ArticlePlant physiology2002
The liverwort contains a lectin that is structurally and evolutionary related to the monocot mannose-binding lectins.
Article in Plant physiology, 2002. 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, 26 citations in OpenAlex.
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- Review
- Classification and phylogenetic analyses of the Arabidopsis and tomato G-type lectin receptor kinases.BMC genomics · 2018Article
- Biochemical characterisation of lectin from Indian hyacinth plant bulbs with potential inhibitory action against human cancer cells.International journal of biological macromolecules · 2017Article
- Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics.International journal of molecular sciences · 2017Article
- The first trimeric Galanthus nivalis agglutinin-related lectin of Orchidaceae was found in Dendrobium pendulum: purification, characterization, and effects of stress factors.Plant cell reports · 2015Article
- Characterization and cloning of GNA-like lectin from the mushroom Marasmius oreades.Glycoconjugate journal · 2012Article
- High mannose-binding lectin with preference for the cluster of alpha1-2-mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses.The Journal of biological chemistry · 2011Article
- The pepper mannose-binding lectin gene CaMBL1 is required to regulate cell death and defense responses to microbial pathogens.Plant physiology · 2011Article
- The liverwort Marchantia polymorpha expresses orthologs of the fungal Agaricus bisporus agglutinin family.Plant physiology · 2007Article
- Phylogenetic and specificity studies of two-domain GNA-related lectins: generation of multispecificity through domain duplication and divergent evolution.The Biochemical journal · 2007Article
- Isolation and characterization of a new mannose-binding lectin gene from Taxus media.Journal of biosciences · 2004Article
- The identification of inducible cytoplasmic/nuclear carbohydrate-binding proteins urges to develop novel concepts about the role of plant lectins.Glycoconjugate journal · 2004Review
- Molecular cloning and characterization of a novel mannose-binding lectin gene from Amorphophallus konjac.Molecular biology reports · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A mannose (Man)-binding lectin has been isolated and characterized from the thallus of the liverwort Marchantia polymorpha. N-terminal sequencing indicated that the M. polymorpha agglutinin (Marpola) shares sequence similarity with the superfamily of monocot Man-binding lectins. Searches in the databases yielded expressed sequence tags encoding Marpola. Sequence analysis, molecular modeling, and docking experiments revealed striking structural similarities between Marpola and the monocot Man-binding lectins. Activity and specificity studies further indicated that Marpola is a much stronger agglutinin than the Galanthus nivalis agglutinin and exhibits a preference for methylated Man and glucose, which is unprecedented within the family of monocot Man-binding lectins. The discovery of Marpola allows us, for the first time, to corroborate the evolutionary relationship between a lectin from a lower plant and a well-established lectin family from flowering plants. In addition, the identification of Marpola sheds a new light on the molecular evolution of the superfamily of monocot Man-binding lectins. Beside evolutionary considerations, the occurrence of a G. nivalis agglutinin homolog in a lower plant necessitates the rethinking of the physiological role of the whole family of monocot Man-binding lectins.
Indexed as
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.