| pubmed-article:11731295 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0003392 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0184898 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0242958 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0600688 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0596040 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C2348519 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0059229 | lld:lifeskim |
| pubmed-article:11731295 | lifeskim:mentions | umls-concept:C0388976 | lld:lifeskim |
| pubmed-article:11731295 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:11731295 | pubmed:dateCreated | 2001-12-3 | lld:pubmed |
| pubmed-article:11731295 | pubmed:abstractText | Ecteinascidin 743 (Et 743), a natural product derived from a marine tunicate, is a potent antitumor agent presently in phase II clinical trials. Et 743 binds in the minor groove of DNA and alkylates N2 of guanine via a unique mechanism involving catalytic activation. The sequence selectivity of Et 743 is governed by different patterns of hydrogen-bonding to DNA, which results in differential reversibility of the covalent adducts. As determined by nuclear magnetic resonance spectroscopy, the preferred sequences 5'-PuGC and 5'-PyGG are stabilized by a hydrogen-bonding network, while the non-preferred sequences 5'-NG(A/T) are much less stabilized due to the lack of a key hydrogen bond to the GC base pair on the 3'-side of the alkylated guanine. | lld:pubmed |
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| pubmed-article:11731295 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11731295 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11731295 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11731295 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11731295 | pubmed:issn | 1074-5521 | lld:pubmed |
| pubmed-article:11731295 | pubmed:author | pubmed-author:KohnHH | lld:pubmed |
| pubmed-article:11731295 | pubmed:author | pubmed-author:HurleyL HLH | lld:pubmed |
| pubmed-article:11731295 | pubmed:author | pubmed-author:GuzmanMM | lld:pubmed |
| pubmed-article:11731295 | pubmed:author | pubmed-author:LiV SVS | lld:pubmed |
| pubmed-article:11731295 | pubmed:author | pubmed-author:BearssDD | lld:pubmed |
| pubmed-article:11731295 | pubmed:author | pubmed-author:Zewail-FooteM... | lld:pubmed |
| pubmed-article:11731295 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11731295 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:11731295 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11731295 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11731295 | pubmed:pagination | 1033-49 | lld:pubmed |
| pubmed-article:11731295 | pubmed:dateRevised | 2008-11-29 | lld:pubmed |
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| pubmed-article:11731295 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11731295 | pubmed:articleTitle | The inefficiency of incisions of ecteinascidin 743-DNA adducts by the UvrABC nuclease and the unique structural feature of the DNA adducts can be used to explain the repair-dependent toxicities of this antitumor agent. | lld:pubmed |
| pubmed-article:11731295 | pubmed:affiliation | Department of Chemistry and Biochemistry, The University of Texas at Autin, 78712, USA. | lld:pubmed |
| pubmed-article:11731295 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11731295 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11731295 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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