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dc.contributor.author오억수-
dc.date.accessioned2016-08-28T12:08:30Z-
dc.date.available2016-08-28T12:08:30Z-
dc.date.issued2011-
dc.identifier.issn0945-053X-
dc.identifier.otherOAK-7473-
dc.identifier.urihttps://dspace.ewha.ac.kr/handle/2015.oak/221538-
dc.description.abstractAn increasing number of functions for syndecan cell surface heparan sulfate proteoglycans have been proposed over the last decade. Moreover, aberrant syndecan regulation has been found to play a critical role in multiple pathologies, including cancers, as well as wound healing and inflammation. As receptors, they have much in common with other molecules on the cell surface. Syndecans are type I transmembrane molecules with cytoplasmic domains that link to the actin cytoskeleton and can interact with a number of regulators. However, they are also highly complex by virtue of their external glycosaminoglycan chains, especially heparan sulfate. This heterodisperse polysaccharide has the potential to interact with many ligands from diverse protein families. Here, we relate the structural features of syndecans to some of their known functions. © 2010 International Society of Matrix Biology.-
dc.languageEnglish-
dc.titleSyndecans as cell surface receptors: Unique structure equates with functional diversity-
dc.typeArticle-
dc.relation.issue2-
dc.relation.volume30-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage93-
dc.relation.lastpage99-
dc.relation.journaltitleMatrix Biology-
dc.identifier.doi10.1016/j.matbio.2010.10.006-
dc.identifier.wosidWOS:000289011100002-
dc.identifier.scopusid2-s2.0-79952107602-
dc.author.googleChoi Y.-
dc.author.googleChung H.-
dc.author.googleJung H.-
dc.author.googleCouchman J.R.-
dc.author.googleOh E.-S.-
dc.contributor.scopusid오억수(7101967153)-
dc.date.modifydate20190901081003-
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자연과학대학 > 생명과학전공 > Journal papers
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