Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (697 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. glycosyltransferases carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called glycation (see maillard reaction).
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Glycosylations; Protein Glycosylation; Glycosylation, Protein; Protein Glycosylations; Sialylation; Sialylations; GlcNAcylation; GlcNAcylations.
Where it fits in the MeSH classification
- Broader topics
- Carbohydrate Metabolism; Organic Chemistry Phenomena
- See also
- Glycoproteins; Protein Processing, Post-Translational; Glycation End Products, Advanced
Related concepts
- Glycosyltransferases
- Glycation
- Maillard Reaction
Research landscape
PubMed indexes 40,788 records tagged with the MeSH heading “Glycosylation” (counts retrieved 2026-10-29). 8,342 of them (20.5%) were published from 2020 onward, and the busiest period so far is 2010-2019 with 12,882 records.
Reviews account for 4,768 records (11.7%) and meta-analyses for 20. Randomized controlled trials number 62 (0.2%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 9,257 |
| 2000-2009 | 10,307 |
| 2010-2019 | 12,882 |
| 2020 onward | 8,342 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 4,768 | 11.7% |
| Meta-analyses | 20 | 0.0% |
| Randomized controlled trials | 62 | 0.2% |
Method: PubMed query "Glycosylation"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-29.
Reading the evidence in molecular biology
Molecular biology establishes mechanisms through controlled experiments, often in simplified systems such as purified proteins, cultured cells or model organisms. Such work can show what is possible in a defined system, but whether a pathway matters in a whole organism or in human disease needs further evidence. Check the experimental system, whether findings were reproduced by independent groups, and whether the authors tested the mechanism directly or inferred it from correlation.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Hallmarks of glycosylation in cancer | 2016 | Review article Design not recorded in structured metadata | 447 | cc by PMID 27007155 · DOI · PMC5085245 |
| Glycolysis and glutaminolysis cooperatively control T cell function by limiting metabolite supply to N-glycosylation | 2017 | Research article Design not recorded in structured metadata | 181 | cc by PMID 28059703 · DOI · PMC5257256 |
| Tunicamycin specifically aggravates ER stress and overcomes chemoresistance in multidrug-resistant gastric cancer cells by inhibiting N-glycosylation | 2018 | Research article Design not recorded in structured metadata | 176 | cc by PMID 30413206 · DOI · PMC6230241 |
| N-Glycosylation Influences the Heterologous Expression of an Unspecific Peroxygenase From Marasmius rotula in Saccharomyces cerevisiae | 2026 | Research article Design not recorded in structured metadata | 0 | cc by PMID 42473306 · DOI · PMC13382365 |
Hallmarks of glycosylation in cancer [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Aberrant glycosylation plays a fundamental role in key pathological steps of tumour development and progression.
- Closing excerpt
- Rather than aberrant glycosylation being itself a hallmark of cancer, another perspective is that glycans play a role in every recognised cancer hallmark.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (108 words)
Aberrant glycosylation plays a fundamental role in key pathological steps of tumour development and progression. Glycans have roles in cancer cell signalling, tumour cell dissociation and invasion, cell-matrix interactions, angiogenesis, metastasis and immune modulation. Aberrant glycosylation is often cited as a 'hallmark of cancer' but is notably absent from both the original hallmarks of cancer and from the next generation of emerging hallmarks. This review discusses how glycosylation is clearly an enabling characteristic that is causally associated with the acquisition of all the hallmark capabilities. Rather than aberrant glycosylation being itself a hallmark of cancer, another perspective is that glycans play a role in every recognised cancer hallmark.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 27007155 · DOI · PMC5085245
Glycolysis and glutaminolysis cooperatively control T cell function by limiting metabolite supply to N-glycosylation [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Rapidly proliferating cells switch from oxidative phosphorylation to aerobic glycolysis plus glutaminolysis, markedly increasing glucose and glutamine catabolism.
- Closing excerpt
- Thus, a primary function of aerobic glycolysis and glutaminolysis is to co-operatively limit metabolite supply to N-glycan biosynthesis, an activity with widespread implications for autoimmunity and cancer.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (148 words)
Rapidly proliferating cells switch from oxidative phosphorylation to aerobic glycolysis plus glutaminolysis, markedly increasing glucose and glutamine catabolism. Although Otto Warburg first described aerobic glycolysis in cancer cells >90 years ago, the primary purpose of this metabolic switch remains controversial. The hexosamine biosynthetic pathway requires glucose and glutamine for de novo synthesis of UDP-GlcNAc, a sugar-nucleotide that inhibits receptor endocytosis and signaling by promoting N-acetylglucosamine branching of Asn (N)-linked glycans. Here, we report that aerobic glycolysis and glutaminolysis co-operatively reduce UDP-GlcNAc biosynthesis and N-glycan branching in mouse T cell blasts by starving the hexosamine pathway of glucose and glutamine. This drives growth and pro-inflammatory TH17 over anti-inflammatory-induced T regulatory (iTreg) differentiation, the latter by promoting endocytic loss of IL-2 receptor-α (CD25). Thus, a primary function of aerobic glycolysis and glutaminolysis is to co-operatively limit metabolite supply to N-glycan biosynthesis, an activity with widespread implications for autoimmunity and cancer.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 28059703 · DOI · PMC5257256
Tunicamycin specifically aggravates ER stress and overcomes chemoresistance in multidrug-resistant gastric cancer cells by inhibiting N-glycosylation [3]
Abstract reading summary — source excerpts
- Opening excerpt
- BackgroundMultidrug resistance remains a major obstacle to successful treatment for patients with gastric cancer (GC).
