ReviewDiscover oncology2025
Altered glycosylation of EVs in cancers: galectin-3-binding protein (LGALS3BP).
Review in Discover oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Liver cancer derived high core fucosylation sEV elict malignancy by activating PI3K/AKT signaling pathway.Cell communication and signaling : CCS · 2026Article
- Glycosylation of Extracellular Vesicles: Analytical and Translational Insights into Biomarker Discovery and Regenerative Medicine.International journal of molecular sciences · 2026Review
- Profiling Protein Citrullination in Extracellular Vesicles by Single-Molecule Detection Using Direct Stochastic Optical Reconstruction Microscopy.Journal of biophotonics · 2026Article
- Identification Of Protein Cargo in Extracellular Vesicles from Macrophages in Progressing and Regressing Tumors.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
introductionExtracellular vesicles (EVs) are membrane-bound structures secreted by various cell types, acting as carriers of complex cargos that facilitate intercellular communication. Their presence in biofluids highlights their potential for disease biomarker identification. Glycans, crucial components of EVs, undergo glycosylation, a key post-translational modification (PTM) involved in many biological processes. Aberrant glycosylation is linked to disease, particularly cancer. AREAS COVERED: This review examines alterations in EV glycosylation patterns in cancer and their biological implications. It synthesizes findings from cell studies and biofluid analyses (including blood and urine), emphasizing the potential of combined glycosylation profiles as circulating cancer detection. Key findings highlight the elevation of terminal sialic acid levels, dysregulation of N-glycan patterns, and the identification of galectin-3-binding protein (LGALS3BP) as a common pattern of altered glycosylated protein in cancer-derived EVs. EXPERT OPINION/COMMENTARY: This review uniquely suggests a novel combination of the altered glycosylation pattern of cancer-derived EVs based on changes observed in current studies. By highlighting specific alterations that differentiate cancer-derived EVs from those of healthy origin, the analysis offers valuable insights into diagnostic and prognostic applications. These findings may facilitate the development of non-invasive biomarkers that enhance early cancer detection and monitoring.
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.