The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate.

Lignende værker

• Proteolytic cleavage of initiation factor eIF-4 gamma in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs.
  af: Ohlmann, T, et al.
  Udgivet: (1995)
• The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E.
  af: Ohlmann, T, et al.
  Udgivet: (1996)
• Control of eIF-2 phosphatase activity in rabbit reticulocyte lysate.
  af: Safer, B, et al.
  Udgivet: (1979)
• Cellular stress in xenopus kidney cells enhances the phosphorylation of eukaryotic translation initiation factor (eIF)4E and the association of eIF4F with poly(A)-binding protein.
  af: Fraser, C S, et al.
  Udgivet: (1999)
• Human Rhinovirus 2A Proteinase Cleavage Sites in Eukaryotic Initiation Factors (eIF) 4GI and eIF4GII Are Different
  af: Gradi, Alessandra, et al.
  Udgivet: (2003)