Evidence map›Paper›PMID 31662460›Full record

ArticlemBio2019

Crystal Structure of African Swine Fever Virus dUTPase Reveals a Potential Drug Target.

Changyao Li, Yan Chai, Hao Song, Changjiang Weng, Jianxun Qi, Yeping Sun, George F Gao

Open access · goldAbstract read
In one paragraph

Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Is dUTPase Enzymatic Activity Truly Essential for Viability?International journal of molecular sciences · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Journal of virology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Deletion of theJournal of virology · 2022
    Article
  19. Article
  20. Review
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

7 authors at 3 institutions in 1 country.

Changyao LiCollege of Veterinary Medicine, China Agricultural University, Beijing, China.
Yan ChaiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Hao SongResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-2811-0370
Changjiang WengState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Jianxun QiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-9358-4732
Yeping SunCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China sunyeping@im.ac.cn gaof@im.ac.cn.
George F GaoCollege of Veterinary Medicine, China Agricultural University, Beijing, China sunyeping@im.ac.cn gaof@im.ac.cn.ORCID 0000-0002-3869-615X
Chinese Academy of Sciences · CNChinese Academy of Agricultural Sciences · CNChinese Center For Disease Control and Prevention · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

E165R, a highly specific dUTP nucleotidohydrolase (dUTPase) encoded by the African swine fever virus (ASFV) genome, is required for productive replication of ASFV in swine macrophages. Here, we solved the high-resolution crystal structures of E165R in its apo state and in complex with its product dUMP. Structural analysis explicitly defined the architecture of the active site of the enzyme as well as the interaction between the active site and the dUMP ligand. By comparing the ASFV E165R structure with dUTPase structures from other species, we found that the active site of E165R is highly similar to those of dUTPases from

Indexed as

African Swine FeverAfrican Swine Fever VirusAnimalsBinding SitesCatalytic DomainCloning, MolecularCrystallography, X-RayDrug Delivery SystemsDrug DesignKineticsModels, MolecularMycobacterium tuberculosisPlasmodium falciparumProtein ConformationPyrophosphatasesSequence AlignmentdUTP pyrophosphatasePyrophosphatasesAfrican swine fever viruscrystal structuredrug targetdUTPaseE165R

Identifiers

PMID31662460
PMCPMC6819664
OpenAlexW2982653137

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.