Synthetic “chaperones”: nanoparticle-mediated refolding of thermally denatured proteins

Lignende værker

• Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding
  af: Török, Zsolt, et al.
  Udgivet: (2001)
• Thermally denatured state determines refolding in lipase: Mutational analysis
  af: Ahmad, Shoeb, et al.
  Udgivet: (2009)
• Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins
  af: Nakamoto, Hitoshi, et al.
  Udgivet: (2014)
• Refolding of urea-denatured adenylate kinase.
  af: Zhang, H j, et al.
  Udgivet: (1998)
• The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro.
  af: Guagliardi, A., et al.
  Udgivet: (1994)