Xenopus small heat shock proteins, Hsp30C and Hsp30D, maintain heat- and chemically denatured luciferase in a folding-competent state

Ítems similars

• Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity
  per: Fernando, Pasan, et al.
  Publicat: (2000)
• A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.
  per: Lee, G J, et al.
  Publicat: (1997)
• Proteasome inhibition induces hsp30 and hsp70 gene expression as well as the acquisition of thermotolerance in Xenopus laevis A6 cells
  per: Young, Jordan T. F., et al.
  Publicat: (2009)
• Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family
  per: Svetlov, Maxim S., et al.
  Publicat: (2006)
• HSP90 Interacts with and Regulates the Activity of Heat Shock Factor 1 in Xenopus Oocytes
  per: Ali, Adnan, et al.
  Publicat: (1998)