Mechanism of small heat shock protein function in vivo. A knock-in mouse model demonstrates that the R49C mutation in αA-crystallin enhances protein insolubility and cell death.

Ítems similars

• Comparative Proteomic Analysis Identifies Age-Dependent Increases in the Abundance of Specific Proteins after Deletion of the Small Heat Shock Proteins αA- and αB-Crystallin
  per: Andley, Usha P., et al.
  Publicat: (2013)
• αA-CRYSTALLIN ASSOCIATES WITH α6 INTEGRIN RECEPTOR COMPLEXES AND REGULATES CELLULAR SIGNALING
  per: Menko, A. Sue, et al.
  Publicat: (2010)
• In Vivo Substrates of the Lens Molecular Chaperones αA-Crystallin and αB-Crystallin
  per: Andley, Usha P., et al.
  Publicat: (2014)
• Autophagy and UPR in alpha-crystallin mutant knock-in mouse models of hereditary cataracts
  per: Andley, Usha P., et al.
  Publicat: (2015)
• In Vivo Lens Deficiency of the R49C αA-Crystallin Mutant
  per: Andley, Usha P., et al.
  Publicat: (2010)