Order out of chaos: assembly of ligand binding sites in heparan sulfate.
By J. Esko, S. Selleck. Annual Review of Biochemistry, 2002
1,488 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology, Organic Chemistry
View Paper: https://www.semanticscholar.org/paper/16a42ae9e3080656ff31721ec1d6ef66bdae98c5
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Citations in the corpus
- Heparan sulphate proteoglycans fine-tune mammalian physiology (2007, background): “During their assembly, they undergo a series of processing reactions involving GlcNAc N-deacetylation and N-sulphation, epimerization of GlcA to IdoA, and O-sulphation that generate relatively short segments of modified sugars interspersed by variable tracts of unmodified sugar”
- SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 (2020, positive): “Like other macromolecules, HS can be divided into subunits, which are operationally defined as disaccharides based on the ability of bacterial enzymes or nitrous acid to cleave the chain into disaccharide units (Esko and Selleck, 2002).”
- The exostosin family: proteins with many functions. (2014, neutral): “ND license. et al., 1998; Esko and Selleck, 2002; Bulow and Hobert, 2006; Bishop et al., 2007; Kreuger and Kjellen, 2012).”
- Biological roles of glycans (2016, background): “Gradients of growth factors can be generated by binding to extracellular matrix glycosaminoglycans such as heparan sulfate, especially in embryonic development (86).”
- Molecular Analysis of 10 Coding Regions from Arabidopsis That Are Homologous to the MUR3 Xyloglucan Galactosyltransferase1 (2004, background): “This class of animal enzymes catalyzes the formation of the extracellular matrix component heparan sulfate, a glycosaminoglycan that is initially synthesized as a linear chain of alternating GlcA and GlcNAc units, and later modified by epimerization and sulfation events (Esko and Selleck, 2002).”
- Functions of heparan sulfate proteoglycans in cell signaling during development (2004, background): “These genes belong to the hereditary multiple exostoses (EXT) family of glycosyltransferases (Esko and Selleck, 2002; Zak et al., 2002), which function in HS chain biosynthesis, and are so-called because in humans EXT1 and EXT2 mutations cause hereditary multiple exostoses (HME), a benign bone…”
- Hereditary multiple exostoses and heparan sulfate polymerization. (2002, background): “As polymerization proceeds, a series of modifications takes place that include N-deacetylation of clustered sets of GlcNAc residues, followed by sulfation of the resulting free amino groups, epimerization of the flanking GlcA to L-iduronic acid (IdoA) and sulfation at C2 of the uronic acids and C6 a”
- Determinants of Glycosaminoglycan (GAG) Structure (2015, background): “The GAG chains possess sub-domains that allow biologically important interactions with a wide variety of regulatory proteins [2–5].”
- Demystifying Heparan Sulfate–Protein Interactions (2014, background): “Although only a few proteins are known to depend on 3-O-sulfation, there will probably be many others because of the large number of HS 3-Osulfotransferases (10, 119).”