Evidence map›Paper›PMID 37740110›Full record

ReviewNature protocols2023

Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins.

Lukasz Kurgan, Gang Hu, Kui Wang, Sina Ghadermarzi, Bi Zhao, Nawar Malhis, Gábor Erdős, Jörg Gsponer, Vladimir N Uversky, Zsuzsanna Dosztányi

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature protocols, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Prediction of Intrinsically Disordered Regions That Bind RNA with DisoRDPbind.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Programming cellular condensates for living materials using an intrinsically disordered protein display platform.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Comparative assessment of binding residue predictions in intrinsically disordered regions.Protein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Evaluation of predictions of disordered binding regions in the CAID2 experiment.Computational and structural biotechnology journal · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Prediction of Disordered Linear Interacting Peptides with CLIP.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  18. Prediction of Intrinsic Disorder Functions with DEPICTER2.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  19. Review
  20. 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

10 authors at 5 institutions in 5 countries.

Lukasz KurganDepartment of Computer Science, Virginia Commonwealth University, Richmond, VA, USA. lkurgan@vcu.edu.ORCID 0000-0002-7749-0314
Gang HuSchool of Statistics and Data Science, LPMC and KLMDASR, Nankai University, Tianjin, China.
Kui WangSchool of Statistics and Data Science, LPMC and KLMDASR, Nankai University, Tianjin, China.
Sina GhadermarziDepartment of Computer Science, Virginia Commonwealth University, Richmond, VA, USA.
Bi ZhaoDepartment of Computer Science, Virginia Commonwealth University, Richmond, VA, USA.
Nawar MalhisMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.ORCID 0000-0002-1317-833X
Gábor ErdősMTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Jörg GsponerMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada. gsponer@msl.ubc.ca.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA. vuversky@usf.edu.
Zsuzsanna DosztányiMTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary. zsuzsanna.dosztanyi@ttk.elte.hu.
Virginia Commonwealth University · USEötvös Loránd University · HUNankai University · CNUniversity of British Columbia · CAUniversity of South Florida · US

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31970649National Science Foundation (NSF) 2125218National Science Foundation (NSF) 2146027
6 · The paper itself

Abstract

Intrinsic disorder is instrumental for a wide range of protein functions, and its analysis, using computational predictions from primary structures, complements secondary and tertiary structure-based approaches. In this Tutorial, we provide an overview and comparison of 23 publicly available computational tools with complementary parameters useful for intrinsic disorder prediction, partly relying on results from the Critical Assessment of protein Intrinsic Disorder prediction experiment. We consider factors such as accuracy, runtime, availability and the need for functional insights. The selected tools are available as web servers and downloadable programs, offer state-of-the-art predictions and can be used in a high-throughput manner. We provide examples and instructions for the selected tools to illustrate practical aspects related to the submission, collection and interpretation of predictions, as well as the timing and their limitations. We highlight two predictors for intrinsically disordered proteins, flDPnn as accurate and fast and IUPred as very fast and moderately accurate, while suggesting ANCHOR2 and MoRFchibi as two of the best-performing predictors for intrinsically disordered region binding. We link these tools to additional resources, including databases of predictions and web servers that integrate multiple predictive methods. Altogether, this Tutorial provides a hands-on guide to comparatively evaluating multiple predictors, submitting and collecting their own predictions, and reading and interpreting results. It is suitable for experimentalists and computational biologists interested in accurately and conveniently identifying intrinsic disorder, facilitating the functional characterization of the rapidly growing collections of protein sequences.

Indexed as

Computational BiologyIntrinsically Disordered ProteinsAmino Acid SequenceDatabases, ProteinIntrinsically Disordered Proteins

Identifiers

PMID37740110
OpenAlexW4386979884

What OpenQuestion holds

Textmetadata
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.