| pubmed-article:18954000 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18954000 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:18954000 | lifeskim:mentions | umls-concept:C0027783 | lld:lifeskim |
| pubmed-article:18954000 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:18954000 | lifeskim:mentions | umls-concept:C0486805 | lld:lifeskim |
| pubmed-article:18954000 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:18954000 | lifeskim:mentions | umls-concept:C0053772 | lld:lifeskim |
| pubmed-article:18954000 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18954000 | pubmed:dateCreated | 2008-10-28 | lld:pubmed |
| pubmed-article:18954000 | pubmed:abstractText | The binding to DNA of Pt-bis-Nt and its modified analogue (Pt*-bis-Nt), which differs from Pt-bis-Nt by the fact that the connecting chain between two netropsin fragments contains two additional glycine residues, has been studied. Elongating the chain in the bis-netropsin molecule increases the cytotoxicity and leads to a complete disappearance of the antiherpetic activity of bis-netropsin. A study of the binding of two bis-netropsins with the oligonucleotide duplex containing an AT cluster, which is present at the replication initiation site of herpes virus (OriS), revealed significant structural differences between complexes of bis-netropsins with this DNA oligomer. It was shown by CD spectroscopy that the binding of Pt-bis-Nt in the elongated conformation and in the form of a hair-pin with the parallel orientation of two bis-netropsin fragments makes a greater contribution than it is the case in the complex formation with Pt*-bis-Nt. At high binding rates, Pt*-bis-Nt binds to the AT cluster in OriS predominantly in the form of associates based on the antiparallel double-stranded pyrrolcarboxyamide motif. The interaction of Pt-bis-Nt and Pt*-bis-Nt with the single-stranded oligonucleotide (64 nt), which corresponds to the upper strand at the replication initiation site of herpes virus (OriS*), was also studied. Substantial differences in the binding of bis-netropsins with OriS* and thermostability of the resulting complexes were found by CD spectroscopy and by studying the melting of complexes of bis-netropsins with OriS*. | lld:pubmed |
| pubmed-article:18954000 | pubmed:language | rus | lld:pubmed |
| pubmed-article:18954000 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18954000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18954000 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18954000 | pubmed:issn | 0006-3029 | lld:pubmed |
| pubmed-article:18954000 | pubmed:author | pubmed-author:Grokhovski?S... | lld:pubmed |
| pubmed-article:18954000 | pubmed:author | pubmed-author:SurovaiaA NAN | lld:pubmed |
| pubmed-article:18954000 | pubmed:author | pubmed-author:BazhulinaN... | lld:pubmed |
| pubmed-article:18954000 | pubmed:author | pubmed-author:Gurski?G vG | lld:pubmed |
| pubmed-article:18954000 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18954000 | pubmed:volume | 53 | lld:pubmed |
| pubmed-article:18954000 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18954000 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18954000 | pubmed:pagination | 744-53 | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:meshHeading | pubmed-meshheading:18954000... | lld:pubmed |
| pubmed-article:18954000 | pubmed:articleTitle | [DNA-binding activity of bis-netropsins containing a cis-diaminoplatinum group between two netropsin fragments]. | lld:pubmed |
| pubmed-article:18954000 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18954000 | pubmed:publicationType | English Abstract | lld:pubmed |
| pubmed-article:18954000 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
