Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils.

By P. Muchowski, Gregor Schaffar, A. Sittler, Erich E. Wanker, M. Hayer-Hartl, F. Hartl. Proceedings of the National Academy of Sciences of the United States of America, 2000

709 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/5b8b7b2d05d50b89bff23f23595a3edaefb46983

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Citations in the corpus

Pathways of cellular proteostasis in aging and disease (2018, background): “In many model systems, exogenous expression of individual chaperone components, such as Hsp70, or up-regulation of multiple chaperones by pharmacologic induction of the stress response has been shown to either prevent toxic aggregation or to direct the formation of less-toxic but still aggregated sp”
Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress (2002, background): “Moreover, aggresomes represent the cell’s response to (nearly) irreversible protein aggregation (e.g., proteins with polyglutamine stretches [Muchowski et al., 2000]); this does not occur with tau protein in transfected cells, which remains either microtubule-bound or highly soluble in the cytosol…”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “In contrast to Hsp104, the molecular chaperones Hsp70 and Hsp40 prevent the assembly of SDS-stable, amyloid-like aggregates of huntingtin, the key disease protein in Huntington's disease, when added during the lag phase of the polymerization reaction [ 19 ].”
Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. (2001, background): “Recently, we have shown in vitro that both Hsp40 and Hsp70 are effective in preventing the formation of SDS-insoluble polyQ-containing fibrillar structures (Muchowski et al., 2000).”
Principles of protein folding, misfolding and aggregation. (2004, background): “[94] Muchowski PJ, Schaffar G, Sittler A, Wanker EE, Hayer-Hartl MK, Hartl FU.”
Modulation of neurodegeneration by molecular chaperones (2005, background): “Several models of polyQ aggregation have been developed in Saccharomyces cerevisiae because chaperones are well characterized in this organism and are highly conserved with their human counterparts, and also because genetic tools are readily available to study the effects of chaperone mutations on”
Converging concepts of protein folding in vitro and in vivo (2009, background): “Interestingly, increasing the levels of molecular chaperones, most prominently members of the Hsp70 family, has been shown to inhibit the formation of such oligomers and to prevent the formation of amyloid aggregates for different disease protein”