pubmed-article:7690419 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7690419 | lifeskim:mentions | umls-concept:C1005556 | lld:lifeskim |
pubmed-article:7690419 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
pubmed-article:7690419 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7690419 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:7690419 | lifeskim:mentions | umls-concept:C1418887 | lld:lifeskim |
pubmed-article:7690419 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:7690419 | pubmed:dateCreated | 1993-10-12 | lld:pubmed |
pubmed-article:7690419 | pubmed:abstractText | The human papillomavirus (HPV) E5 proteins are predicted from DNA sequence analysis to be small hydrophobic molecules, and the HPV type 6 (HPV-6) and HPV-11 E5 proteins share several structural similarities with the bovine papillomavirus type 1 (BPV-1) E5 protein. Also similar to the BPV-1 E5 protein, the HPV-6 and HPV-16 E5 proteins exhibit transforming activity when assayed on NIH 3T3 and C127 cells. In this study, we expressed epitope-tagged E5 proteins from both the "low-risk" HPV-6 and the "high-risk" HPV-16 in order to permit their immunologic identification and biochemical characterization. While the HPV-6 and HPV-16 E5 proteins fail to form disulfide-linked dimers and oligomers, they did resemble the BPV-1 E5 protein in their intracellular localization to the Golgi apparatus, endoplasmic reticulum, and nuclear membranes. In addition, the HPV E5 proteins also bound to the 16-kDa pore-forming protein component of the vacuolar ATPase, a known characteristic of the BPV-1 E5 protein. These studies reveal a common intramembrane localization and potential cellular protein target for both the BPV and HPV E5 proteins. | lld:pubmed |
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pubmed-article:7690419 | pubmed:language | eng | lld:pubmed |
pubmed-article:7690419 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7690419 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7690419 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7690419 | pubmed:month | Oct | lld:pubmed |
pubmed-article:7690419 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:7690419 | pubmed:author | pubmed-author:SchlegelRR | lld:pubmed |
pubmed-article:7690419 | pubmed:author | pubmed-author:ConradMM | lld:pubmed |
pubmed-article:7690419 | pubmed:author | pubmed-author:BubbV JVJ | lld:pubmed |
pubmed-article:7690419 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7690419 | pubmed:volume | 67 | lld:pubmed |
pubmed-article:7690419 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7690419 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7690419 | pubmed:pagination | 6170-8 | lld:pubmed |
pubmed-article:7690419 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:7690419 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:7690419 | pubmed:articleTitle | The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming protein. | lld:pubmed |
pubmed-article:7690419 | pubmed:affiliation | Department of Pathology, Georgetown University Medical School, Washington, D.C. 20007. | lld:pubmed |
pubmed-article:7690419 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7690419 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:7690419 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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