Evidence map›Paper›PMID 27229125›Full record

ReviewCellular and molecular life sciences : CMLS2016

A structural perspective of RNA recognition by intrinsically disordered proteins.

Sushmita Basu, Ranjit Prasad Bahadur

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. G-Quadruplexes: Structural Diversity and Emerging Roles in Biomolecular Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  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. Article
  7. Article
  8. Article
  9. Prediction of Disordered Linear Interacting Peptides with CLIP.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Review
  11. Article
  12. Regulatory role of RNA-binding proteins in microRNA biogenesis.Frontiers in molecular biosciences · 2024
    Review
  13. Review
  14. Article
  15. Challenges in Brugada Syndrome Stratification: InvestigatingInternational journal of molecular sciences · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. RPflex: A Coarse-Grained Network Model for RNA Pocket Flexibility Study.International journal of molecular sciences · 2023
    Article
  20. Role of the RNA-binding protein family in gynecologic cancers.American journal of cancer research · 2023
    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

2 authors.

Sushmita BasuComputational Structural Biology Lab, Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur, 721302, India.
Ranjit Prasad BahadurComputational Structural Biology Lab, Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur, 721302, India. r.bahadur@hijli.iitkgp.ernet.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-RNA recognition is essential for gene expression and its regulation, which is indispensable for the survival of the living organism at one hand, on the other hand, misregulation of this recognition may lead to their extinction. Polymorphic conformation of both the interacting partners is a characteristic feature of such molecular recognition that promotes the assembly. Many RNA binding proteins (RBP) or regions in them are found to be intrinsically disordered, and this property helps them to play a central role in the regulatory processes. Sequence composition and the length of the flexible linkers between RNA binding domains in RBPs are crucial in making significant contacts with its partner RNA. Polymorphic conformations of RBPs can provide thermodynamic advantage to its binding partner while acting as a chaperone. Prolonged extensions of the disordered regions in RBPs also contribute to the stability of the large cellular machines including ribosome and viral assemblies. The involvement of these disordered regions in most of the significant cellular processes makes RBPs highly associated with various human diseases that arise due to their misregulation.

Indexed as

AnimalsDiseaseHumansIntrinsically Disordered ProteinsRibosomesRNARNA, ViralSpliceosomesIntrinsically Disordered ProteinsRNARNA, ViralInduced foldingPolymorphic conformationProtein-RNA recognitionRNA binding proteinsStructural flexibility

Identifiers

PMID27229125
PMCPMC7079799

What OpenQuestion holds

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Registered trials

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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.