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Histidine-rich glycoprotein binds to cell-surface heparan sulfate via its N-terminal domain following Zn 2+ chelation

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dc.contributor.authorJones, Allisonen_AU
dc.contributor.authorHulett, Marken_AU
dc.contributor.authorParish, Christopheren_AU
dc.date.accessioned2015-12-13T22:39:19Z
dc.date.available2015-12-13T22:39:19Z
dc.date.issued2004
dc.date.updated2015-12-11T09:48:13Z
dc.description.abstractHistidine-rich glycoprotein (HRG) is an α2-glycoprotein found in mammalian plasma at high concentrations (∼150 μg/ml) and is distinguished by its high content of histidine and proline. Structurally, HRG is a modular protein consisting of an N-terminal
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/77728
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.sourceJournal of Biological Chemistry
dc.subjectKeywords: Biochemistry; Cells; Chemical bonds; Cytology; Physiology; Fibrinogen; Glycoproteins; Proteins; adaptor protein; alpha2 glycoprotein; chondroitin ABC lyase; complement component C1q; cystatin; fibrinogen; glycosaminoglycan; heparan sulfate; heparanase; he
dc.titleHistidine-rich glycoprotein binds to cell-surface heparan sulfate via its N-terminal domain following Zn 2+ chelation
dc.typeJournal article
local.bibliographicCitation.issue29
local.bibliographicCitation.lastpage30122
local.bibliographicCitation.startpage30114
local.contributor.affiliationJones, Allison, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHulett, Mark, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationParish, Christopher, College of Medicine, Biology and Environment, ANU
local.contributor.authoruidJones, Allison, u9906280
local.contributor.authoruidHulett, Mark, a261320
local.contributor.authoruidParish, Christopher, u6900322
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor110704 - Cellular Immunology
local.identifier.ariespublicationMigratedxPub6530
local.identifier.citationvolume279
local.identifier.doi10.1074/jbc.M401996200
local.identifier.scopusID2-s2.0-3142662536
local.type.statusPublished Version

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