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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
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.
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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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