ReviewAnnals of translational medicine2014
Role of galectins in re-epithelialization of wounds.
Review in Annals of translational medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 48 citations in OpenAlex.
- Trophoblast Extracellular Vesicles as Modulators of Keratinocyte Stress Response and Senescence.Life (Basel, Switzerland) · 2025Article
- Surface-Conjugated Galactose on Electrospun Polycaprolactone Nanofibers: An Innovative Scaffold for Uterine Tissue Engineering.ACS omega · 2024Article
- Mechanisms and modeling of wound repair in the intestinal epithelium.Tissue barriers · 2023Review
- Galectin-2 in Health and Diseases.International journal of molecular sciences · 2022Review
- Increased Expression of Galectin-3 in Skin Fibrosis: Evidence from In Vitro and In Vivo Studies.International journal of molecular sciences · 2022Article
- Regulation of wound healing and fibrosis by galectins.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Galectin-8, cytokines, and the storm.Biochemical Society transactions · 2022Review
- Possible important roles of galectins in the healing of human fetal membranes.Frontiers in endocrinology · 2022Review
- Matricellular proteins in cutaneous wound healing.Frontiers in cell and developmental biology · 2022Review
- Galectins: An Ancient Family of Carbohydrate Binding Proteins with Modern Functions.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Carboxylated-xyloglucan and peptide amphiphile co-assembly in wound healing.Regenerative biomaterials · 2021Article
- Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells.International journal of molecular sciences · 2021Article
- From waste to health: sustainable exploitation of grape pomace seed extract to manufacture antioxidant, regenerative and prebiotic nanovesicles within circular economy.Scientific reports · 2020Article
- A Truncated Galectin-3 Isolated from Skin Mucus of Atlantic SalmonMarine drugs · 2020Article
- Animal Galectins and Plant Lectins as Tools for Studies in Neurosciences.Current neuropharmacology · 2020Review
- Hyaluronic Acid Accelerates Re-epithelialization and Alters Protein Expression in a Human Wound Model.Plastic and reconstructive surgery. Global open · 2019Article
- Decreased Galectin-3 and -7 Expressions in Old-Aged Skin and Their Differential Expression in Skin Equivalents.Annals of dermatology · 2018Article
- Galectin-3 regulation of wound healing and fibrotic processes: insights for chronic skin wound therapeutics.Journal of cell communication and signaling · 2018Review
- Dissecting the Structure-Activity Relationship of Galectin-Ligand Interactions.International journal of molecular sciences · 2018Review
- Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z.International journal of molecular sciences · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Re-epithelialization is a critical contributing process in wound healing in the human body. When this process is compromised, impaired or delayed, serious disorders of wound healing may result that are painful, difficult to treat, and affect a variety of human tissues. Recent studies have demonstrated that members of the galectin class of β-galactoside-binding proteins modulate re-epithelialization of wounds by novel carbohydrate-based recognition systems. Galectins constitute a family of widely distributed carbohydrate-binding proteins with the affinity for the β-galactoside-containing glycans found on many cell surface and extracellular matrix (ECM) glycoproteins. There are 15 members of the mammalian galectin family that so far have been identified. Studies of the role of galectins in wound healing have revealed that galectin-3 promotes re-epithelialization of corneal, intestinal and skin wounds; galectin-7 promotes re-epithelialization of corneal, skin, kidney and uterine wounds; and galectins-2 and -4 promote re-epithelialization of intestinal wounds. Promising prospects for developing novel therapeutic strategies for the treatment of problematic, slow- or non-healing wounds are implicit in the findings that galectins stimulate the re-epithelialization of wounds of the cornea, skin, intestinal tract and kidney. Molecular mechanisms by which galectins modulate the process of wound healing are beginning to emerge and are described in this review.
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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.