Evidence map›Paper›PMID 30615658›Full record

ArticlePLoS pathogens2019

The Vaccinia virion: Filling the gap between atomic and ultrastructure.

Yeva Mirzakhanyan, Paul Gershon

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Structure of the poxvirus core.Nature structural & molecular biology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

2 authors at 1 institution in 1 country.

Yeva MirzakhanyanDepartment of Molecular Biology & Biochemistry, UC-Irvine, Irvine, California, United States of America.
Paul GershonDepartment of Molecular Biology & Biochemistry, UC-Irvine, Irvine, California, United States of America.ORCID 0000-0002-4904-9193
University of California, Irvine · US

Funding

Virus-host interactions: a multi-scale training programT32AI007319 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI SEMLER, BERT L, SHI, YONGSHENG · 1988 to 2024
$2.4M
The Pox Virion Molecular InteractomeR21AI101577 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI GERSHON, PAUL D · 2013 to 2014
$410k
NIAID NIH HHS R21 AI101577NIAID NIH HHS T32 AI007319
6 · The paper itself

Abstract

We have investigated the molecular-level structure of the Vaccinia virion in situ by protein-protein chemical crosslinking, identifying 4609 unique-mass crosslink ions at an effective FDR of 0.33%, covering 2534 unique pairs of crosslinked protein positions, 625 of which were inter-protein. The data were statistically non-random and rational in the context of known structures, and showed biological rationality. Crosslink density strongly tracked the individual proteolytic maturation products of p4a and p4b, the two major virion structural proteins, and supported the prediction of transmembrane domains within membrane proteins. A clear sub-network of four virion structural proteins provided structural insights into the virion core wall, and proteins VP8 and A12 formed a strongly-detected crosslinked pair with an apparent structural role. A strongly-detected sub-network of membrane proteins A17, H3, A27 and A26 represented an apparent interface of the early-forming virion envelope with structures added later during virion morphogenesis. Protein H3 seemed to be the central hub not only for this sub-network but also for an 'attachment protein' sub-network comprising membrane proteins H3, ATI, CAHH(D8), A26, A27 and G9. Crosslinking data lent support to a number of known interactions and interactions within known complexes. Evidence is provided for the membrane targeting of genome telomeres. In covering several orders of magnitude in protein abundance, this study may have come close to the bottom of the protein-protein crosslinkome of an intact organism, namely a complex animal virus.

Indexed as

Computational BiologyMembrane ProteinsTandem Mass SpectrometryVaccinia virusViral Fusion ProteinsVirionMembrane ProteinsViral Fusion Proteins

Identifiers

PMID30615658
PMCPMC6336343
OpenAlexW2907935524

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.