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  <title><![CDATA[(11-0215) Prof. Kevin Bucholtz, Mercer University]]></title>
  <body><![CDATA[<p> Prof. Kevin Bucholtz, Mercer University
</p>
<p>PPAR Î´ and 3Î²-HSD1: Two Stories in Ligand Selectivity
</p>
<p>Organic Chemistry Seminar Series
</p>
<p>Peroxisome Proliferator Activated Receptors (PPAR) are nuclear hormone receptors that are of great interest because of their implications in the metabolic syndrome.  The isotype PPAR Î´, a ligand activated transcription factor, is of significant interest since little is known about its role in biological phenomena.  The human type isoform of 3Î²-hydroxysteroid dehydrogenase/ isomerase (3Î²-HSD1) is a key enzyme in the biosynthesis of active steroid hormones. Human 3Î²-HSD1 is a critical enzyme in the conversion of dehydroepiandrosterone (DHEA) to estradiol in breast tumors.   Both of these biomacromolecules (PPAR Î´ and 3Î²-HSD1)  have been the focus of rationally designed small molecules to selectively interact with each target and used to determine the characteristics of the interaction.  The biological implications of these small molecule interactions are currently being investigated.
</p>
<p>for more information contact <a href="mailto:wendy.kelly@chemistry.gatech.edu">Prof. Wendy Kelly</a> (404-385-1154).</p>]]></body>
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PPAR Î´ and 3Î²-HSD1: Two Stories in Ligand Selectivity

Organic Chemistry Seminar Series]]></value>
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      <value><![CDATA[<strong>Shirley Tomes</strong><br />Chemistry &amp; Biochemistry<br /><a href="http://www.gatech.edu/contact/index.html?id=st81">Contact Shirley Tomes</a><br /><strong>404-894-0591</strong>]]></value>
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