Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography

This publication has 50 references indexed in Scilit:

• The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins
  Biochemical Journal, 1996
• Crystallization and preliminary X‐ray analysis of the monomeric Cu, Zn superoxide dismutase from Escherichia coli
  Protein Science, 1996
• Synthesis and Characterization of a Monomeric Mutant Cu/Zn Superoxide Dismutase with Partially Reconstituted Enzymic Activity
  European Journal of Biochemistry, 1995
• Isolation of an active and heat‐stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli
  FEBS Letters, 1995
• Conserved Patterns in the Cu,Zn Superoxide Dismutase Family
  Journal of Molecular Biology, 1994
• The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
  Cell, 1992
• Assignment of active‐site protons in the ¹H‐NMR spectrum of reduced human Cu/Zn superoxide dismutase
  European Journal of Biochemistry, 1991
• Aspects of the Structure, Function, and Applications of Superoxide Dismutas
  Critical Reviews in Biochemistry, 1987
• Investigation of Cu2Co2SOD and its anion derivatives. Proton NMR and electronic spectra
  Journal of the American Chemical Society, 1985
• The protein data bank: A computer-based archival file for macromolecular structures
  Journal of Molecular Biology, 1977