| pubmed-article:3029283 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C0030393 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:3029283 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:3029283 | pubmed:dateCreated | 1987-4-1 | lld:pubmed |
| pubmed-article:3029283 | pubmed:abstractText | Monoclonal antibodies to the envelope glycoproteins, HN and F, of human parainfluenza virus type 3 were coupled to a Sepharose 4B matrix and used for affinity purification of the viral glycoproteins. The purity of the glycoproteins was demonstrated by SDS-PAGE followed by fluorography or silver staining. The antigenicity of the glycoproteins was determined by immunization of rabbits; polyclonal rabbit antisera demonstrated inhibition of functional activities of the virus glycoproteins. The F glycoprotein, when reconstituted into lipid vesicles, showed distinct spike-like projections similar to those of intact virions. | lld:pubmed |
| pubmed-article:3029283 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3029283 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3029283 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3029283 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:3029283 | pubmed:issn | 0022-1317 | lld:pubmed |
| pubmed-article:3029283 | pubmed:author | pubmed-author:RazSS | lld:pubmed |
| pubmed-article:3029283 | pubmed:author | pubmed-author:CompansR WRW | lld:pubmed |
| pubmed-article:3029283 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3029283 | pubmed:volume | 68 ( Pt 2) | lld:pubmed |
| pubmed-article:3029283 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3029283 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3029283 | pubmed:pagination | 409-18 | lld:pubmed |
| pubmed-article:3029283 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:meshHeading | pubmed-meshheading:3029283-... | lld:pubmed |
| pubmed-article:3029283 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3029283 | pubmed:articleTitle | Glycoproteins of human parainfluenza virus type 3: affinity purification, antigenic characterization and reconstitution into lipid vesicles. | lld:pubmed |
| pubmed-article:3029283 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3029283 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3029283 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3029283 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3029283 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3029283 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3029283 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3029283 | lld:pubmed |
