Protein Self-Assembly in Diseases and Function
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".
Deadline for manuscript submissions: 30 June 2025 | Viewed by 19
Special Issue Editors
Interests: protein folding; protein aggregation; amyloid; diabetes; proteinopathies; proteostasis; protein trafficking; ER quality control; disulfide bonds; autophagy
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Protein self-assembly is central to the pathogenesis of a wide range of degenerative diseases, including Alzheimer's, Parkinson's, and type 2 diabetes. These aberrant protein conformations (called amyloids) can disrupt cellular homeostasis, leading to cell death and tissue degeneration. Over the past two decades, there has been accumulating evidence of functional amyloids involved in a beneficial role in the host organism rather than causing diseases. This idea has been further reinforced with the emergence of biomolecular condensation events in cells that are transient (mostly functional) self-assembled structures involving proteins and other biomolecules like RNA. This Special Issue seeks to illuminate the underlying mechanisms driving protein aggregation and condensation. We aim to address the following critical questions: (1) Why are certain cell types more susceptible to proteinopathies than others? (2) What molecular factors underly the formation of biomolecular condensates? (3) How do cells respond to the beneficial versus toxic effects of aggregated proteins? By understanding these fundamental processes, novel therapeutic targets can be identified to promote or prevent protein self-assembly in cells. We invite submissions of original research and review articles that contribute to our understanding of protein folding, misfolding, and aggregation.
Dr. Anoop Arunagiri
Dr. Srivastav Ranganathan
Guest Editors
Manuscript Submission Information
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Keywords
- protein folding
- protein aggregation
- amyloids
- biomolecular condensates
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