Prion Protein Inhibition of Fast Axonal Transport via CK2 Mechanism

Experimental data from cell biological and pharmacological studies in squid axoplasm and primary cultured neurons reveals inhibition of fast axonal transport as a toxic effect of cellular prion protein. The research identifies casein kinase 2 activation as the molecular mechanism, involving phosphorylation of kinesin motor protein subunits. The dataset supports findings published by author Emiliano Zamponi in 2020.

Use Cases

• Analyze the correlation between PrPc exposure levels and measured inhibition of fast axonal transport in neuronal models
• Investigate CK2 activation patterns as a molecular response to PrPc toxicity across experimental conditions
• Model the phosphorylation impact on kinesin and dynein motor proteins using biochemical assay results
• Validate the dying-back neurodegeneration hypothesis by linking transport inhibition data to prion disease pathology

Strengths

• Data originates from controlled cell biological and pharmacological experiments in isolated squid axoplasm
• Findings are peer-reviewed and published, providing a molecular basis for PrPc toxicity on neuronal transport
• Research identifies a specific kinase (CK2) as a novel therapeutic target for prion diseases

Limitations

• Specific data volume, structure, and column details are unavailable for assessment
• Experimental scope is limited to specific models (squid axoplasm, primary cultured neurons), which may not fully represent human in vivo conditions
• Dataset age from 2020 may not reflect the most recent research in the field

Provenance

Source

Dryad digital repository, authored by Emiliano Zamponi.

Collection Method

Data generated from cell biological, pharmacological, and biochemical experiments.

Freshness

Last updated 2020-06-30.