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sod1-b  -  superoxide dismutase 1, soluble

Xenopus laevis

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Disease relevance of sod1-a


High impact information on sod1-a


Biological context of sod1-a


Anatomical context of sod1-a

  • A PCR product was generated from embryonic chicken spinal cord cDNA using primers designed to conserved regions of the human and bovine amino and carboxyl-terminal coding sequences of the Cu,Zn superoxide dismutase (SOD1, EC gene [7].

Analytical, diagnostic and therapeutic context of sod1-a


  1. Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase. Bordo, D., Matak, D., Djinovic-Carugo, K., Rosano, C., Pesce, A., Bolognesi, M., Stroppolo, M.E., Falconi, M., Battistoni, A., Desideri, A. J. Mol. Biol. (1999) [Pubmed]
  2. Chaperonins dependent increase of Cu,Zn superoxide dismutase production in Escherichia coli. Battistoni, A., Carri, M.T., Steinkühler, C., Rotilio, G. FEBS Lett. (1993) [Pubmed]
  3. Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. Evidence for co-ordinated mutation of charged amino acid residues. Desideri, A., Falconi, M., Polticelli, F., Bolognesi, M., Djinovic, K., Rotilio, G. J. Mol. Biol. (1992) [Pubmed]
  4. Copper-dependent metabolism of Cu,Zn-superoxide dismutase in human K562 cells. Lack of specific transcriptional activation and accumulation of a partially inactivated enzyme. Steinkühler, C., Carrì, M.T., Micheli, G., Knoepfel, L., Weser, U., Rotilio, G. Biochem. J. (1994) [Pubmed]
  5. Developmental expression of Cu,Zn superoxide dismutase in Xenopus. Constant level of the enzyme in oogenesis and embryogenesis. Montesano, L., Carrì, M.T., Mariottini, P., Amaldi, F., Rotilio, G. Eur. J. Biochem. (1989) [Pubmed]
  6. Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis. Schininà, M.E., Barra, D., Bossa, F., Calabrese, L., Montesano, L., Carrì, M.T., Mariottini, P., Amaldi, F., Rotilio, G. Arch. Biochem. Biophys. (1989) [Pubmed]
  7. Characterisation of the chicken Cu,Zn superoxide dismutase gene. Stanton, J.L., Wilton, S.D., Laing, N.G. DNA Seq. (1996) [Pubmed]
  8. Identification of the residues responsible for the alkaline inhibition of Cu,Zn superoxide dismutase: a site-directed mutagenesis approach. Polticelli, F., Battistoni, A., O'Neill, P., Rotilio, G., Desideri, A. Protein Sci. (1996) [Pubmed]
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