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http://purl.uniprot.org/citations/14967025http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14967025http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14967025http://www.w3.org/2000/01/rdf-schema#comment"The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer-dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.org/dc/terms/identifier"doi:10.1021/bi035490x"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.org/dc/terms/identifier"doi:10.1021/bi035490x"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Jiang S."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Jiang S."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Caffrey M."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Caffrey M."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Jacobs A."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Jacobs A."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Laue T.M."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/author"Laue T.M."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/pages"1847-1853"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/pages"1847-1853"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/title"Solution structure of the coxsackievirus and adenovirus receptor domain 1."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/title"Solution structure of the coxsackievirus and adenovirus receptor domain 1."xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/14967025http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/14967025http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14967025
http://purl.uniprot.org/citations/14967025http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14967025