ArticlePlant physiology2007
A novel family of lectins evolutionarily related to class V chitinases: an example of neofunctionalization in legumes.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
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Who cites it
26 citing papers in PubMed, 60 citations in OpenAlex.
- Chitinase-activity-independent anti-insect effect of class V chitinase from fig trees (Ficus carica).Planta · 2025Article
- Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate.Nature communications · 2024Article
- Article
- Using FIBexDB for In-Depth Analysis of Flax Lectin Gene Expression in Response toPlants (Basel, Switzerland) · 2022Article
- 130 years of Plant Lectin Research.Glycoconjugate journal · 2020Review
- Review
- Evolution and functional characterization of pectate lyase PEL12, a member of a highly expanded Clonostachys rosea polysaccharide lyase 1 family.BMC microbiology · 2018Article
- The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search.International journal of molecular sciences · 2017Article
- A single amino acid substitution in a chitinase of the legume Medicago truncatula is sufficient to gain Nod-factor hydrolase activity.Open biology · 2016Article
- Distribution and evolution of the lectin family in soybean (Glycine max).Molecules (Basel, Switzerland) · 2015Article
- Restriction and recruitment-gene duplication and the origin and evolution of snake venom toxins.Genome biology and evolution · 2014Article
- Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs).Bioinformation · 2014Article
- The nodulation factor hydrolase of Medicago truncatula: characterization of an enzyme specifically cleaving rhizobial nodulation signals.Plant physiology · 2013Article
- Article
- Sequence analysis and gene expression of putative oil palm chitinase and chitinase-like proteins in response to colonization of Ganoderma boninense and Trichoderma harzianum.Molecular biology reports · 2013Article
- High-capacity calcium-binding chitinase III from pomegranate seeds (Punica granatum Linn.) is located in amyloplasts.Plant signaling & behavior · 2011Review
- Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum.Plant molecular biology · 2011Article
- The pepper mannose-binding lectin gene CaMBL1 is required to regulate cell death and defense responses to microbial pathogens.Plant physiology · 2011Article
- Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity.Glycoconjugate journal · 2010Article
- Homeolog loss and expression changes in natural populations of the recently and repeatedly formed allotetraploid Tragopogon mirus (Asteraceae).BMC genomics · 2010Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins.
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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.