ArticleNature communications2026
Glycosite mapping and in situ mass spectrometry imaging of MUC2 glycopeptides via on-slide mucinase digestion.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
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Who cites it
2 citing papers in PubMed.
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Evolutionary Balancing of Genetic Consequence and Innovation in Mammals Through Variable Number Tandem Repeats.Genome biology and evolution · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors.
Funding
Abstract
Current analytical techniques are limited in their ability to interrogate the mechanistic relationship between aberrant mucin glycosylation and malignancy. Herein, we describe a method for mapping specific mucin glycoforms in diseased tissue, enabling correlation of the tumor glycan profile with malignant features. Following on-tissue digestion with mucinase StcE, matrix-assisted laser desorption ionization mass spectrometry imaging (MALDI-MSI) deduces the spatial distribution of mucinous O-glycopeptides that are subsequently identified using liquid chromatography coupled to mass spectrometry (LC-MS). Our coupled MS approach reveals a striking mucin 2 (MUC2) expression pattern in three colorectal mucinous adenocarcinomas, in which different glycoforms clearly stratify regions within each tumor. The LC-MS experiments obtain glycoproteomic sequence coverage of MUC2's mucin domains in unprecedented depth, and we also present evidence for an endogenous O-acetylated GalNAc. Overall, this proof-of-concept work underscores the potential of this technique to drive research in oncology and beyond.
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Registered trials
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