Molecular diversity of heparan sulfate.

By J. Esko, U. Lindahl. Journal of Clinical Investigation, 2001

860 citations recorded by the source corpus.

Subfields: Cell Biology, Hematology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d184d4e18dba74e4bba1e4d16ecfaa2d6a42926a

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. B. Crawford
2. Beverly M. Zak
3. Leonard I. Zon
4. J. Esko
5. Xinhua Lin

In Hematology

1. Leonard I. Zon
2. J. Esko

In Molecular Biology

1. David R. Hall
2. Dima Kozakov
3. Bing Xia
4. Dmitri Beglov
5. Kathryn A. Porter
6. Sandor Vajda
7. C. Betsholtz
8. Robert J. Linhardt

Citations in the corpus

• 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”
• The sweet and sour of cancer: glycans as novel therapeutic targets (2005, neutral): “fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=3576">IL-8 )”
• The ClusPro web server for protein-protein docking (2017, background): “Variations in sulfation and hexuronic acid structure result in various HS molecules 61–64 .”
• Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. (2002, background): “The ability to bind heparin is thought to signify the capacity of a secreted molecule to be deposited in the extracellular matrix or on the cell surface, most likely through binding to heparan sulfate proteoglycans (HSPGs; Esko and Lindahl 2001).”
• Roles of heparan-sulphate glycosaminoglycans in cancer (2002, background): “The structural complexity arises from the differential modification of individual disaccharide units within an oligosaccharide chai”
• EXTL3 mutations cause skeletal dysplasia, immune deficiency, and developmental delay (2017, background): “The exostosin (EXT) family of genes encodes glycosyltransferases involved in the initiation of HS biosynthesis and elongation of HS chains (Esko and Lindahl, 2001; Busse et al., 2007).”