| pubmed-article:6327687 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0014230 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0242499 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:6327687 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:6327687 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:6327687 | pubmed:dateCreated | 1984-7-2 | lld:pubmed |
| pubmed-article:6327687 | pubmed:abstractText | The activity of purified Ca2+, Mg2+-dependent endonuclease was inhibited when the enzyme was incubated in a system containing poly(ADP-ribose) synthetase, NAD+, Mg2+, and DNA. All four ingredients were essential to mediate ADP-ribosylation and to demonstrate inhibition of the endonuclease. In the absence of Mg2+, ADP-ribose transferring activity of poly(ADP-ribose) synthetase was stimulated by the addition of purified endonuclease to the reaction mixture in a dose-dependent manner. Analysis of the reaction product showed that the endonuclease was ADP-ribosylated. The average chain length of the initial oligo(ADP-ribose) attached to the enzyme was about 5.9 residues. The oligomer was found to be extensively elongated during the chase experiment using unlabeled NAD+ and Mg2+. The present finding suggests that Mg2+ is essential for the extensive elongation of the oligo(ADP-ribose). The DNA-binding affinity of the modified endonuclease was significantly lower than that of unmodified enzyme. Also, free poly(ADP-ribose) was not an effective inhibitor of the endonuclease. These findings suggest that the observed inhibition of the endonuclease induced by ADP-ribosylation is probably due to an electrostatic repulsion between the substrate (DNA) and poly(ADP-ribose) covalently linked to the endonuclease. Histone H1 and H2B stimulated endonuclease activity and were acceptors of ADP-ribose; however, their capacity to stimulate endonuclease activity remained unchanged after ADP-ribosylation. | lld:pubmed |
| pubmed-article:6327687 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6327687 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6327687 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6327687 | pubmed:month | May | lld:pubmed |
| pubmed-article:6327687 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6327687 | pubmed:author | pubmed-author:TanakaYY | lld:pubmed |
| pubmed-article:6327687 | pubmed:author | pubmed-author:KoideS SSS | lld:pubmed |
| pubmed-article:6327687 | pubmed:author | pubmed-author:YoshiharaKK | lld:pubmed |
| pubmed-article:6327687 | pubmed:author | pubmed-author:KamiyaTT | lld:pubmed |
| pubmed-article:6327687 | pubmed:author | pubmed-author:ItayaAA | lld:pubmed |
| pubmed-article:6327687 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6327687 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6327687 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:6327687 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6327687 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6327687 | pubmed:pagination | 6579-85 | lld:pubmed |
| pubmed-article:6327687 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
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| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
| pubmed-article:6327687 | pubmed:meshHeading | pubmed-meshheading:6327687-... | lld:pubmed |
| pubmed-article:6327687 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6327687 | pubmed:articleTitle | Mechanism of the inhibition of Ca2+, Mg2+-dependent endonuclease of bull seminal plasma induced by ADP-ribosylation. | lld:pubmed |
| pubmed-article:6327687 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6327687 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6327687 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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