Evidence map›Paper›PMID 27048167›Full record

ReviewCell communication and signaling : CCS2016

The new (dis)order in RNA regulation.

Aino I Järvelin, Marko Noerenberg, Ilan Davis, Alfredo Castello

Open access · goldAbstract readReview
In one paragraph

Review in Cell communication and signaling : CCS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed, 1 pooled it
11.3field-weighted citation impact, top 1% 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

138 citing papers in PubMed, 1 synthesis or guideline pooled it, 218 citations in OpenAlex.

  1. Pooled it
  2. Review
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  12. bioRxiv : the preprint server for biology · 2026
    Article
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  17. Review
  18. Article
  19. Contributions of Folded and Disordered Domains to RNA Binding by HNRNPR.bioRxiv : the preprint server for biology · 2025
    Article
  20. Article

78 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 1 institution in 1 country.

Aino I JärvelinDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Marko NoerenbergDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Ilan DavisDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Alfredo CastelloDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. alfredo.castellopalomares@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Medical Research Council MC_UU_12014/10Medical Research Council MR/L019434/1Wellcome Trust 096144
6 · The paper itself

Abstract

RNA-binding proteins play a key role in the regulation of all aspects of RNA metabolism, from the synthesis of RNA to its decay. Protein-RNA interactions have been thought to be mostly mediated by canonical RNA-binding domains that form stable secondary and tertiary structures. However, a number of pioneering studies over the past decades, together with recent proteome-wide data, have challenged this view, revealing surprising roles for intrinsically disordered protein regions in RNA binding. Here, we discuss how disordered protein regions can mediate protein-RNA interactions, conceptually grouping these regions into RS-rich, RG-rich, and other basic sequences, that can mediate both specific and non-specific interactions with RNA. Disordered regions can also influence RNA metabolism through protein aggregation and hydrogel formation. Importantly, protein-RNA interactions mediated by disordered regions can influence nearly all aspects of co- and post-transcriptional RNA processes and, consequently, their disruption can cause disease. Despite growing interest in disordered protein regions and their roles in RNA biology, their mechanisms of binding, regulation, and physiological consequences remain poorly understood. In the coming years, the study of these unorthodox interactions will yield important insights into RNA regulation in cellular homeostasis and disease.

Indexed as

AnimalsHumansIntrinsically Disordered ProteinsModels, MolecularProtein BindingRNARNA-Binding ProteinsRNA SplicingIntrinsically Disordered ProteinsRNARNA-Binding ProteinsArginine-rich motifBasic patchCo- and post-transcriptional RNA regulationGAR repeatIntrinsically disordered proteinPoly-K patchRGG-boxRNA-binding proteinRNA granuleRS repeat

Identifiers

PMID27048167
PMCPMC4822317
OpenAlexW2321301219

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.