| pubmed-article:19362475 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19362475 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:19362475 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:19362475 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:19362475 | lifeskim:mentions | umls-concept:C2002095 | lld:lifeskim |
| pubmed-article:19362475 | lifeskim:mentions | umls-concept:C0125323 | lld:lifeskim |
| pubmed-article:19362475 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:19362475 | pubmed:dateCreated | 2009-5-4 | lld:pubmed |
| pubmed-article:19362475 | pubmed:abstractText | C-terminal-lacking fragments of the anti-mycobacterial peptide lariatin A were obtained by hydrolysis using carboxypeptidase P and their anti-mycobacterial activities were evaluated. Lys17 was found to be essential for their antimicrobial activity. A molecular dynamics simulation, with explicit water molecules, helped determine the structural characteristics of Lys17 of lariatin A. The simulation revealed the dynamic formation and deformation of a salt bridge between the N(xi) atom of Lys17 and the carboxyl group of C-terminal Pro18, which is deemed to be crucial for the compound's anti-mycobacterial activity. | lld:pubmed |
| pubmed-article:19362475 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19362475 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19362475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19362475 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19362475 | pubmed:month | May | lld:pubmed |
| pubmed-article:19362475 | pubmed:issn | 1464-3405 | lld:pubmed |
| pubmed-article:19362475 | pubmed:author | pubmed-author:OmuraSatoshiS | lld:pubmed |
| pubmed-article:19362475 | pubmed:author | pubmed-author:HironoShuichi... | lld:pubmed |
| pubmed-article:19362475 | pubmed:author | pubmed-author:KoizumiYukioY | lld:pubmed |
| pubmed-article:19362475 | pubmed:author | pubmed-author:TomodaHiroshi... | lld:pubmed |
| pubmed-article:19362475 | pubmed:author | pubmed-author:GoudaHiroakiH | lld:pubmed |
| pubmed-article:19362475 | pubmed:author | pubmed-author:IwatsukiMasat... | lld:pubmed |
| pubmed-article:19362475 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19362475 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:19362475 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:19362475 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19362475 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19362475 | pubmed:pagination | 2888-90 | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:meshHeading | pubmed-meshheading:19362475... | lld:pubmed |
| pubmed-article:19362475 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19362475 | pubmed:articleTitle | Lys17 in the 'lasso' peptide lariatin A is responsible for anti-mycobacterial activity. | lld:pubmed |
| pubmed-article:19362475 | pubmed:affiliation | Center for Basic Research, Kitasato University, Shirokane, Minato-ku, Tokyo, Japan. | lld:pubmed |
| pubmed-article:19362475 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19362475 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:19362475 | lld:chembl |
