Evidence map›Paper›PMID 18451263›Full record

ArticlePlant physiology2008

The "old" Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins.

Elke Fouquaert, Willy J Peumans, David F Smith, Paul Proost, Savvas N Savvides, Els J M Van Damme

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. 130 years of Plant Lectin Research.Glycoconjugate journal · 2020
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Lectin domains at the frontiers of plant defense.Frontiers in plant science · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana.Biochemical and biophysical research communications · 2011
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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 4 institutions in 2 countries.

Elke FouquaertLaboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology , Ghent University, 9000 Ghent, Belgium.
Willy J Peumans
David F Smith
Paul Proost
Savvas N Savvides
Els J M Van Damme
Emory University · USGhent University · BEKU Leuven · BERega Institute for Medical Research · BE

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
NIGMS NIH HHS GM62116
6 · The paper itself

Abstract

Molecular cloning of the "old" but still unclassified Euonymus europaeus agglutinin (EEA) demonstrated that the lectin is a homodimeric protein composed of 152 residue subunits. Analysis of the deduced sequence indicated that EEA is synthesized without a signal peptide and undergoes no posttranslational processing apart from the removal of a six-residue N-terminal peptide. Glycan array screening confirmed the previously reported high reactivity of EEA toward blood group B oligosaccharides but also revealed binding to high mannose N-glycans, providing firm evidence for the occurrence of a plant carbohydrate-binding domain that can interact with structurally different glycans. Basic Local Alignment Search Tool searches indicated that EEA shares no detectable sequence similarity with any other lectin but is closely related evolutionarily to a domain that was first identified in some abscisic acid- and salt stress-responsive rice (Oryza sativa) proteins, and, according to the available sequence data, might be ubiquitous in Spermatophyta. Hence, EEA can be considered the prototype of a novel family of presumably cytoplasmic/nuclear proteins that are apparently ubiquitous in plants. Taking into account that some of these proteins are definitely stress related, the present identification of the EEA lectin domain might be a first step in the recognition of the involvement and importance of protein-glycoconjugate interactions in some essential cellular processes in Embryophyta.

Indexed as

ABO Blood-Group SystemAmino Acid SequenceAntimicrobial Cationic PeptidesCloning, MolecularEuonymusMannoseMolecular Sequence DataPlant LectinsPlant ProteinsPolysaccharidesProtein Structure, TertiarySequence Homology, Amino AcidABO Blood-Group SystemAntimicrobial Cationic PeptidesEvonymous europa lectinMannosePlant LectinsPlant ProteinsPolysaccharides

Identifiers

PMID18451263
PMCPMC2442556
OpenAlexW2165556107

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.