ReviewTraffic (Copenhagen, Denmark)2014
Glycosylation of the nuclear pore.
Review in Traffic (Copenhagen, Denmark), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
43 citing papers in PubMed, 67 citations in OpenAlex.
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Perturbing nuclear glycosylation in the mouse preimplantation embryo slows down embryonic development.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025Review
- Cytoplasmic nucleoporin assemblage: the cellular artwork in physiology and disease.Nucleus (Austin, Tex.) · 2024Review
- Rapid and large-scale glycopeptide enrichment strategy based on chemical ligation.National science review · 2024Article
- Review
- Importin-7-dependent nuclear translocation of the Flavivirus core protein is required for infectious virus production.PLoS pathogens · 2024Article
- Impact of distinct FG nucleoporin repeats on Nup98 self-association.Nature communications · 2024Article
- Chemoproteomic profiling of O-GlcNAcylated proteins and identification of O-GlcNAc transferases in rice.Plant biotechnology journal · 2023Article
- Glycan analysis of Lamin A/C protein at G2/M and S phases of the cell cycle.Cell biochemistry and biophysics · 2022Article
- An introduction to dynamic nucleoporins inJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2022Review
- Article
- Cellular Stress Induces Nucleocytoplasmic Transport Deficits Independent of Stress Granules.Biomedicines · 2022Article
- Methods to separate nuclear soluble fractions reflecting localizations in living cells.iScience · 2021Article
- Truncation of the TPR domain of OGT alters substrate and glycosite selection.Analytical and bioanalytical chemistry · 2021Article
- O-GlcNAc modification of nuclear pore complexes accelerates bidirectional transport.The Journal of cell biology · 2021Article
- Article
- Role ofPhysiological reviews · 2021Review
- Nuclear Import of Adeno-Associated Viruses Imaged by High-Speed Single-Molecule Microscopy.Viruses · 2021Review
- Multifunctionality of F-rich nucleoporins.Biochemical Society transactions · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The O-linked β-N-acetylglucosamine (O-GlcNAc) posttranslational modification was first discovered 30 years ago and is highly concentrated in the nuclear pore. In the years since the discovery of this single sugar modification, substantial progress has been made in understanding the biochemistry of O-GlcNAc and its regulation. Nonetheless, O-GlcNAc modification of proteins continues to be overlooked, due in large part to the lack of reliable methods available for its detection. Recently, a new crop of immunological and chemical detection reagents has changed the research landscape. Using these tools, approximately 1000 O-GlcNAc-modified proteins have been identified. While other forms of glycosylation are typically associated with extracellular proteins, O-GlcNAc is abundant on nuclear and cytoplasmic proteins. In particular, phenylalanine-glycine nucleoporins are heavily O-GlcNAc-modified. Recent experiments are beginning to provide insight into the functional implications of O-GlcNAc modification on certain proteins, but its role in the nuclear pore has remained enigmatic. However, tantalizing new results suggest that O-GlcNAc may play roles in regulating nucleocytoplasmic transport.
Indexed as
Identifiers
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.