pubmed-article:16200071 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16200071 | lifeskim:mentions | umls-concept:C0003232 | lld:lifeskim |
pubmed-article:16200071 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
pubmed-article:16200071 | lifeskim:mentions | umls-concept:C0337076 | lld:lifeskim |
pubmed-article:16200071 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
pubmed-article:16200071 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
pubmed-article:16200071 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:16200071 | pubmed:dateCreated | 2005-10-7 | lld:pubmed |
pubmed-article:16200071 | pubmed:abstractText | Here we show that a new class of antibiotics-acyldepsipeptides-has antibacterial activity against Gram-positive bacteria in vitro and in several rodent models of bacterial infection. The acyldepsipeptides are active against isolates that are resistant to antibiotics in clinical application, implying a new target, which we identify as ClpP, the core unit of a major bacterial protease complex. ClpP is usually tightly regulated and strictly requires a member of the family of Clp-ATPases and often further accessory proteins for proteolytic activation. Binding of acyldepsipeptides to ClpP eliminates these safeguards. The acyldepsipeptide-activated ClpP core is capable of proteolytic degradation in the absence of the regulatory Clp-ATPases. Such uncontrolled proteolysis leads to inhibition of bacterial cell division and eventually cell death. | lld:pubmed |
pubmed-article:16200071 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:language | eng | lld:pubmed |
pubmed-article:16200071 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16200071 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16200071 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16200071 | pubmed:month | Oct | lld:pubmed |
pubmed-article:16200071 | pubmed:issn | 1078-8956 | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:LabischinskiH... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:SahlHans-Geor... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:HenningerKers... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:PaulsenHolger... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:SchroederWern... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:EndermannRain... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:RaddatzSiegfr... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:KrollHein-Pet... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:BeyerDieterD | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:Brötz-Oesterh... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:LadelChristop... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:HinzenBerthol... | lld:pubmed |
pubmed-article:16200071 | pubmed:author | pubmed-author:BandowJulia... | lld:pubmed |
pubmed-article:16200071 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16200071 | pubmed:volume | 11 | lld:pubmed |
pubmed-article:16200071 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16200071 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16200071 | pubmed:pagination | 1082-7 | lld:pubmed |
pubmed-article:16200071 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:16200071 | pubmed:meshHeading | pubmed-meshheading:16200071... | lld:pubmed |
pubmed-article:16200071 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16200071 | pubmed:articleTitle | Dysregulation of bacterial proteolytic machinery by a new class of antibiotics. | lld:pubmed |
pubmed-article:16200071 | pubmed:affiliation | Department of Anti-infectives, Bayer HealthCare AG, Pharma Research, Aprather Weg 18a, D-42096 Wuppertal, Germany. heike.broetz-oesterhelt@bayerhealthcare.com | lld:pubmed |
pubmed-article:16200071 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16200071 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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