pubmed-article:3477560 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3477560 | lifeskim:mentions | umls-concept:C1524059 | lld:lifeskim |
pubmed-article:3477560 | lifeskim:mentions | umls-concept:C0031327 | lld:lifeskim |
pubmed-article:3477560 | lifeskim:mentions | umls-concept:C0171196 | lld:lifeskim |
pubmed-article:3477560 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:3477560 | pubmed:dateCreated | 1987-11-20 | lld:pubmed |
pubmed-article:3477560 | pubmed:abstractText | 3-Methyladenine-DNA glycosylase activities have been identified in all eukaryotic cell systems studied. Some of the results from these studies are reviewed here. The enzymes possess molecular weights between 24 X 10(3) and 34 X 10(3), they have a broad pH optimum at approximately pH 8, require double-stranded DNA and act in the absence of any cofactors. The enzyme can excise several different methylated bases from DNA such as 3-methyladenine, 7-methylguanine and 3-methylguanine. The specific activity of this DNA glycosylase in mouse L-cells was found to be a function of the proliferative state of the cell. In vitro quantification of this DNA repair activity in synchronized mouse L-cells suggests that it is regulated within a defined temporal sequence prior to the onset of DNA replication. Using DNA fragments of defined sequences it was observed that the efficiency of removal of the methylated bases is sequence-dependent. | lld:pubmed |
pubmed-article:3477560 | pubmed:language | eng | lld:pubmed |
pubmed-article:3477560 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3477560 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3477560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3477560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3477560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3477560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3477560 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3477560 | pubmed:issn | 0269-3518 | lld:pubmed |
pubmed-article:3477560 | pubmed:author | pubmed-author:KleppeKK | lld:pubmed |
pubmed-article:3477560 | pubmed:author | pubmed-author:OlsenLL | lld:pubmed |
pubmed-article:3477560 | pubmed:author | pubmed-author:NESSA GAG | lld:pubmed |
pubmed-article:3477560 | pubmed:author | pubmed-author:HellandD EDE | lld:pubmed |
pubmed-article:3477560 | pubmed:author | pubmed-author:HaukanesB IBI | lld:pubmed |
pubmed-article:3477560 | pubmed:author | pubmed-author:HauganII | lld:pubmed |
pubmed-article:3477560 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3477560 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:3477560 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3477560 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3477560 | pubmed:pagination | 139-46 | lld:pubmed |
pubmed-article:3477560 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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pubmed-article:3477560 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3477560 | pubmed:articleTitle | Properties and mechanism of action of eukaryotic 3-methyladenine-DNA glycosylases. | lld:pubmed |
pubmed-article:3477560 | pubmed:affiliation | Laboratory of Biotechnology, University of Bergen, Norway. | lld:pubmed |
pubmed-article:3477560 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3477560 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3477560 | lld:pubmed |