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http://purl.uniprot.org/unirules/MF_04125#construct-template-69http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_04125#construct-var-0
http://purl.uniprot.org/unirules/MF_04125#construct-template-69http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_04125#construct-template-69http://spinrdf.org/sp#object"Outer capsid protein VP4: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7."xsd:string
http://purl.uniprot.org/unirules/MF_04125#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_04125#construct-template-69
http://purl.uniprot.org/unirules/MF_04125#construct-template-list-69http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_04125#construct-template-69