| pubmed-article:3481270 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3481270 | lifeskim:mentions | umls-concept:C0019682 | lld:lifeskim |
| pubmed-article:3481270 | lifeskim:mentions | umls-concept:C0019699 | lld:lifeskim |
| pubmed-article:3481270 | lifeskim:mentions | umls-concept:C1709390 | lld:lifeskim |
| pubmed-article:3481270 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:3481270 | lifeskim:mentions | umls-concept:C0205470 | lld:lifeskim |
| pubmed-article:3481270 | lifeskim:mentions | umls-concept:C0243074 | lld:lifeskim |
| pubmed-article:3481270 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3481270 | pubmed:dateCreated | 1988-4-7 | lld:pubmed |
| pubmed-article:3481270 | pubmed:abstractText | The first open reading frame of the HIV genome has been identified as the gag gene. The proteins encoded by this gene are p17 as the amino-terminal protein, p24 as the middle peptide, and p15 as the carboxyl-terminal end. A monoclonal antibody recognizing an antigenic determinant on a fragment of p15 has been developed and designated M35/2F8. This monoclonal has been instrumental in radiosequencing the carboxyl-terminal product of p15, p6, and in determining the cleavage site between this protein and the amino-terminal product, p7. By immunoaffinity chromatography it was also possible to purify p6 from HIV lysates and all p6 containing polyproteins from HIV-infected cells. These results gave more insight into the composition and processing of the HIV gag gene. | lld:pubmed |
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| pubmed-article:3481270 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3481270 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3481270 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3481270 | pubmed:issn | 0889-2229 | lld:pubmed |
| pubmed-article:3481270 | pubmed:author | pubmed-author:GalloR CRC | lld:pubmed |
| pubmed-article:3481270 | pubmed:author | pubmed-author:SarngadharanM... | lld:pubmed |
| pubmed-article:3481270 | pubmed:author | pubmed-author:OroszlanSS | lld:pubmed |
| pubmed-article:3481270 | pubmed:author | pubmed-author:RahmanRR | lld:pubmed |
| pubmed-article:3481270 | pubmed:author | pubmed-author:CopelandT DTD | lld:pubmed |
| pubmed-article:3481270 | pubmed:author | pubmed-author:VeroneseF DFD | lld:pubmed |
| pubmed-article:3481270 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3481270 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:3481270 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3481270 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3481270 | pubmed:pagination | 253-64 | lld:pubmed |
| pubmed-article:3481270 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:3481270 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3481270 | pubmed:articleTitle | Immunological and chemical analysis of P6, the carboxyl-terminal fragment of HIV P15. | lld:pubmed |
| pubmed-article:3481270 | pubmed:affiliation | Bionetics Research, Inc., Rockville, MD 20850. | lld:pubmed |
| pubmed-article:3481270 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3481270 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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