Lotz, Gregor and Legleiter, Justin (2013) The role of amyloidogenic protein oligomerization in neurodegenerative disease. Neurotherapeutics. ISSN 1878-7479; 1933-7213

Abstract

A common pathological hallmark of proteinconformational
brain diseases is the formation of diseasespecific
protein aggregates. In Alzheimer’s disease, these are
comprised of amyloid-β and Tau as opposed to α-synuclein in
Parkinson’s disease and N-terminal fragments of mutant
huntingtin in Huntington’s disease. Most aggregates also sequester
molecular chaperones, a protein family that assists in
the folding, refolding, stabilization, and processing of client
proteins, including misfolded proteins in brain diseases. Molecular
chaperone modulation has achieved remarkable therapeutic
effects in some cellular and preclinical animal models of
protein-conformational diseases. This has raised hope for
chaperone-based strategies to combat these diseases. Here,
we review briefly the functional diversity and medical significance
ofmolecular chaperones, their therapeutic potential, and
common and specific challenges towards clinical application.

Item Type:	Article
Date Deposited:	01 Feb 2017 00:45
Last Modified:	01 Feb 2017 00:45
URI:	https://oak.novartis.com/id/eprint/9888