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Gene Review

GOT2  -  glutamic-oxaloacetic transaminase 2,...

Sus scrofa

 
 
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Disease relevance of GOT2

 

High impact information on GOT2

 

Chemical compound and disease context of GOT2

 

Biological context of GOT2

 

Anatomical context of GOT2

 

Associations of GOT2 with chemical compounds

 

Regulatory relationships of GOT2

 

Other interactions of GOT2

 

Analytical, diagnostic and therapeutic context of GOT2

References

  1. The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Fotheringham, I.G., Dacey, S.A., Taylor, P.P., Smith, T.J., Hunter, M.G., Finlay, M.E., Primrose, S.B., Parker, D.M., Edwards, R.M. Biochem. J. (1986) [Pubmed]
  2. Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions. Cooper, A.J., Bruschi, S.A., Iriarte, A., Martinez-Carrion, M. Biochem. J. (2002) [Pubmed]
  3. Differential effects of heparin on the early and late phases of hepatic ischemia and reperfusion injury in the pig. Liu, W., Pitcher, D.E., Morris, S.L., Pugmire, J.E., Shores, J.T., Ingram, C.E., Glew, R.H., Morris, D.M., Fry, D.E. Shock (1999) [Pubmed]
  4. Selective proteolysis of cytosolic aspartate aminotransferase by a new microbial protease. Nagashima, F., Tanase, S., Higaki, T., Morino, Y., Murao, S., Nishino, T. J. Biochem. (1986) [Pubmed]
  5. Glucose reaction with fumonisin B1 partially reduces its toxicity in swine. Fernández-Surumay, G., Osweiler, G.D., Yaeger, M.J., Hauck, C.C., Hendrich, S., Murphy, P.A. J. Agric. Food Chem. (2004) [Pubmed]
  6. Aspartate aminotransferase-like immunoreactivity as a marker for aspartate/glutamate in guinea pig photoreceptors. Altschuler, R.A., Mosinger, J.L., Harmison, G.G., Parakkal, M.H., Wenthold, R.J. Nature (1982) [Pubmed]
  7. Immunocytochemical localization of aspartate aminotransferase immunoreactivity in cochlear nucleus of the guinea pig. Altschuler, R.A., Neises, G.R., Harmison, G.G., Wenthold, R.J., Fex, J. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  8. Localization of glutaminase-like and aspartate aminotransferase-like immunoreactivity in neurons of cerebral neocortex. Donoghue, J.P., Wenthold, R.J., Altschuler, R.A. J. Neurosci. (1985) [Pubmed]
  9. Contribution to catalysis and stability of the five cysteines in Escherichia coli aspartate aminotransferase. Preparation and properties of a cysteine-free enzyme. Gloss, L.M., Planas, A., Kirsch, J.F. Biochemistry (1992) [Pubmed]
  10. The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes. Kondo, K., Wakabayashi, S., Yagi, T., Kagamiyama, H. Biochem. Biophys. Res. Commun. (1984) [Pubmed]
  11. Effects of poly I:C in porcine iron deficient neutropenia. Gainer, J.H., Guarnieri, J. The Cornell veterinarian. (1985) [Pubmed]
  12. Conformational changes in aspartate aminotransferase. Effect of active site ligands on peptide hydrogen-deuterium exchange. Pfister, K., Sandmeier, E., Berchtold, W., Christen, P. J. Biol. Chem. (1985) [Pubmed]
  13. Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Cyanogen bromide peptides. Sakakibara, R., Kagamiyama, H., Tanase, S., Morino, Y., Wada, H. J. Biol. Chem. (1980) [Pubmed]
  14. Site-specific methylation of a strategic lysyl residue in aspartate aminotransferase. Roberts, W.J., Hubert, E., Iriarte, A., Martinez-Carrion, M. J. Biol. Chem. (1988) [Pubmed]
  15. Refolding of the precursor and mature forms of mitochondrial aspartate aminotransferase after guanidine hydrochloride denaturation. Reyes, A.M., Iriarte, A., Martinez-Carrion, M. J. Biol. Chem. (1993) [Pubmed]
  16. Effects of temperature on the steady-state kinetics and measurement of aspartate aminotransferases. Rej, R., Vanderlinde, R.E. Clin. Chem. (1981) [Pubmed]
  17. Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Tryptic peptides. Kagamiyama, H., Teranishi, K., Tanase, S., Morino, Y., Sakakibara, R., Wada, H. J. Biol. Chem. (1980) [Pubmed]
