ArticleProceedings of the National Academy of Sciences of the United States of America2011
Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 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
112 citing papers in PubMed, 213 citations in OpenAlex.
- Design rules for bioorthogonal glycan-based tools.The Biochemical journal · 2026Review
- An in vivo chemical genetic approach for targeted glycoproteome analysis inbioRxiv : the preprint server for biology · 2026Article
- Iterative Bump-and-Hole Engineering Creates a Bioorthogonal Reporter forJournal of the American Chemical Society · 2026Article
- Iterative Bump-and-hole engineering creates a bioorthogonal reporter forbioRxiv : the preprint server for biology · 2026Article
- Chemoenzymatic Synthesis and Purification of Bioorthogonally Tagged UDP-GlcNAc and UDP-GalNAc Analogues.Current protocols · 2025Article
- Glycosylation in neuroinflammation: mechanisms, implications, and therapeutic strategies for neurodegenerative diseases.Translational neurodegeneration · 2025Review
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Selective bioorthogonal probe for N-glycan hybrid structures.Nature chemical biology · 2025Article
- Article
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024Review
- Metabolic Usage and Glycan Destinations of GlcNAz inACS chemical biology · 2024Article
- Combining Selective Enrichment and a Boosting Approach to Globally and Site-Specifically Characterize Protein Co-translationalAnalytical chemistry · 2023Article
- A bioorthogonal chemistry approach to detect the K1 polysialic acid capsule inRSC chemical biology · 2023Article
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Cell-specific bioorthogonal tagging of glycoproteins.Nature communications · 2022Article
- Nutrient-sensitive protein O-GlcNAcylation shapes daily biological rhythms.Open biology · 2022Review
- Quantification of Protein Glycosylation Using Nanopores.Nano letters · 2022Article
- Spatial and temporal proteomics reveals the distinct distributions and dynamics of O-GlcNAcylated proteins.Cell reports · 2022Article
- Cell-type-specific labeling and profiling of glycans in living mice.Nature chemical biology · 2022Article
- Reengineering of cancer cell surface charges can modulate cell migration.Chemical communications (Cambridge, England) · 2022Article
52 more citing papers are in PubMed but not listed here.
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
The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes. Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells. This strategy is based on metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway. When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins. Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz. We confirmed previous results that GlcNAz can be metabolically interconverted to GalNAz, whereas GlcNAlk does not, thereby yielding a more specific metabolic reporter of O-GlcNAc modification. We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins. Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
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.