Mammalian, Yeast, Bacterial, and Chemical Chaperones Reduce Aggregate Formation and Death in a Cell Model of Oculopharyngeal Muscular Dystrophy

This publication has 32 references indexed in Scilit:

• Stress management – heat shock protein-70 and the regulation of apoptosis
  Trends in Cell Biology, 2001
• Cellular Defenses against Unfolded Proteins
  Neuron, 2001
• From Minichaperone to GroEL 2: Importance of Avidity of the Multisite Ring Structure
  Journal of Molecular Biology, 2000
• Intranuclear inclusions in oculopharyngeal muscular dystrophy contain poly(A) binding protein 2
  Annals of Neurology, 2000
• The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro
  Nucleic Acids Research, 1999
• Nuclear Targeting of Mutant Huntingtin Increases Toxicity
  Molecular and Cellular Neuroscience, 1999
• Aggresomes: A Cellular Response to Misfolded Proteins
  Journal of Cell Biology, 1998
• Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy
  Nature Genetics, 1998
• Polyalanine-Based Peptides as Models for Self-Associated β-Pleated-Sheet Complexes
  Biochemistry, 1997
• Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II
  Nucleic Acids Research, 1995