










<?xml version="1.0" encoding="utf-8"?>
<?xml-stylesheet type="text/css" href="http://52.214.119.220/wiki/skins/common/feed.css?97"?>
<feed xmlns="http://www.w3.org/2005/Atom" xml:lang="en">
		<id>http://52.214.119.220/wiki/index.php?action=history&amp;feed=atom&amp;title=Sandbox_reserved_1753</id>
		<title>Sandbox reserved 1753 - Revision history</title>
		<link rel="self" type="application/atom+xml" href="http://52.214.119.220/wiki/index.php?action=history&amp;feed=atom&amp;title=Sandbox_reserved_1753"/>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;action=history"/>
		<updated>2026-04-11T16:58:14Z</updated>
		<subtitle>Revision history for this page on the wiki</subtitle>
		<generator>MediaWiki 1.11.2</generator>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644268&amp;oldid=prev</id>
		<title>Casimiro Soliz at 20:31, 18 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644268&amp;oldid=prev"/>
				<updated>2022-10-18T20:31:44Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 20:31, 18 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 9:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 9:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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 structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The&amp;lt;scene name='92/927197/Active_site/7'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped the damaged bases out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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 structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The&amp;lt;scene name='92/927197/Active_site/7'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped the damaged bases out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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: #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: #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;/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;/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;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644267&amp;oldid=prev</id>
		<title>Casimiro Soliz at 20:30, 18 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644267&amp;oldid=prev"/>
				<updated>2022-10-18T20:30:55Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 20:30, 18 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 16:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 16:&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;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: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;↑ Schormann N, Ricciardi R, Chattopadhyay D. Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes. Protein Sci. 2014 Dec;23(12):1667-85. doi: 10.1002/pro.2554. Epub 2014 Oct 25. PMID:25252105 doi:http://dx.doi.org/10.1002/pro.2554&lt;/div&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: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;↑ Parikh SS, Mol CD, Slupphaug G, Bharati S, Krokan HE, Tainer JA. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 1998 Sep 1;17(17):5214-26. PMID:9724657 doi:10.1093/emboj/17.17.5214&lt;/div&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: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;↑ Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature. 1996 Nov 7;384(6604):87-92. PMID:8900285 doi:http://dx.doi.org/10.1038/384087a0&lt;/div&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644266&amp;oldid=prev</id>
		<title>Casimiro Soliz at 20:30, 18 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644266&amp;oldid=prev"/>
				<updated>2022-10-18T20:30:39Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 20:30, 18 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 16:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 16:&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;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;__TOC__&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;&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: #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;&amp;lt;/StructureSection&amp;gt;&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;↑ Schormann N, Ricciardi R, Chattopadhyay D. Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes. Protein Sci. 2014 Dec;23(12)&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;1667-85. doi&lt;/ins&gt;: &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;10.1002/pro.2554. Epub 2014 Oct 25. PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;25252105 doi&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;//dx.doi.org/10.1002/pro.2554&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: #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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Human]]&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;↑ Parikh SS&lt;/ins&gt;, Mol &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;CD&lt;/ins&gt;, Slupphaug G, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Bharati S, Krokan HE, Tainer JA. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO &lt;/ins&gt;J&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. 1998 Sep 1;17(17)&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5214-26. PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;9724657 doi&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;10.1093/emboj/17.17.5214&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: #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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Large Structures]]&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;↑ Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature. 1996 Nov 7;384(6604)&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;87&lt;/ins&gt;-&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;92. PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;8900285 doi:http://dx.doi.org/10.1038/384087a0&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: #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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Uridine nucleosidase]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Arvai, A S]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Kavli, B]]&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;/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;[[Category: Krokan&lt;/del&gt;, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;H E]]&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;/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;[[Category: &lt;/del&gt;Mol, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;C D]]&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;/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;[[Category: &lt;/del&gt;Slupphaug&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;G&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]]&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;/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;[[Category: Tainer&lt;/del&gt;, J &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;A]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Dna]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Dna base excision repair]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Dna glycosylase]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Hydrolase&lt;/del&gt;-&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;dna complex]]&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;/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;[[Category&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Uracil]]&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;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644261&amp;oldid=prev</id>
		<title>Casimiro Soliz at 20:16, 18 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644261&amp;oldid=prev"/>
				<updated>2022-10-18T20:16:47Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 20:16, 18 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The &amp;lt;scene name='92/927197/Active_site/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;1&lt;/del&gt;'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped the damaged bases out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The&amp;lt;scene name='92/927197/Active_site/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;7&lt;/ins&gt;'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped the damaged bases out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644045&amp;oldid=prev</id>
		<title>Casimiro Soliz at 02:43, 11 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644045&amp;oldid=prev"/>
				<updated>2022-10-11T02:43:19Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 02:43, 11 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix.ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the damaged bases &lt;/ins&gt;out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644044&amp;oldid=prev</id>
		<title>Casimiro Soliz at 02:39, 11 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644044&amp;oldid=prev"/>
				<updated>2022-10-11T02:39:54Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 02:39, 11 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix&lt;/del&gt;. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix.ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. The dsDNA in the 3D model contains a U G base pair mismatch. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix&lt;/ins&gt;. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix.ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644043&amp;oldid=prev</id>
		<title>Casimiro Soliz at 02:38, 11 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644043&amp;oldid=prev"/>
				<updated>2022-10-11T02:38:06Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 02:38, 11 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.The dsDNA has a 10bp that contains a U G base pair mismatch&lt;/del&gt;. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix.ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. The dsDNA in the 3D model contains a U G base pair mismatch&lt;/ins&gt;. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix.ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644042&amp;oldid=prev</id>
		<title>Casimiro Soliz at 02:35, 11 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644042&amp;oldid=prev"/>
				<updated>2022-10-11T02:35:50Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 02:35, 11 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it.The dsDNA has a 10bp that contains a U G base pair mismatch. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it.The dsDNA has a 10bp that contains a U G base pair mismatch. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.ASN 204 and HIS 268 are responsible for catalyzing the cleavage of the glycosidic bond. TYR 147, PHE 158, and ASN 204 all aid in Uracil excision and replacement with Thymine&lt;/ins&gt;. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644039&amp;oldid=prev</id>
		<title>Casimiro Soliz at 20:51, 10 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644039&amp;oldid=prev"/>
				<updated>2022-10-10T20:51:21Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 20:51, 10 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 2:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 2:&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;StructureSection load='4skn' size='340' side='right'caption='[[4skn]], [[Resolution|resolution]] 2.90&amp;amp;Aring;' scene=''&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='4skn' size='340' side='right'caption='[[4skn]], [[Resolution|resolution]] 2.90&amp;amp;Aring;' scene=''&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;Glycosylase is an enzyme. Its main function is in Base Excision Repair(BER). Base Excision Repair is a DNA repair mechanism that fixes the most common type of DNA damage. BER removes and repairs damaged bases usually these are single-stranded DNA breaks. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;BER &lt;/del&gt;corrects DNA damage that results from small leisures that do not disrupt the double helix&amp;lt;ref&amp;gt;PMID:25252105&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;Glycosylase is an enzyme. Its main function is in Base Excision Repair(BER). Base Excision Repair is a DNA repair mechanism that fixes the most common type of DNA damage&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. BER corrects DNA damage that occurs from oxidation and methylation&lt;/ins&gt;. BER removes and repairs damaged bases usually these are single-stranded DNA breaks. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;It also &lt;/ins&gt;corrects DNA damage that results from small leisures that do not disrupt the double helix&amp;lt;ref&amp;gt;PMID:25252105&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;/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;== 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 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. The dsDNA has a 10bp that contains a U G base pair mismatch&lt;/del&gt;. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.The dsDNA has a 10bp that contains a U G base pair mismatch&lt;/ins&gt;. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/5'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644014&amp;oldid=prev</id>
		<title>Casimiro Soliz at 18:17, 10 October 2022</title>
		<link rel="alternate" type="text/html" href="http://52.214.119.220/wiki/index.php?title=Sandbox_reserved_1753&amp;diff=3644014&amp;oldid=prev"/>
				<updated>2022-10-10T18:17:11Z</updated>
		
