DisProt: intrinsic protein disorder annotation in 2020

Autor: 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
Přispěvatelé: Promponas, Vasilis J. [0000-0003-3352-4831], Universita degli Studi di Padova, Vinča Institute of Nuclear Sciences, University of Belgrade [Belgrade], Stockholm University, Laboratoire Leibniz (Leibniz - IMAG), Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Grenoble (INPG)-Université Joseph Fourier - Grenoble 1 (UJF), Laboratoire de biochimie théorique [Paris] (LBT (UPR_9080)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Reproductive Neuroscience Unit, Department of Obstetrics and Gynecology and Department of Neurobiology, Yale University School of Medicine, Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Modena e Reggio Emilia (UNIMORE), Structural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), Instituto de Biologia Molecular e Celular (IBMC), Hungarian Academy of Sciences (MTA), Institute of Agrobiotechnology, National Center for Research and Technology, Universidad Nacional de Quilmes (UNQ), Université de Genève et Hôpitaux Universitaires de Genève (SIM), Hôpitaux Universitaires de Genève (HUG), Biophysics and Bioinformatics Laboratory, Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona (UAB), Service d'informatique médicale (SIM), Hôpitaux de Genève, Department of Structural Biology, Biophysics Research Group [Budapest] (ELTE-MTA 'Lendület'), Department of Bio-engineering Sciences, Structural Biology Brussels, Faculty of Sciences and Bioengineering Sciences, Informatics and Applied Informatics, Chemistry, Basic (bio-) Medical Sciences, Instituto de Investigação e Inovação em Saúde, Université Joseph Fourier - Grenoble 1 (UJF)-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Vrije Universiteit [Brussels] (VUB), Universitat Autònoma de Barcelona [Barcelona] (UAB), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Disordered proteins
Interface (Java)
Disorder Ontology
[SDV]Life Sciences [q-bio]
Interoperability
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
Ontology (information science)
Biology
03 medical and health sciences
Annotation
Genetics
Database Issue
Databases
Protein

ComputingMilieux_MISCELLANEOUS
Data Curation
030304 developmental biology
Graphical user interface
Structure (mathematical logic)
0303 health sciences
Intrinsically Disordered Proteins / chemistry
Information retrieval
Intrinsically disordered proteins
Data curation
Molecular sequence annotation
business.industry
030302 biochemistry & molecular biology
Intrinsic protein
Biological Ontologies
Molecular Sequence Annotation
[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]
Intrinsically Disordered Proteins
Dark proteome
Ontology
Intrisic protein disorder
Literature curation
business
Biological ontologies
Zdroj: Nucleic Acids Research
Nucleic Acids Res.
Nucleic Acids Research, Oxford University Press, 2019, ⟨10.1093/nar/gkz975⟩
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Hatos, A, Hajdu-Soltész, B, Monzon, A M, Palopoli, N, Álvarez, L, Aykac-Fas, B, Bassot, C, Benítez, G I, Bevilacqua, M, Chasapi, A, Chemes, L, Davey, N E, Davidović, R, Dunker, A K, Elofsson, A, Gobeill, J, Foutel, N S G, Sudha, G, Guharoy, M, Horvath, T, Iglesias, V, Kajava, A V, Kovacs, O P, Lamb, J, Lambrughi, M, Lazar, T, Leclercq, J Y, Leonardi, E, MacEdo-Ribeiro, S, MacOssay-Castillo, M, Maiani, E, Manso, J A, Marino-Buslje, C, Martínez-Pérez, E, Mészáros, B, Mičetić, I, Minervini, G, Murvai, N, Necci, M, Ouzounis, C A, Pajkos, M, Paladin, L, Pancsa, R, Papaleo, E, Parisi, G, Pasche, E, Barbosa Pereira, P J, Promponas, V J, Pujols, J, Quaglia, F, Ruch, P, Salvatore, M, Schad, E, Szabo, B, Szaniszló, T, Tamana, S, Tantos, A, Veljkovic, N, Ventura, S, Vranken, W, Dosztányi, Z, Tompa, P, Tosatto, S C E & Piovesan, D 2020, ' DisProt : Intrinsic protein disorder annotation in 2020 ', Nucleic Acids Research, vol. 48, no. D1, pp. D269-D276 . https://doi.org/10.1093/nar/gkz975
Hyper Article en Ligne
GNOSIS Institutional Repository
HAL-Inserm
Mémoires en Sciences de l'Information et de la Communication
Hes-so: ArODES Open Archive (University of Applied Sciences and Arts Western Switzerland
Diposit Digital de Documents de la UAB
VinaR-Repository of the Vinča Institute of Nuclear Sciences, University of Belgrade
Archivio istituzionale della ricerca-Università di Padova
European Union Open Data Portal
LAReferencia-Red Federada de Repositorios Institucionales de Publicaciones Científicas Latinoamericanas
Sygma
Datacite
UnpayWall
ORCID
Microsoft Academic Graph
PubMed Central
Copenhagen University Research Information System
Hal-Diderot
ISSN: 0305-1048
1362-4962
DOI: 10.1093/nar/gkz975⟩
Popis: 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. Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT) of Argentina [PICT-2015/3367, PICT-2017/1924]; Ministry of Education, Science and Technological Development of the Republic of Serbia [ON173001]; Vetenskapsrådet [2016-03798]; Hungarian National Research, Development, and Innovation Office (NKFIH) [FK-128133]; Italian Ministry of Health Young Investigator Grant [GR-2011-02347754]; Ministerio de Economía y Competitividad (MINECO) [BIO2016-78310-R]; ICREA (ICREA-Academia 2015); Fundac¸ão para a Ciência e a Tecnologia (FCT, Portugal); European Regional Development Fund [POCI-01-0145-FEDER-031173, POCI-01-0145-FEDER-029221]; Mexican National Council of Science and Technology (CONACYT) [215503]; Elixir-GR, Action ‘Reinforcement of the Research and Innovation Infrastructure’, Operational Programme ‘Competitiveness, Entrepreneurship and Innovation’ [NSRF 2014-2020]. co-financed by Greece and the European Union (European Regional Development Fund); Hungarian Academy of Sciences [PREMIUM-2017-48]; Carlsberg Distinguished Fellowship [CF18-0314]; Danmarks Grundforskningsfond [DNRF125]; National Research, Development and Innovation Office [K-125340]; Research Foundation Flanders (FWO) [G.0328.16N]; Hungarian Academy of Sciences [LP2014-18]; OTKA [K108798 and K124670]. This project has received funding from the European Union’s Horizon 2020 research and innovation programme [778247]. Funding for open access charge: European Union’s Horizon 2020 research and innovation programme [778247]. Conflict of interest statement. None declared.
Databáze: OpenAIRE