Evidence map›Paper›PMID 19930663›Full record

ArticleBMC plant biology2009

Proteins with an Euonymus lectin-like domain are ubiquitous in Embryophyta.

Elke Fouquaert, Willy J Peumans, Tom Tm Vandekerckhove, Maté Ongenaert, Els Jm Van Damme

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Saudi journal of biological sciences · 2023
    Article
  3. Article
  4. 130 years of Plant Lectin Research.Glycoconjugate journal · 2020
    Review
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  8. Review
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  17. Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana.Biochemical and biophysical research communications · 2011
    Article
  18. 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

5 authors at 1 institution in 1 country.

Elke FouquaertLaboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.
Willy J Peumans
Tom Tm Vandekerckhove
Maté Ongenaert
Els Jm Van Damme
Ghent University · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCloning of the Euonymus lectin led to the discovery of a novel domain that also occurs in some stress-induced plant proteins. The distribution and the diversity of proteins with an Euonymus lectin (EUL) domain were investigated using detailed analysis of sequences in publicly accessible genome and transcriptome databases.

resultsComprehensive in silico analyses indicate that the recently identified Euonymus europaeus lectin domain represents a conserved structural unit of a novel family of putative carbohydrate-binding proteins, which will further be referred to as the Euonymus lectin (EUL) family. The EUL domain is widespread among plants. Analysis of retrieved sequences revealed that some sequences consist of a single EUL domain linked to an unrelated N-terminal domain whereas others comprise two in tandem arrayed EUL domains. A new classification system for these lectins is proposed based on the overall domain architecture. Evolutionary relationships among the sequences with EUL domains are discussed.

conclusionThe identification of the EUL family provides the first evidence for the occurrence in terrestrial plants of a highly conserved plant specific domain. The widespread distribution of the EUL domain strikingly contrasts the more limited or even narrow distribution of most other lectin domains found in plants. The apparent omnipresence of the EUL domain is indicative for a universal role of this lectin domain in plants. Although there is unambiguous evidence that several EUL domains possess carbohydrate-binding activity further research is required to corroborate the carbohydrate-binding properties of different members of the EUL family.

Indexed as

Evolution, MolecularAntimicrobial Cationic PeptidesComputational BiologyGene Expression ProfilingPhylogenyPlant LectinsPlant ProteinsPlantsProtein Structure, TertiarySequence Analysis, ProteinAntimicrobial Cationic PeptidesEvonymous europa lectinPlant LectinsPlant Proteins

Identifiers

PMID19930663
PMCPMC2788552
OpenAlexW2013102368

What OpenQuestion holds

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LicenceCC BY
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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.