Sarah J. Gibbs

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BACKGROUND Cysteine string protein (CSPalpha) is a synaptic vesicle protein that displays unique anti-neurodegenerative properties. CSPalpha is a member of the conserved J protein family, also called the Hsp40 (heat shock protein of 40 kDa) protein family, whose importance in protein folding has been recognized for many years. Deletion of the CSPalpha in(More)
Several families of proteins called molecular chaperones comprise the cellular machinery that has evolved to maintain protein structure and eliminate misfolded proteins in the cell. In experimental animal models, chaperones have been shown to be powerful inhibitors of neurodegeneration. As such, molecular chaperones represent exciting pharmaceutical targets(More)
In response to a conditioning stress, the expression of a set of molecular chaperones called heat shock proteins is increased. In neurons, stress-induced and constitutively expressed molecular chaperones protect against damage induced by ischemia and neurodegenerative diseases, however the molecular basis of this protection is not known. Here we have(More)
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