ArticleGlycobiology2015
Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis.
Article in Glycobiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.
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.
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Who cites it
65 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.
- GalNAc-T14 promotes metastasis through Wnt dependent HOXB9 expression in lung adenocarcinoma.Oncotarget · 2015Pooled it
- GALNT1 emerges as a potential therapeutic target in breast cancer.Journal of cancer research and clinical oncology · 2026Article
- GalNAc-T13 maintains neurite architecture and memory retention via O-GalNAc glycosylation of seizure protein 6.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Interferon-stimulated gene GALNT2 restricts respiratory virus infections.Nature microbiology · 2026Article
- Article
- GalNT2-mediated O-glycosylation affects pancreas development and function in mice.Scientific reports · 2024Article
- Self-regulation of MGAT4A and MGAT4B activity toward glycoproteins through interaction of lectin domain with their owniScience · 2024Article
- O-glycosylation of SARS-CoV-2 spike protein by host O-glycosyltransferase strengthens its trimeric structure.Acta biochimica et biophysica Sinica · 2024Article
- Article
- An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.Science advances · 2024Article
- Upregulation of GALNT7 in prostate cancer modifies O-glycosylation and promotes tumour growth.Oncogene · 2023Article
- The effect of a methyl group on structure and function: Serine vs. threonine glycosylation and phosphorylation.Frontiers in molecular biosciences · 2023Review
- O-glycosylation and its role in therapeutic proteins.Bioscience reports · 2022Review
- Exploring the glycosylation of mucins by use of O-glycodomain reporters recombinantly expressed in glycoengineered HEK293 cells.The Journal of biological chemistry · 2022Article
- Atomic and Specificity Details of Mucin 1JACS Au · 2022Article
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Impact of Expressing Cells on Glycosylation and Glycan of the SARS-CoV-2 Spike Glycoprotein.ACS omega · 2021Article
- The Role of Data-Independent Acquisition for Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Glycoproteome remodeling in MLL-rearranged B-cell precursor acute lymphoblastic leukemia.Theranostics · 2021Article
- Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021Article
5 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
11 authors at 2 institutions in 2 countries.
Funding
Abstract
N-acetylgalactosaminyltransferase (GalNAc)-type (mucin-type) O-glycosylation is an abundant and highly diverse modification of proteins. This type of O-glycosylation is initiated in the Golgi by a large family of up to 20 homologous polypeptide GalNAc-T isoenzymes that transfer GalNAc to Ser, Thr and possibly Tyr residues. These GalNAc residues are then further elongated by a large set of glycosyltransferases to build a variety of complex O-glycan structures. What determines O-glycan site occupancy is still poorly understood, although it is clear that the substrate specificities of individual isoenzymes and the repertoire of GalNAc-Ts in cells are key parameters. The GalNAc-T isoenzymes are differentially expressed in cells and tissues in principle allowing cells to produce unique O-glycoproteomes dependent on the specific subset of isoforms present. In vitro analysis of acceptor peptide substrate specificities using recombinant expressed GalNAc-Ts has been the method of choice for probing activities of individual isoforms, but these studies have been hampered by biological validation of actual O-glycosylation sites in proteins and number of substrate testable. Here, we present a systematic analysis of the activity of 10 human GalNAc-T isoenzymes with 195 peptide substrates covering known O-glycosylation sites and provide a comprehensive dataset for evaluating isoform-specific contributions to the O-glycoproteome.
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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.