The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

ASS1  -  argininosuccinate synthase 1

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ASS

  • The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nucleotide sequence of the normal bovine cDNA for argininosuccinate synthetase and the mutation present in animals with citrullinemia [1].
  • Mice treated with adenoviral vectors expressing argininosuccinate synthase lived significantly longer than untreated animals (11 days vs 1 day; however, the animals did not exhibit normal weight gain during the experiment, indicating that the therapeutic effectiveness of the transducing virus was suboptimal [2].

High impact information on ASS


Chemical compound and disease context of ASS


Biological context of ASS


Anatomical context of ASS


Associations of ASS with chemical compounds


Other interactions of ASS


Analytical, diagnostic and therapeutic context of ASS


  1. Molecular definition of bovine argininosuccinate synthetase deficiency. Dennis, J.A., Healy, P.J., Beaudet, A.L., O'Brien, W.E. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  2. Evaluation of gene therapy for citrullinaemia using murine and bovine models. Patejunas, G., Lee, B., Dennis, J.A., Healy, P.J., Reeds, P.J., Yu, H., Frazer, M., Mull, B., Warman, A.W., Beaudet, A.L., O'Brien, W.E. J. Inherit. Metab. Dis. (1998) [Pubmed]
  3. Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation. Kumar, S., Lennane, J., Ratner, S. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  4. Regulation of endothelial argininosuccinate synthase expression and NO production by an upstream open reading frame. Pendleton, L.C., Goodwin, B.L., Solomonson, L.P., Eichler, D.C. J. Biol. Chem. (2005) [Pubmed]
  5. Argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells. Goodwin, B.L., Solomonson, L.P., Eichler, D.C. J. Biol. Chem. (2004) [Pubmed]
  6. Prenatal diagnosis of bovine citrullinaemia. Healy, P., Dennis, J., Rawlinson, R., Andersson, L. Res. Vet. Sci. (1993) [Pubmed]
  7. Caveolar localization of arginine regeneration enzymes, argininosuccinate synthase, and lyase, with endothelial nitric oxide synthase. Flam, B.R., Hartmann, P.J., Harrell-Booth, M., Solomonson, L.P., Eichler, D.C. Nitric Oxide (2001) [Pubmed]
  8. Biosynthesis of urea. Molecular and regulatory properties of crystalline argininosuccinate synthetase. Rochovansky, O., Kodowaki, H., Ratner, S. J. Biol. Chem. (1977) [Pubmed]
  9. Hepatic synthesis of canavaninosuccinate from ureidohomoserine and aspartate, and its conversion to guanidinosuccinate. Koller, A., Aldwin, L., Natelson, S. Clin. Chem. (1975) [Pubmed]
  10. Measurement of positional isotope exchange rates in enzyme-catalyzed reactions by fast atom bombardment mass spectrometry: application to argininosuccinate synthetase. Hilscher, L.W., Hanson, C.D., Russell, D.H., Raushel, F.M. Biochemistry (1985) [Pubmed]
  11. Immobilization of urea cycle enzymes. II. Characterization of immobilized argininosuccinate synthetase. Miura, Y., Miyamoto, K., Urabe, H., Nagata, C., Hane, Y. J. Biomed. Mater. Res. (1977) [Pubmed]
  12. Effect of age on activities of urea cycle enzymes in the bovine. Boling, J.A., Nuzum, C.T. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (1975) [Pubmed]
  13. Toxicity and adaptive immune response to intracellular transgenes delivered by helper-dependent vs. first generation adenoviral vectors. Mian, A., Guenther, M., Finegold, M., Ng, P., Rodgers, J., Lee, B. Mol. Genet. Metab. (2005) [Pubmed]
WikiGenes - Universities