| pubmed-article:8123025 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8123025 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:8123025 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8123025 | lifeskim:mentions | umls-concept:C0017797 | lld:lifeskim |
| pubmed-article:8123025 | lifeskim:mentions | umls-concept:C0061472 | lld:lifeskim |
| pubmed-article:8123025 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8123025 | pubmed:dateCreated | 1994-4-1 | lld:pubmed |
| pubmed-article:8123025 | pubmed:abstractText | DNA repair by O6-alkylguanine-DNA-alkyltransferase involves the stoichiometric transfer of the O6-alkyl group from the guanine lesion to the active-site cysteine residues of the protein. Site-directed mutagenesis of glutamic acid 172 of human O6-alkylguanine-DNA-alkyltransferase (EC 2.1.1.63) to glutamine totally abolished the alkyltransferase activity of the protein. This suggests that glutamic acid 172 is crucial to the alkyl transfer. It may act as a general acid (as CO2H) or base (as CO2-), or have a role as a component of a salt-link (-CO2-.....+N-), vital for the structural integrity of the active site. This is the first mutational inactivation of a protein in this family of DNA repair molecules by means of a residue change outside the highly conserved pentet (PCHRV) which includes the active-site cysteine. | lld:pubmed |
| pubmed-article:8123025 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8123025 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8123025 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8123025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8123025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8123025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8123025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8123025 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8123025 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8123025 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:8123025 | pubmed:author | pubmed-author:MargisonG PGP | lld:pubmed |
| pubmed-article:8123025 | pubmed:author | pubmed-author:DouglasK TKT | lld:pubmed |
| pubmed-article:8123025 | pubmed:author | pubmed-author:RaffertyJ AJA | lld:pubmed |
| pubmed-article:8123025 | pubmed:author | pubmed-author:ElderR HRH | lld:pubmed |
| pubmed-article:8123025 | pubmed:author | pubmed-author:SkorvagaMM | lld:pubmed |
| pubmed-article:8123025 | pubmed:author | pubmed-author:TumeltyJJ | lld:pubmed |
| pubmed-article:8123025 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8123025 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:8123025 | pubmed:volume | 199 | lld:pubmed |
| pubmed-article:8123025 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8123025 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8123025 | pubmed:pagination | 285-91 | lld:pubmed |
| pubmed-article:8123025 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:meshHeading | pubmed-meshheading:8123025-... | lld:pubmed |
| pubmed-article:8123025 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8123025 | pubmed:articleTitle | Site-directed mutagenesis of glutamic acid 172 to glutamine completely inactivated human O6-alkylguanine-DNA-alkyltransferase. | lld:pubmed |
| pubmed-article:8123025 | pubmed:affiliation | CRC Department of Carcinogenesis, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester, U.K. | lld:pubmed |
| pubmed-article:8123025 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8123025 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8123025 | lld:pubmed |
