S-Nitrosation of Glutathione Transferase P1-1 Is Controlled by the Conformation of a Dynamic Active Site Helix

Lignende værker

• Impact of domain interchange on conformational stability and equilibrium folding of chimeric class μ glutathione transferases
  af: Luo, Jiann-Kae, et al.
  Udgivet: (2002)
• The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1.
  af: Nathaniel, Chris, et al.
  Udgivet: (2003)
• Characterization of bromosulphophthalein binding to human glutathione S-transferase A1-1: thermodynamics and inhibition kinetics
  af: Kolobe, Doris, et al.
  Udgivet: (2004)
• Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site
  af: Weichsel, Andrzej, et al.
  Udgivet: (2010)
• Electrostatic interactions affecting the active site of class sigma glutathione S-transferase.
  af: Stevens, J M, et al.
  Udgivet: (2000)