Evidence map›Paper›PMID 16895992›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.

Fabiana Renzi, Elisa Caffarelli, Pietro Laneve, Irene Bozzoni, Maurizio Brunori, Beatrice Vallone

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

43 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Biomolecular NMR assignments · 2024
    Article
  4. SnoRNAs: Exploring Their Implication in Human Diseases.International journal of molecular sciences · 2024
    Review
  5. The Upstream 1350~1250 Nucleotide Sequences of the HumanInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Review
  8. Review
  9. Ribonuclease T2 represents a distinct circularly permutated version of the BECR RNases.Protein science : a publication of the Protein Society · 2023
    Article
  10. Apprehending the NADViruses · 2022
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2.Protein science : a publication of the Protein Society · 2020
    Article
  16. Article
  17. Article
  18. 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

6 authors at 3 institutions in 1 country.

Fabiana RenziIstituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, 00185 Rome, Italy.
Elisa Caffarelli
Pietro Laneve
Irene Bozzoni
Maurizio Brunori
Beatrice Vallone
Institute of Molecular Biology and Pathology · ITIstituto Pasteur · ITSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small nucleolar RNAs (snoRNAs) play a key role in eukaryotic ribosome biogenesis. In most cases, snoRNAs are encoded in introns and are released through the splicing reaction. Some snoRNAs are, instead, produced by an alternative pathway consisting of endonucleolytic processing of pre-mRNA. XendoU, the endoribonuclease responsible for this activity, is a U-specific, metal-dependent enzyme that releases products with 2'-3' cyclic phosphate termini. XendoU is broadly conserved among eukaryotes, and it is a genetic marker of nidoviruses, including the severe acute respiratory syndrome coronavirus, where it is essential for replication and transcription. We have determined by crystallography the structure of XendoU that, by refined search methodologies, appears to display a unique fold. Based on sequence conservation, mutagenesis, and docking simulations, we have identified the active site. The conserved structural determinants of this site may provide a framework for attempting to design antiviral drugs to interfere with the infectious nidovirus life cycle.

Indexed as

Protein Structure, TertiaryRNA Processing, Post-TranscriptionalAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayEndoribonucleasesHumansModels, MolecularMolecular Sequence DataProtein FoldingRNA, Small NuclearSequence AlignmentSevere acute respiratory syndrome-related coronavirusUridine MonophosphateVirus ReplicationEndoribonucleasesENDOU protein, XenopusRNA, Small NuclearUridine MonophosphateXenopus Proteins

Identifiers

PMID16895992
PMCPMC1567885
OpenAlexW2071358938

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.