ArticleJournal of the American Society for Mass Spectrometry2014
Reliable determination of site-specific in vivo protein N-glycosylation based on collision-induced MS/MS and chromatographic retention time.
Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 42 citations in OpenAlex.
- Glycomic Profiling Reveals Enhanced Sialylation and Plasma-Derived Fibrinogen Accumulation in the Parkinson's Disease Cerebellum.Molecular neurobiology · 2026Article
- Analysis ofACS omega · 2025Article
- "Small is beautiful" - Examining reliable determination of low-abundant therapeutic antibody glycovariants.Journal of pharmaceutical analysis · 2024Article
- The opportunity cost of automated glycopeptide analysis: case study profiling the SARS-CoV-2 S glycoprotein.Analytical and bioanalytical chemistry · 2021Article
- Representing and Comparing Site-Specific Glycan Abundance Distributions of Glycoproteins.Journal of proteome research · 2021Article
- A Perspective on the Confident Comparison of Glycoprotein Site-Specific Glycosylation in Sample Cohorts.Biochemistry · 2020Review
- Relative Retention Time Estimation Improves N-Glycopeptide Identifications by LC-MS/MS.Journal of proteome research · 2020Article
- Article
- Article
- Study of structure-dependent chromatographic behavior of glycopeptides using reversed phase nanoLC.Electrophoresis · 2017Article
- Article
- Site-specific analysis of changes in the glycosylation of proteins in liver cirrhosis using data-independent workflow with soft fragmentation.Analytical and bioanalytical chemistry · 2017Article
- Site-Specific N-Glycosylation of Recombinant Pentameric and Hexameric Human IgM.Journal of the American Society for Mass Spectrometry · 2016Article
- SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.Molecular & cellular proteomics : MCP · 2016Article
- Maturing Glycoproteomics Technologies Provide Unique Structural Insights into the N-glycoproteome and Its Regulation in Health and Disease.Molecular & cellular proteomics : MCP · 2016Review
- A case for protein-level and site-level specificity in glycoproteomic studies of disease.Glycoconjugate journal · 2016Review
- N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.Glycoconjugate journal · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Site-specific glycopeptide mapping for simultaneous glycan and peptide characterization by MS is difficult because of the heterogeneity and diversity of glycosylation in proteins and the lack of complete fragmentation information for either peptides or glycans with current fragmentation technologies. Indeed, multiple peptide and glycan combinations can readily match the same mass of glycopeptides even with mass errors less than 5 ppm providing considerably ambiguity and analysis of complex mixtures of glycopeptides becomes quite challenging in the case of large proteins. Here we report a novel strategy to reliably determine site-specific N-glycosylation mapping by combining collision-induced dissociation (CID)-only fragmentation with chromatographic retention times of glycopeptides. This approach leverages an experimental pipeline with parallel analysis of glyco- and deglycopeptides. As the test case we chose ABCA4, a large integral membrane protein with 16 predicted sites for N-glycosylation. Taking advantage of CID features such as high scan speed and high intensity of fragment ions together combined with the retention times of glycopeptides to conclusively identify the non-glycolytic peptide from which the glycopeptide was derived, we obtained virtually complete information about glycan compositions and peptide sequences, as well as the N-glycosylation site occupancy and relative abundances of each glycoform at specific sites for ABCA4. The challenges provided by this example provide guidance in analyzing complex relatively pure glycoproteins and potentially even more complex glycoprotein mixtures.
Indexed as
Identifiers
What OpenQuestion holds
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.