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		<title>Aromatase - Revision history</title>
		<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;action=history</link>
		<description>Revision history for this page on the wiki</description>
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			<title>Alexander Berchansky at 14:35, 4 November 2019</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=3104754&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 14:35, 4 November 2019&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. &amp;lt;ref name=&amp;quot;structure&amp;quot;/&amp;gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. &amp;lt;ref name=&amp;quot;structure&amp;quot;/&amp;gt;]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{Clear}}&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structure==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structure==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.&amp;lt;ref name=&amp;quot;structure&amp;quot; /&amp;gt; One important feature of CYPs is the iron-containing &amp;lt;scene name='Sandbox_Reserved_382/Porphyrin/1'&amp;gt;porphyrin&amp;lt;/scene&amp;gt; group at the enzyme active site.&amp;lt;ref&amp;gt; PMID: 16395678 &amp;lt;/ref&amp;gt; The &amp;lt;scene name='Sandbox_Reserved_382/Heme_iron/3'&amp;gt;heme iron&amp;lt;/scene&amp;gt; is within the porphyrin and is considered the reaction center of the enzyme. The &amp;lt;scene name='Sandbox_Reserved_382/Ligand/3'&amp;gt;ligand&amp;lt;/scene&amp;gt; docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.&amp;lt;ref name=&amp;quot;structure&amp;quot; /&amp;gt; An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. &amp;lt;ref name=&amp;quot;structure&amp;quot; /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.&amp;lt;ref name=&amp;quot;structure&amp;quot; /&amp;gt; One important feature of CYPs is the iron-containing &amp;lt;scene name='Sandbox_Reserved_382/Porphyrin/1'&amp;gt;porphyrin&amp;lt;/scene&amp;gt; group at the enzyme active site.&amp;lt;ref&amp;gt; PMID: 16395678 &amp;lt;/ref&amp;gt; The &amp;lt;scene name='Sandbox_Reserved_382/Heme_iron/3'&amp;gt;heme iron&amp;lt;/scene&amp;gt; is within the porphyrin and is considered the reaction center of the enzyme. The &amp;lt;scene name='Sandbox_Reserved_382/Ligand/3'&amp;gt;ligand&amp;lt;/scene&amp;gt; docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.&amp;lt;ref name=&amp;quot;structure&amp;quot; /&amp;gt; An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. &amp;lt;ref name=&amp;quot;structure&amp;quot; /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Mon, 04 Nov 2019 14:35:41 GMT</pubDate>			<dc:creator>Alexander Berchansky</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
		<item>
			<title>Joel L. Sussman at 17:52, 14 January 2017</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=2705510&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 17:52, 14 January 2017&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;StructureSection load='3EQM' size='350' side='right' scene='' caption=''Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] '&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;StructureSection load='3EQM' size='350' side='right' scene='' caption=''Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] '&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] [[Oxidoreductase|1.14.14.1]]) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, [[NADPH-Cytochrome_P450_Reductase|NADPH-cytochrome P450 reductase]]. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] [[Oxidoreductase|1.14.14.1]]) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, [[NADPH-Cytochrome_P450_Reductase|NADPH-cytochrome P450 reductase]]. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Sat, 14 Jan 2017 17:52:21 GMT</pubDate>			<dc:creator>Joel L. Sussman</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
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			<title>Joel L. Sussman at 17:51, 14 January 2017</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=2705509&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 17:51, 14 January 2017&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Structure &lt;/del&gt;load='3EQM' size='&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;400&lt;/del&gt;' &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;frame&lt;/del&gt;='&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;true&lt;/del&gt;' &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;align&lt;/del&gt;='&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;right&lt;/del&gt;' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;scene='Insert optional scene name here' /&lt;/del&gt;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;StructureSection &lt;/ins&gt;load='3EQM' size='&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;350&lt;/ins&gt;' &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;side&lt;/ins&gt;='&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;right&lt;/ins&gt;' &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;scene&lt;/ins&gt;='' caption=&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'&lt;/ins&gt;'Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] '&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] [[Oxidoreductase|1.14.14.1]]) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, [[NADPH-Cytochrome_P450_Reductase|NADPH-cytochrome P450 reductase]]. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] [[Oxidoreductase|1.14.14.1]]) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, [[NADPH-Cytochrome_P450_Reductase|NADPH-cytochrome P450 reductase]]. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 22:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 23:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*'''Aromatase Excess Syndrome'''&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*'''Aromatase Excess Syndrome'''&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.&amp;lt;ref&amp;gt; PMID: 9543166 &amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.&amp;lt;ref&amp;gt; PMID: 9543166 &amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/StructureSection&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==3D structures of aromatase==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==3D structures of aromatase==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Sat, 14 Jan 2017 17:51:55 GMT</pubDate>			<dc:creator>Joel L. Sussman</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