- Closing excerpt
- ConclusionsOur results suggest that tumor-targeted glycosylation inhibition may be a feasible strategy to reverse chemoresistance in GC patients.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (225 words)
BackgroundMultidrug resistance remains a major obstacle to successful treatment for patients with gastric cancer (GC). Recently, glycosylation has been demonstrated to play a vital role in the acquisition of multidrug resistance. As a potent inhibitor of glycosylation, tunicamycin (Tu) has shown marked antitumor activities in various cancers. In the present study, we attempted to determine the exact effect of Tu on the chemoresistance of GC.MethodsThe cytotoxic effects of drugs on GC cells were evaluated by cell viability assays, and apoptosis was detected by flow cytometry. PCR, western blot analysis, immunofluorescence staining and canonical inhibitors were employed to identify the underlying mechanisms of the specific effects of Tu on multidrug-resistant (MDR) GC cells.ResultsFor the first time, we found that MDR GC cells were more sensitive to Tu-induced cell death than the parental cells and that the increased sensitivity might correlate with basal endoplasmic reticulum (ER) stress. In addition, Tu dramatically increased chemotherapy-induced apoptosis by evoking ER stress in GC cells, particularly MDR cells. Further study indicated that these effects were highly dependent on glycosylation inhibition by Tu, rather than its role as a canonical ER stress inducer. Besides, autophagy was markedly triggered by Tu, and blocking autophagy enhanced the combined effects of Tu and chemotherapy on MDR GC cells.ConclusionsOur results suggest that tumor-targeted glycosylation inhibition may be a feasible strategy to reverse chemoresistance in GC patients.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 30413206 · DOI · PMC6230241
N-Glycosylation Influences the Heterologous Expression of an Unspecific Peroxygenase From Marasmius rotula in Saccharomyces cerevisiae [4]
Abstract reading summary — source excerpts
- Opening excerpt
- N-Linked glycosylation can have a significant impact on the yield of heterologously expressed proteins secreted by Saccharomyces cerevisiae.
- Closing excerpt
- cerevisiae.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (216 words)
N-Linked glycosylation can have a significant impact on the yield of heterologously expressed proteins secreted by Saccharomyces cerevisiae. The yeast is a widely used host for the expression of unspecific peroxygenases (UPOs), a subclass of peroxide-dependent oxidoreductases with high potential for industrial biocatalytic applications. However, the effects of N-glycosylation on the expression of recombinant UPOs have not yet been investigated. Here, we studied respective protein modification on the expression of a UPO from Marasmius rotula, belonging to the protein subfamily of short peroxygenases, in S. cerevisiae. Two of the three N-glycosylation sites that are actually occupied in rMroUPO were eliminated by substituting asparagine at positions N43 and N151 with serine. The single substitutions led to reduced amounts of secreted rMroUPO, with N43S having the highest impact (almost four times lower protein amount compared to the native enzyme) and N151S having a moderate effect. In the next step, the glycosylation probability at position 43 was enhanced by replacing the serine in the corresponding sequon with threonine, which increased the expression of the rMroUPO variant. The concentration of active UPO in the concentrated culture supernatant of the glycosylation-optimised variant S45T was twice as high as that of the native rMroUPO. The results suggest that N-linked glycosylation is an important factor for successful heterologous UPO expression in S. cerevisiae.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 42473306 · DOI · PMC13382365
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Glycosylation in health and disease [5]
- Research article Vertebrate protein glycosylation: diversity, synthesis and function [6]
- Research article The impact of glycosylation on the biological function and structure of human immunoglobulins [7]
- Research article Glycobiology [8]
- Research article Mechanisms and principles of N-linked protein glycosylation [9]
- Research article A two-way street: reciprocal regulation of metabolism and signalling [10]
References
- Munkley J, Elliott DJ. Hallmarks of glycosylation in cancer. . 2016. PMID 27007155 · DOI · PMC5085245
- Araujo L, Khim P, Mkhikian H, Mortales CL, Demetriou M, Demetriou M. Glycolysis and glutaminolysis cooperatively control T cell function by limiting metabolite supply to N-glycosylation. . 2017. PMID 28059703 · DOI · PMC5257256
- Wu J, Chen S, Liu H, Zhang Z, Ni Z, Chen J, et al.. Tunicamycin specifically aggravates ER stress and overcomes chemoresistance in multidrug-resistant gastric cancer cells by inhibiting N-glycosylation. . 2018. PMID 30413206 · DOI · PMC6230241
- Schramm M, Schmidtke KU, Kolaczek Y, Jehmlich N, Hofrichter M, Scheibner K. N-Glycosylation Influences the Heterologous Expression of an Unspecific Peroxygenase From Marasmius rotula in Saccharomyces cerevisiae. . 2026. PMID 42473306 · DOI · PMC13382365
- Reily C, Stewart TJ, Renfrow MB, Novak J. Glycosylation in health and disease. Nat Rev Nephrol. 2019. PMID 30858582 · DOI · PMC6590709
- Moremen KW, Tiemeyer M, Nairn AV. Vertebrate protein glycosylation: diversity, synthesis and function. Nat Rev Mol Cell Biol. 2012. PMID 22722607 · DOI · PMC3934011
- Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol. 2007. PMID 17029568 · DOI
- Rademacher TW, Parekh RB, Dwek RA. Glycobiology. Annu Rev Biochem. 1988. PMID 3052290 · DOI
- Schwarz F, Aebi M. Mechanisms and principles of N-linked protein glycosylation. Curr Opin Struct Biol. 2011. PMID 21978957 · DOI
- Wellen KE, Thompson CB. A two-way street: reciprocal regulation of metabolism and signalling. Nat Rev Mol Cell Biol. 2012. PMID 22395772 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-29.
See how EvidenceLib is built. Spotted an error? Email support@evidencehelix.com.
Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.