The dysregulation of protein folding is a hallmark for several diseases. Not surprisingly, molecular chaperones (being custodians of cellular proteostasis) are largely implicated in the pathophysiology of a number of diseases, such as cancers and neurodegenerative diseases. Generally, chaperones have housekeeping functions that include stabilizing nascent polypeptides to ensure that they are correctly folded into their functional native conformations. Under stress conditions, chaperones facilitate the refolding of stress-induced misfolded proteins. Molecular chaperones are particularly interesting because they have a unique ability to associate with a large clientome of target proteins, facilitating their refolding. In addition, they tend to function with specific co-factors that seem to have differential effects on their specific cellular functions. Chaperones are upregulated by stress, thus their physiological roles in cells, as well as their potential application as biomarkers, has increasingly become an interesting focal point in several disease models.
The goal of this Research Topic is to gather research and review articles that report on the roles of molecular chaperones in the progression of model diseases including neurodegenerative, cardiovascular and parasitic diseases, among others. We also anticipate gathering reports that focus on not only on the functional, but also the structural and proteomic aspects of molecular chaperones and how these impact on human diseases. In addition, we also want to gather articles looking into prospects of targeting molecular chaperones with small molecule inhibitors towards the identification of novel therapies.
We welcome research and review articles covering, but not limited to, the following aspects:
• Proteomic profiling of molecular chaperones in disease models
• Characterization of unique molecular chaperone protein domains and impact on disease pathophysiology
• Heat shock proteins and human disease
• Targeting molecular chaperones in novel therapies
• Molecular chaperones as biomarkers
The dysregulation of protein folding is a hallmark for several diseases. Not surprisingly, molecular chaperones (being custodians of cellular proteostasis) are largely implicated in the pathophysiology of a number of diseases, such as cancers and neurodegenerative diseases. Generally, chaperones have housekeeping functions that include stabilizing nascent polypeptides to ensure that they are correctly folded into their functional native conformations. Under stress conditions, chaperones facilitate the refolding of stress-induced misfolded proteins. Molecular chaperones are particularly interesting because they have a unique ability to associate with a large clientome of target proteins, facilitating their refolding. In addition, they tend to function with specific co-factors that seem to have differential effects on their specific cellular functions. Chaperones are upregulated by stress, thus their physiological roles in cells, as well as their potential application as biomarkers, has increasingly become an interesting focal point in several disease models.
The goal of this Research Topic is to gather research and review articles that report on the roles of molecular chaperones in the progression of model diseases including neurodegenerative, cardiovascular and parasitic diseases, among others. We also anticipate gathering reports that focus on not only on the functional, but also the structural and proteomic aspects of molecular chaperones and how these impact on human diseases. In addition, we also want to gather articles looking into prospects of targeting molecular chaperones with small molecule inhibitors towards the identification of novel therapies.
We welcome research and review articles covering, but not limited to, the following aspects:
• Proteomic profiling of molecular chaperones in disease models
• Characterization of unique molecular chaperone protein domains and impact on disease pathophysiology
• Heat shock proteins and human disease
• Targeting molecular chaperones in novel therapies
• Molecular chaperones as biomarkers