ArticleGlycobiology2018
Glycosyltransferase genes that cause monogenic congenital disorders of glycosylation are distinct from glycosyltransferase genes associated with complex diseases.
Article in Glycobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 58 citations in OpenAlex.
- Orthodox vs. Paradox: Supporting the Central Dogma With Sugar Code.Proteomics · 2026Review
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- FUT1- and GAL3ST2-mediated cellular glycan remodeling broadly restricts sialic acid-dependent viral infections.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Emerging Roles of Post-Translational Modifications in Metabolic Homeostasis and Type 2 Diabetes.International journal of molecular sciences · 2025Review
- Integrated in vivo functional screens and multiomics analyses identify α-2,3-sialylation as essential for melanoma maintenance.Science advances · 2025Article
- Urinary extracellular vesicle N-glycomics identifies diagnostic glycosignatures for bladder cancer.Nature communications · 2025Article
- O-GalNAc glycans are enriched in neuronal tracts and regulate nodes of Ranvier.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NMR Chemical Shift Prediction of Glycopeptides and Glycoproteins Aided by the Computer Program CASPER.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Unique Glycans in Synaptic Glycoproteins in Mouse Brain.ACS chemical neuroscience · 2024Article
- Developing glycoproteomics reveals the role of posttranslational glycosylation in the physiological and pathological processes of male reproduction.iMetaOmics · 2024Article
- Integrated Systems Analysis Deciphers Transcriptome and Glycoproteome Links in Alzheimer's Disease.bioRxiv : the preprint server for biology · 2024Article
- Mutations in Glycosyltransferases and Glycosidases: Implications for Associated Diseases.Biomolecules · 2024Article
- Sugar-coated bullets: Unveiling the enigmatic mystery 'sweet arsenal' in osteoarthritis.Heliyon · 2024Review
- GALNT2, an O-glycosylating enzyme, is a critical regulator of radioresistance of non-small cell lung cancer: evidence from an integrated multi-omics analysis.Cell biology and toxicology · 2023Article
- Review
- The Mutual Relationship between Glycosylation and Non-Coding RNAs in Cancer and Other Physio-Pathological Conditions.International journal of molecular sciences · 2022Review
- A Sweet Warning: Mucin-Type O-Glycans in Cancer.Cells · 2022Review
- Developments and perspectives in high-throughput protein glycomics: enabling the analysis of thousands of samples.Glycobiology · 2022Article
- Article
- Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues.Nature communications · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 3 countries.
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Abstract
Glycosylation of proteins, lipids and proteoglycans in human cells involves at least 167 identified glycosyltransferases (GTfs), and these orchestrate the biosynthesis of diverse types of glycoconjugates and glycan structures. Mutations in this part of the genome-the GTf-genome-cause more than 58 rare, monogenic congenital disorders of glycosylation (CDGs). They are also statistically associated with a large number of complex phenotypes, diseases or predispositions to complex diseases based on Genome-Wide Association Studies (GWAS). CDGs are extremely rare and often with severe medical consequences. In contrast, GWAS are likely to identify more common genetic variations and generally involve less severe and distinct traits. We recently confirmed that structural defects in GTf genes are extremely rare, which seemed at odds with the large number of GWAS pointing to GTf-genes. To resolve this issue, we surveyed the GTf-genome for reported CDGs and GWAS candidates; we found little overlap between the two groups of genes. Moreover, GTf-genes implicated by CDG or GWAS appear to constitute different classes with respect to their: (i) predicted roles in glycosylation pathways; (ii) potential for partial redundancy by closely homologous genes; and (iii) transcriptional regulation as evaluated by RNAseq data. Our analysis suggest that more complex traits are caused by dysregulation rather than structural deficiency of GTfs, which suggests that some glycosylation reactions may be predicted to be under tight regulation for fine-tuning of important biological functions.
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