Evidence map›Paper›PMID 19501254›Full record

ArticleAntiviral research2009

Flaviviral methyltransferase/RNA interaction: structural basis for enzyme inhibition.

Mario Milani, Eloise Mastrangelo, Michela Bollati, Barbara Selisko, Etienne Decroly, Mickaël Bouvet, Bruno Canard, Martino Bolognesi

Open access · greenAbstract read
In one paragraph

Article in Antiviral research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

35 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Exploring the Targets of Dengue Virus and Designs of Potential Inhibitors.Combinatorial chemistry & high throughput screening · 2024
    Article
  5. Article
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  8. RNA regulatory processes in RNA virus biology.Wiley interdisciplinary reviews. RNA · 2019
    Review
  9. Frontiers in cellular and infection microbiology · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 2 countries.

Mario MilaniDepartment of Biomolecular Sciences and Biotechnology, University of Milano, Milano, Italy.
Eloise Mastrangelo
Michela Bollati
Barbara Selisko
Etienne Decroly
Mickaël Bouvet
Bruno Canard
Martino Bolognesi
University of Milan · ITArchitecture et Fonction des Macromolécules Biologiques · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flaviviruses are the causative agents of severe diseases such as Dengue or Yellow fever. The replicative machinery used by the virus is based on few enzymes including a methyltransferase, located in the N-terminal domain of the NS5 protein. Flaviviral methyltransferases are involved in the last two steps of the mRNA capping process, transferring a methyl group from S-adenosyl-L-methionine onto the N7 position of the cap guanine (guanine-N7 methyltransferase) and the ribose 2'O position of the first nucleotide following the cap guanine (nucleoside-2'O methyltransferase). The RNA capping process is crucial for mRNA stability, protein synthesis and virus replication. Such an essential function makes methyltransferases attractive targets for the design of antiviral drugs. In this context, starting from the crystal structure of Wesselsbron flavivirus methyltransferase, we elaborated a mechanistic model describing protein/RNA interaction during N7 methyl transfer. Next we used an in silico docking procedure to identify commercially available compounds that would display high affinity for the methyltransferase active site. The best candidates selected were tested in vitro to assay their effective inhibition on 2'O and N7 methyltransferase activities on Wesselsbron and Dengue virus (Dv) methyltransferases. The results of such combined computational and experimental screening approach led to the identification of a high-potency inhibitor.

Indexed as

Crystallography, X-RayFlavivirusMethyltransferasesModels, MolecularProtein BindingRNA CapsRNA, ViralViral Nonstructural ProteinsMethyltransferasesNS5 protein, flavivirusRNA CapsRNA, ViralViral Nonstructural Proteins

Identifiers

PMID19501254
PMCPMC7127253
OpenAlexW2053236406

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.