Stressing out Hsp90 in neurotoxic proteinopathies Journal Article


Authors: Inda, C.; Bolaender, A.; Wang, T.; Gandu, S. R.; Koren, J. 3rd
Article Title: Stressing out Hsp90 in neurotoxic proteinopathies
Abstract: A toxic accumulation of proteins is the hallmark pathology of several neurodegenerative disorders. Protein accumulation is regularly prevented by the network of molecular chaperone proteins, including and especially Hsp90. For reasons not yet elucidated, Hsp90 and the molecular chaperones interact with, but do not degrade, these toxic proteins resulting in the pathogenic accumulation of proteins such as tau, in Alzheimer’s Disease, and α-synuclein, in Parkinson’s Disease. In this review, we describe the associations between Hsp90 and the pathogenic and driver proteins of several neurodegenerative disorders. We additionally describe how the inhibition of Hsp90 promotes the degradation of both mutant and pathogenic protein species in models of neurodegenerative diseases. We also examine the current state of Hsp90 inhibitors capable of crossing the blood-brain barrier; compounds which may be capable of slowing, preventing, and possible reversing neurodegenerative diseases. © 2016 Bentham Science Publishers.
Keywords: dna; hsp90; neurodegenerative disease; α -synuclein
Journal Title: Current Topics in Medicinal Chemistry
Volume: 16
Issue: 25
ISSN: 1568-0266
Publisher: Bentham Science Publishers  
Date Published: 2016-01-01
Start Page: 2829
End Page: 2838
Language: English
PROVIDER: scopus
PMCID: PMC4995127
PUBMED: 27072699
DOI: 10.2174/1568026616666160413141350
DOI/URL:
Notes: Review -- Export Date: 3 October 2016 -- Source: Scopus
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MSK Authors
  1. John Koren
    12 Koren
  2. Tai   Wang
    7 Wang
  3. Srinivasa Reddy Gandu
    1 Gandu