ReviewMolecular oncology2010
Glycan gene expression signatures in normal and malignant breast tissue; possible role in diagnosis and progression.
Review in Molecular oncology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.
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
86 citing papers in PubMed, 1 synthesis or guideline pooled it, 170 citations in OpenAlex.
- Fucosyltransferase 8 is Overexpressed and Influences Clinical Outcomes in Lung Adenocarcinoma Patients.Pathology oncology research : POR · 2022Pooled it
- Markers of Inflammation and Incident Breast Cancer Risk in the Women's Health Study.American journal of epidemiology · 2018Trial
- Glycan and glycoprotein signatures in tumor-induced liver alterations in a murine breast cancer model.Molecular genetics and genomics : MGG · 2026Article
- Functional regulation of GlycoRNA and progress in malignant tumors.Journal of translational medicine · 2026Review
- Evaluating the CRP Interactome: Insights into Possible Novel Roles in Cellular Signaling and Tumorigenicity.Current issues in molecular biology · 2025Review
- Altered Cell SurfaceJournal of proteome research · 2025Article
- GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau.Nature communications · 2025Article
- Identification of the specific characteristics of neuroendocrine prostate cancer: Immune status, hub genes and treatment.Translational oncology · 2025Article
- Roles of core fucosylation modification in immune system and diseases.Cell insight · 2025Review
- Glycosylation in Cancer.Handbook of experimental pharmacology · 2025Review
- Decoding the glycoproteome: a new frontier for biomarker discovery in cancer.Journal of hematology & oncology · 2024Review
- When a negative (charge) is not a positive: sialylation and its role in cancer mechanics and progression.Frontiers in oncology · 2024Review
- The sialyl-Tn antigen synthase genes regulates migration-proliferation dichotomy in prostate cancer cells under hypoxia.Glycoconjugate journal · 2023Article
- Association of Glycosylation-Related Genes with Different Patterns of Immune Profiles and Prognosis in Cervical Cancer.Journal of personalized medicine · 2023Article
- Targeting the stage-specific embryonic antigen (SSEA)-0 tumor neoantigen.Current trends in immunology · 2023Article
- Efficient TurboID-based proximity labelling method for identifying terminal sialic acid glycosylation in living cells.Acta biochimica et biophysica Sinica · 2022Article
- High-Throughput Glycomic Methods.Chemical reviews · 2022Review
- Pathological implication of protein post-translational modifications in cancer.Molecular aspects of medicine · 2022Review
- An Integrated Mass Spectrometry-Based Glycomics-Driven Glycoproteomics Analytical Platform to Functionally Characterize Glycosylation Inhibitors.Molecules (Basel, Switzerland) · 2022Article
- Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation is the stepwise procedure of covalent attachment of oligosaccharide chains to proteins or lipids, and alterations in this process have been associated with malignant transformation. Simultaneous analysis of the expression of all glycan-related genes clearly gives the advantage of enabling a comprehensive view of the genetic background of the glycobiological changes in cancer cells. Studies focusing on the expression of the whole glycome have now become possible, which prompted us to review the present knowledge on glycosylation in relation to breast cancer diagnosis and progression, in the light of available expression data from tumors and breast tissue of healthy individuals. We used various data resources to select a set of 419 functionally relevant genes involved in synthesis, degradation and binding of N-linked and O-linked glycans, Lewis antigens, glycosaminoglycans (chondroitin, heparin and keratan sulfate in addition to hyaluronan) and glycosphingolipids. Such glycans are involved in a number of processes relevant to carcinogenesis, including regulation of growth factors/growth factor receptors, cell-cell adhesion and motility as well as immune system modulation. Expression analysis of these glycan-related genes revealed that mRNA levels for many of them differ significantly between normal and malignant breast tissue. An associative analysis of these genes in the context of current knowledge of their function in protein glycosylation and connection(s) to cancer indicated that synthesis, degradation and adhesion mediated by glycans may be altered drastically in mammary carcinomas. Although further analysis is needed to assess how changes in mRNA levels of glycan genes influence a cell's glycome and the precise role that such altered glycan structures play in the pathogenesis of the disease, lessons drawn from this study may help in determining directions for future research in the rapidly-developing field of glycobiology.
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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.