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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
48
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pubmed:dateCreated |
2006-12-7
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pubmed:abstractText |
Endo III and Endo VIII are major E. coli DNA glycosylases that remove oxidatively damaged pyrimidine bases. In the present study, we have compared the damage specificity of human homologues of Endo III (hNTHl) and Endo VIII (hNEIL1 and hNEIL2) to elucidate the repair role in cells. hNTH1 and hNEIL1 recognized a similar spectra of bases lesions, but the preference of damage including the stereoisomers of thymine glycol was significantly different between hNTH1 and hNEIL1. hNEIL2 exhibited a strong AP lyase activity but the N-glycosylase activity for the tested oxidative base lesions was marginal.
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pubmed:language |
eng
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pubmed:journal |
|
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1746-8272
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
175-6
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pubmed:dateRevised |
2007-9-19
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pubmed:meshHeading |
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pubmed:year |
2004
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pubmed:articleTitle |
Damage specificity of human DNA glycosylases for oxidative pyrimidine lesions.
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pubmed:affiliation |
Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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