Welcome to Amyloid Explorer, a public repository for structural analysis of full-length amyloid fibril core structures.

Amyloid Explorer was created through manual curation and automated analysis (using the FoldX force field) of structurally resolved full-length protein amyloid fibrils.

This database contains a full list of amyloid protein entries that provide visual representation of structural and thermodynamic cross-comparisons between amyloid strains. This supports their structural analysis based on similarities in disease type, structural layout and thermodynamic profiling.

Browsing mode supports the generation of user defined datasets of amyloid polymorphs filtered by protein, disease, experimental method and conditions, structure resolution, mutations and depositing authorship.

3D representations of amyloid fibril cores can be viewed and compared through integrated molecular graphics plugin interfaces that are adjusted dynamically on-site, while links are provided to users that support downloadable selections of polymorph subsets. Database entries also contain information on disease-related mutations and experimentally determined aggregation prone regions (APRs).

Users are welcome to submit new amyloid fibril structure entries by using the submit button on the top-right corner of their screen.

For additional information users can contact us at amyloid-explorer@switchlab.org.

By proceeding, you are agreeing with the terms and conditions of use.

References

When using the content of the database, please cite the following:

• Louros N, van der Kant R, Schymkowitz J, Rousseau F (2022) StAmP-DB: A platform for structures of polymorphic amyloid fibril cores. Bioinformatics. doi:10.1093/bioinformatics/btac126
• Van der Kant, R. Louros, N. Schymkowitz, J. and F. Rousseau, Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs. Structure, 2022.
• Duran-Romaña, R., Schymkowitz, J., Rousseau, F. & Louros, N. Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturation. Nature Communications, in press.