pubmed-article:18216112 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C1564874 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C0557351 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C1136102 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:18216112 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:18216112 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:18216112 | pubmed:dateCreated | 2008-3-12 | lld:pubmed |
pubmed-article:18216112 | pubmed:abstractText | Degradation of de novo-generated adeno-associated virus type 5 (AAV5) Rep52 and capsid proteins is part of the limited target specificity displayed by adenovirus type 5 E4Orf6-E1B-55k as part of a cullin 5-containing E3 ligase complex. Both Rep and capsid proteins can be found in the ligase complex, and their presence is dependent on interaction between E4Orf6 and elongins B and C. Degradation of AAV5 proteins can be inhibited by a dominant-negative ubiquitin that prevents chain elongation or by small interfering RNA directed against cullin 5. | lld:pubmed |
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pubmed-article:18216112 | pubmed:language | eng | lld:pubmed |
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pubmed-article:18216112 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18216112 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18216112 | pubmed:month | Apr | lld:pubmed |
pubmed-article:18216112 | pubmed:issn | 1098-5514 | lld:pubmed |
pubmed-article:18216112 | pubmed:author | pubmed-author:PintelDavid... | lld:pubmed |
pubmed-article:18216112 | pubmed:author | pubmed-author:NayakRamnathR | lld:pubmed |
pubmed-article:18216112 | pubmed:author | pubmed-author:FarrisK... | lld:pubmed |
pubmed-article:18216112 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18216112 | pubmed:volume | 82 | lld:pubmed |
pubmed-article:18216112 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18216112 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18216112 | pubmed:pagination | 3803-8 | lld:pubmed |
pubmed-article:18216112 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:18216112 | pubmed:meshHeading | pubmed-meshheading:18216112... | lld:pubmed |
pubmed-article:18216112 | pubmed:meshHeading | pubmed-meshheading:18216112... | lld:pubmed |
pubmed-article:18216112 | pubmed:meshHeading | pubmed-meshheading:18216112... | lld:pubmed |
pubmed-article:18216112 | pubmed:meshHeading | pubmed-meshheading:18216112... | lld:pubmed |
pubmed-article:18216112 | pubmed:meshHeading | pubmed-meshheading:18216112... | lld:pubmed |
pubmed-article:18216112 | pubmed:meshHeading | pubmed-meshheading:18216112... | lld:pubmed |
pubmed-article:18216112 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18216112 | pubmed:articleTitle | E4Orf6-E1B-55k-dependent degradation of de novo-generated adeno-associated virus type 5 Rep52 and capsid proteins employs a cullin 5-containing E3 ligase complex. | lld:pubmed |
pubmed-article:18216112 | pubmed:affiliation | Department of Molecular Microbiology and Immunology, University of Missouri-Columbia, School of Medicine, Life Sciences Center, Columbia, Missouri 65211, USA. | lld:pubmed |
pubmed-article:18216112 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18216112 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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