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    <title>DSpace Community: Biochemistry</title>
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        <rdf:li resource="http://hdl.handle.net/2440/31045" />
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  <item rdf:about="http://hdl.handle.net/2440/53277">
    <title>The bHLH/Per-Arnt-Sim transcription factor SIM2 regulates muscle transcript myomesin2 via a novel, non-canonical E-box sequence</title>
    <link>http://hdl.handle.net/2440/53277</link>
    <description>Title: The bHLH/Per-Arnt-Sim transcription factor SIM2 regulates muscle transcript myomesin2 via a novel, non-canonical E-box sequence&lt;br/&gt;&lt;br/&gt;Author: Woods, Susan Lesley; Farrall, Alexandra Louise; Procko, Carl; Whitelaw, Murray Leslie&lt;br/&gt;&lt;br/&gt;Abstract: Despite a growing number of descriptive studies that show Single-minded 2 (Sim2) is not only essential for murine survival, but also upregulated in colon, prostate and pancreatic tumours, there is a lack of direct target genes identified for this basic helix–loop–helix/PAS transcription factor. We have performed a set of microarray experiments aimed at identifying genes that are differentially regulated by SIM2, and successfully verified that the Myomesin2 (Myom2) gene is SIM2-responsive. Although SIM2 has been reported to be a transcription repressor, we find that SIM2 induces transcription of Myom2 and activates the Myom2 promoter sequence when co-expressed with the heterodimeric partner protein, ARNT1, in human embryonic kidney cells. Truncation and mutation of the Myom2 promoter sequence, combined with chromatin immunoprecipitation studies in cells, has lead to the delineation of a non-canonical E-box sequence 5'-AACGTG-3' that is bound by SIM2/ARNT1 heterodimers. Interestingly, in immortalized human myoblasts knock down of Sim2 results in increased levels of Myom2 RNA, suggesting that SIM2 is acting as a repressor in these cells and so its activity is likely to be highly context dependent. This is the first report of a direct SIM2/ARNT1 target gene with accompanying analysis of a functional response element.</description>
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  <item rdf:about="http://hdl.handle.net/2440/53201">
    <title>Robert Henry Symons 1934-2006</title>
    <link>http://hdl.handle.net/2440/53201</link>
    <description>Title: Robert Henry Symons 1934-2006&lt;br/&gt;&lt;br/&gt;Author: Rogers, George Ernest; Elliott, William Herdman</description>
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  <item rdf:about="http://hdl.handle.net/2440/31045">
    <title>In vivo actions of IGF analogues with poor affinities for IGFPs: Metabolic and growth effects in pigs of different ages and GH responsiveness</title>
    <link>http://hdl.handle.net/2440/31045</link>
    <description>Title: In vivo actions of IGF analogues with poor affinities for IGFPs: Metabolic and growth effects in pigs of different ages and GH responsiveness&lt;br/&gt;&lt;br/&gt;Author: Walton, P. E.; Dunshea, F. R.; Ballard, Francis John</description>
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  <item rdf:about="http://hdl.handle.net/2440/31044">
    <title>The 25-Hydroxyvitamin D 24-Hydroxylase</title>
    <link>http://hdl.handle.net/2440/31044</link>
    <description>Title: The 25-Hydroxyvitamin D 24-Hydroxylase&lt;br/&gt;&lt;br/&gt;Author: Omdahl, John L.; May, B.&lt;br/&gt;&lt;br/&gt;Abstract: This chapter reviews the role of 25-hydroxyvitamin D 24-hydroxylase in vitamin D metabolism. The 24-hydroxylase enzyme is a widely distributed component of the vitamin D pathway. It is regulated by a spectrum of hormones and functions to synthesise 24-hydroxylated metabolites, with preferential action in promoting bone mineralization and possibly other undisclosed cellular functions that may become evident through the use of gene knockout models. It also plays a central role in directing the metabolic turnover of several 25-hydroxylated vitamin D metabolites.</description>
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