ArticleJournal of the American Society for Mass Spectrometry2017
Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology.
Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 24 citations in OpenAlex.
- Stabilizing Proteins by Chemical Cross-Linking: Insights into Conformation, Unfolding, and Aggregation Using Native Ion Mobility Mass Spectrometry.Analytical chemistry · 2025Article
- The Characterization of Ancient Methanococcales Malate Dehydrogenases Reveals That Strong Thermal Stability Prevents Unfolding Under Intense γ-Irradiation.Molecular biology and evolution · 2024Article
- Development of an Automated, High-Throughput Methodology for Native Mass Spectrometry and Collision-Induced Unfolding.Analytical chemistry · 2023Article
- Studying protein structure and function by native separation-mass spectrometry.Nature reviews. Chemistry · 2022Review
- β-Hairpin Peptide Mimics Decrease Human Islet Amyloid Polypeptide (hIAPP) Aggregation.Frontiers in cell and developmental biology · 2021Article
- Transient multimers modulate conformer abundances of prion protein monomer through conformational selection.Scientific reports · 2019Article
- Liquid-phase separations coupled with ion mobility-mass spectrometry for next-generation biopharmaceutical analysis.Expert review of proteomicsReview
Corrections and comments
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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
Noncovalent interactions are essential for the structural organization of biomacromolecules in cells. For this reason, the study of the biophysical, dynamic, and architectural interactions among biomacromolecules is essential. Since mass spectrometry requires compatible solutions while preserving the noncovalent bonding network, we envisioned that size exclusion chromatography coupled with ion mobility and mass spectrometry would be a valuable technique to desalt the initial sample and provide solution and gas-phase structural information in a single stage experiment. Such coupling allowed obtaining information on solution protein complex composition with SEC separation and on authenticity and purity with IMS-MS. Our study demonstrated that such coupling is compatible, useful, as well as suitable for a routine analysis, in pharmaceutical industry, for example. Mobility data were reliable and injected standards allowed calibrating the collision cross-section scale. Graphical Abstract ᅟ.
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Registered trials
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