Amyloid fibrils are formed when soluble proteins misfold into highly ordered insoluble fibrillar aggregates which affect various organs and tissues. Tissue deposition of amyloid fibrils (or amyloid deposition) is the main hallmark of a group of disorders called "amyloidoses". Curiously, fibril deposition has been also recorded as a complication in a number of other neurodegenerative or endocrine diseases. To date, amyloidoses are roughly classified, owing to their tremendous heterogeneity.
AmyCo, a freely available collection of amyloidoses and other clinical disorders related to amyloid deposition, classifies 75 diseases into 2 distinct categories: 1) Amyloidosis and 2) Clinical conditions associated with amyloidosis.
Each database entry is annotated with the precursor proteins (causative proteins), co-deposited proteins of amyloid deposits and affected tissues or organs. Database entries are also supplemented with detailed annotation and are linked to ICD-10, MeSH, OMIM, PubMed, AmyPro and UniProtKB databases.
AmyCo is the largest repository containing information about amyloidoses and diseases related to amyloid deposition. It is hoped that it will aid clinical scientists and researchers, in need of a comprehensive resource, referencing biological information on amyloidoses.
|Total Number of Diseases:||75|
|Total Number of Amyloidogenic Proteins:||83|
Nastou, K.C., Nasi, G.I., Tsiolaki, P.L., Litou, Z.I., Iconomidou, V.A.
AmyCo: the Amyloidoses Collection
bioRxiv 479279; doi: https://doi.org/10.1101/479279