Evidence map›Paper›PMID 25982526›Full record

ArticleStructure (London, England : 1993)2015

A Mimivirus Enzyme that Participates in Viral Entry.

Thomas Klose, Dominik A Herbst, Hanyu Zhu, Joann P Max, Hilkka I Kenttämaa, Michael G Rossmann

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.1field-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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Surface fibrils on the particles of nucleocytoviruses: A review.Experimental biology and medicine (Maywood, N.J.) · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Giant viruses of themicroLife · 2022
    Article
  8. Article
  9. Review
  10. Functional and evolutionary analysis of viral proteins containing a Rossmann-like fold.Protein science : a publication of the Protein Society · 2018
    Article
  11. Review
  12. The rare sugarThe Journal of biological chemistry · 2017
    Article
  13. Review
  14. Amoebae, Giant Viruses, and Virophages Make Up a Complex, Multilayered Threesome.Frontiers in cellular and infection microbiology · 2017
    Review
  15. Giant Viruses of Amoebas: An Update.Frontiers in microbiology · 2016
    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

6 authors at 1 institution in 1 country.

Thomas KloseDepartment of Biological Sciences, Purdue University, 240 South Martin Jischke Drive, West Lafayette, IN 47907-2032, USA.
Dominik A HerbstDepartment of Biological Sciences, Purdue University, 240 South Martin Jischke Drive, West Lafayette, IN 47907-2032, USA.
Hanyu ZhuDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Joann P MaxDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Hilkka I KenttämaaDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Michael G RossmannDepartment of Biological Sciences, Purdue University, 240 South Martin Jischke Drive, West Lafayette, IN 47907-2032, USA. Electronic address: mr@purdue.edu.
Purdue University West Lafayette · US

Funding

STRUCTURE OF A SMALL SPHERICAL VIRUSR37AI011219 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI ROSSMANN, MICHAEL G · 1986 to 2015
$6.6M
STRUCTURE OF A SMALL SPHERICAL VIRUSR01AI011219 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 1985 to 2020
$2.4M
NIAID NIH HHS AI011219NIAID NIH HHS R01 AI011219NIAID NIH HHS R37 AI011219
6 · The paper itself

Abstract

Mimivirus was initially identified as a bacterium because its dense, 125-nm-long fibers stained Gram-positively. These fibers probably play a role during the infection of some host cells. The normal hosts of Mimivirus are unknown, but in the laboratory Mimivirus is usually propagated in amoeba. The structure of R135, a major component of the fibrous outer layer of Mimivirus, has been determined to 2-Å resolution. The protein's structure is similar to that of members of the glucose-methanol-choline oxidoreductase family, which have an N-terminal FAD binding domain and a C-terminal substrate recognition domain. The closest homolog to R135 is an aryl-alcohol oxidase that participates in lignin biodegradation of plant cell walls. Thus R135 might participate in the degradation of their normal hosts, including some lignin-containing algae.

Indexed as

Models, MolecularVirus InternalizationChromatography, High Pressure LiquidCrystallographyDimerizationElectrophoresis, Polyacrylamide GelHost-Pathogen InteractionsMass SpectrometryMimiviridaeMolecular StructureProtein BindingProtein ConformationSubstrate SpecificityViral Structural ProteinsViral Structural Proteins

Identifiers

PMID25982526
PMCPMC4456301
OpenAlexW1895018799

What OpenQuestion holds

Textmetadata
LicenceTDM
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.