ArticleJournal of the American Society for Mass Spectrometry2018
Comparison of Collisional and Electron-Based Dissociation Modes for Middle-Down Analysis of Multiply Glycosylated Peptides.
Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Optimization of LC-ExD methods for glycopeptides on an Omnitrap-Orbitrap platform.Analytical and bioanalytical chemistry · 2026Article
- Autonomous Dissociation-type Selection for Glycoproteomics Using a Real-Time Library Search.Journal of proteome research · 2024Article
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Direct and Detailed Site-Specific Glycopeptide Characterization by Higher-Energy Electron-Activated Dissociation Tandem Mass Spectrometry.Analytical chemistry · 2024Article
- Revealing the human mucinome.Nature communications · 2022Article
- Measuring change in glycoprotein structure.Current opinion in structural biology · 2022Review
- Improved Protein and PTM Characterization with a Practical Electron-Based Fragmentation on Q-TOF Instruments.Journal of the American Society for Mass Spectrometry · 2021Article
- Developing mass spectrometry for the quantitative analysis of neuropeptides.Expert review of proteomics · 2021Review
- What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?Biomolecules · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Calculating Glycoprotein Similarities From Mass Spectrometric Data.Molecular & cellular proteomics : MCP · 2021Review
- Electron-Based Dissociation Is Needed for O-Glycopeptides Derived from OpeRATOR Proteolysis.Analytical chemistry · 2020Article
- A Perspective on the Confident Comparison of Glycoprotein Site-Specific Glycosylation in Sample Cohorts.Biochemistry · 2020Review
- Optimal Dissociation Methods Differ forJournal of proteome research · 2020Article
- A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.Analytical chemistry · 2020Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- Advancing Solutions to the Carbohydrate Sequencing Challenge.Journal of the American Chemical Society · 2019Review
- Capturing site-specific heterogeneity with large-scale N-glycoproteome analysis.Nature communications · 2019Article
- Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry.RSC advances · 2018Review
- Sequence Ion Structures and Dissociation Chemistry of Deprotonated Sucrose Anions.Journal of the American Society for Mass Spectrometry · 2018Article
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7 authors.
Funding
Abstract
Analysis of singly glycosylated peptides has evolved to a point where large-scale LC-MS analyses can be performed at almost the same scale as proteomics experiments. While collisionally activated dissociation (CAD) remains the mainstay of bottom-up analyses, it performs poorly for the middle-down analysis of multiply glycosylated peptides. With improvements in instrumentation, electron-activated dissociation (ExD) modes are becoming increasingly prevalent for proteomics experiments and for the analysis of fragile modifications such as glycosylation. While these methods have been applied for glycopeptide analysis in isolated studies, an organized effort to compare their efficiencies, particularly for analysis of multiply glycosylated peptides (termed here middle-down glycoproteomics), has not been made. We therefore compared the performance of different ExD modes for middle-down glycopeptide analyses. We identified key features among the different dissociation modes and show that increased electron energy and supplemental activation provide the most useful data for middle-down glycopeptide analysis. Graphical Abstract.
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