Mechanism of Cu,Zn-Superoxide Dismutase Activation by the Human Metallochaperone hCCS

This publication has 36 references indexed in Scilit:

• X-ray Crystallographic and Analytical Ultracentrifugation Analyses of Truncated and Full-Length Yeast Copper Chaperones for SOD (LYS7): A Dimer−Dimer Model of LYS7−SOD Association and Copper Delivery^,
  Biochemistry, 2000
• Crystal Structure of the Second Domain of the Human Copper Chaperone for Superoxide Dismutase^,
  Biochemistry, 2000
• Intracellular copper routing: the role of copper chaperones
  Trends in Biochemical Sciences, 2000
• Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase
  Science, 1999
• Alternative Routes for Entry of HgX₂ into the Active Site of Mercuric Ion Reductase Depend on the Nature of the X Ligands
  Biochemistry, 1999
• Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase
  Biochemistry, 1989
• Mutagenesis of the N- and C-terminal cysteine pairs of Tn501 mercuric ion reductase: consequences for bacterial detoxification of mercurials
  Biochemistry, 1989
• Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry
  Biochemistry, 1989
• The determination of iron with 1,10-phenanthroline
  Talanta, 1961
• Bathophenanthrolinedisulphonic acid and bathocuproinedisulphonic acid, water soluble reagents for iron and copper
  Talanta, 1961