ArticleScientific reports2017
Identification of Extracellular Segments by Mass Spectrometry Improves Topology Prediction of Transmembrane Proteins.
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 13 papers.
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13 citing papers in PubMed, 20 citations in OpenAlex.
- Decoding the Apical-Basal Surfaceome of Colon Epithelial Cells via Side-Selective Biotinylation.Biomolecules · 2026Article
- Optimization of Methods for the Quantitative Analysis of Global Cell Surface Proteome and Cell Surface Polarization.International journal of molecular sciences · 2025Article
- Therapy-induced senescence is a transient drug resistance mechanism in breast cancer.Molecular cancer · 2025Article
- 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
- LeishMANIAdb: a comparative resource for Leishmania proteins.Database : the journal of biological databases and curation · 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
- PolarProtPred: predicting apical and basolateral localization of transmembrane proteins using putative short linear motifs and deep learning.Bioinformatics (Oxford, England) · 2021Article
- CIRFESS: An Interactive Resource for Querying the Set of Theoretically Detectable Peptides for Cell Surface and Extracellular Enrichment Proteomic Studies.Journal of the American Society for Mass Spectrometry · 2020Article
- Partial proteolysis improves the identification of the extracellular segments of transmembrane proteins by surface biotinylation.Scientific reports · 2020Article
- Covalently modified carboxyl side chains on cell surface leads to a novel method toward topology analysis of transmembrane proteins.Scientific reports · 2019Article
- A split ubiquitin system to reveal topology and released peptides of membrane proteins.BMC biotechnology · 2017Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transmembrane proteins play crucial role in signaling, ion transport, nutrient uptake, as well as in maintaining the dynamic equilibrium between the internal and external environment of cells. Despite their important biological functions and abundance, less than 2% of all determined structures are transmembrane proteins. Given the persisting technical difficulties associated with high resolution structure determination of transmembrane proteins, additional methods, including computational and experimental techniques remain vital in promoting our understanding of their topologies, 3D structures, functions and interactions. Here we report a method for the high-throughput determination of extracellular segments of transmembrane proteins based on the identification of surface labeled and biotin captured peptide fragments by LC/MS/MS. We show that reliable identification of extracellular protein segments increases the accuracy and reliability of existing topology prediction algorithms. Using the experimental topology data as constraints, our improved prediction tool provides accurate and reliable topology models for hundreds of human transmembrane proteins.
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