ArticleNature communications2022
Characterization of protein unfolding by fast cross-linking mass spectrometry using di-ortho-phthalaldehyde cross-linkers.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Development of proteome-derived cyclic peptide libraries via ortho-phthalaldehyde-assisted cyclization.iScience · 2026Article
- To cleave or not to cleave: a systemic evaluation of DSS versus DSSO for cross-linking mass spectrometry analysis.Molecular systems biology · 2026Article
- Spontaneous Non-Catalyzed Molecular Reactions and Interactions in the Human Body: Biomedical Implications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- In Situ Construction of Imidazopyridinium Fluorescent Labels for Bioconjugation.Angewandte Chemie (International ed. in English) · 2026Article
- Covalent modification and liposomal delivery of hydroxytyrosol-soy protein complexes: A strategy to improve stability, functionality, and bioavailability.Food chemistry: X · 2026Article
- A Brief Progress in Methods for Deciphering Protein-Protein Interaction Networks.International journal of molecular sciences · 2026Review
- A practical guide to sample preparation for immunoprecipitation coupled with mass spectrometry analysis ofmicroPublication biology · 2026Article
- Clickable Dialdehyde-Amine Polymerization (cDAP).JACS Au · 2025Article
- Cysteine-enabled cleavability to advance cross-linking mass spectrometry for global analysis of endogenous protein-protein interactions.Nature communications · 2025Article
- In-situ cross-linking mass spectrometry reveals compartment-specific proteasomal interactions and structural heterogeneity.Nature communications · 2025Article
- Transient Cross-linking Mass Spectrometry: Taking Conformational Snapshots of Proteins.Analytical chemistry · 2025Article
- Molecular mechanism of proteolytic cleavage-dependent activation of CadC-mediated response to acid in E. coli.Communications biology · 2024Article
- Chemical cross-linking and mass spectrometry enabled systems-level structural biology.Current opinion in structural biology · 2024Review
- Dissecting diazirine photo-reaction mechanism for protein residue-specific cross-linking and distance mapping.Nature communications · 2024Article
- Cross-link assisted spatial proteomics to map sub-organelle proteomes and membrane protein topologies.Nature communications · 2024Article
- A chemical proteomics approach for global mapping of functional lysines on cell surface of living cell.Nature communications · 2024Article
- Enhancing protein dynamics analysis with hydrophilic polyethylene glycol cross-linkers.Briefings in bioinformatics · 2024Article
- Recent Advances in Protein Folding Pathway Prediction through Computational Methods.Current medicinal chemistry · 2024Review
- New advances in cross-linking mass spectrometry toward structural systems biology.Current opinion in chemical biology · 2023Review
- Deciphering intercellular signaling complexes by interaction-guided chemical proteomics.Nature communications · 2023Article
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chemical cross-linking of proteins coupled with mass spectrometry is widely used in protein structural analysis. In this study we develop a class of non-hydrolyzable amine-selective di-ortho-phthalaldehyde (DOPA) cross-linkers, one of which is called DOPA2. Cross-linking of proteins with DOPA2 is 60-120 times faster than that with the N-hydroxysuccinimide ester cross-linker DSS. Compared with DSS cross-links, DOPA2 cross-links show better agreement with the crystal structures of tested proteins. More importantly, DOPA2 has unique advantages when working at low pH, low temperature, or in the presence of denaturants. Using staphylococcal nuclease, bovine serum albumin, and bovine pancreatic ribonuclease A, we demonstrate that DOPA2 cross-linking provides abundant spatial information about the conformations of progressively denatured forms of these proteins. Furthermore, DOPA2 cross-linking allows time-course analysis of protein conformational changes during denaturant-induced unfolding.
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