Protein Aggregation—Accident, Threat or Organized Assembly?
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".
Deadline for manuscript submissions: 15 March 2025 | Viewed by 344
Special Issue Editor
Interests: protein structure and function; protein folding; protein-protein interactions; protein dynamics; type III secretion system; bacterial pathogens; non-coding RNA structure; protein overexpression
Special Issue Information
Dear Colleagues,
Most cellular processes are thought to be coordinated by supramolecular assemblies of well-folded proteins interacting accurately and specifically with one another. When this assembly loses its specificity, mostly comprises a single protein component, is often misfolded, and exhibits limited solubility, it is characterized as aggregation. Protein aggregation is implicated in the pathology of several diseases (e.g., amyloid formation in neurodegenerative diseases). It can result from the overexpression of proteins and potentially act as a protective measure against undesirable, aberrant, or toxic proteins in bacteria (inclusion bodies), but it could also represent a method of compartmentalizing cellular processes in membrane-less “phase-separated” organelles. This Special Issue aims to illuminate this “dark side” of protein intracellular assembly at the biochemical/biophysical level as well as the cellular and organismal level.
Submissions of both original research and review articles are welcome. Manuscripts focusing on the mechanistic aspects of protein aggregation and subcellular localization and organization are particularly encouraged.
Dr. Efstratios Mylonas
Guest Editor
Manuscript Submission Information
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Keywords
- protein aggregation
- protein misfolding
- amyloids
- inclusion bodies
- phase separation
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