Evidence map›Paper›PMID 25389274›Full record

ArticleNucleic acids research2014

Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA.

Dominik Theler, Cyril Dominguez, Markus Blatter, Julien Boudet, Frédéric H-T Allain

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

160 citing papers in PubMed, 1 synthesis or guideline pooled it, 243 citations in OpenAlex.

  1. Pooled it
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  8. KIAA1429-mediated MCellular & molecular biology letters · 2025
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  9. mMolecules (Basel, Switzerland) · 2025
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  10. mRNA (New York, N.Y.) · 2025
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  11. Targeting RNA adenosine editing and modification enzymes for RNA therapeutics.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
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  12. Functions and therapeutic applications of pseudouridylation.Nature reviews. Molecular cell biology · 2025
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  13. Review
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  15. De novo assembly of RNA mCell reports · 2025
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  16. FMR1 KH0-KH1 domains coordinate mExperimental cell research · 2025
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  20. The role of NJournal of virology · 2025
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100 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

5 authors at 2 institutions in 1 country.

Dominik ThelerInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.
Cyril DominguezInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.
Markus BlatterInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.
Julien BoudetInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.
Frédéric H-T AllainInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland allain@mol.biol.ethz.ch.
Board of the Swiss Federal Institutes of Technology · CHETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N(6)A methylation is the most abundant RNA modification occurring within messenger RNA. Impairment of methylase or demethylase functions are associated with severe phenotypes and diseases in several organisms. Beside writer and eraser enzymes of this dynamic RNA epigenetic modification, reader proteins that recognize this modification are involved in numerous cellular processes. Although the precise characterization of these reader proteins remains unknown, preliminary data showed that most potential reader proteins contained a conserved YT521-B homology (YTH) domain. Here we define the YTH domain of rat YT521-B as a N(6)-methylated adenosine reader domain and report its solution structure in complex with a N(6)-methylated RNA. The structure reveals a binding preference for NGANNN RNA hexamer and a deep hydrophobic cleft for m(6)A recognition. These findings establish a molecular function for YTH domains as m(6)A reader domains and should guide further studies into the biological functions of YTH-containing proteins in m(6)A recognition.

Indexed as

AdenosineAnimalsBinding SitesGuanineMethylationModels, MolecularNerve Tissue ProteinsNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiaryRatsRNARNA-Binding ProteinsSerine-Arginine Splicing FactorsAdenosineGuanineNerve Tissue ProteinsN-methyladenosineRNARNA-Binding ProteinsSerine-Arginine Splicing FactorsYthdc1 protein, rat

Identifiers

PMID25389274
PMCPMC4267619
OpenAlexW2101636211

What OpenQuestion 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 OpenQuestion graph.