ArticleAnalytical chemistry2020
Low Collision Energy Fragmentation in Structure-Specific Glycoproteomics Analysis.
Article in Analytical chemistry, 2020. 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, 40 citations in OpenAlex.
- Integrative Analysis of Fucosylated Tetra Glycoforms in Hepatocellular Carcinoma: A NanoLC-PRM-MS/MS and Machine Learning Approach.Journal of proteome research · 2025Article
- Extracting informative glycan-specific ions from glycopeptide MS/MS spectra with GlyCounter.bioRxiv : the preprint server for biology · 2025Article
- Proteogenomics in Nephrology: A New Frontier in Nephrological Research.Current issues in molecular biology · 2024Review
- Mass Spectrometry Analysis of Glycopeptides Enriched by Anion Exchange-Mediated Methods Reveals PolyLacNAc-ExtendedAnalytical chemistry · 2024Article
- Inclusion of deuterated glycopeptides provides increased sequence coverage in hydrogen/deuterium exchange mass spectrometry analysis of SARS-CoV-2 spike glycoprotein.Rapid communications in mass spectrometry : RCM · 2024Article
- Can We BoostJournal of the American Society for Mass Spectrometry · 2024Article
- Direct and Detailed Site-Specific Glycopeptide Characterization by Higher-Energy Electron-Activated Dissociation Tandem Mass Spectrometry.Analytical chemistry · 2024Article
- Analysis of the N-glycosylation profiles of the spike proteins from the Alpha, Beta, Gamma, and Delta variants of SARS-CoV-2.Analytical and bioanalytical chemistry · 2023Article
- "Ghost" Fragment Ions in Structure and Site-Specific Glycoproteomics Analysis.Analytical chemistry · 2023Article
- "Ghost" fragment ions in structure and site-specific glycoproteomics analysis.bioRxiv : the preprint server for biology · 2023Article
- Application of StrucGP in medical immunology: site-specific N-glycoproteomic analysis of macrophages.Frontiers of medicine · 2023Article
- Diversity Matters: Optimal Collision Energies for Tandem Mass Spectrometric Analysis of a Large Set of N-Glycopeptides.Journal of proteome research · 2022Article
- Site-specific glycosylation of SARS-CoV-2: Big challenges in mass spectrometry analysis.Proteomics · 2022Review
- Prediction of Intact N-Glycopeptide Retention Time Windows in Hydrophilic Interaction Liquid Chromatography.Molecules (Basel, Switzerland) · 2022Article
- Measuring change in glycoprotein structure.Current opinion in structural biology · 2022Review
- Glycoforms of human prostate-specific membrane antigen (PSMA) in human cells and prostate tissue.The Prostate · 2022Article
- The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021Review
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- N- and O-Glycosylation of the SARS-CoV-2 Spike Protein.Analytical chemistry · 2021Article
- Glycoproteomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Glycosylation is a major post-translational modification of proteins that regulates many biological processes including protein folding, structure stability, receptor activation, and immune responses. The glycans attached to proteins represent an important determinant of the protein interaction-specificity and maintain the 3D structure of proteins. Mass spectrometry (MS) is one of the most efficient tools used in the current studies of glycoproteins and structure of their glycoforms. Collision energy (CE) is a crucial instrument parameter that can be exploited to improve structural resolution because different linkages of glycan units show different stabilities under CID/HCD fragmentation. Here we report the utility of CE modulation for qualitative and quantitative analysis of site- and structure-specific glycoforms of proteins. Using CE modulation, we were able to break selectively specific glycan linkages on intact glycopeptides and get, to some degree, structure-specific mass spectrometric signals. Structure- and CE-specific oxonium ions provide sufficient information for the resolution of outer arm structure motifs with recognized biological functions. The complementary Y-ions, generated under optimized low CE (soft) conditions, provide additional structural information including features specific to the chitobiose core. This methodology of multiple CE fragmentation without merging spectral information can significantly improve confidence of glycopeptide identification and structural resolution by providing additional information to the established glycopeptide-search algorithms and tools.
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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.