| http://purl.uniprot.org/citations/28720894 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28720894 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28720894 | http://www.w3.org/2000/01/rdf-schema#comment | "Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41598-017-06062-w"xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41598-017-06062-w"xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "Cong Y."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "Cong Y."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "de Haan C.A.M."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "de Haan C.A.M."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "Kriegenburg F."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "Kriegenburg F."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "Reggiori F."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/author | "Reggiori F."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/name | "Sci. Rep."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/name | "Sci. Rep."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/pages | "5740"xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/pages | "5740"xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/title | "Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/title | "Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers."xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/volume | "7"xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://purl.uniprot.org/core/volume | "7"xsd:string |
| http://purl.uniprot.org/citations/28720894 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28720894 |
| http://purl.uniprot.org/citations/28720894 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28720894 |