ArticleRapid communications in mass spectrometry : RCM2012
Quantification of glycopeptides by multiple reaction monitoring liquid chromatography/tandem mass spectrometry.
Article in Rapid communications in mass spectrometry : RCM, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 78 citations in OpenAlex.
- Fast NMR-Based Assessment of Cancer-Associated Protein Glycosylations from Serum Samples.Analytical chemistry · 2025Article
- Decoding the glycoproteome: a new frontier for biomarker discovery in cancer.Journal of hematology & oncology · 2024Review
- Targeted Glycoproteomics Analysis Using MRM/PRM Approaches.Methods in molecular biology (Clifton, N.J.) · 2024Article
- LC-MS/MS Quantitation of HILIC-EnrichedBiomolecules · 2023Article
- Multi-Attribute Monitoring Method for Process Development of Engineered Antibody for Site-Specific Conjugation.Journal of the American Society for Mass Spectrometry · 2023Article
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- Mass spectrometry based biomarkers for early detection of HCC using a glycoproteomic approach.Advances in cancer research · 2023Review
- Article
- Selective reaction monitoring approach using structure-defined synthetic glycopeptides for validating glycopeptide biomarkers pre-determined by bottom-up glycoproteomics.RSC advances · 2022Article
- Review
- Calculating Glycoprotein Similarities From Mass Spectrometric Data.Molecular & cellular proteomics : MCP · 2021Review
- Mass spectrometry in clinical glycomics: The path from biomarker identification to clinical implementation.Clinical mass spectrometry (Del Mar, Calif.) · 2020Review
- A Perspective on the Confident Comparison of Glycoprotein Site-Specific Glycosylation in Sample Cohorts.Biochemistry · 2020Review
- Review
- Optimized Fragmentation for Quantitative Analysis of Fucosylated N-Glycoproteins by LC-MS-MRM.Analytical chemistry · 2019Article
- Glycoproteomic markers of hepatocellular carcinoma-mass spectrometry based approaches.Mass spectrometry reviews · 2019Review
- Differential Quantitative Determination of Site-Specific Intact N-Glycopeptides in Serum Haptoglobin between Hepatocellular Carcinoma and Cirrhosis Using LC-EThcD-MS/MS.Journal of proteome research · 2019Article
- Liquid Chromatography-Tandem Mass Spectrometry Approach for Determining Glycosidic Linkages.Analytical chemistry · 2018Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein glycosylation has a major influence on functions of proteins. Studies have shown that aberrations in glycosylation are indicative of disease conditions. This has prompted major research activities for comparative studies of glycoproteins in biological samples. Multiple reaction monitoring (MRM) is a highly sensitive technique which has been recently explored for quantitative proteomics. In this work, MRM was adopted for quantification of glycopeptides derived from both model glycoproteins and depleted human blood serum using glycan oxonium ions as transitions. The utilization of oxonium ions aids in identifying the different types of glycans bound to peptide backbones. MRM experiments were optimized by evaluating different parameters that have a major influence on quantification of glycopeptides, which include MRM time segments, number of transitions, and normalized collision energies. The results indicate that oxonium ions could be adopted for the characterization and quantification of glycopeptides in general, eliminating the need to select specific transitions for individual precursor ions. Also, the specificity increased with the number of transitions and a more sensitive analysis can be obtained by providing specific time segments. This approach can be applied to comparative and quantitative studies of glycopeptides in biological samples as illustrated for the case of depleted blood serum sample.
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.