MobiDB: 10 years of intrinsically disordered proteins.

Autor:	Piovesan D; Department of Biomedical Sciences, University of Padova, Padova, Italy., Del Conte A; Department of Biomedical Sciences, University of Padova, Padova, Italy., Clementel D; Department of Biomedical Sciences, University of Padova, Padova, Italy., Monzon AM; Department of Information Engineering, University of Padova, Padova, Italy., Bevilacqua M; Department of Biomedical Sciences, University of Padova, Padova, Italy., Aspromonte MC; Department of Biomedical Sciences, University of Padova, Padova, Italy., Iserte JA; Bioinformatics Unit, Fundación Instituto Leloir, Buenos Aires, Argentina., Orti FE; Bioinformatics Unit, Fundación Instituto Leloir, Buenos Aires, Argentina., Marino-Buslje C; Bioinformatics Unit, Fundación Instituto Leloir, Buenos Aires, Argentina., Tosatto SCE; Department of Biomedical Sciences, University of Padova, Padova, Italy.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2023 Jan 06; Vol. 51 (D1), pp. D438-D444.
DOI:	10.1093/nar/gkac1065
Abstrakt:	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. (© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Databáze:	MEDLINE
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