ReviewGlycoconjugate journal2004
Galectin-4 in normal tissues and cancer.
Review in Glycoconjugate journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 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
73 citing papers in PubMed, 162 citations in OpenAlex.
- Trial
- Galectin-4 contributes to the maintenance of expression and activation of multiple receptor-type kinases involved in peritoneal metastasis.Scientific reports · 2026Article
- Association of Elevated Galectin-4 Concentrations with Obesity, Diabetes, and Cardiovascular Diseases.International journal of molecular sciences · 2025Review
- Inhibitory Effect of Fucoidan Analogs on Highly Metastatic Gastric Cancer Cells via Galectin-4 Inhibition.International journal of molecular sciences · 2025Article
- Review
- Multifaceted roles of Galectins: from carbohydrate binding to targeted cancer therapy.Biomarker research · 2025Review
- Application of a human lectin array to rapid in vitro screening of sugar-based epitopes that can be used as targeting tags for therapeutics.Glycobiology · 2025Article
- Article
- The impact of glycosylation on the structure, function, and interactions of CD14.Glycobiology · 2024Article
- Galectin-4 is associated with diabetes and obesity in a heart failure population.Scientific reports · 2023Observational
- Galectin-4 Is Involved in the Structural Changes of Glycosphingolipid Glycans in Poorly Differentiated Gastric Cancer Cells with High Metastatic Potential.International journal of molecular sciences · 2023Article
- Chimera and Tandem-Repeat Type Galectins: The New Targets for Cancer Immunotherapy.Biomolecules · 2023Review
- Oligosaccharide Ligands of Galectin-4 and Its Subunits: Multivalency Scores Highly.Molecules (Basel, Switzerland) · 2023Article
- Suppression of galectin-4 attenuates peritoneal metastasis of poorly differentiated gastric cancer cells.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2023Article
- Apoptosis: aJournal for immunotherapy of cancer · 2023Review
- Galectins and galectin-mediated autophagy regulation: new insights into targeted cancer therapy.Biomarker research · 2023Review
- Cytosolic galectin-4 enchains bacteria, restricts their motility, and promotes inflammasome activation in intestinal epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Blessed Union of Glycobiology and Immunology: A Marriage That Worked.Medicines (Basel, Switzerland) · 2023Review
- Review
- Galectin-4 as a Novel Biomarker of Neonatal Intestinal Injury.Digestive diseases and sciences · 2022Article
13 more citing papers are in PubMed but not listed here.
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
No grant is acknowledged in the PubMed record.
Abstract
Galectin-4 belongs to a subfamily of galectins composed of two carbohydrate recognition domains within the same peptide chain. The two domains have all the conserved galectin signature amino acids, but their overall sequences are only approximately 40% identical. Both domains bind lactose with a similar affinity as other galectins, but their respective preferences for other disaccharides, and larger saccharides, are distinctly different. Thus galectin-4 has a property of a natural cross-linker, but in a modified sense since each domain prefers a different subset of ligands. Similarly to other galectins, galectin-4 is synthesized as a cytosolic protein, but can be externalized. During development and in adult normal tissues, galectin-4 is expressed only in the alimentary tract, from the tongue to the large intestine. It is often found in relatively insoluble complexes, as a component of either adherens junctions or lipid rafts in the microvillus membrane, and it has been proposed to stabilize these structures. Strong expression of galectin-4 can be induced, however, in cancers from other tissues including breast and liver. Within a collection of human epithelial cancer cell lines, galectin-4 is overexpressed and soluble in those forming highly differentiated polarized monolayers, but absent in less differentiated ones. In cultured cells, intracellular galectin-4 may promote resistance to nutrient starvation, whereas--as an extracellular protein--it can mediate cell adhesion. Because of its distinct induction in breast and other cancers, it may be a valuable diagnostic marker and target for the development of inhibitory carbohydrate-based drugs.
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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.