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			<title>Michal Harel at 08:03, 3 December 2013</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1870265&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 08:03, 3 December 2013&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 22:&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*'''Aromatase Excess Syndrome'''&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*'''Aromatase Excess Syndrome'''&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.&amp;lt;ref&amp;gt; PMID: 9543166 &amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.&amp;lt;ref&amp;gt; PMID: 9543166 &amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==3D structures of aromatase==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;See human P450 19 family in [[Cytochrome P450]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== References ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== References ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 03 Dec 2013 08:03:50 GMT</pubDate>			<dc:creator>Michal Harel</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
		<item>
			<title>David Canner at 03:54, 23 October 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1594311&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 03:54, 23 October 2012&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] [[Oxidoreductase|1.14.14.1]]) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] [[Oxidoreductase|1.14.14.1]]) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[NADPH-Cytochrome_P450_Reductase|&lt;/ins&gt;NADPH-cytochrome P450 reductase&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]]&lt;/ins&gt;. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 23 Oct 2012 03:54:14 GMT</pubDate>			<dc:creator>David Canner</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
		<item>
			<title>David Canner at 03:53, 23 October 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1594309&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 03:53, 23 October 2012&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] 1.14.14.1) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] ([[EC]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Oxidoreductase|&lt;/ins&gt;1.14.14.1&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]]&lt;/ins&gt;) belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 23 Oct 2012 03:53:00 GMT</pubDate>			<dc:creator>David Canner</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
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			<title>David Canner at 03:52, 23 October 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1594308&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 03:52, 23 October 2012&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Aromatase]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;([[EC]] 1.14.14.1) &lt;/ins&gt;belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 23 Oct 2012 03:52:32 GMT</pubDate>			<dc:creator>David Canner</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
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			<title>David Canner at 03:51, 23 October 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1594306&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 12:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Aromatase Inhibitors ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Aromatase Inhibitors ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.&amp;lt;ref&amp;gt; &amp;quot;Aromatase Inhibitors&amp;quot; [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] &amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.&amp;lt;ref&amp;gt; &amp;quot;Aromatase Inhibitors&amp;quot; [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] &amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;There are three aromatase inhibitors that are often used in the treatment of breast cancer:&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;There are three aromatase inhibitors that are often used in the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Pharmaceutical Drugs|&lt;/ins&gt;treatment&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]] &lt;/ins&gt;of breast &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[&lt;/ins&gt;cancer&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]]&lt;/ins&gt;:&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*Arimidex (Anastrozole)&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*Arimidex (Anastrozole)&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*Aromasin (Exemestane)&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;*Aromasin (Exemestane)&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 23 Oct 2012 03:51:07 GMT</pubDate>			<dc:creator>David Canner</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
		<item>
			<title>David Canner at 03:50, 23 October 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1594305&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 03:50, 23 October 2012&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;== Introduction ==&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[&lt;/ins&gt;Aromatase&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]] &lt;/ins&gt;belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'''&lt;/del&gt;Aromatase&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;''' &lt;/del&gt;belongs to the [[Cytochrome P450]] family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 23 Oct 2012 03:50:10 GMT</pubDate>			<dc:creator>David Canner</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
		<item>
			<title>Michal Harel at 07:48, 4 January 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=Aromatase&amp;diff=1340086&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 07:48, 4 January 2012&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione [[3eqm]] ' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Introduction ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Introduction ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;'''Aromatase''' belongs to the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;cytochrome &lt;/del&gt;P450 family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;'''Aromatase''' belongs to the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Cytochrome &lt;/ins&gt;P450&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]] &lt;/ins&gt;family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.&amp;lt;ref&amp;gt; PMID:21125383 &amp;lt;/ref&amp;gt; In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.&amp;lt;ref&amp;gt;  PMID: 11427156 &amp;lt;/ref&amp;gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring&amp;lt;ref name=&amp;quot;structure&amp;quot;&amp;gt; Ghosh, D., Griswold, J., Erman, M., Pangborn, W. &amp;quot; X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site&amp;quot; ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]&amp;lt;/ref&amp;gt;. Aromatase converts androstenedione to estrogen and testosterone to estradiol.&amp;lt;ref name=&amp;quot;products&amp;quot; /&amp;gt; Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 04 Jan 2012 07:48:37 GMT</pubDate>			<dc:creator>Michal Harel</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:Aromatase</comments>		</item>
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