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Anna N. Melidoni

Researcher at European Bioinformatics Institute

Publications -  15
Citations -  2626

Anna N. Melidoni is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Embryonic stem cell & Cellular differentiation. The author has an hindex of 8, co-authored 13 publications receiving 2224 citations. Previous affiliations of Anna N. Melidoni include Queen Mary University of London & University of Ioannina.

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An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Yuxiang Jiang, +156 more
- 07 Sep 2016 - 
TL;DR: The second critical assessment of functional annotation (CAFA), a timed challenge to assess computational methods that automatically assign protein function, was conducted by as mentioned in this paper. But the results of the CAFA2 assessment are limited.

Additional file 1 of An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Yuxiang Jiang, +146 more
TL;DR: The second critical assessment of functional annotation (CAFA) conducted, a timed challenge to assess computational methods that automatically assign protein function, revealed that the definition of top-performing algorithms is ontology specific, that different performance metrics can be used to probe the nature of accurate predictions, and the relative diversity of predictions in the biological process and human phenotype ontologies.
Journal ArticleDOI

An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Yuxiang Jiang, +145 more
TL;DR: The second Critical Assessment of Functional Annotation (CAFA) challenge as mentioned in this paper was the first attempt to assess computational methods that automatically assign protein function. And the results of CAFA2 showed that computational function prediction is improving.
Journal ArticleDOI

The complex portal - an encyclopaedia of macromolecular complexes

TL;DR: The IntAct molecular interaction database has created a new, free, open-source, manually curated resource, the Complex Portal (www.ebi.ac.uk/intact/complex), through which protein complexes from major model organisms are being collated and made available for search, viewing and download.