| pubmed-article:2941933 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2941933 | lifeskim:mentions | umls-concept:C0001483 | lld:lifeskim |
| pubmed-article:2941933 | lifeskim:mentions | umls-concept:C0042769 | lld:lifeskim |
| pubmed-article:2941933 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:2941933 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2941933 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:2941933 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2941933 | pubmed:dateCreated | 1986-8-15 | lld:pubmed |
| pubmed-article:2941933 | pubmed:abstractText | We have investigated the role of poly(ADP)-ribosylation of adenoviral proteins in virus infection. Viral core proteins V and the precursor to protein VII were shown to be in vivo and in vitro acceptors of ADP-ribose. In vivo ADP-ribosylation was restricted to viral proteins as the histones were not labeled during the late phase of infection. The ADP-ribosylated core proteins were assembled into mature virus particles. In vitro ADP-ribosylation of adenoviral core proteins performed with purified poly(ADP-ribose) polymerase led to relaxation of the chromatin structure of both ts1 and wild type pyridine cores and pentonless particles and triggered the complete dissociation of wild type particles. A critical role for poly(ADP)-ribosylation in virus infection was confirmed by measuring the effect of the inhibitors 3-aminobenzamide and nicotinamide on virus particle yield and infectivity. Both inhibitors depressed particle yield by up to 9-fold, but infectivity was reduced by up to 10(4)-fold. These results suggest that ADP-ribosylation of adenovirus core proteins may have a role in virus decapsidation. | lld:pubmed |
| pubmed-article:2941933 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2941933 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2941933 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2941933 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2941933 | pubmed:issn | 0168-1702 | lld:pubmed |
| pubmed-article:2941933 | pubmed:author | pubmed-author:PoirierG GGG | lld:pubmed |
| pubmed-article:2941933 | pubmed:author | pubmed-author:WeberJJ | lld:pubmed |
| pubmed-article:2941933 | pubmed:author | pubmed-author:de MurciaGG | lld:pubmed |
| pubmed-article:2941933 | pubmed:author | pubmed-author:MorioMM | lld:pubmed |
| pubmed-article:2941933 | pubmed:author | pubmed-author:KhanR MRM | lld:pubmed |
| pubmed-article:2941933 | pubmed:author | pubmed-author:LamarreDD | lld:pubmed |
| pubmed-article:2941933 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2941933 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:2941933 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2941933 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2941933 | pubmed:pagination | 313-29 | lld:pubmed |
| pubmed-article:2941933 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2941933 | pubmed:meshHeading | pubmed-meshheading:2941933-... | lld:pubmed |
| pubmed-article:2941933 | pubmed:meshHeading | pubmed-meshheading:2941933-... | lld:pubmed |
| pubmed-article:2941933 | pubmed:meshHeading | pubmed-meshheading:2941933-... | lld:pubmed |
| pubmed-article:2941933 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2941933 | pubmed:articleTitle | Possible role of ADP-ribosylation of adenovirus core proteins in virus infection. | lld:pubmed |
| pubmed-article:2941933 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2941933 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| family:PF03228.9 | family:pubmed | pubmed-article:2941933 | lld:pfam |
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