Serum Amyloid A 2.2 Refolds into a Octameric Oligomer that Slowly Converts to a More Stable Hexamer

Lignende værker

• Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature
  af: Ye, Zhuqiu, et al.
  Udgivet: (2011)
• Pathogenic Serum Amyloid A 1.1 Shows a Long Oligomer-rich Fibrillation Lag Phase Contrary to the Highly Amyloidogenic Non-pathogenic SAA2.2
  af: Srinivasan, Saipraveen, et al.
  Udgivet: (2013)
• Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer
  af: Wang, Limin, et al.
  Udgivet: (2005)
• Characterization of the Oligomerization and Aggregation of Human Serum Amyloid A
  af: Patke, Sanket, et al.
  Udgivet: (2013)
• Influence of the Carboxy-Terminus of Serum Amyloid A On Protein Oligomerization, Misfolding, and Fibril Formation
  af: Patke, Sanket, et al.
  Udgivet: (2012)