ReviewGlycobiology2012
Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.
Review in Glycobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 493 papers.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
493 citing papers in PubMed, 854 citations in OpenAlex.
- Discovery of a secretedGut microbes · 2026Article
- MUC17 and the intestinal glycocalyx: structure, regulation, and barrier function in health and disease.Bioscience reports · 2026Review
- Design rules for bioorthogonal glycan-based tools.The Biochemical journal · 2026Review
- Hinge-region Cys-to-Ser mutation enables homogeneous DAR6 anti-c-Met biparatopic ADCs with tolerable O-glycosylation.Antibody therapeutics · 2026Article
- Structural Basis of a High-Affinity Antibody Binding to Glycoprotein with Glycocalyx Decay.JACS Au · 2026Article
- An in vivo chemical genetic approach for targeted glycoproteome analysis inbioRxiv : the preprint server for biology · 2026Article
- Nanosuspension-based Ocular Therapeutics for Infection Control: Integrating Mucin Interactions and Tear Film Dynamics.AAPS PharmSciTech · 2026Review
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Integrative Principal Component-QTL Mapping Identifies Genetic Modifiers of Tumor and Metabolic Traits inInternational journal of molecular sciences · 2026Article
- Beyond the sugar coating: mucin-type O-Glycosylation as an underappreciated player in brain function and disease.Molecular psychiatry · 2026Review
- Targeting Golgi-STING Signaling to Reprogram Innate and Adaptive Immunity for the Treatment of Implant-Associated Infections.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Cancer-associated alterations in O-GalNAc glycosylation.Glycobiology · 2026Review
- Distinct O-Linked Glycosylation Systems in Signaling and Immune Regulation.International journal of molecular sciences · 2026Review
- Xylt2 Knockout Eliminates O-Xylosylation and Enhances Bone Morphogenetic Protein 2 Production in Chinese Hamster Ovary Cells.Biotechnology journal · 2026Article
- A Synergistic Inhibitor Development Strategy Against Human UDP-Galactose-4-Epimerase.Angewandte Chemie (International ed. in English) · 2026Article
- Sex differences in cardiac recovery and ventricular gene expression in a rat model of donation after circulatory death.Biology of sex differences · 2026Article
- CCHFV GP38 and GP85 interact with cell-surface glycosaminoglycans.Npj viruses · 2026Article
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Glucuronolactone Promotes Mucin Sulfation to Alleviate Deoxynivalenol-Induced Intestinal Injury via Microbiota-Dependent and -Independent AHR Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 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
433 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Glycosylation of proteins is an essential process in all eukaryotes and a great diversity in types of protein glycosylation exists in animals, plants and microorganisms. Mucin-type O-glycosylation, consisting of glycans attached via O-linked N-acetylgalactosamine (GalNAc) to serine and threonine residues, is one of the most abundant forms of protein glycosylation in animals. Although most protein glycosylation is controlled by one or two genes encoding the enzymes responsible for the initiation of glycosylation, i.e. the step where the first glycan is attached to the relevant amino acid residue in the protein, mucin-type O-glycosylation is controlled by a large family of up to 20 homologous genes encoding UDP-GalNAc:polypeptide GalNAc-transferases (GalNAc-Ts) (EC 2.4.1.41). Therefore, mucin-type O-glycosylation has the greatest potential for differential regulation in cells and tissues. The GalNAc-T family is the largest glycosyltransferase enzyme family covering a single known glycosidic linkage and it is highly conserved throughout animal evolution, although absent in bacteria, yeast and plants. Emerging studies have shown that the large number of genes (GALNTs) in the GalNAc-T family do not provide full functional redundancy and single GalNAc-T genes have been shown to be important in both animals and human. Here, we present an overview of the GalNAc-T gene family in animals and propose a classification of the genes into subfamilies, which appear to be conserved in evolution structurally as well as functionally.
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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.