ArticleGlycobiology2017
Identification of lectin counter-receptors on cell membranes by proximity labeling.
Article in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 31 citations in OpenAlex.
- Proximity Labeling and Genetic Screening Reveal that DSG2 is a Counter Receptor of Siglec-9 and Suppresses Macrophage Phagocytosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Tools to investigate the cell surface: Proximity as a central concept in glycoRNA biology.Cell chemical biology · 2024Review
- The glycoimmune checkpoint receptor Siglec-7 interacts with T-cell ligands and regulates T-cell activation.The Journal of biological chemistry · 2024Article
- Proximity labeling technologies to illuminate glycan-protein interactions.Current opinion in chemical biology · 2023Review
- Proximity-Dependent In Vivo Biotin Labeling for Interactome Mapping in Marchantia polymorpha.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Radius measurement via super-resolution microscopy enables the development of a variable radii proximity labeling platform.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reading the glyco-code: New approaches to studying protein-carbohydrate interactions.Current opinion in structural biology · 2022Review
- Seeing the forest through the trees: characterizing the glycoproteome.Trends in biochemical sciences · 2022Review
- Advances in glycoscience to understand viral infection and colonization.Nature methods · 2022Article
- SUGAR-seq enables simultaneous detection of glycans, epitopes, and the transcriptome in single cells.Science advances · 2021Article
- Deciphering molecular interactions by proximity labeling.Nature methods · 2021Review
- Recent Progress in the Methodologies to Identify Physiological Ligands of Siglecs.Frontiers in immunology · 2021Review
- Proximity-dependent labeling methods for proteomic profiling in living cells: An update.Wiley interdisciplinary reviews. Developmental biology · 2021Review
- Activation of regulatory T cells triggers specific changes in glycosylation associated with Siglec-1-dependent inflammatory responses.Wellcome open research · 2021Article
- Siglec Signaling in the Tumor Microenvironment.Frontiers in immunology · 2021Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lectin-glycan interactions play important roles in many biological systems, but the nature of glycoprotein counter-receptors expressed on cell membranes is often poorly understood. To help overcome this problem, we developed a method based on proximity labeling technology. Using a peroxidase-coupled lectin, addition of H2O2 and tyramide-biotin substrates leads to generation of short-range biotin radicals that biotinylate proteins in the immediate vicinity of the bound lectin, which can subsequently be identified. As a proof-of-principle, sialoadhesin-horseradish peroxidase-human IgG1 Fc recombinant protein constructs were precomplexed with anti-Fc antibodies, bound to human erythrocytes and reacted with H2O2 and tyramide-SS-biotin. The erythrocyte membrane protein with strongest biotinylation was identified as glycophorin A, in agreement with early studies using lectin overlay and reglycosylation approaches. As a further test of the method, the plant lectin MAL II was conjugated with horseradish peroxidase and used in proximity labeling of human erythrocytes. Glycophorin A was again selectively labeled, which is consistent with previous reports that MAL II has high affinity for glycophorin. This method could be applied to other lectins to identify their membrane counter-receptors.
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.