Evidence map›Paper›PMID 32203412›Full record

ArticleNature chemical biology2020

Atomic structure of potato virus X, the prototype of the Alphaflexiviridae family.

Alessandro Grinzato, Eaazhisai Kandiah, Chiara Lico, Camilla Betti, Selene Baschieri, Giuseppe Zanotti

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.3field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Switch-like compaction of poly(ADP-ribose) upon cation binding.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Citrus sudden death-associated virus as a new expression vector for rapidBiotechnology reports (Amsterdam, Netherlands) · 2022
    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 2 countries.

Alessandro GrinzatoDepartment of Biomedical Sciences, University of Padua, Padua, Italy.ORCID http://orcid.org/0000-0001-6307-3053
Eaazhisai KandiahEuropean Synchrotron Radiation Facility, Grenoble, France.
Chiara LicoLaboratory of Biotechnology, ENEA Casaccia Research Center, Rome, Italy.ORCID http://orcid.org/0000-0001-8475-5141
Camilla BettiLaboratory of Biotechnology, ENEA Casaccia Research Center, Rome, Italy.ORCID http://orcid.org/0000-0003-3522-6440
Selene BaschieriLaboratory of Biotechnology, ENEA Casaccia Research Center, Rome, Italy.ORCID http://orcid.org/0000-0001-7147-7840
Giuseppe ZanottiDepartment of Biomedical Sciences, University of Padua, Padua, Italy. giuseppe.zanotti@unipd.it.ORCID http://orcid.org/0000-0002-0945-6501
National Agency for New Technologies, Energy and Sustainable Economic Development · ITUniversity of Padua · ITEuropean Synchrotron Radiation Facility · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Potato virus X (PVX) is a positive-sense single-stranded RNA (ssRNA) filamentous plant virus belonging to the Alphaflexiviridae family, considered in recent years as a tool for nanotechnology applications. We present the cryo-electron microscopy structure of the PVX particle at a resolution of 2.2 Å. The well-defined density of the coat proteins and of the genomic RNA allowed a detailed analysis of protein-RNA interactions, including those mediated by solvent molecules. The particle is formed by repeated segments made of 8.8 coat proteins, forming a left-handed helical structure. The RNA runs in an internal crevice along the virion, packaged in 5-nucleotide repeats in which the first four bases are stacked in the classical way, while the fifth is rotated and nearly perpendicular. The resolution of the structure described here suggests a mechanism for the virion assembly and potentially provides a platform for the rational design of antiviral compounds and for the use of PVX in nanotechnology.

Indexed as

CapsidCapsid ProteinsCryoelectron MicroscopyModels, MolecularPotexvirusRNA, ViralVirionCapsid ProteinsRNA, Viral

Identifiers

PMID32203412
OpenAlexW3012147804

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.