		<summary type="html">&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&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 18:17, 10 October 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&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;== Uracil-DNA Glycosylase ==&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;== Uracil-DNA Glycosylase ==&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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The dsDNA has a 10bp that contains a U G base pair mismatch. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;2&lt;/del&gt;'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;The structure of Glycosylase has a couple of different forms in terms of its general structure there is Adenine and Uracil Glycosylase. DNA Uracil-Glycosylase specifically looks for any Uracil in the double-stranded DNA. It looks for Uracil in dsDNA because uracil is only found in RNA. So if a Uracil is found in dsDNA then that means one of the strands has been damaged and needs repair. When Uracil-DNA Glycosylase finds the &amp;lt;scene name='92/927197/Uracil/4'&amp;gt;Uracil&amp;lt;/scene&amp;gt; site it binds to it. The &amp;lt;scene name='92/927197/Active_site/1'&amp;gt;Active Site&amp;lt;/scene&amp;gt; of Uracil Glycosylase; D145, Y147, F158, N204, H268, L272 is what binds to the double-stranded DNA with the damaged lesion. Then a nucleotide-flipping mechanism flips the site of repair out of the double helix. The dsDNA has a 10bp that contains a U G base pair mismatch. This is what allows the &amp;lt;scene name='92/927197/Uracil_glycolysis_interaction/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5&lt;/ins&gt;'&amp;gt;Uracil_Glycosylase interaction&amp;lt;/scene&amp;gt; and flipping of the damaged site out of the double helix. When flipped out of the helix &amp;lt;scene name='92/927197/Arg_side_chain/1'&amp;gt;ARG 272 side chain&amp;lt;/scene&amp;gt; takes its place in the minor groove since AP sites can be mutagenic&amp;lt;ref&amp;gt;PMID:8900285&amp;lt;/ref&amp;gt;. The Uracil is then replaced with a Thymine. This is because Uracil and Thymine have identical base pairing properties. Thymine happens to have greater resistance to photochemical mutations which is why we see it in dsDNA and not Uracil. &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;/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;/table&gt;</summary>
		<author><name>Casimiro Soliz</name></author>	</entry>

	</feed>