Evidence map›Paper›PMID 25611135›Full record

ArticleJournal of the American Chemical Society2015

Structure and thermodynamics of N6-methyladenosine in RNA: a spring-loaded base modification.

Caroline Roost, Stephen R Lynch, Pedro J Batista, Kun Qu, Howard Y Chang, Eric T Kool

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. 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 266 papers.

0numbers the graph read from it
0cells of the map it votes in
266citing papers in PubMed
16.9field-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

266 citing papers in PubMed, 416 citations in OpenAlex.

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  15. Comprehensive analysis and validation of mBMC veterinary research · 2026
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  19. Effects of NBioconjugate chemistry · 2025
    Article
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206 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Caroline RoostDepartment of Chemistry, ‡Howard Hughes Medical Institute and Program in Epithelial Biology, Stanford University , Stanford, California 94305, United States.
Stephen R Lynch
Pedro J Batista
Kun Qu
Howard Y Chang
Eric T Kool
Stanford University · USHoward Hughes Medical Institute · US

Funding

Special EquipmentP50HG007735 · NHGRI · STANFORD UNIVERSITY · PI CHANG, HOWARD Y · 2014 to 2018
$15.2M
Structural Motifs in RNAR01HG004361 · NHGRI · STANFORD UNIVERSITY · PI CHANG, HOWARD Y · 2007 to 2018
$4.7M
Templated Chemistry for RNA AnalysisR01GM068122 · NIGMS · STANFORD UNIVERSITY · PI KOOL, ERIC T. · 2003 to 2016
$3.5M
POLYFLUOROPHORES ASSEMBLED ON A DNA SCAFFOLDR01GM067201 · NIGMS · STANFORD UNIVERSITY · PI KOOL, ERIC T. · 2003 to 2011
$2.2M
DNA-carbon Assemblies for Multispectral ImagingR01GM106067 · NIGMS · STANFORD UNIVERSITY · PI KOOL, ERIC T. · 2014 to 2017
$1.2M
NHGRI NIH HHS P50 HG007735NHGRI NIH HHS P50-HG007735NHGRI NIH HHS R01 HG004361NHGRI NIH HHS R01-HG004361NIGMS NIH HHS GM067201NIGMS NIH HHS GM068122NIGMS NIH HHS R01 GM067201NIGMS NIH HHS R01 GM068122NIGMS NIH HHS R01 GM106067
6 · The paper itself

Abstract

N(6)-Methyladenosine (m(6)A) modification is hypothesized to control processes such as RNA degradation, localization, and splicing. However, the molecular mechanisms by which this occurs are unclear. Here, we measured structures of an RNA duplex containing m(6)A in the GGACU consensus, along with an unmodified RNA control, by 2D NMR. The data show that m(6)A-U pairing in the double-stranded context is accompanied by the methylamino group rotating from its energetically preferred syn geometry on the Watson-Crick face to the higher-energy anti conformation, positioning the methyl group in the major groove. Thermodynamic measurements of m(6)A in duplexes reveal that it is destabilizing by 0.5-1.7 kcal/mol. In contrast, we show that m(6)A in unpaired positions base stacks considerably more strongly than the unmodified base, adding substantial stabilization in single-stranded locations. Transcriptome-wide nuclease mapping of methylated RNA secondary structure from human cells reveals a structural transition at methylated adenosines, with a tendency to single-stranded structure adjacent to the modified base.

Indexed as

AdenineAdenosineBase PairingCell LineHumansMethylationModels, MolecularRibonucleasesRNARNA StabilityThermodynamicsAdenineAdenosineN-methyladenosineRibonucleasesRNA

Identifiers

PMID25611135
PMCPMC4405242
OpenAlexW1991058622

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.