ArticleThe Journal of biological chemistry
The nucleocytosolic O-fucosyltransferase SPINDLY affects protein expression and virulence in Toxoplasma gondii.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- O-fucosylation affects abundance but not localization of select nucleocytoplasmic proteins in toxoplasma gondii.Glycobiology · 2025Article
- A tale of two sugars: O-GlcNAc and O-fucose orchestrate growth, development, and acclimation in plants.Trends in biochemical sciences · 2025Review
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.mSphere · 2025Article
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.bioRxiv : the preprint server for biology · 2024Article
- Spindly is a nucleocytosolic O-fucosyltransferase in Dictyostelium and related proteins are widespread in protists and bacteria.Glycobiology · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
- SPINDLY O-fucosylates nuclear and cytoplasmic proteins involved in diverse cellular processes in plants.Plant physiology · 2023Article
- Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY.Nature communications · 2022Article
- Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants.Current opinion in structural biology · 2021Review
- Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective.Molecular & cellular proteomics : MCP · 2021Review
- Nitrogen Supply and Host-Plant Genotype Modulate the Transcriptomic Profile ofFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Once considered unusual, nucleocytoplasmic glycosylation is now recognized as a conserved feature of eukaryotes. While in animals, O-GlcNAc transferase (OGT) modifies thousands of intracellular proteins, the human pathogen Toxoplasma gondii transfers a different sugar, fucose, to proteins involved in transcription, mRNA processing, and signaling. Knockout experiments showed that TgSPY, an ortholog of plant SPINDLY and paralog of host OGT, is required for nuclear O-fucosylation. Here we verify that TgSPY is the nucleocytoplasmic O-fucosyltransferase (OFT) by 1) complementation with TgSPY-MYC
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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.