Evidence map›Paper›PMID 29955037›Full record

ArticleNature communications2018

Global pairwise RNA interaction landscapes reveal core features of protein recognition.

Qin Zhou, Nikesh Kunder, José Alberto De la Paz, Alexandra E Lasley, Vandita D Bhat, Faruck Morcos, Zachary T Campbell

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  7. In vivo functional phenotypes from a computational epistatic model of evolution.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  15. Metabolomics Analysis of Viral Therapeutics.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Epistatic contributions promote the unification of incompatible models of neutral molecular evolution.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Article
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

7 authors at 1 institution in 1 country.

Qin ZhouDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA.
Nikesh KunderDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA.
José Alberto De la PazDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA.ORCID http://orcid.org/0000-0002-5053-4807
Alexandra E LasleyDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA.
Vandita D BhatDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA.
Faruck MorcosDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA. Faruckm@utdallas.edu.ORCID http://orcid.org/0000-0001-6208-1561
Zachary T CampbellDepartment of Biological Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA. Zachary.Campbell@utdallas.edu.ORCID http://orcid.org/0000-0002-3768-6996
The University of Texas at Dallas · US

Funding

3’ End Regulation in Nociceptor PlasticityR01NS100788 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI CAMPBELL, ZACHARY · 2017 to 2021
$2.0M
NINDS NIH HHS R01 NS100788
6 · The paper itself

Abstract

RNA-protein interactions permeate biology. Transcription, translation, and splicing all hinge on the recognition of structured RNA elements by RNA-binding proteins. Models of RNA-protein interactions are generally limited to short linear motifs and structures because of the vast sequence sampling required to access longer elements. Here, we develop an integrated approach that calculates global pairwise interaction scores from in vitro selection and high-throughput sequencing. We examine four RNA-binding proteins of phage, viral, and human origin. Our approach reveals regulatory motifs, discriminates between regulated and non-regulated RNAs within their native genomic context, and correctly predicts the consequence of mutational events on binding activity. We design binding elements that improve binding activity in cells and infer mutational pathways that reveal permissive versus disruptive evolutionary trajectories between regulated motifs. These coupling landscapes are broadly applicable for the discovery and characterization of protein-RNA recognition at single nucleotide resolution.

Indexed as

Amino Acid SequenceBacteriophage lambdaBinding SitesCloning, MolecularEscherichia coliGene ExpressionGene Products, tatGenetic VectorsHigh-Throughput Nucleotide SequencingHumansImmunodeficiency Virus, BovineModels, MolecularNucleic Acid ConformationProtein BindingProtein Structure, SecondaryRecombinant ProteinsGene Products, tatN protein, Bacteriophage lambdaRecombinant ProteinsRNARNA-Binding ProteinsRNA NucleotidyltransferasesTUT7 protein, humanViral Regulatory and Accessory Proteins

Identifiers

PMID29955037
PMCPMC6023938
OpenAlexW2808854531

What Socratic holds

Textmetadata
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 Socratic graph.