The Role of Heat Shock Proteins: From Molecular Mechanisms to Therapeutics: 2nd Edition
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".
Deadline for manuscript submissions: 20 February 2025 | Viewed by 2129
Special Issue Editor
Interests: cell stress and chaperones; heat shock proteins; cancer; malaria
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Many heat shock proteins (HSPs) are essential for survival and play a critical role as molecular chaperones in maintaining cellular proteostasis through the integration of protein folding and degradation pathways. There have been extensive advances in our understanding of the mechanism by which co-chaperones regulate molecular chaperones. However, it is becoming generally accepted that HSPs have additional cellular functions beyond their role in proteostasis, and we are only just beginning to understand their biological function from a whole-of-organism perspective. HSPs are also linked to a range of different human disorders (e.g., cancer, diabetes, autoimmune disease, neurodegeneration, muscular dystrophies, and chronic heart failure) and infectious diseases (e.g., viral, microbial, and parasitic infections including malaria and trypanosomiasis), with changes in their expression and localization linked to disease pathology. While HSPs are highly conserved from bacteria to humans, structure–function studies are revealing subtle yet distinct differences across species and between normal and diseased cells. Hence, HSPs are now considered bona fide drug-targets in the fight against disease and infection. Contributions to this Special Issue will provide new insights into the mechanisms of action of HSPs, deepen our understanding of their biological role in health and disease, and reveal novel HSP-based therapeutic opportunities, especially innovative drug discovery insights.
Prof. Dr. Gregory Blatch
Guest Editor
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Keywords
- heat shock proteins
- molecular chaperones
- co-chaperones
- protein folding
- chronic diseases
- infectious diseases
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