ReviewCurrent opinion in structural biology2019
Polypeptide GalNAc-Ts: from redundancy to specificity.
Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 1 of them a synthesis 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
70 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Pooled it
- Discovery of a secretedGut microbes · 2026Article
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- mRNA Display for Identifying Peptide Substrates of Enzymes.Biochemistry · 2026Review
- A Synergistic Inhibitor Development Strategy Against Human UDP-Galactose-4-Epimerase.Angewandte Chemie (International ed. in English) · 2026Article
- The Critical Role of GALNTs-Regulated O-GalNAc Glycosylation in Cancer Malignancy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- An in vitro approach for simulating divergent Golgi O-glycosylation of tumor-associated MUC1 from normal MUC1.Nature communications · 2026Article
- Synthesis of Polyhydroxylated Pyrrolidinyl Analogs of Sugar Nucleotides. Experimental and Computational Studies on Their Interactions With GalNAC-T's.Chembiochem : a European journal of chemical biology · 2026Article
- PA14 domain of glycosyltransferase B4GALNT3 is a lectin that binds to sulfated glycan ligands.The Journal of biological chemistry · 2026Article
- Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026Review
- Intestinal Mucin Glycosylation: Structural Regulation, Homeostasis Maintenance and Disease Association.Biomolecules · 2025Review
- Posttranslational sialylation and its impact on neutrophil recruitment.Journal of leukocyte biology · 2025Review
- Loss of GalNAc-T14 links O-glycosylation defects to alterations in B cell homing in IgA nephropathy.The Journal of clinical investigation · 2025Article
- Charge matters: how flanking substrate charge modulates O-glycan Core elongation.Glycobiology · 2025Article
- Global characterization of mouse testis O-glycoproteome landscape during spermatogenesis.Nature communications · 2025Article
- Altered O-glycosylation of βThe FEBS journal · 2025Article
- SLC10A7 regulates O-GalNAc glycosylation and CaCellular and molecular life sciences : CMLS · 2025Article
- Exploring the Conformational Changes and Dynamics of Mucins in Their Free State and in Complex with Mucin-Binding Proteins Using NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Breaking Down the Bottlebrush: Atomically Detailed Structural Dynamics of Mucins.Journal of chemical information and modeling · 2024Article
- O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy.Glycobiology · 2024Review
10 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
4 authors.
Funding
Abstract
Mucin-type O-glycosylation is a post-translational modification (PTM) that is predicted to occur in more than the 80% of the proteins that pass through the Golgi apparatus. This PTM is initiated by a family of polypeptide GalNAc-transferases (GalNAc-Ts) that modify Ser and Thr residues of proteins through the addition of a GalNAc moiety. These enzymes are type II membrane proteins that consist of a Golgi luminal catalytic domain connected by a flexible linker to a ricin type lectin domain. Together, both domains account for the different glycosylation preferences observed among isoenzymes. Although it is well accepted that most of the family members share some degree of redundancy toward their protein and glycoprotein substrates, it has been recently found that several GalNAc-Ts also possess activity toward specific targets. Despite the high similarity between isoenzymes, structural differences have recently been reported that are key to understanding the molecular basis of both their redundancy and specificity. The present review focuses on the molecular aspects of the protein substrate recognition and the different glycosylation preferences of these enzymes, which in turn will serve as a roadmap to the rational design of specific modulators of mucin-type O-glycosylation.
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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.