| Literature DB >> 31713636 |
András Hatos1, Borbála Hajdu-Soltész2, Alexander M Monzon1, Nicolas Palopoli3, Lucía Álvarez4, Burcu Aykac-Fas5, Claudio Bassot6, Guillermo I Benítez3, Martina Bevilacqua1, Anastasia Chasapi7, Lucia Chemes4,8, Norman E Davey9, Radoslav Davidović10, A Keith Dunker11, Arne Elofsson6, Julien Gobeill12, Nicolás S González Foutel4, Govindarajan Sudha6, Mainak Guharoy13,14, Tamas Horvath15, Valentin Iglesias16, Andrey V Kajava17,18, Orsolya P Kovacs15, John Lamb6, Matteo Lambrughi5, Tamas Lazar13,14, Jeremy Y Leclercq17, Emanuela Leonardi19,20, Sandra Macedo-Ribeiro21, Mauricio Macossay-Castillo13,14, Emiliano Maiani5, José A Manso21, Cristina Marino-Buslje22, Elizabeth Martínez-Pérez22, Bálint Mészáros2, Ivan Mičetić1, Giovanni Minervini1, Nikoletta Murvai15, Marco Necci1, Christos A Ouzounis7, Mátyás Pajkos2, Lisanna Paladin1, Rita Pancsa15, Elena Papaleo5,23, Gustavo Parisi3, Emilie Pasche12, Pedro J Barbosa Pereira21, Vasilis J Promponas24, Jordi Pujols16, Federica Quaglia1, Patrick Ruch12, Marco Salvatore6, Eva Schad15, Beata Szabo15, Tamás Szaniszló2, Stella Tamana24, Agnes Tantos15, Nevena Veljkovic10, Salvador Ventura16, Wim Vranken13,14,25, Zsuzsanna Dosztányi2, Peter Tompa13,14,15, Silvio C E Tosatto1,26, Damiano Piovesan1.
Abstract
The Database of Protein Disorder (DisProt, URL: https://disprot.org) provides manually curated annotations of intrinsically disordered proteins from the literature. Here we report recent developments with DisProt (version 8), including the doubling of protein entries, a new disorder ontology, improvements of the annotation format and a completely new website. The website includes a redesigned graphical interface, a better search engine, a clearer API for programmatic access and a new annotation interface that integrates text mining technologies. The new entry format provides a greater flexibility, simplifies maintenance and allows the capture of more information from the literature. The new disorder ontology has been formalized and made interoperable by adopting the OWL format, as well as its structure and term definitions have been improved. The new annotation interface has made the curation process faster and more effective. We recently showed that new DisProt annotations can be effectively used to train and validate disorder predictors. We believe the growth of DisProt will accelerate, contributing to the improvement of function and disorder predictors and therefore to illuminate the 'dark' proteome.Entities:
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Year: 2020 PMID: 31713636 PMCID: PMC7145575 DOI: 10.1093/nar/gkz975
Source DB: PubMed Journal: Nucleic Acids Res ISSN: 0305-1048 Impact factor: 16.971