ArticleMolecules (Basel, Switzerland)2023
Oligosaccharide Ligands of Galectin-4 and Its Subunits: Multivalency Scores Highly.
Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Galectin-4 contributes to the maintenance of expression and activation of multiple receptor-type kinases involved in peritoneal metastasis.Scientific reports · 2026Article
- Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.Microbial biotechnology · 2026Article
- Glycan synthesis with SpyCatcher-SpyTag immobilized Leloir-glycosyltransferases.Applied microbiology and biotechnology · 2025Article
- Inhibitory Effect of Fucoidan Analogs on Highly Metastatic Gastric Cancer Cells via Galectin-4 Inhibition.International journal of molecular sciences · 2025Article
- Human Milk Oligosaccharides Multivalently Presented on Defined Synthetic Neo-Glycoproteins Are Nanomolar Ligands of Tandem-Repeat Galectins.Biomacromolecules · 2025Article
- Characterization of HOL-30: a novel tandem-repeat galectin from the marine spongeBBA advances · 2025Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Galectins are carbohydrate-binding lectins that modulate the proliferation, apoptosis, adhesion, or migration of cells by cross-linking glycans on cell membranes or extracellular matrix components. Galectin-4 (Gal-4) is a tandem-repeat-type galectin expressed mainly in the epithelial cells of the gastrointestinal tract. It consists of an N- and a C-terminal carbohydrate-binding domain (CRD), each with distinct binding affinities, interconnected with a peptide linker. Compared to other more abundant galectins, the knowledge of the pathophysiology of Gal-4 is sparse. Its altered expression in tumor tissue is associated with, for example, colon, colorectal, and liver cancers, and it increases in tumor progression, and metastasis. There is also very limited information on the preferences of Gal-4 for its carbohydrate ligands, particularly with respect to Gal-4 subunits. Similarly, there is virtually no information on the interaction of Gal-4 with multivalent ligands. This work shows the expression and purification of Gal-4 and its subunits and presents a structure-affinity relationship study with a library of oligosaccharide ligands. Furthermore, the influence of multivalency is demonstrated in the interaction with a model lactosyl-decorated synthetic glycoconjugate. The present data may be used in biomedical research for the design of efficient ligands of Gal-4 with diagnostic or therapeutic potential.
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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.