Evidence map›Paper›PMID 28232901›Full record

ArticleIntrinsically disordered proteins2016

How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe.

Philippe Lieutaud, François Ferron, Alexey V Uversky, Lukasz Kurgan, Vladimir N Uversky, Sonia Longhi

Abstract read
In one paragraph

Article in Intrinsically disordered proteins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. MultilevelCurrent research in structural biology · 2026
    Article
  2. Review
  3. IsoProDB: an integrated map of human protein isoforms for accelerated research.Database : the journal of biological databases and curation · 2026
    Article
  4. Prediction of Intrinsically Disordered Regions That Bind RNA with DisoRDPbind.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Article
  7. Evaluation of predictions of disordered binding regions in the CAID2 experiment.Computational and structural biotechnology journal · 2025
    Review
  8. Article
  9. Prediction of Disordered Linear Interacting Peptides with CLIP.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Prediction of Intrinsic Disorder Functions with DEPICTER2.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  11. Prediction of Disordered Linkers Using APOD.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. Accurate and Fast Prediction of Intrinsic Disorder Using flDPnn.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

6 authors.

Philippe LieutaudAix-Marseille Université, AFMB UMR, Marseille, France; CNRS, AFMB UMR, Marseille, France.
François FerronAix-Marseille Université, AFMB UMR, Marseille, France; CNRS, AFMB UMR, Marseille, France.
Alexey V UverskyCenter for Data Analytics and Biomedical Informatics, Department of Computer and Information Sciences, College of Science and Technology, Temple University , Philadelphia, PA, USA.
Lukasz KurganDepartment of Computer Science, Virginia Commonwealth University , Richmond, VA, USA.
Vladimir N UverskyDepartment of Molecular Medicine and USF Health Byrd Alzheimer Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.
Sonia LonghiAix-Marseille Université, AFMB UMR, Marseille, France; CNRS, AFMB UMR, Marseille, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the last 2 decades it has become increasingly evident that a large number of proteins are either fully or partially disordered. Intrinsically disordered proteins lack a stable 3D structure, are ubiquitous and fulfill essential biological functions. Their conformational heterogeneity is encoded in their amino acid sequences, thereby allowing intrinsically disordered proteins or regions to be recognized based on properties of these sequences. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental for delineating boundaries of protein domains amenable to structural determination with X-ray crystallization. This article discusses a comprehensive selection of databases and methods currently employed to disseminate experimental and putative annotations of disorder, predict disorder and identify regions involved in induced folding. It also provides a set of detailed instructions that should be followed to perform computational analysis of disorder.

Indexed as

disorder databases and metaserversinduced foldingintrinsically disordered proteinsintrinsically disordered regionsintrinsic disorderprediction methods

Identifiers

PMID28232901
PMCPMC5314888

What OpenQuestion holds

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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.