  18. Resonance Raman spectra of the pyridoxal coenzyme in aspartate aminotransferase. Evidence for pyridine protonation and a novel photochemical H/D exchange at the imine carbon atom. Benecky, M.J., Copeland, R.A., Rava, R.P., Feldhaus, R., Scott, R.D., Metzler, C.M., Metzler, D.E., Spiro, T.G. J. Biol. Chem. (1985) [Pubmed]
  19. The covalent structure of mitochondrial aspartate aminotransferase from chicken. Identification of segments of the polypeptide chain invariant specifically in the mitochondrial isoenzyme. Graf-Hausner, U., Wilson, K.J., Christen, P. J. Biol. Chem. (1983) [Pubmed]
  20. Presequence binding factor-dependent and -independent import of proteins into mitochondria. Murakami, K., Tanase, S., Morino, Y., Mori, M. J. Biol. Chem. (1992) [Pubmed]
  21. Mechanism of the irreversible inhibition of aspartate aminotransferase by the bacterial toxin L-2-amino-4-methoxy-trans-3-butenoic acid. Rando, R.R., Relyea, N., Cheng, L. J. Biol. Chem. (1976) [Pubmed]
  22. Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the alpha-ketoglutarate dehydrogenase complex. Fahien, L.A., MacDonald, M.J., Teller, J.K., Fibich, B., Fahien, C.M. J. Biol. Chem. (1989) [Pubmed]
  23. Regulation of hepatic gluconeogenesis in the guinea pig by fatty acids and ammonia. Jomain-Baum, M., Hanson, R.W. J. Biol. Chem. (1975) [Pubmed]
  24. Different reactivity of mitochondrial and cytoplasmic aspartate aminotransferases toward an affinity labeling reagent analog of the coenzyme. Riva, F., Carotti, D., Barra, D., Giartosio, A., Turano, C. J. Biol. Chem. (1980) [Pubmed]
  25. A spin label substrate analogue as active site-directed modifying agent. Tryptophan 140 of aspartate aminotransferase. Iriarte, A., Martinez-Carrion, M. J. Biol. Chem. (1983) [Pubmed]
  26. Prolactin stimulates transcription of aspartate aminotransferase in prostate cells. Franklin, R.B., Ekiko, D.B., Costello, L.C. Mol. Cell. Endocrinol. (1992) [Pubmed]
  27. Large-scale purification and some properties of the mitochondrial aspartate aminotransferase from pig heart. Barra, D., Bossa, F., Doonan, S., Fahmy, H.M., Martini, F., Hughes, G.J. Eur. J. Biochem. (1976) [Pubmed]
  28. Concomitant purification of three porcine heart mitochondrial enzymes: citrate synthase, aspartate aminotransferase, and malate dehydrogenase. McEvily, A.J., Flint, A.J., Harrison, J.H. Anal. Biochem. (1985) [Pubmed]
  29. Limited proteolysis as a probe of conformational changes in aspartate aminotransferase from Sulfolobus solfataricus. Arnone, M.I., Birolo, L., Giamberini, M., Cubellis, M.V., Nitti, G., Sannia, G., Marino, G. Eur. J. Biochem. (1992) [Pubmed]
  30. The ionization states of the 5'-phosphate group in the various coenzyme forms bound to mitochondrial aspartate aminotransferase. Sanchez-Ruiz, J.M., Iriarte, A., Martinez-Carrion, M. Arch. Biochem. Biophys. (1991) [Pubmed]
  31. Slow-cooling protocols for crystallographic refinement by simulated annealing. Brünger, A.T., Krukowski, A., Erickson, J.W. Acta Crystallogr., A, Found. Crystallogr. (1990) [Pubmed]
  32. Cloning and sequence analysis of a cDNA encoding porcine mitochondrial aspartate aminotransferase precursor. Joh, T., Nomiyama, H., Maeda, S., Shimada, K., Morino, Y. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  33. Coenzyme active site occupancy as an indicator of independence of the subunits of mitochondrial aspartate aminotransferase. Iriarte, A., Farach, H.A., Martinez-Carrion, M. J. Biol. Chem. (1984) [Pubmed]
  34. Differential scanning calorimetry of cytoplasmic aspartate transaminase. Relimpio, A., Iriarte, A., Chlebowski, J.F., Martinez-Carrion, M. J. Biol. Chem. (1981) [Pubmed]
  35. Partial purification and characterization of aspartate aminotransferases from seedling oat leaves. Reed, R.E., Hess, J.L. J. Biol. Chem. (1975) [Pubmed]
 
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