Evidence map›Paper›PMID 24121435›Full record

ArticleNature2013

The structure of the box C/D enzyme reveals regulation of RNA methylation.

Audrone Lapinaite, Bernd Simon, Lars Skjaerven, Magdalena Rakwalska-Bange, Frank Gabel, Teresa Carlomagno

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

81 citing papers in PubMed, 169 citations in OpenAlex.

  1. Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. Emergent microenvironments of nucleoli.Nucleus (Austin, Tex.) · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Advances in the structure and function of the nucleolar protein fibrillarin.Frontiers in cell and developmental biology · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Ribosomal RNA 2'-Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

21 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

6 authors at 2 institutions in 2 countries.

Audrone LapinaiteEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
Bernd Simon
Lars Skjaerven
Magdalena Rakwalska-Bange
Frank Gabel
Teresa Carlomagno
European Molecular Biology Laboratory · DEInstitut de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-transcriptional modifications are essential to the cell life cycle, as they affect both pre-ribosomal RNA processing and ribosome assembly. The box C/D ribonucleoprotein enzyme that methylates ribosomal RNA at the 2'-O-ribose uses a multitude of guide RNAs as templates for the recognition of rRNA target sites. Two methylation guide sequences are combined on each guide RNA, the significance of which has remained unclear. Here we use a powerful combination of NMR spectroscopy and small-angle neutron scattering to solve the structure of the 390 kDa archaeal RNP enzyme bound to substrate RNA. We show that the two methylation guide sequences are located in different environments in the complex and that the methylation of physiological substrates targeted by the same guide RNA occurs sequentially. This structure provides a means for differential control of methylation levels at the two sites and at the same time offers an unexpected regulatory mechanism for rRNA folding.

Indexed as

RNA Processing, Post-TranscriptionalApoproteinsArchaeal ProteinsBiocatalysisChromosomal Proteins, Non-HistoneMethylationModels, MolecularMultiprotein ComplexesNucleic Acid ConformationPyrococcus furiosusRibonucleoproteins, Small NucleolarRNA, ArchaealRNA FoldingRNA, RibosomalRNA, Small UntranslatedApoproteinsArchaeal ProteinsChromosomal Proteins, Non-HistonefibrillarinMultiprotein ComplexesRibonucleoproteins, Small NucleolarRNA, ArchaealRNA, RibosomalRNA, Small Untranslated

Identifiers

PMID24121435
OpenAlexW1997436081

What OpenQuestion holds

Textmetadata
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.