ReviewCurrent opinion in chemical biology2023
Proximity labeling technologies to illuminate glycan-protein interactions.
Review in Current opinion in chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 14 citations in OpenAlex.
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Recent Advances in Proximity Labeling-Based Subcellular Proteomic Mapping.Molecular & cellular proteomics : MCP · 2026Review
- A Brief Progress in Methods for Deciphering Protein-Protein Interaction Networks.International journal of molecular sciences · 2026Review
- Mapping GlycoRNAs on an Exosomal Surface.Journal of the American Chemical Society · 2026Article
- Mapping the placental galectin-3 interactome identifies CD9 and ITGB1 as functional glycoprotein counterreceptors during syncytialization.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Tools to investigate the cell surface: Proximity as a central concept in glycoRNA biology.Cell chemical biology · 2024Review
- Protein oxidation of fucose environments (POFE) reveals fucose-protein interactions.Chemical science · 2024Article
- Chemical and Biological Strategies for Profiling Protein-Protein Interactions in Living Cells.Chemistry, an Asian journal · 2023Review
- Mass spectrometry-based methods for investigating the dynamics and organization of the surfaceome: exploring potential clinical implications.Expert review of proteomicsReview
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
Glycosylation is a ubiquitous post-translational modification read by glycan-binding proteins (GBP) to encode important functions, but a robust understanding of these interactions and their consequences can be challenging to uncover. Glycan-GBP interactions are transient and weak, making them difficult to capture, and glycosylation is dynamic and heterogenous, necessitating study in native cellular environments to identify endogenous ligands. Proximity labeling, an experimental innovation that labels biomolecules close to a protein of interest, has recently emerged as a powerful strategy to overcome these limitations, allowing interactors to be tagged in cells for subsequent enrichment and identification by mass spectrometry-based proteomics. We will describe this nascent technique and discuss its applications in the last five years with different GBP classes, including Siglecs, galectins, and non-human lectins.
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.