Evidence map›Paper›PMID 33291838›Full record

ReviewBiomolecules2020

Comparative Assessment of Intrinsic Disorder Predictions with a Focus on Protein and Nucleic Acid-Binding Proteins.

Akila Katuwawala, Lukasz Kurgan

Open access · goldAbstract readComparative StudyReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 13% of its field
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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Pooled it
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  9. 1D2DSimScore: A novel method for comparing contacts in biomacromolecules and their complexes.Protein science : a publication of the Protein Society · 2023
    Article
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  16. Deep learning in prediction of intrinsic disorder in proteins.Computational and structural biotechnology journal · 2022
    Review
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Akila KatuwawalaDepartment of Computer Science, Virginia Commonwealth University, Richmond, VA 23284, USA.ORCID 0000-0003-3106-4843
Lukasz KurganDepartment of Computer Science, Virginia Commonwealth University, Richmond, VA 23284, USA.ORCID 0000-0002-7749-0314
Virginia Commonwealth University · US

Funding

National Science Foundation 1617369
6 · The paper itself

Abstract

With over 60 disorder predictors, users need help navigating the predictor selection task. We review 28 surveys of disorder predictors, showing that only 11 include assessment of predictive performance. We identify and address a few drawbacks of these past surveys. To this end, we release a novel benchmark dataset with reduced similarity to the training sets of the considered predictors. We use this dataset to perform a first-of-its-kind comparative analysis that targets two large functional families of disordered proteins that interact with proteins and with nucleic acids. We show that limiting sequence similarity between the benchmark and the training datasets has a substantial impact on predictive performance. We also demonstrate that predictive quality is sensitive to the use of the well-annotated order and inclusion of the fully structured proteins in the benchmark datasets, both of which should be considered in future assessments. We identify three predictors that provide favorable results using the new benchmark set. While we find that VSL2B offers the most accurate and robust results overall, ESpritz-DisProt and SPOT-Disorder perform particularly well for disordered proteins. Moreover, we find that predictions for the disordered protein-binding proteins suffer low predictive quality compared to generic disordered proteins and the disordered nucleic acids-binding proteins. This can be explained by the high disorder content of the disordered protein-binding proteins, which makes it difficult for the current methods to accurately identify ordered regions in these proteins. This finding motivates the development of a new generation of methods that would target these difficult-to-predict disordered proteins. We also discuss resources that support users in collecting and identifying high-quality disorder predictions.

Indexed as

Intrinsically Disordered ProteinsComputational BiologyDatabases, ProteinDNA-Binding ProteinsHumansNucleic AcidsProtein BindingRNA-Binding ProteinsDNA-Binding ProteinsIntrinsically Disordered ProteinsNucleic AcidsRNA-Binding Proteinsintrinsically disordered proteinsintrinsic disorderpredictionpredictive performanceprotein-nucleic acids interactionsprotein-protein interactions

Identifiers

PMID33291838
PMCPMC7762010
OpenAlexW3106923909

What OpenQuestion holds

Textmetadata
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.