ArticleThe Journal of biological chemistry2012
Cross-comparison of protein recognition of sialic acid diversity on two novel sialoglycan microarrays.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
What it found
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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.
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Who cites it
85 citing papers in PubMed.
- Oral streptococci utilize a Siglec-like domain of serine-rich repeat adhesins to preferentially target platelet sialoglycans in human blood.PLoS pathogens · 2014Trial
- Versatile Glycan Probes for Multiplatform Investigation of Glycan Interactions with Proteins, Viruses, and Cells.Nature communications · 2026Article
- An atlas of human siglecs integrates expression, affinity, and cis/trans sialoglycan recognition profiles.Nature communications · 2026Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Preclinical Evaluation of a Near-Infrared Labelled Antibody Targeting the Tumour Associated Xenoantigen N-Glycolyl-Neuraminic Acid GM3 Ganglioside.Molecular imaging and biology · 2025Article
- Article
- Broad-Spectrum Legionaminic Acid-Specific Antibodies in Pooled Human IgGs Revealed by Glycan Microarrays with Chemoenzymatically Synthesized Nonulosonosides.Molecules (Basel, Switzerland) · 2024Article
- Serum antibody screening using glycan arrays.Chemical Society reviews · 2024Review
- The avian influenza A virus receptor SA-α2,3-Gal is expressed in the porcine nasal mucosa sustaining the pig as a mixing vessel for new influenza viruses.Virus research · 2024Article
- A systematic review reveals conflicting evidence for the prevalence of antibodies against the sialic acid 'xenoautoantigen' Neu5Gc in humans and the need for a standardised approach to quantification.Frontiers in molecular biosciences · 2024Review
- Effect of Gravity on Bacterial Adhesion to Heterogeneous Surfaces.Pathogens (Basel, Switzerland) · 2023Article
- A Holistic 4D Approach to Optimize Intrinsic and Extrinsic Factors Contributing to Variability in Microarray Biosensing in Glycomics.Sensors (Basel, Switzerland) · 2023Article
- Article
- A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities.ACS chemical biology · 2022Article
- The Sialyl Lewis X Glycan Receptor Facilitates Infection of Subtype H7 Avian Influenza A Viruses.Journal of virology · 2022Article
- CarboGrove: a resource of glycan-binding specificities through analyzed glycan-array datasets from all platforms.Glycobiology · 2022Article
- Sialoglycan-binding patterns of bacterial ABThe Journal of biological chemistry · 2022Article
- Chemoenzymatic Synthesis of Sialosides Containing 7-The Journal of organic chemistry · 2021Article
- A Neoglycoprotein-Immobilized Fluorescent Magnetic Bead Suspension Multiplex Array for Galectin-Binding Studies.Molecules (Basel, Switzerland) · 2021Article
- Noncovalent microarrays from synthetic amino-terminating glycans: Implications in expanding glycan microarray diversity and platform comparison.Glycobiology · 2021Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
20 authors.
Funding
Abstract
DNA and protein arrays are commonly accepted as powerful exploratory tools in research. This has mainly been achieved by the establishment of proper guidelines for quality control, allowing cross-comparison between different array platforms. As a natural extension, glycan microarrays were subsequently developed, and recent advances using such arrays have greatly enhanced our understanding of protein-glycan recognition in nature. However, although it is assumed that biologically significant protein-glycan binding is robustly detected by glycan microarrays, there are wide variations in the methods used to produce, present, couple, and detect glycans, and systematic cross-comparisons are lacking. We address these issues by comparing two arrays that together represent the marked diversity of sialic acid modifications, linkages, and underlying glycans in nature, including some identical motifs. We compare and contrast binding interactions with various known and novel plant, vertebrate, and viral sialic acid-recognizing proteins and present a technical advance for assessing specificity using mild periodate oxidation of the sialic acid chain. These data demonstrate both the diversity of sialic acids and the analytical power of glycan arrays, showing that different presentations in different formats provide useful and complementary interpretations of glycan-binding protein specificity. They also highlight important challenges and questions for the future of glycan array technology and suggest that glycan arrays with similar glycan structures cannot be simply assumed to give similar results.
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Registered trials
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