SynthesisCells2020
A Systematic Review on the Implications of O-linked Glycan Branching and Truncating Enzymes on Cancer Progression and Metastasis.
Synthesis in Cells, 2020. 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, 79 citations in OpenAlex.
- Unique N-glycoproteomics and phosphoproteomics of mucins predict clinical outcomes in pancreatic ductal adenocarcinoma.Cancer letters · 2026Article
- Distinct glycosyltransferase expression governs organ-specific survival in pancreatic cancer metastasis.Oncogene · 2026Article
- GCNT3 and ST3GAL1 expression correlates with HER2 status and MUC1/β-catenin/Cyclin D1 axis in breast cancer.BMC cancer · 2026Article
- GlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis.Analytical chemistry · 2025Article
- Edible Bird Nest Supplementation Enhances Male Reproductive Function: Current Insights and Future Horizons.Foods (Basel, Switzerland) · 2025Review
- Glycosylation in cancer: mechanisms, diagnostic markers, and therapeutic applications.Molecular and cellular biochemistry · 2025Review
- Neurogenic locus notch homolog protein 1 (NOTCH 1) SNP informatics coupled with intrinsically disordered regions and post-translational modifications reveals the complex structural crosstalk of Lung Adenocarcinoma (LUAD).Frontiers in bioinformatics · 2025Article
- Leucine zipper-based SAIM imaging identifies therapeutic agents to disrupt the cancer cell glycocalyx for enhanced immunotherapy.bioRxiv : the preprint server for biology · 2024Article
- Cosmc regulates O-glycan extension in murine hepatocytes.Glycobiology · 2024Article
- Progress of Exosomal LncRNAs in Pancreatic Cancer.International journal of molecular sciences · 2024Review
- Substrate O-glycosylation actively regulates extracellular proteolysis.Protein science : a publication of the Protein Society · 2024Article
- Characterizing Glycosylation of Adeno-Associated Virus Serotype 9 Capsid Proteins Generated from HEK293 Cells through Glycopeptide Mapping and Released Glycan Analysis.Microorganisms · 2024Article
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- Detection of Tn-antigen in breast and prostate cancer models by VVL-labeled red dye-doped nanoparticles.Nanomedicine (London, England) · 2024Article
- Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments.Frontiers in immunology · 2024Review
- Article
- Mucin Glycans: A Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023Review
- Review
- Oxidative Release ofAnalytical chemistry · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Glycosylation is the most commonly occurring post-translational modifications, and is believed to modify over 50% of all proteins. The process of glycan modification is directed by different glycosyltransferases, depending on the cell in which it is expressed. These small carbohydrate molecules consist of multiple glycan families that facilitate cell-cell interactions, protein interactions, and downstream signaling. An alteration of several types of O-glycan core structures have been implicated in multiple cancers, largely due to differential glycosyltransferase expression or activity. Consequently, aberrant O-linked glycosylation has been extensively demonstrated to affect biological function and protein integrity that directly result in cancer growth and progression of several diseases. Herein, we provide a comprehensive review of several initiating enzymes involved in the synthesis of O-linked glycosylation that significantly contribute to a number of different cancers.
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.