ArticleThe Journal of cell biology2007
Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist and fungal organisms.
Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Glycosylation modification: a trigger for obesity and its complications?Molecular medicine (Cambridge, Mass.) · 2026Review
- Immunomodulation by glycosylation: bridging glycobiology to adaptive immunity and therapeutic innovation.Frontiers in immunology · 2026Review
- Posttranslational sialylation and its impact on neutrophil recruitment.Journal of leukocyte biology · 2025Review
- Glycosylation: mechanisms, biological functions and clinical implications.Signal transduction and targeted therapy · 2024Review
- N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome.Experientia supplementum (2012) · 2021Review
- Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells.Glycobiology · 2019Review
- Quantitative Profiling of N-linked Glycosylation Machinery in YeastMolecular & cellular proteomics : MCP · 2018Article
- Single-subunit oligosaccharyltransferases ofThe Journal of biological chemistry · 2017Article
- Bacterial N-Glycosylation Efficiency Is Dependent on the Structural Context of Target Sequons.The Journal of biological chemistry · 2016Article
- The multiple evolutionary origins of the eukaryotic N-glycosylation pathway.Biology direct · 2016Article
- Virulence-Associated Enzymes of Cryptococcus neoformans.Eukaryotic cell · 2015Review
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Effects of N-glycan precursor length diversity on quality control of protein folding and on protein glycosylation.Seminars in cell & developmental biology · 2015Review
- Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum.Seminars in cell & developmental biology · 2015Review
- Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- N-linked protein glycosylation in the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- OST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylation.Journal of cell science · 2013Article
- A combined system for engineering glycosylation efficiency and glycan structure in Saccharomyces cerevisiae.Applied and environmental microbiology · 2013Article
- Review
- The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases.Glycobiology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The dolichol-linked oligosaccharide Glc3Man9GlcNAc2-PP-Dol is the in vivo donor substrate synthesized by most eukaryotes for asparagine-linked glycosylation. However, many protist organisms assemble dolichol-linked oligosaccharides that lack glucose residues. We have compared donor substrate utilization by the oligosaccharyltransferase (OST) from Trypanosoma cruzi, Entamoeba histolytica, Trichomonas vaginalis, Cryptococcus neoformans, and Saccharomyces cerevisiae using structurally homogeneous dolichol-linked oligosaccharides as well as a heterogeneous dolichol-linked oligosaccharide library. Our results demonstrate that the OST from diverse organisms utilizes the in vivo oligo saccharide donor in preference to certain larger and/or smaller oligosaccharide donors. Steady-state enzyme kinetic experiments reveal that the binding affinity of the tripeptide acceptor for the protist OST complex is influenced by the structure of the oligosaccharide donor. This rudimentary donor substrate selection mechanism has been refined in fungi and vertebrate organisms by the addition of a second, regulatory dolichol-linked oligosaccharide binding site, the presence of which correlates with acquisition of the SWP1/ribophorin II subunit of the OST complex.
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What OpenQuestion holds
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.