ArticleGlycobiology2013
6-alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin type-1 repeats by protein O-fucosyltransferases 1 and 2.
Article in Glycobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.Nature chemical biology · 2025Article
- ProteinMolecules (Basel, Switzerland) · 2025Review
- In vivo evidence for GDP-fucose transport in the absence of transporter SLC35C1 and putative transporter SLC35C2.The Journal of biological chemistry · 2023Article
- Lfng and Dll3 cooperate to modulate protein interactions in cis and coordinate oscillatory Notch pathway activation in the segmentation clock.Developmental biology · 2022Article
- POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.Journal of bioenergetics and biomembranes · 2021Article
- Article
- Differential Labeling of Glycoproteins with Alkynyl Fucose Analogs.International journal of molecular sciences · 2020Article
- Inhibition of Delta-induced Notch signaling using fucose analogs.Nature chemical biology · 2018Article
- The Function of Fucosylation in Progression of Lung Cancer.Frontiers in oncology · 2018Review
- Biological functions of fucose in mammals.Glycobiology · 2017Review
- Marine Antibody-Drug Conjugates: Design Strategies and Research Progress.Marine drugs · 2017Review
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2.Nature chemical biology · 2016Article
- Chemical Lectinology: Tools for Probing the Ligands and Dynamics of Mammalian Lectins In Vivo.Chemistry & biology · 2015Review
- Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.Current biology : CB · 2015Article
- Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathway.Molecular and cellular biology · 2015Article
- O-fucosylation of the notch ligand mDLL1 by POFUT1 is dispensable for ligand function.PloS one · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein O-fucosyltransferase 1 (Pofut1) and protein O-fucosyltransferase 2 (Pofut2) add O-linked fucose at distinct consensus sequences in properly folded epidermal growth factor (EGF)-like repeats and thrombospondin type-1 (TSR) repeats, respectively. Glycan chain elongation past O-fucose can occur to yield a tetrasaccharide on EGF repeats and a disaccharide on TSRs. Elimination of Pofut1 in mice causes embryonic lethality with Notch-like phenotypes demonstrating that O-fucosylation of Notch is essential for its function. Similarly, elimination of Pofut2 results in an early embryonic lethal phenotype in mice, although the molecular mechanism for the lethality is unknown. The recent development of sugar analogs has revolutionized the study of glycans by providing a convenient method for labeling and tracking glycosylation. In order to study O-fucosylation, we took advantage of the recently developed reporter, 6-alkynyl fucose. Using the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC), or "click" reaction, azido-biotin allows tagging and detection of 6AF-modified proteins. Here we examine whether proteins containing EGF repeats or TSRs with O-fucose consensus sequences are specifically modified with 6AF in cell culture. Using mass spectrometry (MS), we demonstrate that 6AF is efficiently incorporated onto the appropriate consensus sequences on EGF repeats and TSRs. Furthermore, the elongation of the O-fucose monosaccharide on EGF repeats and TSRs is not hampered when 6AF is used. These results show that 6AF is efficiently utilized in a truly bioorthogonal manner by Pofut1, Pofut2 and the enzymes that elongate O-fucose, providing evidence that 6AF is a significant new tool in the study of protein O-fucosylation.
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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 Socratic graph.