Misfolding §

Group: 4 #group-4

Relations §

• Proteasome Dysfunction: Misfolded proteins can overwhelm the proteasome, which is responsible for degrading damaged or misfolded proteins, leading to their accumulation.
• Prion Diseases: Prion diseases, such as Creutzfeldt-Jakob disease, are caused by the misfolding of prion proteins, which can propagate their abnormal conformation to other prion proteins.
• Molecular Chaperones: Molecular chaperones are proteins that assist in the proper folding and refolding of other proteins, helping to prevent misfolding and aggregation.
• Amyloid Fibrils: Misfolded proteins can form amyloid fibrils, which are insoluble and can accumulate in tissues, causing various diseases.
• Neurodegenerative Diseases: Protein misfolding and aggregation are implicated in the pathogenesis of many neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, and Huntington’s diseases.
• Endoplasmic Reticulum Stress: Misfolded proteins can accumulate in the endoplasmic reticulum, leading to endoplasmic reticulum stress and the activation of the unfolded protein response.
• Protein Aggregation: Misfolding of proteins can lead to the formation of protein aggregates, which are insoluble and can disrupt cellular functions.
• Protein Folding: Protein misfolding is a deviation from the normal protein folding process, which is essential for proper protein structure and function.
• Chaperone Proteins: Chaperone proteins assist in the proper folding of proteins and can help prevent misfolding and aggregation.
• Oxidative Stress: Oxidative stress can promote protein misfolding and aggregation, contributing to the development of various diseases.
• Protein Folding: Misfolding of proteins can lead to the formation of insoluble aggregates.