rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2008-3-31
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pubmed:abstractText |
The Hsp70 molecular chaperones are ATPases that play critical roles in the pathogenesis of many human diseases, including breast cancer. Hsp70 ATP hydrolysis is relatively weak but is stimulated by J domain-containing proteins. We identified pyrimidinone-peptoid hybrid molecules that inhibit cell proliferation with greater potency than previously described Hsp70 modulators. In many cases, anti-proliferative activity correlated with inhibition of J domain stimulation of Hsp70.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1464-3391
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pubmed:author |
pubmed-author:BrodskyJeffrey LJL,
pubmed-author:ChovatiyaRaj JRJ,
pubmed-author:DayBilly WBW,
pubmed-author:HurynDonna MDM,
pubmed-author:JamesonNora ENE,
pubmed-author:PipasJames MJM,
pubmed-author:TurnerDavid MDM,
pubmed-author:WernerStefanS,
pubmed-author:WipfPeterP,
pubmed-author:WrightChristine MCM,
pubmed-author:ZhuGuangyuG
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3291-301
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
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pubmed:year |
2008
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pubmed:articleTitle |
Pyrimidinone-peptoid hybrid molecules with distinct effects on molecular chaperone function and cell proliferation.
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pubmed:affiliation |
Department of Biological Sciences, University of Pittsburgh, 274 Crawford Hall, Pittsburgh, PA 15260, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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