Advances in Research on Chaperones and Proteostasis
A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Cell Biology and Pathology".
Deadline for manuscript submissions: closed (31 January 2024) | Viewed by 226
Special Issue Editor
Interests: extracellular proteostasis; extracellular chaperones; amyotrophic lateral sclerosis; neuroimmunology; flow cytometry; purinergic signalling
Special Issue Information
Dear Colleagues,
Proteostasis (protein homeostasis) encompasses protein synthesis, folding, localization, and degradation, and plays an essential role in organismal function and viability. Molecular chaperones are key players in maintaining proteostasis in both the intra- and extracellular environments and prevent undesirable protein–protein interactions. Misfolding proteins may self-interact to form either unstructured (amorphous) or β-sheet-rich fibrillar (amyloid) aggregates, and chaperones play important roles in preventing these interactions or the clearance of aggregates. The dysfunction of proteostasis plays a role in a number of diseases, including cancer and diabetes, but most notably in neurodegenerative diseases, including Alzheimer’s disease, Parkinson’s disease, and amyotrophic lateral sclerosis.
Advancement of our understanding of chaperones and proteostasis highlights potential therapeutic targets for the treatment of these diseases. However, prior to this, we need to further advance our knowledge of both intracellular and extracellular proteostasis and the roles of molecular chaperones in these systems. Therefore, we cordially invite contributions to this Issue of any studies focused on proteostasis, from basic research to clinical applications.
Dr. Nicholas J. Geraghty
Guest Editor
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Keywords
- chaperones
- proteostasis
- cellular function
- protein folding
- aggregation
- cytotoxicity
- neurodegeneration
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