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          <dc:description>Since DNA-induced conformational changes in estrogen receptors affected recruitment of transcriptional coregulatory proteins, we examined differential recruitment of novel proteins. One novel protein was isolated and identified by protein sequencing as TAF-I beta, a protein previously implicated in acetylation, transcription and phosphorylation. TAF-I beta not only associates with ER in a cell environment, but also inhibits acetylation of histones and ER alpha  in vitro and decreases ER alpha acetylation in vivo. Therefore, TAF-I beta may alter ER-mediated transcription by changing acetylation of ER or histones or both. Taken together, these data indicate that estrogen receptors associate with a variety of regulatory proteins and that interaction with these factors is affected both by an initial interaction with DNA and further modulated by receptor conformations induced by individual ERE sequences.</dc:description>
          <dc:contributor>Nardulli, Ann M.</dc:contributor>
          <dc:creator>Loven, Margaret Anne</dc:creator>
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Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
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          <dc:description>110 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2002.</dc:description>
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          <dc:identifier>(MiAaPQ)AAI3044163</dc:identifier>
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          <dc:subject>Biology, Molecular</dc:subject>
          <dc:title>Estrogen Receptors: Interaction With Estrogen Response Elements and Estrogen Receptor-Associated Proteins</dc:title>
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            <department>Molecular and Integrative Physiology</department>
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            <grantor>University of Illinois at Urbana-Champaign</grantor>
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