ArticleThe Plant cell1998
A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases.
Article in The Plant cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 42 citations in OpenAlex.
- Predicting the role of β-GAL genes in bean under abiotic stress and genome-wide characterization of β-GAL gene family members.Protoplasma · 2025Article
- Genetic dissection of monosaccharides contents in rice whole grain using genome-wide association study.The plant genome · 2023Article
- Identification of quantitative trait loci and candidate genes for primary metabolite content in strawberry fruit.Horticulture research · 2019Article
- The Intergenic Interplay betweenFrontiers in plant science · 2017Article
- The Putative O-Linked N-Acetylglucosamine Transferase SPINDLY Inhibits Class I TCP Proteolysis to Promote Sensitivity to Cytokinin.Plant physiology · 2016Article
- O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection.Virology · 2013Article
- O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates stress-induced heat shock protein expression in a GSK-3beta-dependent manner.The Journal of biological chemistry · 2010Article
- O-GlcNAc signaling in the cardiovascular system.Circulation research · 2010Review
- O-GlcNAc protein modification in plants: Evolution and function.Biochimica et biophysica acta · 2010Review
- Reciprocal phosphorylation and glycosylation recognition motifs control NCAPP1 interaction with pumpkin phloem proteins and their cell-to-cell movement.The Plant cell · 2007Article
- Identification of secret agent as the O-GlcNAc transferase that participates in Plum pox virus infection.Journal of virology · 2005Article
- A novel short-root gene encodes a glucosamine-6-phosphate acetyltransferase required for maintaining normal root cell shape in rice.Plant physiology · 2005Article
- The plant nuclear envelope.Planta · 2004Review
- The nuclear pore complex.Plant molecular biology · 1998Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several glycoproteins that are present at the nuclear rim and at the nuclear pore complex of tobacco suspension-cultured cells are modified by O-linked oligosaccharides with terminal N-acetylglucosamine (GlcNAc). Here, we report on the purification of several of these glycoproteins, which are referred to as terminal GlcNAc (tGlcNAc) proteins. In vitro galactosylation of the tGlcNAc proteins generated glycoproteins with terminal galactosyl-beta-1, 4-GlcNAc and thus permitted their isolation by Erythrina crystagalli agglutinin affinity chromatography. Peptide sequence information derived from one tGlcNAc protein with an apparent molecular mass of 40 to 43 kD, designated gp40, made it possible to clone its gene. Interestingly, gp40 has 28 to 34% amino acid identity to aldose-1-epimerases from bacteria, and no gene encoding an aldose-1-epimerase has been isolated previously from higher organisms. Polyclonal antibodies were generated against recombinant gp40. Consistent with its purification as a putative nuclear pore complex protein, gp40 was localized to the nuclear rim, as shown by biochemical fractionation and immunofluorescence microscopy.
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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.