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MobiDB: 10 years of intrinsically disordered proteins
The MobiDB database (URL: https://mobidb.org/) is a knowledge base of intrinsically disordered proteins. MobiDB aggregates disorder annotations derived from the literature and from experimental evidence along with predictions for all known protein sequences. MobiDB generates new knowledge and captur...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9825420/ https://www.ncbi.nlm.nih.gov/pubmed/36416266 http://dx.doi.org/10.1093/nar/gkac1065 |
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author | Piovesan, Damiano Del Conte, Alessio Clementel, Damiano Monzon, Alexander Miguel Bevilacqua, Martina Aspromonte, Maria Cristina Iserte, Javier A Orti, Fernando E Marino-Buslje, Cristina Tosatto, Silvio C E |
author_facet | Piovesan, Damiano Del Conte, Alessio Clementel, Damiano Monzon, Alexander Miguel Bevilacqua, Martina Aspromonte, Maria Cristina Iserte, Javier A Orti, Fernando E Marino-Buslje, Cristina Tosatto, Silvio C E |
author_sort | Piovesan, Damiano |
collection | PubMed |
description | The MobiDB database (URL: https://mobidb.org/) is a knowledge base of intrinsically disordered proteins. MobiDB aggregates disorder annotations derived from the literature and from experimental evidence along with predictions for all known protein sequences. MobiDB generates new knowledge and captures the functional significance of disordered regions by processing and combining complementary sources of information. Since its first release 10 years ago, the MobiDB database has evolved in order to improve the quality and coverage of protein disorder annotations and its accessibility. MobiDB has now reached its maturity in terms of data standardization and visualization. Here, we present a new release which focuses on the optimization of user experience and database content. The major advances compared to the previous version are the integration of AlphaFoldDB predictions and the re-implementation of the homology transfer pipeline, which expands manually curated annotations by two orders of magnitude. Finally, the entry page has been restyled in order to provide an overview of the available annotations along with two separate views that highlight structural disorder evidence and functions associated with different binding modes. |
format | Online Article Text |
id | pubmed-9825420 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-98254202023-01-10 MobiDB: 10 years of intrinsically disordered proteins Piovesan, Damiano Del Conte, Alessio Clementel, Damiano Monzon, Alexander Miguel Bevilacqua, Martina Aspromonte, Maria Cristina Iserte, Javier A Orti, Fernando E Marino-Buslje, Cristina Tosatto, Silvio C E Nucleic Acids Res Database Issue The MobiDB database (URL: https://mobidb.org/) is a knowledge base of intrinsically disordered proteins. MobiDB aggregates disorder annotations derived from the literature and from experimental evidence along with predictions for all known protein sequences. MobiDB generates new knowledge and captures the functional significance of disordered regions by processing and combining complementary sources of information. Since its first release 10 years ago, the MobiDB database has evolved in order to improve the quality and coverage of protein disorder annotations and its accessibility. MobiDB has now reached its maturity in terms of data standardization and visualization. Here, we present a new release which focuses on the optimization of user experience and database content. The major advances compared to the previous version are the integration of AlphaFoldDB predictions and the re-implementation of the homology transfer pipeline, which expands manually curated annotations by two orders of magnitude. Finally, the entry page has been restyled in order to provide an overview of the available annotations along with two separate views that highlight structural disorder evidence and functions associated with different binding modes. Oxford University Press 2022-11-23 /pmc/articles/PMC9825420/ /pubmed/36416266 http://dx.doi.org/10.1093/nar/gkac1065 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Database Issue Piovesan, Damiano Del Conte, Alessio Clementel, Damiano Monzon, Alexander Miguel Bevilacqua, Martina Aspromonte, Maria Cristina Iserte, Javier A Orti, Fernando E Marino-Buslje, Cristina Tosatto, Silvio C E MobiDB: 10 years of intrinsically disordered proteins |
title | MobiDB: 10 years of intrinsically disordered proteins |
title_full | MobiDB: 10 years of intrinsically disordered proteins |
title_fullStr | MobiDB: 10 years of intrinsically disordered proteins |
title_full_unstemmed | MobiDB: 10 years of intrinsically disordered proteins |
title_short | MobiDB: 10 years of intrinsically disordered proteins |
title_sort | mobidb: 10 years of intrinsically disordered proteins |
topic | Database Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9825420/ https://www.ncbi.nlm.nih.gov/pubmed/36416266 http://dx.doi.org/10.1093/nar/gkac1065 |
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