Molecular Chaperones in Neurodegenerative Diseases: Mechanistic Role and Therapeutic Potential
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biophysics: Structure, Dynamics, and Function".
Deadline for manuscript submissions: 31 March 2026 | Viewed by 16
Special Issue Editor
Special Issue Information
Dear Colleagues,
Molecular chaperones regulate multiple aspects of protein processing in normal and disease conditions. In particular, during normal conditions, heat shock proteins (Hsps), such as molecular chaperones Hsp90 and Hsp70, are involved in protein folding and degradation. In abnormal conditions, mutation or posttranslational modification of a disease-associated protein leads to changes in chaperone complex processing, protein misfolding, and aggregation. A better understanding of the role of these chaperones and their co-chaperones in neurodegenerative diseases will provide mechanistic insights into disease progression and potentially lead to new therapeutic options. The focus of this special issue is on the mechanistic and therapeutic potential of molecular chaperones in Alzheimer's disease, Parkinson’s disease, Huntington's disease, Amyotrophic Lateral Sclerosis, and other neurodegenerative disorders.
Dr. Umesh Kumar Jinwal
Guest Editor
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Keywords
- molecular chaperones
- neurodegenerative diseases
- Hsp90
- Hsp70
- Alzheimer's Disease
- Parkinson’s Disease
- Huntington's disease
- amyotrophic lateral sclerosis
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