StAmP-DB: a platform for structures of polymorphic amyloid fibril cores

• DOI: 10.1093/bioinformatics/btac126
• Publication Date: 2022-02-22T12:32:45Z
• Authors: Nikolaos Louros; Rob van der Kant; Joost Schymkowitz; Frederic Rousseau
• Keywords: Amyloid; 0303 health sciences; 03 medical and health sciences; Humans; Neurodegenerative Diseases

AbstractSummaryAmyloid polymorphism is emerging as a key property that is differentially linked to various conformational diseases, including major neurodegenerative disorders, but also as a feature that potentially relates to complex structural mechanisms mediating transmissibility barriers and selective vulnerability of amyloids. In response to the rapidly expanding number of amyloid fibril structures formed by full-length proteins, we here have developed StAmP-DB, a public database that supports the curation and cross-comparison of experimentally determined three-dimensional amyloid polymorph structures.Availability and implementationStAmP-DB is freely accessible for queries and downloads at https://stamp.switchlab.org.