Evidence map›Paper›PMID 24402442›Full record

ArticleNature communications2014

Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation.

Miroslaw Smietanski, Maria Werner, Elzbieta Purta, Katarzyna H Kaminska, Janusz Stepinski, Edward Darzynkiewicz, Marcin Nowotny, Janusz M Bujnicki

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Trinucleotide mRNA Cap AnalogueJournal of the American Chemical Society · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. CMTr mediated 2'-RNA (New York, N.Y.) · 2022
    Article
  19. 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

8 authors at 3 institutions in 1 country.

Miroslaw Smietanski1] Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland [2] Laboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland.
Maria WernerLaboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland.
Elzbieta PurtaLaboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland.
Katarzyna H KaminskaLaboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland.
Janusz StepinskiDivision of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw, ul. Zwirki i Wigury 93, PL-02-089 Warsaw, Poland.
Edward Darzynkiewicz1] Division of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw, ul. Zwirki i Wigury 93, PL-02-089 Warsaw, Poland [2] Centre of New Technologies, University of Warsaw, ul. Zwirki i Wigury 93, PL-02-089 Warsaw, Poland.
Marcin NowotnyLaboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland.
Janusz M Bujnicki1] Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, ul. ks. Trojdena 4, PL-02-109 Warsaw, Poland [2] Laboratory of Bioinformatics, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, ul. Umultowska 89, PL-61-614 Poznan, Poland.
International Institute of Molecular and Cell Biology · PLUniversity of Warsaw · PLAdam Mickiewicz University in Poznań · PL

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The 5' cap of human messenger RNA contains 2'-O-methylation of the first and often second transcribed nucleotide that is important for its processing, translation and stability. Human enzymes that methylate these nucleotides, termed CMTr1 and CMTr2, respectively, have recently been identified. However, the structures of these enzymes and their mechanisms of action remain unknown. In the present study, we solve the crystal structures of the active CMTr1 catalytic domain in complex with a methyl group donor and a capped oligoribonucleotide, thereby revealing the mechanism of specific recognition of capped RNA. This mechanism differs significantly from viral enzymes, thus providing a framework for their specific targeting. Based on the crystal structure of CMTr1, a comparative model of the CMTr2 catalytic domain is generated. This model, together with mutational analysis, leads to the identification of residues involved in RNA and methyl group donor binding.

Indexed as

Crystallography, X-RayHumansMethyltransferasesModels, MolecularProtein Structure, TertiaryRNA CapsRNA, MessengerRNA Processing, Post-TranscriptionalCMTR1 protein, humanCMTR2 protein, humanMethyltransferasesRNA CapsRNA, Messenger

Identifiers

PMID24402442
PMCPMC3941023
OpenAlexW2023176508

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.