ArticleBiomolecules2012
Promiscuity of the euonymus carbohydrate-binding domain.
Article in Biomolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Mutation of a gene with PWWP domain confers salt tolerance in rice.Plant molecular biology · 2025Article
- Article
- Plant lectins: Handymen at the cell surface.Cell surface (Amsterdam, Netherlands) · 2022Review
- Mucin Glycans Signal through the Sensor Kinase RetS to Inhibit Virulence-Associated Traits in Pseudomonas aeruginosa.Current biology : CB · 2021Article
- Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.International journal of molecular sciences · 2019Review
- Messages From the Past: New Insights in Plant Lectin Evolution.Frontiers in plant science · 2019Article
- Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa).Rice (New York, N.Y.) · 2017Article
- Article
- Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics.International journal of molecular sciences · 2017Article
- Evolution and structural diversification of Nictaba-like lectin genes in food crops with a focus on soybean (Glycine max).Annals of botany · 2017Article
- Protein-carbohydrate interactions as part of plant defense and animal immunity.Molecules (Basel, Switzerland) · 2015Review
- Distribution and evolution of the lectin family in soybean (Glycine max).Molecules (Basel, Switzerland) · 2015Article
- Insights into animal and plant lectins with antimicrobial activities.Molecules (Basel, Switzerland) · 2015Review
- Lectin domains at the frontiers of plant defense.Frontiers in plant science · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Plants synthesize small amounts of carbohydrate-binding proteins on exposure to stress. For example, on exposure to drought, high salt, wounding and by treatment with some plant hormones or by pathogen attack. In contrast to the 'classical' plant lectins that are mostly located in the vacuolar compartment, this new class of inducible lectins is present in the cytoplasm and in the nucleus. Taking into account that any physiological role of plant lectins most likely relies on their specific carbohydrate-binding activity and specificity, the discovery of these stress-related lectins provides strong evidence for the importance of protein-carbohydrate-interactions in plant cells. Hitherto, six families of such nucleocytoplasmic lectins have been identified in plants. This review will focus on the nucleocytoplasmic lectins with one or more Euonymus lectin (EUL) domain(s). The carbohydrate-binding specificity of EUL proteins from a monocot, a dicot and a lower plant has been compared. Furthermore, modeling of the different EUL domains revealed a similar ß-trefoil fold consisting of three bundles of ß-sheet organized around a pseudo three-fold symmetry axis. Despite the sequence similarity and the conserved amino acids in the binding site, glycan array analyses showed that the EUL domain has a promiscuous carbohydrate-binding site capable of accommodating high mannose N-glycans, blood group B related structures and galactosylated epitopes.
Identifiers
What OpenQuestion holds
Registered trials
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.