ArticleOncogene2003
Homodimeric galectin-7 (p53-induced gene 1) is a negative growth regulator for human neuroblastoma cells.
Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 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
51 citing papers in PubMed, 149 citations in OpenAlex.
- The Galectin Family in Colorectal Cancer: Integrating Molecular Mechanisms with Diagnostic, Prognostic, and Therapeutic Perspectives.Biomedicines · 2026Review
- Correlation of Galectin Family Expression with Glioblastoma Progression and Survival.International journal of molecular sciences · 2025Article
- Review
- Unraveling the GMACS bio & med chem Au · 2025Article
- Multifaceted roles of Galectins: from carbohydrate binding to targeted cancer therapy.Biomarker research · 2025Review
- Galectin 7 leads to a relative reduction in CD4+ T cells, mediated by PD-1.Scientific reports · 2024Article
- Galectin-7 reprograms skin carcinogenesis by fostering innate immune evasive programs.Cell death and differentiation · 2023Article
- Galectins and galectin-mediated autophagy regulation: new insights into targeted cancer therapy.Biomarker research · 2023Review
- Galectin Family Members: Emerging Novel Targets for Lymphoma Therapy?Frontiers in oncology · 2022Review
- Galectins as Emerging Glyco-Checkpoints and Therapeutic Targets in Glioblastoma.International journal of molecular sciences · 2021Review
- Structural Characterization of Rat Galectin-5, an N-Tailed Monomeric Proto-Type-like Galectin.Biomolecules · 2021Article
- Functions and Inhibition of Galectin-7, an Emerging Target in Cellular Pathophysiology.Biomolecules · 2021Review
- Imitating evolution's tinkering by protein engineering reveals extension of human galectin-7 activity.Histochemistry and cell biology · 2021Article
- Structural insight into the binding of human galectins to corneal keratan sulfate, its desulfated form and related saccharides.Scientific reports · 2020Article
- Pro4 prolyl peptide bond isomerization in human galectin-7 modulates the monomer-dimer equilibrum to affect function.The Biochemical journal · 2020Article
- How galectins have become multifunctional proteins.Histology and histopathology · 2020Review
- Sweetening the hallmarks of cancer: Galectins as multifunctional mediators of tumor progression.The Journal of experimental medicine · 2020Review
- Differential Proteome Analysis of Human Neuroblastoma Xenograft Primary Tumors and Matched Spontaneous Distant Metastases.Scientific reports · 2018Article
- Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.Scientific reports · 2018Article
- The Role of Galectins in Cervical Cancer Biology and Progression.BioMed research international · 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
12 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extracellular functions of galectin-7 (p53-induced gene 1) are largely unknown. On the surface of neuroblastoma cells (SK-N-MC), the increased GM1 density, a result of upregulated ganglioside sialidase activity, is a key factor for the switch from proliferation to differentiation. We show by solid-phase and cell assays that the sugar chain of this ganglioside is a ligand for galectin-7. In serum-supplemented proliferation assays, galectin-7 reduced neuroblastoma cell growth without the appearance of features characteristic for classical apoptosis. The presence of galectin-3 blocked this effect, which mechanistically resembles that of galectin-1. By virtue of carbohydrate binding, galectin-7 thus exerts neuroblastoma growth control similar to galectin-1 despite their structural differences. In addition to p53-linked proapoptotic activity intracellularly, galectin-7, acting as a lectin on the cell surface, appears to be capable of reducing cancer cell proliferation in susceptible systems.
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.