| pubmed-article:18926799 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18926799 | lifeskim:mentions | umls-concept:C1175743 | lld:lifeskim |
| pubmed-article:18926799 | lifeskim:mentions | umls-concept:C0524816 | lld:lifeskim |
| pubmed-article:18926799 | lifeskim:mentions | umls-concept:C2700116 | lld:lifeskim |
| pubmed-article:18926799 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18926799 | pubmed:dateCreated | 2008-11-14 | lld:pubmed |
| pubmed-article:18926799 | pubmed:abstractText | The severe acute respiratory syndrome (SARS) is a contagious disease that killed hundreds and sickened thousands of people worldwide between November 2002 and July 2003. The nucleocapsid (N) protein of the coronavirus responsible for this disease plays a critical role in viral assembly and maturation and is of particular interest because of its potential as an antiviral target or vaccine candidate. Refolding of SARS N-protein during production and purification showed the presence of two additional protein bands by SDS-PAGE. Mass spectroscopy (MALDI, SELDI, and LC/MS) confirmed that the bands are proteolytic products of N-protein and the cleavage sites are four SR motifs in the serine-arginine-rich region-sites not suggestive of any known protease. Furthermore, results of subsequent testing for contaminating protease(s) were negative: cleavage appears to be due to inherent instability and/or autolysis. The importance of N-protein proteolysis to viral life cycle and thus to possible treatment directions are discussed. | lld:pubmed |
| pubmed-article:18926799 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18926799 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18926799 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18926799 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18926799 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18926799 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18926799 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18926799 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18926799 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:18926799 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:18926799 | pubmed:author | pubmed-author:MarkJohnJ | lld:pubmed |
| pubmed-article:18926799 | pubmed:author | pubmed-author:FournierSylvi... | lld:pubmed |
| pubmed-article:18926799 | pubmed:author | pubmed-author:CyrTerryT | lld:pubmed |
| pubmed-article:18926799 | pubmed:author | pubmed-author:HeffordMary... | lld:pubmed |
| pubmed-article:18926799 | pubmed:author | pubmed-author:LiXuguangX | lld:pubmed |
| pubmed-article:18926799 | pubmed:author | pubmed-author:JaentschkeBoz... | lld:pubmed |
| pubmed-article:18926799 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18926799 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:18926799 | pubmed:volume | 377 | lld:pubmed |
| pubmed-article:18926799 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18926799 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18926799 | pubmed:pagination | 429-33 | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:meshHeading | pubmed-meshheading:18926799... | lld:pubmed |
| pubmed-article:18926799 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18926799 | pubmed:articleTitle | SARS coronavirus: unusual lability of the nucleocapsid protein. | lld:pubmed |
| pubmed-article:18926799 | pubmed:affiliation | Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2. | lld:pubmed |
| pubmed-article:18926799 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:1489678 | entrezgene:pubmed | pubmed-article:18926799 | lld:entrezgene |
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