ArticleThe Journal of biological chemistry2024
Chemical modification of hyaluronan oligosaccharides differentially modulates hyaluronan-hyaladherin interactions.
Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Absolute Quantification and Spatial Mapping of Hyaluronic Acid in Histological Tissue Sections.ACS measurement science au · 2026Article
- New Bioinformatic Insight into CD44: Classification of Human Variants and Structural Analysis of CD44 Targeting.International journal of molecular sciences · 2025Article
- Hyaluronic Acid in Immune Response.Biomolecules · 2025Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The glycosaminoglycan hyaluronan (HA) is a ubiquitous, nonsulfated polysaccharide with diverse biological roles mediated through its interactions with HA-binding proteins (HABPs). Most HABPs belong to the Link module superfamily, including the major HA receptor, CD44, and secreted protein TSG-6, which catalyzes the covalent transfer of heavy chains from inter-α-inhibitor onto HA. The structures of the HA-binding domains (HABDs) of CD44 (HABD_CD44) and TSG-6 (Link_TSG6) have been determined and their interactions with HA extensively characterized. The mechanisms of binding are different, with Link_TSG6 interacting with HA primarily via ionic and CH-π interactions, whereas HABD_CD44 binds solely via hydrogen bonds and van der Waals forces. Here, we exploit these differences to generate HA oligosaccharides, chemically modified at their reducing ends, that bind specifically and differentially to these target HABPs. Hexasaccharides (HA
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Registered trials
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