Evidence map›Paper›PMID 22573863›Full record

ArticleJournal of virology2012

Crystal structure of the superfamily 1 helicase from Tomato mosaic virus.

Masaki Nishikiori, Shigeru Sugiyama, Hongyu Xiang, Mayumi Niiyama, Kazuhiro Ishibashi, Tsuyoshi Inoue, Masayuki Ishikawa, Hiroyoshi Matsumura, Etsuko Katoh

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. 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
8.5field-weighted citation impact, top 2% 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, 57 citations in OpenAlex.

  1. Review
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  4. Methotrexate, an anti-inflammatory drug, inhibits Hepatitis E viral replication.Journal of enzyme inhibition and medicinal chemistry · 2023
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  7. Review
  8. Review
  9. Review on Structures of Pesticide Targets.International journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Structural insights into RNA recognition by the Chikungunya virus nsP2 helicase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Structural basis for the recognition-evasion arms race between Tomato mosaic virus and the resistance gene Tm-1.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

9 authors at 2 institutions in 1 country.

Masaki NishikioriDivision of Plant Sciences, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan.
Shigeru Sugiyama
Hongyu Xiang
Mayumi Niiyama
Kazuhiro Ishibashi
Tsuyoshi Inoue
Masayuki Ishikawa
Hiroyoshi Matsumura
Etsuko Katoh
Institute of Agrobiological Sciences · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genomes of the Tomato mosaic virus and many other plant and animal positive-strand RNA viruses of agronomic and medical importance encode superfamily 1 helicases. Although helicases play important roles in viral replication, the crystal structures of viral superfamily 1 helicases have not been determined. Here, we report the crystal structure of a fragment (S666 to Q1116) of the replication protein from Tomato mosaic virus. The structure reveals a novel N-terminal domain tightly associated with a helicase core. The helicase core contains two RecA-like α/β domains without any of the accessory domain insertions that are found in other superfamily 1 helicases. The N-terminal domain contains a flexible loop, a long α-helix, and an antiparallel six-stranded β-sheet. On the basis of the structure, we constructed deletion mutants of the S666-to-Q1116 fragment and performed split-ubiquitin-based interaction assays in Saccharomyces cerevisiae with TOM1 and ARL8, host proteins that are essential for tomato mosaic virus RNA replication. The results suggested that both TOM1 and ARL8 interact with the long α-helix in the N-terminal domain and that TOM1 also interacts with the helicase core. Prediction of secondary structures in other viral superfamily 1 helicases and comparison of those structures with the S666-to-Q1116 structure suggested that these helicases have a similar fold. Our results provide a structural basis of viral superfamily 1 helicases.

Indexed as

Amino Acid SequenceBinding SitesGTP PhosphohydrolasesModels, MolecularMutationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryRNA HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence DeletionTobamovirusUbiquitin-Protein LigasesGTP PhosphohydrolasesRNA HelicasesSaccharomyces cerevisiae ProteinsTOM1 protein, S cerevisiaeUbiquitin-Protein Ligases

Identifiers

PMID22573863
PMCPMC3416300
OpenAlexW2124246106

What OpenQuestion holds

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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.