| pubmed-article:10946227 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10946227 | lifeskim:mentions | umls-concept:C0077845 | lld:lifeskim |
| pubmed-article:10946227 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10946227 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10946227 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:10946227 | pubmed:issue | 3-4 | lld:pubmed |
| pubmed-article:10946227 | pubmed:dateCreated | 2000-11-13 | lld:pubmed |
| pubmed-article:10946227 | pubmed:abstractText | Deamination of cytosine to uracil is one of the major pro-mutagenic events in DNA, causing G:C-->A:T transition mutations if not repaired before replication. Repair of uracil-DNA is achieved in a base-excision pathway initiated by a uracil-DNA glycosylase (UDG) enzyme of which four families have so far been identified. Family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by 'base-sampling' probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. This allows a broader specificity so that some Family-2 enzymes can excise uracil and 3, N(4)-ethenocytosine from mismatches with guanine. Although structures are not yet available for Family-3 (SMUG) and Family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family. | lld:pubmed |
| pubmed-article:10946227 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10946227 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10946227 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10946227 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10946227 | pubmed:issn | 0027-5107 | lld:pubmed |
| pubmed-article:10946227 | pubmed:author | pubmed-author:PearlL HLH | lld:pubmed |
| pubmed-article:10946227 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10946227 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:10946227 | pubmed:volume | 460 | lld:pubmed |
| pubmed-article:10946227 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10946227 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10946227 | pubmed:pagination | 165-81 | lld:pubmed |
| pubmed-article:10946227 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10946227 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10946227 | pubmed:articleTitle | Structure and function in the uracil-DNA glycosylase superfamily. | lld:pubmed |
| pubmed-article:10946227 | pubmed:affiliation | Section of Structural Biology and CRC DNA Repair Enzyme Group, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, SW3 6JB, London, UK. laurence@icr.ac.uk | lld:pubmed |
| pubmed-article:10946227 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10946227 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10946227 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:10946227 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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