Evidence map›Paper›PMID 30607034›Full record

ArticleNature biotechnology2019

Comprehensive identification of RNA-protein interactions in any organism using orthogonal organic phase separation (OOPS).

Rayner M L Queiroz, Tom Smith, Eneko Villanueva, Maria Marti-Solano, Mie Monti, Mariavittoria Pizzinga, Dan-Mircea Mirea, Manasa Ramakrishna, Robert F Harvey, Veronica Dezi and 3 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 217 papers.

0numbers the graph read from it
0cells of the map it votes in
217citing papers in PubMed
17.2field-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

217 citing papers in PubMed, 394 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The isolated HEPN domain of SACSIN exhibits RNA-binding activity.Cellular and molecular life sciences : CMLS · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 1 country.

Rayner M L QueirozCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK.
Tom SmithCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-0697-8777
Eneko VillanuevaCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK. ev318@cam.ac.uk.ORCID http://orcid.org/0000-0002-3585-8846
Maria Marti-SolanoMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0003-0373-8927
Mie MontiCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-0617-9457
Mariavittoria PizzingaMRC Toxicology Unit, University of Cambridge, Leicester, UK.
Dan-Mircea MireaCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK.
Manasa RamakrishnaMRC Toxicology Unit, University of Cambridge, Leicester, UK.ORCID http://orcid.org/0000-0002-5736-8311
Robert F HarveyMRC Toxicology Unit, University of Cambridge, Leicester, UK.ORCID http://orcid.org/0000-0002-0023-1146
Veronica DeziMRC Toxicology Unit, University of Cambridge, Leicester, UK.
Gavin H ThomasDepartment of Biology, University of York, York, UK.
Anne E WillisMRC Toxicology Unit, University of Cambridge, Leicester, UK.
Kathryn S LilleyCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK. k.s.lilley@bioc.cam.ac.uk.ORCID http://orcid.org/0000-0003-0594-6543
University of Cambridge · GBMRC Laboratory of Molecular Biology · GBUniversity of York · GB

Funding

Medical Research Council MC_U105185859Medical Research Council MC_UP_A600_1023Medical Research Council MC_UU_00025/7Wellcome Trust 110071Wellcome Trust 110170
6 · The paper itself

Abstract

Existing high-throughput methods to identify RNA-binding proteins (RBPs) are based on capture of polyadenylated RNAs and cannot recover proteins that interact with nonadenylated RNAs, including long noncoding RNA, pre-mRNAs and bacterial RNAs. We present orthogonal organic phase separation (OOPS), which does not require molecular tagging or capture of polyadenylated RNA, and apply it to recover cross-linked protein-RNA and free protein, or protein-bound RNA and free RNA, in an unbiased way. We validated OOPS in HEK293, U2OS and MCF10A human cell lines, and show that 96% of proteins recovered were bound to RNA. We show that all long RNAs can be cross-linked to proteins, and recovered 1,838 RBPs, including 926 putative novel RBPs. OOPS is approximately 100-fold more efficient than existing methods and can enable analyses of dynamic RNA-protein interactions. We also characterize dynamic changes in RNA-protein interactions in mammalian cells following nocodazole arrest, and present a bacterial RNA-interactome for Escherichia coli. OOPS is compatible with downstream proteomics and RNA sequencing, and can be applied in any organism.

Indexed as

Cell Line, TumorCluster AnalysisCross-Linking ReagentsEscherichia coliGlycoproteinsHEK293 CellsHumansNocodazoleProtein BindingProteomeProteomicsRNARNA, BacterialRNA-Binding ProteinsRNA, Long NoncodingRNA, MessengerCross-Linking ReagentsGlycoproteinsNocodazoleProteomeRNARNA, BacterialRNA-Binding ProteinsRNA, Long NoncodingRNA, MessengerThymidine

Identifiers

PMID30607034
PMCPMC6591131
OpenAlexW2907992023

What OpenQuestion holds

Textmetadata
LicenceTDM
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.