bp(HBP:misfolding)

Entity

Name

misfolding

Namespace

HBP

Namespace Version

20190222

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/cfd2ee89d1a71126da8b5f452544b7fe43be67e7/export/hbp-names.belns

HSP70s function in a variety of basic cellular quality control and maintenance processes, such as proper folding of newly synthesized proteins, along with preventing protein misfolding and aggregation through the binding of exposed hydrophobic residues. PubMed:27491084

Our summary (Table 1) points towards specific sHSPs that play a prominent role in misfolding diseases, as judged by frequency of observations, including CRYAB, HSPB1, HSPB3 and HSPB8 (each 7×), HSPB6 (6×), and CRYAA (5×) (Fig. 1). PubMed:27491084

Free radicals-derived protein modification can result in either gain- or loss-of-function due to the protein misfolding or unfolding. PubMed:24563850

The three sensors of ER proteotoxic stress facilitate contra- dictory responses since they either promote cell survival by decreasing the misfolded protein and/or oxidative load, or, if UPR fails, they promote the activation of apoptotic pathways that eventually result in cell death [57]. PubMed:24563850

EPMs alter the targeted proteins, which however remain fully functional, while NEPMs may induce protein unfolding or misfolding resulting in increased proteome instability. PubMed:24563850

HSP70 chaperones have a diverse array of cellular functions but their major role is to ensure correct folding of newly synthesized proteins and to perform the refolding of proteins that are misfolded and/or aggregated. PubMed:24563850

PDI is a redox sensitive chaperone that acts not only as a sensor but also as a protein involved in the processing of oxidized proteins and in preventing misfolding and/or aggregation of proteins. PubMed:24563850

Our summary (Table 1) points towards specific sHSPs that play a prominent role in misfolding diseases, as judged by frequency of observations, including CRYAB, HSPB1, HSPB3 and HSPB8 (each 7×), HSPB6 (6×), and CRYAA (5×) (Fig. 1). PubMed:27491084

In those organismal states (e.g. ageing or diseases) where the chaperone network becomes deregulated, the accumulating non-native, misfolded or unfolded proteins can form (among others) fibrils, amyloids or large amorphous aggregates [15]. PubMed:24563850