ArticleAnalytical chemistry2023
Development of an Antibody-Based Platform for the Analysis of Immune Cell-Specific N-linked Glycosylation.
Article in Analytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Single-cell mass spectrometry imaging: platform advances for multimodal spatial omics.Analytical and bioanalytical chemistry · 2026Review
- MIMIC: a flexible pipeline to register and summarize IMC-MSI experiments.Communications biology · 2026Article
- Mucosal glycans: key drivers of the development of inflammatory bowel disease and a potential new therapeutic target.Nature reviews. Gastroenterology & hepatology · 2026Review
- Spatial atlasing of N-glycosylation in healthy control and clear cell renal cell carcinoma tissues linked with immune checkpoint inhibition response by MALDI mass spectrometry imaging.Analytica chimica acta · 2025Article
- A mass spectrometry-based assay for mouse IgG N-glycan screening in biofluids.Analytical and bioanalytical chemistry · 2025Article
- Spatial omics-based machine learning algorithms for the early detection of hepatocellular carcinoma.Communications medicine · 2024Article
- HScience advances · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
N-linked glycosylation plays an important role in both the innate and adaptive immune response through the modulation of cell surface receptors as well as general cell-to-cell interactions. The study of immune cell N-glycosylation is gaining interest but is hindered by the complexity of cell-type-specific N-glycan analysis. Analytical techniques such as chromatography, LC-MS/MS, and the use of lectins are all currently used to analyze cellular glycosylation. Issues with these analytical techniques include poor throughput, which is often limited to a single sample at a time, lack of structural information, the need for a large amount of starting materials, and the requirement for cell purification, thereby reducing their feasibility for N-glycan study. Here, we report the development of a rapid antibody array-based approach for the capture of specific nonadherent immune cells coupled with MALDI-IMS to analyze cellular N-glycosylation. This workflow is adaptable to multiple N-glycan imaging approaches such as the removal or stabilization and derivatization of terminal sialic acid residues providing unique avenues of analysis that have otherwise not been explored in immune cell populations. The reproducibility, sensitivity, and versatility of this assay provide an invaluable tool for researchers and clinical applications, significantly expanding the field of glycoimmunology.
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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.