ArticleThe Biochemical journal2000
Photoaffinity labelling with P3-(4-azidoanilido)uridine 5'-triphosphate identifies gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Disruption of MaPigA, a phosphatidylinositol-N-acetylglucosaminyltransferase subunit gene, promotes cuticle penetration and immune evasion through enhancing cell wall α-1,3-glucan in Metarhizium anisopliae.Pest management science · 2026Article
- GNPNAT1 acts as a prognostic biomarker associated with immune infiltration in lung adenocarcinoma and promotes the proliferation and invasion of cancer cells.Discover oncology · 2025Article
- To each its own: Mechanisms of cross-talk between GPI biosynthesis and cAMP-PKA signaling in Candida albicans versus Saccharomyces cerevisiae.The Journal of biological chemistry · 2024Review
- GNPNAT1 Predicts Poor Prognosis and Cancer Development in Non-Small Cell Lung Cancer.Cancer management and research · 2022Article
- The Glycosylphosphatidylinositol biosynthesis pathway in human diseases.Orphanet journal of rare diseases · 2020Review
- Paroxysmal nocturnal haemoglobinuria.Nature reviews. Disease primers · 2017Review
- Biosynthesis and deficiencies of glycosylphosphatidylinositol.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2014Review
- Review
- Photoaffinity probes for studying carbohydrate biology.Journal of carbohydrate chemistry · 2012Article
- Convergent extension movements in growth plate chondrocytes require gpi-anchored cell surface proteins.Development (Cambridge, England) · 2009Article
- Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family.BMC evolutionary biology · 2008Article
- The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component.Molecular biology of the cell · 2005Article
- Gpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a subunit of the initial enzyme for glycosylphosphatidylinositol anchor biosynthesis.Eukaryotic cell · 2005Article
- Biosynthesis of glycosylphosphatidylinositol is essential to the survival of the protozoan parasite Toxoplasma gondii.Eukaryotic cell · 2003Article
- The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA).Journal of bacteriology · 2003Article
- Molecular genetics of paroxysmal nocturnal hemoglobinuria.International journal of hematology · 2003Review
- Genes for glycosylphosphatidylinositol toxin biosynthesis in Plasmodium falciparum.Infection and immunity · 2002Article
- Relationship between aplastic anemia and paroxysmal nocturnal hemoglobinuria.International journal of hematology · 2002Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Glycosylphosphatidylinositols (GPIs) are made by all eukaryotes. The first step in their synthesis is the transfer of GlcNAc from UDP-GlcNAc to phosphatidylinositol (PI). Four proteins in mammals and at least three in yeast make up a complex that carries out this reaction. Three of the proteins are highly conserved between yeast and mammals: the Gpi1 protein, the Pig-C/Gpi2 protein and the Pig-A/Gpi3 protein. The function of the individual subunits is not known, but of the three, the Pig-A/Gpi3 proteins resemble members of a large family of nucleotide-sugar-utilizing glycosyltransferases. To establish whether Gpi3p is the UDP-GlcNAc-binding subunit of the yeast GlcNAc-PI synthetic complex, we tested its ability to become cross-linked to the photoactivatable substrate analogue P(3)-(4-azidoanilido)-uridine 5'-triphosphate (AAUTP). We report that Gpi3p bearing the FLAG epitope at its C-terminus becomes cross-linked to AAUTP[alpha-(32)P], but that Gpi2p-FLAG does not. Furthermore, Gpi3p-FLAG expressed in Escherichia coli is also cross-linked. These results indicate that Gpi3p is the UDP-GlcNAc-binding and probable catalytic subunit of the GlcNAc-PI synthetic complex.
Indexed as
Identifiers
10970797PMC1221315W2132266885What 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.