ArticleBiochimica et biophysica acta. General subjects2018
Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans.
Article in Biochimica et biophysica acta. General subjects, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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
7 citing papers in PubMed, 1 synthesis or guideline pooled it.
- MALDI-TOF mass spectrometry as a diagnostic tool in human and veterinary helminthology: a systematic review.Parasites & vectors · 2019Pooled it
- Increasing Complexity of the N-Glycome During Caenorhabditis Development.Molecular & cellular proteomics : MCP · 2023Article
- Negative-mode mass spectrometry in the analysis of invertebrate, fungal, and protist N-glycans.Mass spectrometry reviews · 2022Review
- Formation and fragmentation of doubly and triply charged ions in the negative ion spectra of neutral N-glycans from viral and other glycoproteins.Analytical and bioanalytical chemistry · 2021Article
- Comparisons of N-glycans across invertebrate phyla.Parasitology · 2019Review
- Structures and functions of invertebrate glycosylation.Open biology · 2019Review
- N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms. The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans. Unusually, this organism has three different GlcNAc-TI genes (gly-12, gly-13 and gly-14); therefore, a complete abolition of GlcNAc-TI activity required the generation of a triple knock-out strain. Previously, the compositions of N-glycans from this mutant were described, but no detailed structures. Using an off-line HPLC-MALDI-TOF-MS approach combined with exoglycosidase digestions and MS/MS, we reveal that the multiple hexose residues of the N-glycans of the gly-12;gly-13;gly-14 triple mutant are not just mannose, but include galactoses in three different positions (β-intersecting, β-bisecting and α-terminal) on isomeric forms of Hex
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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.