ArticleScientific reports2019
Covalently modified carboxyl side chains on cell surface leads to a novel method toward topology analysis of transmembrane proteins.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Decoding the Apical-Basal Surfaceome of Colon Epithelial Cells via Side-Selective Biotinylation.Biomolecules · 2026Article
- Surfaceome Capture by Multiplex Biotinylation Enables Enhanced Identification of Cell Surface Proteins by Mass Spectrometry.Molecular & cellular proteomics : MCP · 2026Article
- Article
- Optimized Biotinylated Peptide Detection Method for Characterizing the Cell Surface Proteome.Methods in molecular biology (Clifton, N.J.) · 2025Article
- UniTmp: unified resources for transmembrane proteins.Nucleic acids research · 2024Article
- Membrane Protein Binding Interactions Studied in Live Cells via Diethylpyrocarbonate Covalent Labeling Mass Spectrometry.Analytical chemistry · 2023Article
- Comprehensive Discovery of the Accessible Primary Amino Group-Containing Segments from Cell Surface Proteins by Fine-Tuning a High-Throughput Biotinylation Method.International journal of molecular sciences · 2022Article
- Distinguishing Histidine Tautomers in Proteins Using Covalent Labeling-Mass Spectrometry.Analytical chemistry · 2022Article
- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- PolarProtPred: predicting apical and basolateral localization of transmembrane proteins using putative short linear motifs and deep learning.Bioinformatics (Oxford, England) · 2021Article
- Nongenetic Bioconjugation Strategies for Modifying Cell Membranes and Membrane Proteins: A Review.Bioconjugate chemistry · 2020Review
- Partial proteolysis improves the identification of the extracellular segments of transmembrane proteins by surface biotinylation.Scientific reports · 2020Article
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Authors and funding
8 authors.
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Abstract
The research on transmembrane proteins (TMPs) is quite widespread due to their biological importance. Unfortunately, only a little amount of structural data is available of TMPs. Since technical difficulties arise during their high-resolution structure determination, bioinformatics and other experimental approaches are widely used to characterize their low-resolution structure, namely topology. Experimental and computational methods alone are still limited to determine TMP topology, but their combination becomes significant for the production of reliable structural data. By applying amino acid specific membrane-impermeable labelling agents, it is possible to identify the accessible surface of TMPs. Depending on the residue-specific modifications, new extracellular topology data is gathered, allowing the identification of more extracellular segments for TMPs. A new method has been developed for the experimental analysis of TMPs: covalent modification of the carboxyl groups on the accessible cell surface, followed by the isolation and digestion of these proteins. The labelled peptide fragments and their exact modification sites are identified by nanoLC-MS/MS. The determined peptides are mapped to the primary sequences of TMPs and the labelled sites are utilised as extracellular constraints in topology predictions that contribute to the refined low-resolution structure data of these proteins.
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