Evidence map›Paper›PMID 37904585›Full record

ArticleNucleic acids research2024

DisProt in 2024: improving function annotation of intrinsically disordered proteins.

Maria Cristina Aspromonte, Maria Victoria Nugnes, Federica Quaglia, Adel Bouharoua, DisProt Consortium, Silvio C E Tosatto, Damiano Piovesan

Erratum issuedAbstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

91 citing papers in PubMed.

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  19. An interpretable molecular framework for predicting cancer driver missense mutations.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  20. Article

31 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Maria Cristina AspromonteDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0002-4937-6952
Maria Victoria NugnesDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0001-8399-7907
Federica QuagliaDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0002-0341-4888
Adel BouharouaDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
DisProt Consortium
Silvio C E TosattoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-4525-7793
Damiano PiovesanDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0001-8210-2390

Funding

European Cooperation in Science and Technology CA21160Horizon 2020 778247University of Padova
6 · The paper itself

Abstract

DisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements, including a broader representation of functions and an enhanced curation process. These improvements aim to increase both the quality of annotations and their coverage at the sequence level. Higher coverage has been achieved by adopting additional evidence codes. Quality of annotations has been improved by systematically applying Minimum Information About Disorder Experiments (MIADE) principles and reporting all the details of the experimental setup that could potentially influence the structural state of a protein. The DisProt database now includes new thematic datasets and has expanded the adoption of Gene Ontology terms, resulting in an extensive functional repertoire which is automatically propagated to UniProtKB. Finally, we show that DisProt's curated annotations strongly correlate with disorder predictions inferred from AlphaFold2 pLDDT (predicted Local Distance Difference Test) confidence scores. This comparison highlights the utility of DisProt in explaining apparent uncertainty of certain well-defined predicted structures, which often correspond to folding-upon-binding fragments. Overall, DisProt serves as a comprehensive resource, combining experimental evidence of disorder information to enhance our understanding of intrinsically disordered proteins and their functional implications.

Indexed as

Databases, ProteinIntrinsically Disordered ProteinsGene OntologyMolecular Sequence AnnotationIntrinsically Disordered Proteins

Identifiers

PMID37904585
PMCPMC10767923

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.