Special Issue "Molecular Chaperones: Protein Folding, Proteostasis, and Diseases"
Deadline for manuscript submissions: 15 December 2023 | Viewed by 3487
Interests: protein folding; folding diseases; proteostasis; homeostasis; signal transduction
Special Issues, Collections and Topics in MDPI journals
Special Issue in International Journal of Molecular Sciences: The Day Break of Hormesis
Special Issue in International Journal of Molecular Sciences: Molecular Chaperones 2.0
Special Issue in International Journal of Molecular Sciences: Molecular Chaperones 3.0
Molecular chaperones have been shown to mediate the folding of many post-translational proteins in prokaryotes, archaea, and eukaryotes. The structures of individual molecular chaperones have been elucidated in detail by X-ray crystallography and cryo-electron microscopy. It has also been reported that molecular chaperones are essential for viral replication.
Mammalian molecular chaperones, such as HSP60, HSP70, and HSP90, may exert their physiological functions independently, or co-chaperones may be required. In addition, interactions between multiple chaperones, e.g., HSP70-HOP-HSP90, can lead to new physiological functions.
It has also been reported that incorrect folding of proteins can lead to diseases such as amyloid fibre formation. Furthermore, molecular chaperones have been reported to be involved in various diseases, including various types of cancer. Thus, when homeostasis is not maintained, various diseases can be expected to occur.
This Special Issue welcomes research on the structure and physiological functions of molecular chaperones to clarify how molecular chaperones interact with client proteins, proteostasis in various diseases, etc., and to highlight the impact of molecular chaperones on human health, homeostatic function maintenance, and disease, including the affinity of molecular chaperone inhibitors and various drugs with molecular chaperones and physiological function regulation.
Prof. Dr. Hideaki Itoh
Manuscript Submission Information
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