Evidence map›Paper›PMID 26439842›Full record

ArticlePloS one2015

Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins.

Mihaly Varadi, Fruzsina Zsolyomi, Mainak Guharoy, Peter Tompa

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

68 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Prediction of Intrinsically Disordered Regions That Bind RNA with DisoRDPbind.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Comparative assessment of binding residue predictions in intrinsically disordered regions.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Review
  7. Prediction of Disordered Linear Interacting Peptides with CLIP.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  8. Evaluation of predictions of disordered binding regions in the CAID2 experiment.Computational and structural biotechnology journal · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Surveying the global landscape of post-transcriptional regulators.Nature structural & molecular biology · 2023
    Article
  15. Article
  16. RPflex: A Coarse-Grained Network Model for RNA Pocket Flexibility Study.International journal of molecular sciences · 2023
    Article
  17. Article
  18. CIZ1 in Xist seeded assemblies at the inactive X chromosome.Frontiers in cell and developmental biology · 2023
    Review
  19. Article
  20. Review

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

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

4 authors at 2 institutions in 2 countries.

Mihaly VaradiStructural Biology Research Center (SBRC), Flemish Institute of Biotechnology (VIB), Brussels, Belgium; Structural Biology Brussel (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Fruzsina ZsolyomiStructural Biology Research Center (SBRC), Flemish Institute of Biotechnology (VIB), Brussels, Belgium; Structural Biology Brussel (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Mainak GuharoyStructural Biology Research Center (SBRC), Flemish Institute of Biotechnology (VIB), Brussels, Belgium; Structural Biology Brussel (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Peter TompaStructural Biology Research Center (SBRC), Flemish Institute of Biotechnology (VIB), Brussels, Belgium; Structural Biology Brussel (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium; Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Vrije Universiteit Brussel · BEHungarian Academy of Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have never been fully assessed. Here, through large-scale analysis of comprehensive protein sequence and structure datasets we demonstrate the prevalence of intrinsic structural disorder in RNA-binding proteins and domains. We addressed their functionality through a quantitative description of the evolutionary conservation of disordered segments involved in binding, and investigated the structural implications of flexibility in terms of conformational stability and interface formation. We conclude that the functional role of intrinsically disordered protein segments in RNA-binding is two-fold: first, these regions establish extended, conserved electrostatic interfaces with RNAs via induced fit. Second, conformational flexibility enables them to target different RNA partners, providing multi-functionality, while also ensuring specificity. These findings emphasize the functional importance of intrinsically disordered regions in RNA-binding proteins.

Indexed as

Amino Acid SequenceModels, MolecularProtein ConformationRNA-Binding ProteinsRNA-Binding Proteins

Identifiers

PMID26439842
PMCPMC4595337
OpenAlexW2207875562

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.