The fibril_one on‐line database: Mutations, experimental conditions, and trends associated with amyloid fibril formation

The association of amyloid fibril formation with a number of important diseases, and the extensive study of this process in vitro, has resulted in a large literature containing a vast amount of information about the fibril formation process. This includes mutations and experimental conditions that p...

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Bibliographic Details
Published in:Protein science 2002-07, Vol.11 (7), p.1862-1866
Main Authors: Siepen, Jennifer A., Westhead, David R.
Format: Article
Language:English
Subjects:
Amyloid beta-Peptides - metabolism
Amyloidosis
Databases, Protein
For the Record
Humans
Internet
MySQL
pathogenic mutations
protein misfolding
protein stability
Web interface
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Summary:The association of amyloid fibril formation with a number of important diseases, and the extensive study of this process in vitro, has resulted in a large literature containing a vast amount of information about the fibril formation process. This includes mutations and experimental conditions that promote or protect against fibril formation. A database (fibril_one) was designed to hold information relating to the formation of fibrils. It was populated by extensive searches of the literature and other databases. A powerful World Wide Web query interface to the database was developed, enabling a simple and effective method to view amyloidogenic mutations associated with specific proteins. The Web interface was used to identify trends in the data. This revealed that mutations promoting fibril formation through altered folding tend to be associated with destabilization of the native fold. In particular, tendancies of mutations to disrupt the native secondary structure and packing in the hydrophobic core were discovered to be significant. Query access to the database is available freely on the World Wide Web at http://www.bioinformatics.leeds.ac.uk/group/online/fibril_one.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.0204302