Protein Misfolding & Aggregation

Protein aggregation is observed in a number of neurodegenerative disorders, including Alzheimer’s disease, Huntington’s disease, and Parkinson’s disease. In PD, misfolded alpha-synuclein is found in aggregates. These protein aggregates are a characteristic clinical feature of PD, though it remains unclear whether protein aggregation is a protective measure or pathogenic mechanism. Dysfunction of molecular chaperones, which ordinarily function to prevent newly synthesized proteins from misfolding and aggregating, has also been hypothesized to play a role in PD.

10 Mar 2009 10:29 AM EST
Expression of Hsp70 was shown to prevent dopaminergic neuronal loss associated with alpha-synuclein in Drosophila and interference with endogenous chaperone activity accelerated alpha-synuclein toxicity. ... 
Hot Topics@SfN 2009
19 Oct 2009
Intracellular levels of APP (amyloid precursor protein) holoprotein were shown to be modulated by iron by a mechanism that is similar to the translation control of the ferritin L- and H mRNAs by ... 
18 Sep 2009
I am interested in the last bullet point raised from the MJFF meeting. It is an interesting question related to the MJFF  Target Validation program. MJFF has funded work on several intriguing ... 
11 Sep 2009
I am very interested in ideas that have been discussed around how to develop "two-hit" models for PD.  While genetic models have been demonstrated to be extremely useful for certain experiments ... 
30 Jun 2009
The proteostasis mechanisms regulate the amount of misfolded proteins (eg, alpha-synuclein) to limit the damage caused by aggregates. In this group, members are encouraged to participate in ... 
10 Jun 2009
This group aims to promote interactions, collaborations and the exchange of ideas of those members interested in developing or characterizing genetic disease models, particularly mouse models. ...