ReviewSignal transduction and targeted therapy2024
Glycosylation: mechanisms, biological functions and clinical implications.
Review in Signal transduction and targeted therapy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers, 2 of them syntheses that pooled it.
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
248 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- Epilepsy characteristics in patients with muscle-eye-brain disease: A systematic review of electroclinical features.Epileptic disorders : international epilepsy journal with videotape · 2026Pooled it
- A systematic review of protein post-translational modifications in sepsis.Molecular biology reports · 2025Pooled it
- A sequentially activated afterglow probe for AND-gated imaging of alpha-fetoprotein in hepatocellular carcinoma.Bioactive materials · 2027Article
- The dynamics of glycosylation in trophoblast cells: development, function, and pregnancy-related disorders.Annals of medicine · 2026Review
- Aberrant sialylation in cancer: From molecular mechanisms to potential therapeutics.Genes & diseases · 2026Review
- Hinge-region Cys-to-Ser mutation enables homogeneous DAR6 anti-c-Met biparatopic ADCs with tolerable O-glycosylation.Antibody therapeutics · 2026Article
- Sweetening the bonds: how O-GlcNAcylation modulates cell adhesion.Acta pharmacologica Sinica · 2026Review
- Biomaterial engineering of the tumor glycocalyx for cancer immunotherapy.Materials today. Bio · 2026Review
- The protein sequence modulates terminal GalNAc incorporation during N-glycan biosynthesis.Glycobiology · 2026Article
- Using Synthetic Glycans to Investigate Anti-Glycan Antibodies and Explore Their Medical Potential.Angewandte Chemie (International ed. in English) · 2026Review
- HMGB1 Post-Translational Modifications in Epstein-Barr Virus-Associated Nasopharyngeal Carcinoma: Current Evidence, Emerging Mechanistic Concepts, and Unresolved Questions.International journal of molecular sciences · 2026Review
- An engineered nanopore identifies saccharides, amino acids, peptides and ribonucleotides.Nature biotechnology · 2026Article
- Orthodox vs. Paradox: Supporting the Central Dogma With Sugar Code.Proteomics · 2026Review
- Mannose supports lung cancer metabolism during glycolytic limitation.EMBO reports · 2026Article
- The role of SUMOylation in regulating proteins that drive neuronal disease progression.Biochemistry and biophysics reports · 2026Review
- Heparan Sulfate Proteoglycans: Master Regulators of Cellular Signaling, Tissue Development, and Neural Function.Journal of neuroscience research · 2026Review
- Protein Posttranslational Modifications in Immunity: Molecular Mechanisms and Therapeutic Targets.MedComm · 2026Review
- Hepatic control of immunometabolism: implications for the pathogenesis, diagnosis and treatment of rheumatic diseases.Nature reviews. Rheumatology · 2026Review
- Navigating the glycomics landscape with CE-MS: advances in sample preparation and analytical strategies.The Analyst · 2026Review
- Review
188 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
3 authors.
Funding
Abstract
Protein post-translational modification (PTM) is a covalent process that occurs in proteins during or after translation through the addition or removal of one or more functional groups, and has a profound effect on protein function. Glycosylation is one of the most common PTMs, in which polysaccharides are transferred to specific amino acid residues in proteins by glycosyltransferases. A growing body of evidence suggests that glycosylation is essential for the unfolding of various functional activities in organisms, such as playing a key role in the regulation of protein function, cell adhesion and immune escape. Aberrant glycosylation is also closely associated with the development of various diseases. Abnormal glycosylation patterns are closely linked to the emergence of various health conditions, including cancer, inflammation, autoimmune disorders, and several other diseases. However, the underlying composition and structure of the glycosylated residues have not been determined. It is imperative to fully understand the internal structure and differential expression of glycosylation, and to incorporate advanced detection technologies to keep the knowledge advancing. Investigations on the clinical applications of glycosylation focused on sensitive and promising biomarkers, development of more effective small molecule targeted drugs and emerging vaccines. These studies provide a new area for novel therapeutic strategies based on glycosylation.
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.