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

Nikolaos Louros; Rob van der Kant; Joost Schymkowitz; Frederic Rousseau

doi:10.1093/bioinformatics/btac126

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

Bioinformatics. 2022 Apr 28;38(9):2636-2638. doi: 10.1093/bioinformatics/btac126.

Authors

Nikolaos Louros^{1

2}, Rob van der Kant^{1

2}, Joost Schymkowitz^{1

2}, Frederic Rousseau^{1

2}

Affiliations

¹ Switch Laboratory, VIB-KU Leuven Center for Brain & Disease Research, 3000 Leuven, Belgium.
² Department of Cellular and Molecular Medicine, KU Leuven, 3000 Leuven, Belgium.

PMID: 35199146
DOI: 10.1093/bioinformatics/btac126

Abstract

Summary: Amyloid 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 implementation: StAmP-DB is freely accessible for queries and downloads at https://stamp.switchlab.org.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amyloid* / chemistry
Humans
Neurodegenerative Diseases*

Substances

Amyloid