| pubmed-article:1372272 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1372272 | lifeskim:mentions | umls-concept:C1955880 | lld:lifeskim |
| pubmed-article:1372272 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:1372272 | lifeskim:mentions | umls-concept:C1148813 | lld:lifeskim |
| pubmed-article:1372272 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1372272 | pubmed:dateCreated | 1992-4-20 | lld:pubmed |
| pubmed-article:1372272 | pubmed:abstractText | A method for the rapid preparation of a defined substrate to monitor RNase H activity has been developed. Using this substrate, we have investigated the RNase H activities of the different forms of recombinant HIV-1 and HIV-2 reverse transcriptase (RT) in detail. As we report here, RNase H activity is associated only with the dimeric forms (p51/p66 or p66/p66) of the enzymes. | lld:pubmed |
| pubmed-article:1372272 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1372272 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1372272 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1372272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1372272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1372272 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1372272 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1372272 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:1372272 | pubmed:author | pubmed-author:GoodyR SRS | lld:pubmed |
| pubmed-article:1372272 | pubmed:author | pubmed-author:MüllerBB | lld:pubmed |
| pubmed-article:1372272 | pubmed:author | pubmed-author:RestleTT | lld:pubmed |
| pubmed-article:1372272 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1372272 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:1372272 | pubmed:volume | 300 | lld:pubmed |
| pubmed-article:1372272 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1372272 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1372272 | pubmed:pagination | 97-100 | lld:pubmed |
| pubmed-article:1372272 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:1372272 | pubmed:meshHeading | pubmed-meshheading:1372272-... | lld:pubmed |
| pubmed-article:1372272 | pubmed:meshHeading | pubmed-meshheading:1372272-... | lld:pubmed |
| pubmed-article:1372272 | pubmed:meshHeading | pubmed-meshheading:1372272-... | lld:pubmed |
| pubmed-article:1372272 | pubmed:meshHeading | pubmed-meshheading:1372272-... | lld:pubmed |
| pubmed-article:1372272 | pubmed:meshHeading | pubmed-meshheading:1372272-... | lld:pubmed |
| pubmed-article:1372272 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1372272 | pubmed:articleTitle | RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms. | lld:pubmed |
| pubmed-article:1372272 | pubmed:affiliation | Abteilung Biophysik, Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:1372272 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1372272 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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