Evidence map›Paper›PMID 30879411›Full record

ArticleRNA biology2019

Bisubstrate analogues as structural tools to investigate m

Stephanie Oerum, Marjorie Catala, Colette Atdjian, Franck Brachet, Luc Ponchon, Pierre Barraud, Laura Iannazzo, Louis Droogmans, Emmanuelle Braud, Mélanie Ethève-Quelquejeu and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Engineering Bisubstrates to Target mChemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Ghost authors revealed: The structure and function of human NWiley interdisciplinary reviews. RNA · 2023
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. RNA methyltransferase METTL16: Targets and function.Wiley interdisciplinary reviews. RNA · 2022
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. 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

11 authors at 2 institutions in 2 countries.

Stephanie Oeruma Laboratoire d'Expression génétique microbienne, Institut de Biologie Physico-Chimique, IBPC, CNRS , Université Paris Diderot , Paris , France.
Marjorie Catalaa Laboratoire d'Expression génétique microbienne, Institut de Biologie Physico-Chimique, IBPC, CNRS , Université Paris Diderot , Paris , France.
Colette Atdjianb Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques, CNRS , Université Paris Descartes , Paris , France.ORCID 0000-0003-3600-7848
Franck Brachetc Institut de Biologie Physico-Chimique , IBPC, CNRS , Paris , France.
Luc Ponchond Laboratoire de Cristallographie et RMN biologiques , CNRS, Université Paris Descartes , Paris , France.
Pierre Barrauda Laboratoire d'Expression génétique microbienne, Institut de Biologie Physico-Chimique, IBPC, CNRS , Université Paris Diderot , Paris , France.ORCID 0000-0003-4460-8360
Laura Iannazzob Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques, CNRS , Université Paris Descartes , Paris , France.
Louis Droogmanse Laboratoire de Microbiologie , Université libre de Bruxelles (ULB) , Gosselies , Belgium.
Emmanuelle Braudb Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques, CNRS , Université Paris Descartes , Paris , France.
Mélanie Ethève-Quelquejeub Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques, CNRS , Université Paris Descartes , Paris , France.
Carine Tisnéa Laboratoire d'Expression génétique microbienne, Institut de Biologie Physico-Chimique, IBPC, CNRS , Université Paris Diderot , Paris , France.ORCID 0000-0001-5534-4650
Centre National de la Recherche Scientifique · FRUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA methyltransferases (MTases) catalyse the transfer of a methyl group to their RNA substrates using most-often S-adenosyl-L-methionine (SAM) as cofactor. Only few RNA-bound MTases structures are currently available due to the difficulties in crystallising RNA:protein complexes. The lack of complex structures results in poorly understood RNA recognition patterns and methylation reaction mechanisms. On the contrary, many cofactor-bound MTase structures are available, resulting in well-understood protein:cofactor recognition, that can guide the design of bisubstrate analogues that mimic the state at which both the substrate and the cofactor is bound. Such bisubstrate analogues were recently synthesized for proteins monomethylating the N6-atom of adenine (m

Indexed as

AdenineCatalytic DomainEnzyme InhibitorsEscherichia coli ProteinsMethyltransferasesModels, MolecularMolecular ConformationProtein BindingTemperatureAdenineEnzyme InhibitorsEscherichia coli ProteinsMethyltransferasesN(6)-methoxyadenineRlmJ protein, E colibisubstrate analoguesinhibitormAmethyltransferaseRlmJRNA bindingRNA MTasesSAM analogueTrmK

Identifiers

PMID30879411
PMCPMC6546350
OpenAlexW2921466479

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.