ArticleAnalytical chemistry2018
Top-Down Characterization of Proteins with Intact Disulfide Bonds Using Activated-Ion Electron Transfer Dissociation.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Isotope Decluttering Reduces Spectral Complexity while Maintaining Protein Structure.Analytical chemistry · 2026Article
- Article
- Leveraging Ion-Ion and Ion-Photon Activation to Improve the Sequencing of Proteins Carrying Multiple Disulfide Bonds: The Human Serum Albumin Case Study.Journal of the American Society for Mass Spectrometry · 2024Article
- Development of a Novel Label-Free Subunit HILIC-MS Method for Domain-Specific Free Thiol Identification and Quantitation in Therapeutic Monoclonal Antibodies.Journal of the American Society for Mass Spectrometry · 2024Article
- Mobility-Assisted Pseudo-MSJournal of the American Society for Mass Spectrometry · 2024Article
- Characterization of a Monoclonal Antibody by Native and Denaturing Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins.The Analyst · 2022Article
- Deciphering combinatorial post-translational modifications by top-down mass spectrometry.Current opinion in chemical biology · 2022Review
- Characterization of the T4 gp32-ssDNA complex by native, cross-linking, and ultraviolet photodissociation mass spectrometry.Chemical science · 2021Article
- Enhancing Top-Down Analysis Using Chromophore-Assisted Infrared Multiphoton Dissociation from (Phospho)peptides to Protein Assemblies.Analytical chemistry · 2020Article
- Top-Down Characterization of an Intact Monoclonal Antibody Using Activated Ion Electron Transfer Dissociation.Analytical chemistry · 2020Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- Capillary Zone Electrophoresis-Tandem Mass Spectrometry with Activated Ion Electron Transfer Dissociation for Large-scale Top-down Proteomics.Journal of the American Society for Mass Spectrometry · 2019Article
- Capillary zone electrophoresis-mass spectrometry for top-down proteomics.Trends in analytical chemistry : TRAC · 2019Article
- Top-Down Analysis of Disulfide-Linked Proteins Using Photoinduced Radical Reactions and ET-DDC.International journal of mass spectrometry · 2019Article
- Middle-Down Multi-Attribute Analysis of Antibody-Drug Conjugates with Electron Transfer Dissociation.Analytical chemistry · 2019Article
- Capturing site-specific heterogeneity with large-scale N-glycoproteome analysis.Nature communications · 2019Article
- Simplified identification of disulfide, trisulfide, and thioether pairs with 213 nm UVPD.The Analyst · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Here we report the fragmentation of disulfide linked intact proteins using activated-ion electron transfer dissociation (AI-ETD) for top-down protein characterization. This fragmentation method is then compared to the alternative methods of beam-type collisional activation (HCD), electron transfer dissociation (ETD), and electron transfer and higher-energy collision dissociation (EThcD). We analyzed multiple precursor charge states of the protein standards bovine insulin, α-lactalbumin, lysozyme, β-lactoglobulin, and trypsin inhibitor. In all cases, we found that AI-ETD provides a boost in protein sequence coverage information and the generation of fragment ions from within regions enclosed by disulfide bonds. AI-ETD shows the largest improvement over the other techniques when analyzing highly disulfide linked and low charge density precursor ions. This substantial improvement is attributed to the concurrent irradiation of the gas phase ions while the electron-transfer reaction is taking place, mitigating nondissociative electron transfer, helping unfold the gas phase protein during the electron transfer event, and preventing disulfide bond reformation. We also show that AI-ETD is able to yield comparable sequence coverage information when disulfide bonds are left intact relative to proteins that have been reduced and alkylated. This work demonstrates that AI-ETD is an effective fragmentation method for the analysis of proteins with intact disulfide bonds, dramatically enhancing sequence ion generation and total sequence coverage compared to HCD and ETD.
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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.