Molecular Chaperones
Group: 4 #group-4
Relations
- Cellular Stress Response: Molecular chaperones are key components of the cellular stress response, helping cells cope with various stressors that can disrupt protein folding.
- Fold Resistance: Molecular chaperones are proteins that assist in the proper folding of other proteins, helping to increase their fold resistance and prevent misfolding.
- Misfolding: Molecular chaperones are proteins that assist in the proper folding and refolding of other proteins, helping to prevent misfolding and aggregation.
- Protein Folding: Molecular chaperones assist in the proper folding of proteins into their functional three-dimensional structures.
- Molecular Chaperone Machinery: Molecular chaperones work together in a coordinated machinery to facilitate protein folding and prevent aggregation.
- Protein Aggregation: Molecular chaperones can bind to misfolded proteins and prevent their aggregation, which is implicated in various neurodegenerative diseases.
- Protein Quality Control: Molecular chaperones are essential components of the protein quality control system, which ensures the proper folding and degradation of proteins.
- Neurodegenerative Diseases: Dysfunction of molecular chaperones and protein misfolding are associated with the pathogenesis of neurodegenerative diseases like Alzheimer’s and Parkinson’s.
- Protein Misfolding: Molecular chaperones help prevent protein misfolding, which can lead to the formation of toxic protein aggregates.
- Proteostasis: Molecular chaperones play a crucial role in maintaining proteostasis, the balance between protein synthesis, folding, and degradation.
- Heat Shock Proteins: Many molecular chaperones belong to the family of heat shock proteins, which are induced in response to cellular stress.
- Protein Trafficking: Molecular chaperones assist in the proper trafficking and localization of proteins within the cell.
- Chaperone Proteins: Molecular chaperones are a class of chaperone proteins that assist in protein folding and prevent aggregation.