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rdf:type |
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lifeskim:mentions |
umls-concept:C0002146,
umls-concept:C0205147,
umls-concept:C0243077,
umls-concept:C0392747,
umls-concept:C1145667,
umls-concept:C1366876,
umls-concept:C1527178,
umls-concept:C1554963,
umls-concept:C1705938,
umls-concept:C1833235,
umls-concept:C2698650
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pubmed:issue |
16
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pubmed:dateCreated |
2010-8-3
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pubmed:abstractText |
We have optimized a novel series of potent p38 MAP kinase inhibitors based on an alpha-ketoamide scaffold through structure based design that due to their extended molecular architecture bind, in addition to the ATP site, to an allosteric pocket. In vitro ADME, in vivo PK and efficacy studies show these compounds to have drug-like characteristics and have resulted in the nomination of a development candidate which is currently in phase II clinical trials for the oral treatment of inflammatory conditions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1464-3405
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pubmed:author |
pubmed-author:BomanErikE,
pubmed-author:CeideSusana CondeSC,
pubmed-author:ChangChau-DungCD,
pubmed-author:DahlRussellR,
pubmed-author:DalesandroDavidD,
pubmed-author:DelaetNancy G JNG,
pubmed-author:ErbEricE,
pubmed-author:ErnstJustin TJT,
pubmed-author:GibbsAndrewA,
pubmed-author:KahlJeffreyJ,
pubmed-author:KesslerLindaL,
pubmed-author:KucharskiJeffJ,
pubmed-author:LarsonChristopher JCJ,
pubmed-author:LumChristopherC,
pubmed-author:LundströmJanJ,
pubmed-author:MillerStephenS,
pubmed-author:MontalbanAntonio GarridoAG,
pubmed-author:NakanishiHiroshiH,
pubmed-author:RobertsEdwardE,
pubmed-author:SaiahEddineE,
pubmed-author:SullivanRobertR,
pubmed-author:UrbanJanJ,
pubmed-author:ZhijunWangW
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pubmed:issnType |
Electronic
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pubmed:day |
15
|
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4819-24
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pubmed:meshHeading |
pubmed-meshheading:20663667-Administration, Oral,
pubmed-meshheading:20663667-Allosteric Site,
pubmed-meshheading:20663667-Amides,
pubmed-meshheading:20663667-Animals,
pubmed-meshheading:20663667-Anti-Inflammatory Agents, Non-Steroidal,
pubmed-meshheading:20663667-Binding Sites,
pubmed-meshheading:20663667-Cell Line,
pubmed-meshheading:20663667-Computer Simulation,
pubmed-meshheading:20663667-Humans,
pubmed-meshheading:20663667-Protein Binding,
pubmed-meshheading:20663667-Protein Kinase Inhibitors,
pubmed-meshheading:20663667-Rats,
pubmed-meshheading:20663667-Structure-Activity Relationship,
pubmed-meshheading:20663667-p38 Mitogen-Activated Protein Kinases
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pubmed:year |
2010
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pubmed:articleTitle |
Optimization of alpha-ketoamide based p38 inhibitors through modifications to the region that binds to the allosteric site.
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pubmed:affiliation |
Drug Discovery, Kémia, Inc., 5871 Oberlin Drive, Suite 100, San Diego, CA 92121, USA. catalaba@hotmail.com
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pubmed:publicationType |
Journal Article
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