ArticleAnalytical chemistry2015
A Method for In-Depth Structural Annotation of Human Serum Glycans That Yields Biological Variations.
Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 68 citations in OpenAlex.
- Hierarchical Channeled Graphitized Nanoarchitecture as a Diagnostic Platform for Maternal Fever Warning.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Isomeric diversity of GlcNAc(ManScientific reports · 2026Article
- Large-scale serum N-glycomics tracks N-glycosylation dynamics in hepatocellular carcinoma progression and enables early diagnosis.Nature communications · 2026Article
- Development and application of GlycanDIA workflow for glycomic analysis.Nature communications · 2025Article
- High Abundance of Unusual High MannoseACS omega · 2024Article
- Chromatograms and Mass Spectra of High-Mannose and PaucimannoseJournal of proteome research · 2024Article
- Identification of the High MannoseAnalytical chemistry · 2023Article
- Advances in protein glycosylation and its role in tissue repair and regeneration.Glycoconjugate journal · 2023Review
- Identification of human milk oligosaccharide positional isomers by combining IMS-CID-IMS and cryogenic IR spectroscopy.The Analyst · 2023Article
- Integrating age, BMI, and serum N-glycans detected by MALDI mass spectrometry to classify suspicious mammogram findings as benign lesions or breast cancer.Scientific reports · 2022Article
- Quantitative clinical glycomics strategies: A guide for selecting the best analysis approach.Mass spectrometry reviews · 2022Review
- Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions.The Journal of cell biology · 2022Article
- Food glycomics: Dealing with unexpected degradation of oligosaccharides during sample preparation and analysis.Journal of food and drug analysis · 2022Article
- In-depth characterization of non-human sialic acid (Neu5Gc) in human serum using label-free ZIC-HILIC/MRM-MS.Analytical and bioanalytical chemistry · 2021Article
- Structural identification of N-glycan isomers using logically derived sequence tandem mass spectrometry.Communications chemistry · 2021Article
- Glycosylation Biomarkers Associated with Age-Related Diseases and Current Methods for Glycan Analysis.International journal of molecular sciences · 2021Review
- Identification of Differential N-Glycan Compositions in the Serum and Tissue of Colon Cancer Patients by Mass Spectrometry.Biology · 2021Article
- Magnetic porous carbon-dependent platform for the determination of N-glycans from urine exosomes.Mikrochimica acta · 2021Article
- Clinically Viable Assay for Monitoring Uromodulin Glycosylation.Journal of the American Society for Mass Spectrometry · 2021Article
- Glycomic profiling and the mammalian brain.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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
Glycosylation is an important post-translational modification of proteins present in the vast majority of human proteins. For this reason, they are potentially new sources of biomarkers and active targets of therapeutics and vaccines. However, the absence of a biosynthetic template as in the genome and the general complexity of the structures have limited the development of methods for comprehensive structural analysis. Even now, the exact structures of many abundant N-glycans in serum are not known. Structural elucidation of oligosaccharides remains difficult and time-consuming. Here, we introduce a means of rapidly identifying released N-glycan structures using their accurate masses and retention times based on a glycan library. This serum glycan library, significantly expanded from a previous one covering glycans released from a handful of serum glycoproteins, has more than 170 complete and partial structures and constructed instead from whole serum. The method employs primarily nanoflow liquid chromatography and accurate mass spectrometry. The method allows us to readily profile N-glycans in biological fluids with deep structural analysis. This approach is used to determine the relative abundances and variations in the N-glycans from several individuals providing detailed variations in the abundances of the important N-glycans in blood.
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.