| pubmed-article:2843295 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2843295 | lifeskim:mentions | umls-concept:C1325725 | lld:lifeskim |
| pubmed-article:2843295 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:2843295 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:2843295 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:2843295 | lifeskim:mentions | umls-concept:C0040674 | lld:lifeskim |
| pubmed-article:2843295 | lifeskim:mentions | umls-concept:C1158498 | lld:lifeskim |
| pubmed-article:2843295 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2843295 | pubmed:dateCreated | 1988-10-25 | lld:pubmed |
| pubmed-article:2843295 | pubmed:abstractText | Yeast Ty1 elements are retrotransposons that transpose via an RNA intermediate found in a virus-like particle (Ty-VLP). A Ty-encoded reverse transcriptase activity found inside the particles is capable of giving rise to full-length reverse transcripts. The predominant form of these reverse transcripts is a full-length linear duplex DNA. We have developed a cell-free system for transposition of Ty1 DNA molecules into a bacteriophage lambda target. Purified Ty-VLPs and target DNA are the only macromolecular components required for the transposition reaction. A TYB-encoded protein, p90-TYB, contains amino acid sequences that are similar to those of retroviral integrase proteins. Mutations in the integrase coding region abolish transposition both in vivo and in vitro. | lld:pubmed |
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| pubmed-article:2843295 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2843295 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2843295 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2843295 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2843295 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:2843295 | pubmed:author | pubmed-author:BoekeJ DJD | lld:pubmed |
| pubmed-article:2843295 | pubmed:author | pubmed-author:EichingerD... | lld:pubmed |
| pubmed-article:2843295 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2843295 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:2843295 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:2843295 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2843295 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2843295 | pubmed:pagination | 955-66 | lld:pubmed |
| pubmed-article:2843295 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2843295 | pubmed:meshHeading | pubmed-meshheading:2843295-... | lld:pubmed |
| pubmed-article:2843295 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2843295 | pubmed:articleTitle | The DNA intermediate in yeast Ty1 element transposition copurifies with virus-like particles: cell-free Ty1 transposition. | lld:pubmed |
| pubmed-article:2843295 | pubmed:affiliation | Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205. | lld:pubmed |
| pubmed-article:2843295 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2843295 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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