ArticleNature communications2019
Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- To cleave or not to cleave: a systemic evaluation of DSS versus DSSO for cross-linking mass spectrometry analysis.Molecular systems biology · 2026Article
- Global profiling of arginine reactivity and ligandability in the human proteome.Nature chemistry · 2026Article
- Towards a universal cross-linking mass spectrometry approach for protein structure analysis with homo-bi-functional photo-activatable cross-linkers.Communications biology · 2025Article
- Internal Ubiquitin Electrophiles for Covalent Trapping and Inhibition of Deubiquitinases.Chembiochem : a European journal of chemical biology · 2025Article
- Profiling the proteome-wide selectivity of diverse electrophiles.Nature chemistry · 2025Article
- Assembly of mTORC3 Involves Binding of ETV7 to Two Separate Sequences in the mTOR Kinase Domain.International journal of molecular sciences · 2024Article
- A chemical proteomics approach for global mapping of functional lysines on cell surface of living cell.Nature communications · 2024Article
- Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure.Protein science : a publication of the Protein Society · 2024Review
- Hydrogen sulfide improves salt tolerance through persulfidation of PMA1 in Arabidopsis.Plant cell reports · 2023Article
- Conformational Dynamics of the Activated GLP-1 Receptor-GACS central science · 2023Article
- Chemical Conjugation to Less Targeted Proteinogenic Amino Acids.Chembiochem : a European journal of chemical biology · 2022Review
- Chemoselective Covalent Modification of K-Ras(G12R) with a Small Molecule Electrophile.Journal of the American Chemical Society · 2022Article
- Characterization of protein unfolding by fast cross-linking mass spectrometry using di-ortho-phthalaldehyde cross-linkers.Nature communications · 2022Article
- Interfaces with Structure Dynamics of the Workhorses from Cells Revealed through Cross-Linking Mass Spectrometry (CLMS).Biomolecules · 2021Review
- Review
- Cleavable Cross-Linkers and Mass Spectrometry for the Ultimate Task of Profiling Protein-Protein Interaction NetworksJournal of proteome research · 2021Review
- Photocaged Quinone Methide Crosslinkers for Light-Controlled Chemical Crosslinking of Protein-Protein and Protein-DNA Complexes.Angewandte Chemie (International ed. in English) · 2019Article
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chemical cross-linking of proteins coupled with mass spectrometry analysis (CXMS) is widely used to study protein-protein interactions (PPI), protein structures, and even protein dynamics. However, structural information provided by CXMS is still limited, partly because most CXMS experiments use lysine-lysine (K-K) cross-linkers. Although superb in selectivity and reactivity, they are ineffective for lysine deficient regions. Herein, we develop aromatic glyoxal cross-linkers (ArGOs) for arginine-arginine (R-R) cross-linking and the lysine-arginine (K-R) cross-linker KArGO. The R-R or K-R cross-links generated by ArGO or KArGO fit well with protein crystal structures and provide information not attainable by K-K cross-links. KArGO, in particular, is highly valuable for CXMS, with robust performance on a variety of samples including a kinase and two multi-protein complexes. In the case of the CNGP complex, KArGO cross-links covered as much of the PPI interface as R-R and K-K cross-links combined and improved the accuracy of Rosetta docking substantially.
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