ArticleActa crystallographica. Section D, Biological crystallography2012
Structure of a tetrameric galectin from Cinachyrella sp. (ball sponge).
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 21 citations in OpenAlex.
- Structural Characterization of a Proto-Type Galectin fromMicroorganisms · 2026Article
- Sponge Galectins: Structure, Evolution, and Function.ACS omega · 2026Review
- Afil, a Lectin fromMicroorganisms · 2025Article
- Evolution and function of galectins inBBA advances · 2025Article
- Characterization of HOL-30: a novel tandem-repeat galectin from the marine spongeBBA advances · 2025Article
- Novel Galectins Purified from the SpongeMarine drugs · 2024Article
- Purification of Recombinant Galectins from Different Species Using Distinct Affinity Chromatography Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Review
- Marine sponge lectins: actual status on properties and biological activities.Molecules (Basel, Switzerland) · 2014Review
- Modulation of ionotropic glutamate receptor function by vertebrate galectins.The Journal of physiology · 2014Article
- Recent progress in neuroactive marine natural products.Natural product reports · 2014Review
- Isolation of novel prototype galectins from the marine ball sponge Cinachyrella sp. guided by their modulatory activity on mammalian glutamate-gated ion channels.Glycobiology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The galectins are a family of proteins that bind with highest affinity to N-acetyllactosamine disaccharides, which are common constituents of asparagine-linked complex glycans. They play important and diverse physiological roles, particularly in the immune system, and are thought to be critical metastatic agents for many types of cancer cells, including gliomas. A recent bioactivity-based screen of marine sponge (Cinachyrella sp.) extract identified an ancestral member of the galectin family based on its unexpected ability to positively modulate mammalian ionotropic glutamate receptor function. To gain insight into the mechanistic basis of this activity, the 2.1 Å resolution X-ray structure of one member of the family, galectin CchG-1, is reported. While the protomer exhibited structural similarity to mammalian prototype galectin, CchG-1 adopts a novel tetrameric arrangement in which a rigid toroidal-shaped 'donut' is stabilized in part by the packing of pairs of vicinal disulfide bonds. Twofold symmetry between binding-site pairs provides a basis for a model for interaction with ionotropic glutamate receptors.
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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.