DisProt: intrinsic protein disorder annotation in 2020. Issue Volume 48:Issue D1(2020) (12th November 2019)
- Record Type:
- Journal Article
- Title:
- DisProt: intrinsic protein disorder annotation in 2020. Issue Volume 48:Issue D1(2020) (12th November 2019)
- Main Title:
- DisProt: intrinsic protein disorder annotation in 2020
- Authors:
- Hatos, András
Hajdu-Soltész, Borbála
Monzon, Alexander M
Palopoli, Nicolas
Álvarez, Lucía
Aykac-Fas, Burcu
Bassot, Claudio
Benítez, Guillermo I
Bevilacqua, Martina
Chasapi, Anastasia
Chemes, Lucia
Davey, Norman E
Davidović, Radoslav
Dunker, A Keith
Elofsson, Arne
Gobeill, Julien
Foutel, Nicolás S González
Sudha, Govindarajan
Guharoy, Mainak
Horvath, Tamas
Iglesias, Valentin
Kajava, Andrey V
Kovacs, Orsolya P
Lamb, John
Lambrughi, Matteo
Lazar, Tamas
Leclercq, Jeremy Y
Leonardi, Emanuela
Macedo-Ribeiro, Sandra
Macossay-Castillo, Mauricio
Maiani, Emiliano
Manso, José A
Marino-Buslje, Cristina
Martínez-Pérez, Elizabeth
Mészáros, Bálint
Mičetić, Ivan
Minervini, Giovanni
Murvai, Nikoletta
Necci, Marco
Ouzounis, Christos A
Pajkos, Mátyás
Paladin, Lisanna
Pancsa, Rita
Papaleo, Elena
Parisi, Gustavo
Pasche, Emilie
Barbosa Pereira, Pedro J
Promponas, Vasilis J
Pujols, Jordi
Quaglia, Federica
Ruch, Patrick
Salvatore, Marco
Schad, Eva
Szabo, Beata
Szaniszló, Tamás
Tamana, Stella
Tantos, Agnes
Veljkovic, Nevena
Ventura, Salvador
Vranken, Wim
Dosztányi, Zsuzsanna
Tompa, Peter
Tosatto, Silvio C E
Piovesan, Damiano
… (more) - Abstract:
- 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.
- Is Part Of:
- Nucleic acids research. Volume 48:Issue D1(2020)
- Journal:
- Nucleic acids research
- Issue:
- Volume 48:Issue D1(2020)
- Issue Display:
- Volume 48, Issue 1 (2020)
- Year:
- 2020
- Volume:
- 48
- Issue:
- 1
- Issue Sort Value:
- 2020-0048-0001-0000
- Page Start:
- D269
- Page End:
- D276
- Publication Date:
- 2019-11-12
- Subjects:
- Nucleic acids -- Periodicals
Molecular biology -- Periodicals
572.805 - Journal URLs:
- http://nar.oxfordjournals.org/ ↗
http://www.ncbi.nlm.nih.gov/pmc/journals/4 ↗
http://ukcatalogue.oup.com/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1093/nar/gkz975 ↗
- Languages:
- English
- ISSNs:
- 0305-1048
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6183.850000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12688.xml