Proteostasis and Protein Aggregation in Neurodegeneration – PPAN
NOTE: Starts with the October 2026 Council round submission dates (Cycle I due dates). This study section was evaluated as part of CSR’s ENQUIRE process to align study sections with advances in science. Learn more about ENQUIRE.
The Proteostasis and Protein Aggregation in Neurodegeneration study section reviews applications examining how defects in protein synthesis, folding, degradation and aggregation lead to neurodegeneration. Proposals examining prion mechanisms and prion-like spreading of neurotoxic proteins are also reviewed.
Disorders of interest include Alzheimer’s disease, frontotemporal dementias, tauopathies, synucleinopathies, amyloidosis, TDP-43 proteinopathies, Parkinson’s disease, spinal muscular atrophy, amyotrophic lateral sclerosis and frontotemporal dementias, repeat expansion diseases, spinobulbar muscular atrophy, spinocerebellar, peripheral neuropathy, and Friedreich’s ataxias, and prion diseases. Applications may include studies with cellular and molecular endpoints in vitro, in cells, and/or in vivo including higher vertebrate animal genetic models as well as model organisms such as C. elegans, Drosophila, Yeast and zebrafish.
Review Dates
Topics
- Consequences of disturbances in proteostasis and LLPS in neurodegeneration: abnormal protein folding, aggregation, clearance and spreading in the context of neurodegenerative diseases.
- Delineation of cellular and physiological effects of aggregated proteins/ peptides (e.g., beta amyloid, tau, alpha-synuclein, TDP-43, c9orf72) on neuronal function.
- Characterization of abnormal protein processing associated with neurodegenerative disorders.
- Stress granule biology and compensatory/protective mechanisms
- Dipeptide repeat proteins and their mechanisms of production and toxicity
- Defects in protein synthesis, degradation, folding and posttranslational modifications leading to cell stress and neurodegeneration
- Amplification and transmission of pathogenic protein conformers.
