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Appears in Networks 2

In-Edges 7

p(FPLX:HSPA) decreases bp(HBP:misfolding) View Subject | View Object

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

p(FPLX:HSPB) association bp(HBP:misfolding) View Subject | View Object

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

a(CHEBI:radical) increases bp(HBP:misfolding) View Subject | View Object

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

bp(GO:"response to endoplasmic reticulum stress") decreases bp(HBP:misfolding) View Subject | View Object

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

bp(HBP:"non-enzymatic protein modification") increases bp(HBP:misfolding) View Subject | View Object

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

p(FPLX:HSPA) decreases bp(HBP:misfolding) View Subject | View Object

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

p(HGNCGENEFAMILY:"Protein disulfide isomerases") decreases bp(HBP:misfolding) View Subject | View Object

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

Out-Edges 2

bp(HBP:misfolding) association p(FPLX:HSPB) View Subject | View Object

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

bp(HBP:misfolding) increases path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

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

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.