Protein Aggregation
Group: 4 #group-4
Relations
- Prions: Prions are associated with the abnormal aggregation of misfolded proteins.
- Folding in Biology: Misfolded proteins can aggregate into insoluble clumps, which can be toxic to cells.
- Chaperone Proteins: Chaperone proteins assist in proper protein folding and can prevent protein aggregation.
- Oxidative Stress: Oxidative stress can promote protein misfolding and aggregation.
- Protein Folding Landscapes: Protein aggregation is often associated with kinetic trapping in local minima on the folding landscape.
- Protein Misfolding: Protein misfolding can lead to the formation of protein aggregates, which can be toxic to cells.
- Amyloid Fibrils: Amyloid fibrils are insoluble fibrous protein aggregates formed during protein aggregation.
- Proteostasis: Proteostasis refers to the cellular mechanisms that maintain protein homeostasis and prevent protein aggregation.
- Fold Resistance: Proteins with low fold resistance are more prone to aggregate, which is a common feature of many protein misfolding diseases.
- Molecular Chaperones: Molecular chaperones can bind to misfolded proteins and prevent their aggregation, which is implicated in various neurodegenerative diseases.
- Neurodegenerative Diseases: Protein aggregation is implicated in various neurodegenerative diseases.
- Misfolding: Misfolding of proteins can lead to the formation of protein aggregates, which are insoluble and can disrupt cellular functions.
- Endoplasmic Reticulum Stress: Endoplasmic reticulum stress can lead to the accumulation of misfolded proteins and protein aggregation.
- Misfolded Proteins: Protein aggregation involves the abnormal accumulation of misfolded proteins.