A binding motif for Hsp90 in the A chains of ADP-ribosylating toxins that move from the endoplasmic reticulum to the cytosol

Eitemau Tebyg

• HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol
  gan: Burress, Helen, et al.
  Cyhoeddwyd: (2019)
• Hsp90 Is Required for Transfer of the Cholera Toxin A1 Subunit from the Endoplasmic Reticulum to the Cytosol
  gan: Taylor, Michael, et al.
  Cyhoeddwyd: (2010)
• Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide
  gan: Krukenberg, Kristin A, et al.
  Cyhoeddwyd: (2009)
• The Cholera Toxin A1(3) Subdomain Is Essential for Interaction with ADP-Ribosylation Factor 6 and Full Toxic Activity but Is Not Required for Translocation from the Endoplasmic Reticulum to the Cytosol
  gan: Teter, Ken, et al.
  Cyhoeddwyd: (2006)
• Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation
  gan: Banerjee, Tuhina, et al.
  Cyhoeddwyd: (2016)