Substrate depletion analysis as an approach to the pre-steady-state anticooperative kinetics of aminoacyl adenylate formation by tryptophanyl-tRNA synthetase from beef pancreas. Merle, M., Graves, P.V., Labouesse, B. Biochemistry (1984) [Pubmed]
  8. Mutual conformational changes of tryptophanyl-tRNA synthetase and tRNATrp in the course of their specific interaction. Beresten, S., Scheinker, V., Favorova, O., Kisselev, L. Eur. J. Biochem. (1983) [Pubmed]
  9. Tryptophanyl-tRNA synthetase in cell lines resistant to tryptophan analogs. Paley, E.L., Baranov, V.N., Alexandrova, N.M., Kisselev, L.L. Exp. Cell Res. (1991) [Pubmed]
  10. The effect of tRNA and tryptophanyl adenylate on limited proteolysis of beef pancreas tryptophanyl-tRNA synthetase. Scheinker, V.S., Beresten, S.F., Degtyarev, S.K., Kisselev, L.L. Nucleic Acids Res. (1979) [Pubmed]
  11. Affinity labelling of tryptophanyl-tRNA synthetase with mesitoyl-AMP. Madoyan, I.A., Favorova, O.O., Kovaleva, G.K., Sokolova, N.I., Shabarova, Z.A., Kisselev, L.L. FEBS Lett. (1981) [Pubmed]
  12. P1,P3-bis(5'-adenosyl)triphosphate (Ap3A) as a substrate and a product of mammalian tryptophanyl-tRNA synthetase. Merkulova, T., Kovaleva, G., Kisselev, L. FEBS Lett. (1994) [Pubmed]
  13. Carbohydrates in mammalian tryptophanyl-tRNA synthetase. Kovaleva, G.K., Zheltova, A.O., Nikitushkina, T.V., Egorov, T.A., Musoljamov, A.C.h., Kisselev, L.L. FEBS Lett. (1992) [Pubmed]
  14. Nucleoside triphosphatase activity associated with the N-terminal domain of mammalian tryptophanyl-tRNA synthetase. Kovaleva, G., Nikitushkina, T., Kisselev, L. FEBS Lett. (1993) [Pubmed]
  15. Bovine tryptophanyl-tRNA synthetase and glyceraldehyde-3-phosphate dehydrogenase form a complex. Filonenko, V.V., Beresten, S.F., Rubikaite, B.I., Kisselev, L.L. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  16. Bovine tryptophanyl-tRNA synthetase. A zinc metalloenzyme. Kisselev, L.L., Favorova, O.O., Nurbekov, M.K., Dmitriyenko, S.G., Engelhardt, W.A. Eur. J. Biochem. (1981) [Pubmed]
  17. Anticooperative binding of L-tryptophan to tryptophanyl-tRNA synthetase from beef pancreas. Study at equilibrium by dialysis and changes in spectroscopic properties. Graves, P.V., Mazat, J.P., Juguelin, H., Labouesse, J., Labouesse, B. Eur. J. Biochem. (1979) [Pubmed]
  18. Binding stoichiometry of tRNATrp and tryptophanyl-tRNA synthetase from bovine pancreas under pH conditions of maximum activity. Analysis by ultracentrifugation, fluorescence quenching and chemical modification. Fournier, M., Plantard, C., Labouesse, B., Labouesse, J. Biochim. Biophys. Acta (1987) [Pubmed]
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