ArticleAnalytical chemistry2016
Online Hydrophobic Interaction Chromatography-Mass Spectrometry for Top-Down Proteomics.
Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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The trial behind it
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
37 citing papers in PubMed.
- Online native hydrophobic interaction chromatography-mass spectrometry of antibody-drug conjugates.mAbs · 2025Article
- Native Top-Down Proteomics of Endogenous Protein Complexes Enabled by Online Two-Dimensional Liquid Chromatography.Analytical chemistry · 2025Article
- Nanoflow Size Exclusion Chromatography-Native Mass Spectrometry of Intact Proteoforms and Protein Complexes.Analytical chemistry · 2025Article
- Extensive Biotransformation Profiling of AZD8205, an Anti-B7-H4 Antibody-Drug Conjugate, Elucidates Pathways Underlying Its StabilityAnalytical chemistry · 2024Article
- Recent Contributions of Proteomics to Our Understanding of Reversible NJournal of proteome research · 2024Review
- Native Top-Down Mass Spectrometry for Characterizing Sarcomeric Proteins Directly from Cardiac Tissue Lysate.Journal of the American Society for Mass Spectrometry · 2024Article
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023Article
- A protocol for setting-up robust hydrophobic interaction chromatography targeting the analysis of intact proteins and monoclonal antibodies.Analytical science advances · 2022Article
- Studying protein structure and function by native separation-mass spectrometry.Nature reviews. Chemistry · 2022Review
- Collision Cross Sections for Native Proteomics: Challenges and Opportunities.Journal of proteome research · 2022Article
- Article
- Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021Review
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
- Top-down proteomics: challenges, innovations, and applications in basic and clinical research.Expert review of proteomics · 2020Article
- Current LC-MS-based strategies for characterization and quantification of antibody-drug conjugates.Journal of pharmaceutical analysis · 2020Review
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- Deep Intact Proteoform Characterization in Human Cell Lysate Using High-pH and Low-pH Reversed-Phase Liquid Chromatography.Journal of the American Society for Mass Spectrometry · 2019Article
- Review
- Native Reversed-Phase Liquid Chromatography: A Technique for LCMS of Intact Antibody-Drug Conjugates.Analytical chemistry · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Recent progress in top-down proteomics has led to a demand for mass spectrometry (MS)-compatible chromatography techniques to separate intact proteins using volatile mobile phases. Conventional hydrophobic interaction chromatography (HIC) provides high-resolution separation of proteins under nondenaturing conditions but requires high concentrations of nonvolatile salts. Herein, we introduce a series of more-hydrophobic HIC materials that can retain proteins using MS-compatible concentrations of ammonium acetate. The new HIC materials appear to function as a hybrid form of conventional HIC and reverse phase chromatography. The function of the salt seems to be preserving protein structure rather than promoting retention. Online HIC-MS is feasible for both qualitative and quantitative analysis. This is demonstrated with standard proteins and a complex cell lysate. The mass spectra of proteins from the online HIC-MS exhibit low charge-state distributions, consistent with those commonly observed in native MS. Furthermore, HIC-MS can chromatographically separate proteoforms differing by minor modifications. Hence, this new HIC-MS combination is promising for top-down proteomics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.