Protein Misfolding and Aggregation: From Molecular Mechanisms to Human Diseases
A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Biophysics".
Deadline for manuscript submissions: 20 July 2025 | Viewed by 516
Special Issue Editors
Interests: biomolecular condensates; amyloid fibrils; neurodegenerative diseases; intrinsically disordered proteins
Special Issue Information
Dear Colleagues,
Most proteins in the cell need to fold into defined three-dimensional structures to accomplish their evolutionarily derived functions. Protein folding is a nuanced process encoded by, and dependent on, the intrinsic properties of the primary amino acid sequence as well as cellular protein quality control machinery such as chaperons and protein degradation systems. Misfolded proteins can aggregate into toxic oligomers, or amyloid fibrils, and are associated with diseases including Alzheimer’s and Parkinson’s diseases as well as type II diabetes. These amyloid deposits share a common cross-β structure regardless of their primary amino acid sequences. Recent studies have demonstrated biomolecular condensate formation as an additional commonality inherent to some amyloid-forming proteins. The emergent biophysical properties of condensates can modulate protein aggregation; thus, an understanding of the structural and kinetic basis of amyloid formation as well as the protein quality control machinery is important for understanding protein misfolding diseases and the downstream development of therapeutics. This Special Issue calls for diverse and comprehensive overviews that illustrate protein misfolding and neurodegenerative diseases from biophysical, biochemical, or cellular biological perspectives.
Dr. Xinrui Gui
Dr. Jinjun Wu
Guest Editors
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Keywords
- protein aggregation
- amyloid fibrils
- protein quality control
- neurodegenerative diseases
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