ArticleGlycobiology2020
Microarray analyses of closely related glycoforms reveal different accessibilities of glycan determinants on N-glycan branches.
Article in Glycobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Versatile Glycan Probes for Multiplatform Investigation of Glycan Interactions with Proteins, Viruses, and Cells.Nature communications · 2026Article
- Glucose-dependent glycosphingolipid biosynthesis fuels CD8Cell metabolism · 2025Article
- Specificity of widely used lectins as probed with oligosaccharide and plant polysaccharide arrays.Histochemistry and cell biology · 2024Article
- Syntactic sugars: crafting a regular expression framework for glycan structures.Bioinformatics advances · 2024Article
- Computational insights into the circular permutation roles on ConA binding and structural stability.Current research in structural biology · 2024Article
- Structural Analysis and Characterization of an Antiproliferative Lectin fromInternational journal of molecular sciences · 2023Article
- Absolute Affinities from Quantitative Shotgun Glycomics Using Concentration-Independent (COIN) Native Mass Spectrometry.ACS central science · 2023Article
- Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin.ACS central science · 2022Article
- CarboGrove: a resource of glycan-binding specificities through analyzed glycan-array datasets from all platforms.Glycobiology · 2022Article
- Systematic synthesis of bisectedChemical science · 2022Article
- A photo-cross-linking GlcNAc analog enables covalent capture of N-linked glycoprotein-binding partners on the cell surface.Cell chemical biology · 2022Article
- Combined Analysis of Multiple Glycan-Array Datasets: New Explorations of Protein-Glycan Interactions.Analytical chemistry · 2021Article
- Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021Review
- Terminal Epitope-Dependent Branch Preference of Siglecs TowardFrontiers in molecular biosciences · 2021Article
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Authors and funding
7 authors.
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Abstract
Glycans mediate a wide variety of biological roles via recognition by glycan-binding proteins (GBPs). Comprehensive knowledge of such interaction is thus fundamental to glycobiology. While the primary binding feature of GBPs can be easily uncovered by using a simple glycan microarray harboring limited numbers of glycan motifs, their fine specificities are harder to interpret. In this study, we prepared 98 closely related N-glycoforms that contain 5 common glycan epitopes which allowed the determination of the fine binding specificities of several plant lectins and anti-glycan antibodies. These N-glycoforms differ from each other at the monosaccharide level and were presented in an identical format to ensure comparability. With the analysis platform we used, it was found that most tested GBPs have preferences toward only one branch of the complex N-glycans, and their binding toward the epitope-presenting branch can be significantly affected by structures on the other branch. Fine specificities described here are valuable for a comprehensive understanding and applications of GBPs.
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