Evidence map›Paper›PMID 25626080›Full record

ReviewRNA biology2014

RNA methyltransferases involved in 5' cap biosynthesis.

Magdalena Byszewska, Mirosław Śmietański, Elżbieta Purta, Janusz M Bujnicki

Open access · hybridAbstract readReview
In one paragraph

Review in RNA biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

51 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. SnoRNAs: Exploring Their Implication in Human Diseases.International journal of molecular sciences · 2024
    Review
  6. 2'-RNA (New York, N.Y.) · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Methyltransferases ofBiomolecules · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. An Altered Metabolism in Leukocytes ShowingFrontiers in molecular biosciences · 2022
    Article
  20. Structure-function analysis of the nsp14 N7-guanine methyltransferase reveals an essential role inProceedings of the National Academy of Sciences of the United States of America · 2021
    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

4 authors at 2 institutions in 3 countries.

Magdalena Byszewskaa International Institute of Molecular and Cell Biology ; Warsaw , Poland.
Mirosław Śmietański
Elżbieta Purta
Janusz M Bujnicki
International Institute of Molecular and Cell Biology · PLInstitute of Molecular Biology and Biotechnology · BG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes and viruses that infect them, the 5' end of mRNA molecules, and also many other functionally important RNAs, are modified to form a so-called cap structure that is important for interactions of these RNAs with many nuclear and cytoplasmic proteins. The RNA cap has multiple roles in gene expression, including enhancement of RNA stability, splicing, nucleocytoplasmic transport, and translation initiation. Apart from guanosine addition to the 5' end in the most typical cap structure common to transcripts produced by RNA polymerase II (in particular mRNA), essentially all cap modifications are due to methylation. The complexity of the cap structure and its formation can range from just a single methylation of the unprocessed 5' end of the primary transcript, as in mammalian U6 and 7SK, mouse B2, and plant U3 RNAs, to an elaborate m(7)Gpppm(6,6)AmpAmpCmpm(3)Um structure at the 5' end of processed RNA in trypanosomes, which are formed by as many as 8 methylation reactions. While all enzymes responsible for methylation of the cap structure characterized to date were found to belong to the same evolutionarily related and structurally similar Rossmann Fold Methyltransferase superfamily, that uses the same methyl group donor, S-adenosylmethionine; the enzymes also exhibit interesting differences that are responsible for their distinct functions. This review focuses on the evolutionary classification of enzymes responsible for cap methylation in RNA, with a focus on the sequence relationships and structural similarities and dissimilarities that provide the basis for understanding the mechanism of biosynthesis of different caps in cellular and viral RNAs. Particular attention is paid to the similarities and differences between methyltransferases from human cells and from human pathogens that may be helpful in the development of antiviral and antiparasitic drugs.

Indexed as

RNA Processing, Post-TranscriptionalAnimalsHumansMethylationMiceModels, MolecularRNA CapsRNA, MessengerRNA, ProtozoanRNA, ViralS-AdenosylmethioninetRNA MethyltransferasesTrypanosomaVirusesRNA CapsRNA, MessengerRNA, ProtozoanRNA, ViralS-AdenosylmethioninetRNA Methyltransferasesantiviral drugscapcrystallographymethylationmodified nucleotidesmRNApost-transcriptional modificationRNA maturationRNA modificationtrypanosomes

Identifiers

PMID25626080
PMCPMC4615557
OpenAlexW1950241215

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.