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dc.contributor.authorJayson, Gordon Cen
dc.contributor.authorHansen, Sen
dc.contributor.authorMiller, Gen
dc.contributor.authorCole, Claire Len
dc.contributor.authorRushton, Grahamen
dc.contributor.authorAvizienyte, Egleen
dc.contributor.authorGardiner, Jen
dc.date.accessioned2015-09-17T11:09:48Zen
dc.date.available2015-09-17T11:09:48Zen
dc.date.issued2015-09-18en
dc.identifier.citationSynthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology. 2015, 51 (72):13846-9 Chem Communen
dc.identifier.issn1364-548Xen
dc.identifier.pmid26234943en
dc.identifier.doi10.1039/c5cc05222jen
dc.identifier.urihttp://hdl.handle.net/10541/577424en
dc.description.abstractThe multigram-scale synthesis of a sulfation-site programmed heparin-like dodecasaccharide is described. Evaluation alongside dodecasaccharides lacking this single glucosamine O6-sulfation, or having per-O6-sulfation, shows that site-specific modification of the terminal glucosamine dramatically interconverts regulation of in vitro and in vivo biology mediated by the two important chemokines, CXCL12 (SDF1α) or CXCL8 (IL-8).
dc.language.isoenen
dc.rightsArchived with thanks to Chemical communications (Cambridge, England)en
dc.titleSynthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology.en
dc.typeArticleen
dc.contributor.departmentChristie Hospital, Institute of Cancer Studies, University of Manchester, Manchester, M20 4BX, UKen
dc.identifier.journalChemical Communicationsen
html.description.abstractThe multigram-scale synthesis of a sulfation-site programmed heparin-like dodecasaccharide is described. Evaluation alongside dodecasaccharides lacking this single glucosamine O6-sulfation, or having per-O6-sulfation, shows that site-specific modification of the terminal glucosamine dramatically interconverts regulation of in vitro and in vivo biology mediated by the two important chemokines, CXCL12 (SDF1α) or CXCL8 (IL-8).


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