ArticleAnalytical chemistry2024
Oxidative Release of Natural Glycans: Unraveling the Mechanism for Rapid N-Glycan Glycomics Analysis.
Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Oxidative Release of Natural Glycans (ORNG): Preparation of Truncated N-glycans for Engineering Glycoproteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Streamlined gram-scale natural N-glycan production using reversible tagging after oxidative release of natural glycans.Communications chemistry · 2025Article
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.
Funding
Abstract
N-glycosylation is a critical post-translational modification involved in various biosynthetic pathways and disease mechanisms. In this study, we present an optimized oxidative release of natural glycans (ORNG) method using household bleach that enables the rapid and efficient release of N-glycans from biological samples. We thoroughly investigated the ORNG mechanism, identifying key intermediates and side products and providing valuable insights into the oxidative release process. The method is highly efficient, releasing a wide range of N-glycans, including high-mannose, hybrid, and complex structures, with minimal sample processing. Our ORNG-based specific N-glycan profiling approach has demonstrated high sensitivity and efficiency, particularly in releasing N-glycans resistant to enzymatic digestion, such as core α3-fucosylated N-glycans from soy protein. Validation through mass spectrometry confirmed the method's ability to accurately profile N-glycans from complex biological samples, including human serum, with results comparable to traditional PNGase F digestion. The ORNG-based method's scalability, versatility, and use of low-cost reagents make it especially suited for large-scale glycomics studies. Furthermore, the mass spectrometry data revealed that the ORNG-based method achieves high sensitivity and specificity, positioning it as a robust alternative for comprehensive glycan profiling and functional studies. Our findings highlight ORNG's potential to advance N-glycomics, offering promising improvements in speed, efficiency, and breadth of glycan analysis.
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.