ArticleGlycoconjugate journal2014
Novel roles for O-linked glycans in protein folding.
Article in Glycoconjugate journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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.
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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.
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Who cites it
44 citing papers in PubMed.
- Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.The Journal of biological chemistry · 2026Article
- O-mannosylation and furin processing are critical maturation events for the KIAA1549 protein implicated in pediatric pilocytic astrocytomas.The Journal of biological chemistry · 2026Article
- Glycosylation as a dynamic regulator of RLR and cGAS-STING innate immune signalling pathways.Communications biology · 2026Review
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Transformer-based Deep Learning for Glycan Structure Inference from Tandem Mass Spectrometry.bioRxiv : the preprint server for biology · 2025Article
- Glycosylation editing: an innovative therapeutic opportunity in precision oncology.Molecular and cellular biochemistry · 2025Review
- Substrate O-glycosylation actively regulates extracellular proteolysis.Protein science : a publication of the Protein Society · 2024Article
- Glycan Modifications as Regulators of Stem Cell Fate.Biology · 2024Review
- Exploring the diverse biological significance and roles of fucosylated oligosaccharides.Frontiers in molecular biosciences · 2024Review
- Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- O-fucosylation stabilizes the TSR3 motif in thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond.The Journal of biological chemistry · 2022Article
- Significant Roles of NotchMolecules (Basel, Switzerland) · 2022Review
- Hydrocephalus in mouse B3glct mutants is likely caused by defects in multiple B3GLCT substrates in ependymal cells and subcommissural organ.Glycobiology · 2021Article
- Current Views on the Roles ofBiomolecules · 2021Review
- Glycosylation in Cervical Cancer: New Insights and Clinical Implications.Frontiers in oncology · 2021Review
- The Importance of Glycosylation in COVID-19 Infection.Advances in experimental medicine and biology · 2021Article
- FGDB: Database of follicle stimulating hormone glycans.Computational and structural biotechnology journal · 2021Article
- The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1.The Journal of biological chemistry · 2020Article
- Xylosyl Extension ofCells · 2020Article
- Post-translational protein modifications in schizophrenia.NPJ schizophrenia · 2020Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
N-Glycosylation has long been linked to protein folding and quality control in the endoplasmic reticulum (ER). Recent work has shown that O-linked glycosylation and the corresponding glycosyltransferases also participate in this important function. Notably, Protein O-fucosyltransferase 1 (Ofut1/Pofut1), a soluble, ER localized enzyme that fucosylates Epidermal Growth Factor-like (EGF) repeats, functions as a chaperone involved in the proper localization of the Notch receptor in certain contexts. Pofut2, a related enzyme that modifies Thrombospondin type I repeats (TSRs), has also been hypothesized to play a role in the folding and quality control of TSR-containing proteins. Both enzymes only modify fully folded substrates suggesting that they are able to distinguish between folded and unfolded structures. Pofuts have known physiological relevance and are conserved across metazoans. Though consensus sequences for O-fucosylation have been established and structures of both Pofuts have been studied, the mechanism of how they participate in protein folding is not known. This article discusses past and recent advances made in novel roles for these protein O-glycosyltransferases.
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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.