| pubmed-article:2935422 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2935422 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
| pubmed-article:2935422 | lifeskim:mentions | umls-concept:C0027270 | lld:lifeskim |
| pubmed-article:2935422 | lifeskim:mentions | umls-concept:C0032405 | lld:lifeskim |
| pubmed-article:2935422 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:2935422 | lifeskim:mentions | umls-concept:C0439282 | lld:lifeskim |
| pubmed-article:2935422 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:2935422 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:2935422 | pubmed:dateCreated | 1986-3-6 | lld:pubmed |
| pubmed-article:2935422 | pubmed:abstractText | Calf thymus and rat liver poly(ADP-ribose) polymerase enzymes, and the polymerase present in extracts of rat liver nuclei synthesize unstable mono-ADP-ribose protein adducts at 100 nM or lower NAD concentrations. The isolated enzyme-mono-ADP-ribose adduct hydrolyses to ADP-ribose and enzyme protein at pH values slightly above 7.0 indicating a continuous release of ADP-ribose from NAD through this enzyme-bound intermediate under physiological conditions. NH2OH at pH 7.0 hydrolyses the mono-ADP-ribose enzyme adduct. Desamino NAD and some other homologs at nanomolar concentrations act as 'forward' activators of the initiating mono-ADP-ribosylation reaction. These NAD analogs at micromolar concentrations do not affect polymer formation that takes place at micromolar NAD concentrations. Benzamides at nanomolar concentrations also activate mono-ADP-ribosylation of the enzyme, but at higher concentrations inhibit elongation at micromolar NAD as substrate. In nuclei, the enzyme molecule extensively auto-ADP-ribosylates itself, whereas histones are trans-ADP-ribosylated to a much lower extent. The unstable mono-ADP-ribose enzyme adduct represents an initiator intermediate in poly ADP-ribosylation. | lld:pubmed |
| pubmed-article:2935422 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2935422 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2935422 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2935422 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2935422 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2935422 | pubmed:author | pubmed-author:KunEE | lld:pubmed |
| pubmed-article:2935422 | pubmed:author | pubmed-author:BauerP IPI | lld:pubmed |
| pubmed-article:2935422 | pubmed:author | pubmed-author:HakamAA | lld:pubmed |
| pubmed-article:2935422 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2935422 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:2935422 | pubmed:volume | 195 | lld:pubmed |
| pubmed-article:2935422 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2935422 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2935422 | pubmed:pagination | 331-8 | lld:pubmed |
| pubmed-article:2935422 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:meshHeading | pubmed-meshheading:2935422-... | lld:pubmed |
| pubmed-article:2935422 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2935422 | pubmed:articleTitle | Mechanisms of poly(ADP-ribose) polymerase catalysis; mono-ADP-ribosylation of poly(ADP-ribose) polymerase at nanomolar concentrations of NAD. | lld:pubmed |
| pubmed-article:2935422 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2935422 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2935422 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2935422 | lld:pubmed |
