ArticleScientific reports2016
Impact of sialic acids on the molecular dynamic of bi-antennary and tri-antennary glycans.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Sialic acids cleavage induced by elastin-derived peptides impairs the interaction between insulin and its receptor in adipocytes 3T3-L1.Journal of physiology and biochemistry · 2024Article
- Unveiling sialoglycans' immune mastery in pregnancy and their intersection with tumor biology.Frontiers in immunology · 2024Review
- Neuraminidase-1: A Sialidase Involved in the Development of Cancers and Metabolic Diseases.Cancers · 2022Review
- A Multiscale Molecular Dynamic Analysis Reveals the Effect of Sialylation on EGFR Clustering in a CRISPR/Cas9-Derived Model.International journal of molecular sciences · 2022Article
- Haptoglobin polymorphism affects its N-glycosylation pattern in serum.Journal of mass spectrometry and advances in the clinical lab · 2022Article
- Structure-guided mutagenesis of a mucin-selective metalloprotease from Akkermansia muciniphila alters substrate preferences.The Journal of biological chemistry · 2022Article
- Native Ion Mobility-Mass Spectrometry-Enabled Fast Structural Interrogation of Labile Protein Surface Modifications at the Intact Protein Level.Analytical chemistry · 2022Article
- Identification of Isomeric N-Glycans by Conformer Distribution Fingerprinting using Ion Mobility Mass Spectrometry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Umbrella Visualization: A method of analysis dedicated to glycan flexibility with UnityMol.Methods (San Diego, Calif.) · 2020Article
- Quantification of the α2-6 Sialic Acid Linkage in Branched N-Glycan Structures with Capillary Nanogel Electrophoresis.Analytical chemistry · 2020Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialic acids (SA) are monosaccharides that can be located at the terminal position of glycan chains on a wide range of proteins. The post-translational modifications, such as N-glycan chains, are fundamental to protein functions. Indeed, the hydrolysis of SA by specific enzymes such as neuraminidases can lead to drastic modifications of protein behavior. However, the relationship between desialylation of N-glycan chains and possible alterations of receptor function remains unexplored. Thus, the aim of the present study is to establish the impact of SA removal from N-glycan chains on their conformational behavior. We therefore undertook an in silico investigation using molecular dynamics to predict the structure of an isolated glycan chain. We performed, for the first time, 3 independent 500 ns simulations on bi-antennary and tri-antennary glycan chains displaying or lacking SA. We show that desialylation alters both the preferential conformation and the flexibility of the glycan chain. This study suggests that the behavior of glycan chains induced by presence or absence of SA may explain the changes in the protein function.
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