Conserved Arginines at the P-Protein Stalk Binding Site and the Active Site Are Critical for Ribosome Interactions of Shiga Toxins but Do Not Contribute to Differences in the Affinity of the A1 Subunits for the Ribosome

Antzeko izenburuak

• The A1 Subunit of Shiga Toxin 2 Has Higher Affinity for Ribosomes and Higher Catalytic Activity than the A1 Subunit of Shiga Toxin 1
  nork: Basu, Debaleena, et al.
  Argitaratua: (2015)
• Do the A Subunits Contribute to the Differences in the Toxicity of Shiga Toxin 1 and Shiga Toxin 2?
  nork: Basu, Debaleena, et al.
  Argitaratua: (2015)
• Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2
  nork: Chiou, Jia-Chi, et al.
  Argitaratua: (2011)
• Interaction of Ricin and Shiga Toxins with Ribosomes
  nork: Tumer, Nilgun E., et al.
  Argitaratua: (2012)
• Arginine Residues on the Opposite Side of the Active Site Stimulate the Catalysis of Ribosome Depurination by Ricin A Chain by Interacting with the P-protein Stalk
  nork: Li, Xiao-Ping, et al.
  Argitaratua: (2013)