Hyperphosphorylation of the Rotavirus NSP5 Protein Is Independent of Serine 67 or NSP2, and the Intrinsic Insolubility of NSP5 Is Regulated by Cellular Phosphatases

Lignende værker

• Hyperphosphorylation of the Rotavirus NSP5 Protein Is Independent of Serine 67, NSP2, or the Intrinsic Insolubility of NSP5 and Is Regulated by Cellular Phosphatases
  af: Sen, Adrish, et al.
  Udgivet: (2006)
• The Formation of Viroplasm-Like Structures by the Rotavirus NSP5 Protein Is Calcium Regulated and Directed by a C-Terminal Helical Domain
  af: Sen, Adrish, et al.
  Udgivet: (2007)
• Uncoupling substrate and activation functions of rotavirus NSP5: Phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation
  af: Eichwald, Catherine, et al.
  Udgivet: (2004)
• Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
  af: Blackhall, J, et al.
  Udgivet: (1997)
• Recombinant Rotaviruses Rescued by Reverse Genetics Reveal the Role of NSP5 Hyperphosphorylation in the Assembly of Viral Factories
  af: Papa, Guido, et al.
  Udgivet: (2019)