Amyloids in Neurodegenerative Diseases
This special issue belongs to the section "Medicinal Chemistry".
Special Issue Information
Dear Colleagues,
Several peptides and proteins possess amino acid sequences that are prone to convert from their native physiological conformation into toxic aggregates. Misfolded, pathologically altered proteins (amyloids) form deposits in distinctive regions of the human central nervous system (CNS) in increasingly common neurodegenerative diseases (NDDs), such as Alzheimer’s, Parkinson’s, and prion diseases. In this Special Issue, we describe the formation of amyloids from precursors and their nucleated polymerization. The mechanisms of generating cellular dysfunction and cell-to-cell transmission of amyloids are also shown. We summarize genetic factors and mutations that determine amyloid formation and toxicity. We show the activity of the complex proteostasis network for degrading and clearing amyloids in the CNS. This Special Issue provides a forum for the dissemination of the most recent results on the formation and structure of different amyloid assemblies and their role in the pathomechanisms of NDDs. We also summarize recent developments of novel therapeutic strategies for combatting currently incurable NDDs.
Prof. Dr. Botond Penke
Guest Editor
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Keywords
- APP processing and Aβ formation
- Folding and misfolding: methods for studying amyloid structures, and aggregation
- Nucleated polymerization of Aβ to oligomers, protofibrils and fibrils
- Tau protein, aggregation to neurofibrillary tangles
- Aβ-tau interactions
- Aβ and tau interaction with proteins, subcellular organelles, and glial cells
- signalization disturbances
- Aβ and tau interactions with membrane lipids
- cell-to-cell transmission
- α-Synuclein, huntingtin, and prion protein
- Proteostasis pathways: amyloid degradation and clearance
- Drug development against amyloids such as Aβ and tau
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Published Papers
Molecules - ISSN 1420-3049