pubmed-article:8480423 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0001753 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0582263 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C1418578 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0851287 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
pubmed-article:8480423 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
pubmed-article:8480423 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8480423 | pubmed:dateCreated | 1993-5-27 | lld:pubmed |
pubmed-article:8480423 | pubmed:abstractText | Two kinds of unrelated African swine fever virus proteins of 220 kDa have been identified by means of two-dimensional gel electrophoresis and immunoprecipitation analysis. One species, named pp220 and identified as the precursor of the major structural protein p150, was found to be a moderately acidic protein (pl near 7) expressed after the replication of the viral DNA. The second species, a cluster of 220-kDa proteins with slightly different isoelectric points (pl ranging from 5 to 6), was found to be a homooligomeric complex formed by an early 32-kDa protein. This component was identified as the viral phosphoprotein p32, the most immunogenic early protein of African swine fever virus. A detailed characterization of its oligomeric structure is reported. | lld:pubmed |
pubmed-article:8480423 | pubmed:language | eng | lld:pubmed |
pubmed-article:8480423 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8480423 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8480423 | pubmed:month | May | lld:pubmed |
pubmed-article:8480423 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:8480423 | pubmed:author | pubmed-author:ViñuelaEE | lld:pubmed |
pubmed-article:8480423 | pubmed:author | pubmed-author:AndrénBB | lld:pubmed |
pubmed-article:8480423 | pubmed:author | pubmed-author:Simón-MateoCC | lld:pubmed |
pubmed-article:8480423 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8480423 | pubmed:volume | 194 | lld:pubmed |
pubmed-article:8480423 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8480423 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8480423 | pubmed:pagination | 284-93 | lld:pubmed |
pubmed-article:8480423 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8480423 | pubmed:meshHeading | pubmed-meshheading:8480423-... | lld:pubmed |
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pubmed-article:8480423 | pubmed:meshHeading | pubmed-meshheading:8480423-... | lld:pubmed |
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pubmed-article:8480423 | pubmed:meshHeading | pubmed-meshheading:8480423-... | lld:pubmed |
pubmed-article:8480423 | pubmed:meshHeading | pubmed-meshheading:8480423-... | lld:pubmed |
pubmed-article:8480423 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8480423 | pubmed:articleTitle | Characterization of two African swine fever virus 220-kDa proteins: a precursor of the major structural protein p150 and an oligomer of phosphoprotein p32. | lld:pubmed |
pubmed-article:8480423 | pubmed:affiliation | Centro de Biología Molecular (C.S.I.C.-U.A.M.), Facultad de Ciencias, Universidad Autónoma, Cantoblancó, Madrid, Spain. | lld:pubmed |
pubmed-article:8480423 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8480423 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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