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Amyloid. 2019 Sep;26(3):112-117. doi: 10.1080/13506129.2019.1603143. Epub 2019 May 16.

AmyCo: the amyloidoses collection.

Author information

1
a Section of Cell Biology and Biophysics, Department of Biology, School of Sciences, National and Kapodistrian University of Athens , Panepistimiopolis , Athens , Greece.

Abstract

Amyloid fibrils are formed when soluble proteins misfold into highly ordered insoluble fibrillar aggregates and affect various organs and tissues. The deposition of amyloid fibrils 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 pathological conditions, including well-known neurodegenerative or endocrine diseases. To date, amyloidoses are roughly classified, owing to their tremendous heterogeneity. In this work, we introduce AmyCo, a freely available collection of amyloidoses and clinical disorders related to amyloid deposition. AmyCo classifies 75 diseases associated with amyloid deposition into two distinct categories, namely 1) amyloidosis and 2) clinical conditions associated with amyloidosis. Each database entry is annotated with the major protein component (causative protein), other components of amyloid deposits and affected tissues or organs. Database entries are also supplemented with appropriate detailed annotation and are referenced to ICD-10, MeSH, OMIM, PubMed, AmyPro and UniProtKB databases. To our knowledge, AmyCo is the first attempt towards the creation of a complete and an up-to-date repository, containing information about amyloidoses and diseases related to amyloid deposition. The AmyCo web interface is available at http://bioinformatics.biol.uoa.gr/amyco .

KEYWORDS:

Amyloid; aggregation; amyloid deposits; amyloidosis; database

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