ArticleACS chemical biology2016
Protein Sialylation Regulates a Gene Expression Signature that Promotes Breast Cancer Cell Pathogenicity.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- Enzymatic activity-independent NANS stabilizes LATS2 to drive growth and therapeutic resistance in HR+/HER2- breast cancer.Nature communications · 2026Article
- The Plasma Glycome Differences Between Women with PCOS and Healthy Controls.International journal of molecular sciences · 2026Article
- A mass spectrometry-based strategy allows signature metabolite identification in tear fluid from people with diabetic cataracts.Nature communications · 2025Article
- A20 restriction of nitric oxide production restores macrophage bioenergetic balance.bioRxiv : the preprint server for biology · 2025Article
- ST6GalNAc-I regulates tumor cell sialylation via NECTIN2/MUC5AC-mediated immunosuppression and angiogenesis in non-small cell lung cancer.The Journal of clinical investigation · 2025Article
- Ketomimetic nutrients remodel the glycocalyx and trigger a metabolic defense in breast cancer cells.Cancer & metabolism · 2025Article
- Profiling the regulatory landscape of sialylation through miRNA targeting of CMP- sialic acid synthetase.The Journal of biological chemistry · 2025Article
- Multilevel plasticity and altered glycosylation drive aggressiveness in hypoxic and glucose-deprived bladder cancer cells.iScience · 2025Article
- Sialylation-related gene signature predict prognosis and immunotherapy efficacy in low- and high-grade glioma: a PCA-based stratification study.Frontiers in oncology · 2025Article
- Article
- A Multiscale Molecular Dynamic Analysis Reveals the Effect of Sialylation on EGFR Clustering in a CRISPR/Cas9-Derived Model.International journal of molecular sciences · 2022Article
- Sialic acid: an attractive biomarker with promising biomedical applications.Asian biomedicine : research, reviews and news · 2022Review
- The different prognostic significance of polysialic acid and CD56 expression in tumor cells and lymphocytes identified in breast cancer.NPJ breast cancer · 2022Article
- Selective Enrichment of Sialylglycopeptides Enabled by Click Chemistry and Dynamic Covalent Exchange.Analytical chemistry · 2022Article
- TMT-Based Multiplexed Quantitation ofACS omega · 2022Article
- Dynamic tracing of sugar metabolism reveals the mechanisms of action of synthetic sugar analogs.Glycobiology · 2022Article
- Desalting Paper Spay Mass Spectrometry (DPS-MS) for Rapid Detection of Glycans and Glycoconjugates.International journal of mass spectrometry · 2021Article
- N-Glycan profiling of chondrocytes and fibroblast-like synoviocytes: Towards functional glycomics in osteoarthritis.Proteomics. Clinical applications · 2021Article
- Siglec Signaling in the Tumor Microenvironment.Frontiers in immunology · 2021Review
- Innate immune checkpoints for cancer immunotherapy: expanding the scope of non T cell targets.Annals of translational medicine · 2020Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Many mechanisms have been proposed for how heightened aerobic glycolytic metabolism fuels cancer pathogenicity, but there are still many unexplored pathways. Here, we have performed metabolomic profiling to map glucose incorporation into metabolic pathways upon transformation of mammary epithelial cells by 11 commonly mutated human oncogenes. We show that transformation of mammary epithelial cells by oncogenic stimuli commonly shunts glucose-derived carbons into synthesis of sialic acid, a hexosamine pathway metabolite that is converted to CMP-sialic acid by cytidine monophosphate N-acetylneuraminic acid synthase (CMAS) as a precursor to glycoprotein and glycolipid sialylation. We show that CMAS knockdown leads to elevations in intracellular sialic acid levels, a depletion of cellular sialylation, and alterations in the expression of many cancer-relevant genes to impair breast cancer pathogenicity. Our study reveals the heretofore unrecognized role of sialic acid metabolism and protein sialylation in regulating the expression of genes that maintain breast cancer pathogenicity.
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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.