Adjust Text Size:change font sizechange font sizechange font sizechange font sizechange font sizechange font size

Featured Research

Can we predict who is at risk of facing cognitive issues in PD and address them earlier? These are the questions being pursued by Dr. Goldman of the PDF Research Center at Rush University Medical Center.

Learn More

PDF Grant Programs

Are you interested in furthering Parkinson's science? View PDF's open grant programs.

Learn More


A model in which heat shock protein 90 targets protein-folding clefts: Rationale for a new approach to neuroprotective treatment of protein folding diseases.

PDF's targeted PubMed search provides you with access to journal articles from the last 90 days that may be pertinent to Parkinson's disease research. 

Not what you're looking for? Do you need informational publications about Parkinson's targeted for people living with Parkinson's, caregivers and family members?  Please browse PDF's educational materials and programs - which are all available electronically or in print.  Order for yourself, a loved one or in bulk for your patients or support group.

Exp Biol Med (Maywood) 2014 Jul;

Authors: William B Pratt, Yoshihiro Morishima, Jason E Gestwicki, Andrew P Lieberman, Yoichi Osawa

In an EBM Minireview published in 2010, we proposed that the heat shock protein (Hsp)90/Hsp70-based chaperone machinery played a major role in determining the selection of proteins that have undergone oxidative or other toxic damage for ubiquitination and proteasomal degradation. The proposal was based on a model in which the Hsp90 chaperone machinery regulates signaling by modulating ligand-binding clefts. The model provides a framework for thinking about the development of neuroprotective therapies for protein-folding diseases like Alzheimer's disease (AD), Parkinson's disease (PD), and the polyglutamine expansion disorders, such as Huntington's disease (HD) and spinal and bulbar muscular atrophy (SBMA). Major aberrant proteins that misfold and accumulate in these diseases are "client" proteins of the abundant and ubiquitous stress chaperone Hsp90. These Hsp90 client proteins include tau (AD), ?-synuclein (PD), huntingtin (HD), and the expanded glutamine androgen receptor (polyQ AR) (SBMA). In this Minireview, we update our model in which Hsp90 acts on protein-folding clefts and show how it forms a rational basis for developing drugs that promote the targeted elimination of these aberrant proteins.

PMID: 24990484 [PubMed - as supplied by publisher]

See More

Back to PubMed Articles