Evidence map›Paper›PMID 25690795›Full record

ReviewViruses2015

Poxviral ankyrin proteins.

Michael H Herbert, Christopher J Squire, Andrew A Mercer

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Pathogens (Basel, Switzerland) · 2025
    Article
  8. Infection and immunity · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. A comprehensive review of monkeypox virus and mpox characteristics.Frontiers in cellular and infection microbiology · 2024
    Review
  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

3 authors at 2 institutions in 1 country.

Michael H HerbertSchool of Biological Sciences, University of Auckland, Auckland 1010, New Zealand. mher065@aucklanduni.ac.nz.
Christopher J SquireSchool of Biological Sciences, University of Auckland, Auckland 1010, New Zealand. c.squire@auckland.ac.nz.
Andrew A MercerVirus Research Unit, Department of Microbiology and Immunology, University of Otago, Dunedin 9016, New Zealand. andy.mercer@otago.ac.nz.
University of Auckland · NZUniversity of Otago · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multiple repeats of the ankyrin motif (ANK) are ubiquitous throughout the kingdoms of life but are absent from most viruses. The main exception to this is the poxvirus family, and specifically the chordopoxviruses, with ANK repeat proteins present in all but three species from separate genera. The poxviral ANK repeat proteins belong to distinct orthologue groups spread over different species, and align well with the phylogeny of their genera. This distribution throughout the chordopoxviruses indicates these proteins were present in an ancestral vertebrate poxvirus, and have since undergone numerous duplication events. Most poxviral ANK repeat proteins contain an unusual topology of multiple ANK motifs starting at the N-terminus with a C-terminal poxviral homologue of the cellular F-box enabling interaction with the cellular SCF ubiquitin ligase complex. The subtle variations between ANK repeat proteins of individual poxviruses suggest an array of different substrates may be bound by these protein-protein interaction domains and, via the F-box, potentially directed to cellular ubiquitination pathways and possible degradation. Known interaction partners of several of these proteins indicate that the NF-κB coordinated anti-viral response is a key target, whilst some poxviral ANK repeat domains also have an F-box independent affect on viral host-range.

Indexed as

Ankyrin RepeatAmino Acid MotifsAnkyrinsF-Box MotifsHost-Pathogen InteractionsNF-kappa BPhylogenyPoxviridaeProtein BindingViral ProteinsAnkyrinsNF-kappa BViral Proteins

Identifiers

PMID25690795
PMCPMC4353913
OpenAlexW1972124261

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.