ArticleScientific reports2017
Biotin-transfer from a trifunctional crosslinker for identification of cell surface receptors of soluble protein ligands.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- [Novel technologies for large-scale analysis of cell surface glycoprotein interactions and their applications].Se pu = Chinese journal of chromatography · 2026Article
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- Identification of a Novel Subset of Human Airway Epithelial Basal Stem Cells.International journal of molecular sciences · 2024Article
- Cell surface protein-protein interaction profiling for biological network analysis and novel target discovery.Life medicine · 2024Review
- Deciphering intercellular signaling complexes by interaction-guided chemical proteomics.Nature communications · 2023Article
- Systematic characterization of extracellular glycoproteins using mass spectrometry.Mass spectrometry reviews · 2023Review
- Discovery of antibodies and cognate surface targets for ovarian cancer by surface profiling.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Identifying Receptors for Neuropeptides and Peptide Hormones: Challenges and Recent Progress.ACS chemical biology · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Advances in high-throughput methods for the identification of virus receptors.Medical microbiology and immunology · 2020Review
- Article
- Design, Synthesis, and Evaluation of a Diazirine Photoaffinity Probe for Ligand-Based Receptor Capture Targeting G Protein-Coupled Receptors.Molecular pharmacology · 2019Article
- Glycomics and Proteomics Approaches to Investigate Early Adenovirus-Host Cell Interactions.Journal of molecular biology · 2018Review
- HATRIC-based identification of receptors for orphan ligands.Nature communications · 2018Article
- Mass spectrometry-based methods for investigating the dynamics and organization of the surfaceome: exploring potential clinical implications.Expert review of proteomicsReview
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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
Here we describe a novel crosslinker and its application as a biotin-transfer reagent to identify cell surface receptors of soluble protein ligands on live cells. This crosslinker contains three functional groups: an aldehyde-reactive aminooxy group, a sulfhydryl, and a biotin (ASB). It is readily synthesized via a 3-step addition reaction using standard solid-phase peptide synthesis methods and commercially available intermediates, allowing access to laboratories without specialized synthetic chemistry capabilities. For the biotin-transfer method, ASB is linked to a protein ligand through the sulfhydryl group in a two-step process that allows the introduction of a disulfide bond between the ligand and the crosslinker. Incubation of the labelled ligand with oxidized live cells leads to the formation of crosslinks with aldehyde-containing glycans on the cell surface receptor. Subsequent reduction of the disulfide bond results in biotin transfer from the ligand to the cell surface receptor. Protein biotinylation that is mediated by ligand binding to its receptor is differentiated from background biotinylation events by comparison with a similarly labelled control protein using comparative proteomic mass spectrometry to quantify streptavidin-bound proteins. Using this method, we successfully identified the cell surface receptors of a peptide hormone, a monoclonal antibody, and a single-domain antibody-Fc fusion construct.
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