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		<title>6t7t - Revision history</title>
		<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;action=history</link>
		<description>Revision history for this page on the wiki</description>
		<language>en</language>
		<generator>MediaWiki 1.11.2</generator>
		<lastBuildDate>Wed, 08 Apr 2026 05:06:53 GMT</lastBuildDate>
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			<title>OCA at 06:23, 11 April 2020</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3190497&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;
			&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 06:23, 11 April 2020&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&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;SX load='6t7t' size='340' side='right' viewer='molstar' caption='[[6t7t]], [[Resolution|resolution]] 3.10&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;SX load='6t7t' size='340' side='right' viewer='molstar' caption='[[6t7t]], [[Resolution|resolution]] 3.10&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;== Structural highlights ==&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;== Structural highlights ==&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;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] is a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) Saccharomyces cerevisiae (strain atcc 204508 / s288c)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;oca&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;weizmann.ac.il/oca-docs&lt;/del&gt;/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&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;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] is a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) Saccharomyces cerevisiae (strain atcc 204508 / s288c)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteopedia&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org&lt;/ins&gt;/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&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;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;oca&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;weizmann.ac.il/oca-docs&lt;/del&gt;/fgij/fg.htm?mol=6t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7t OCA], [http://pdbe.org/6t7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7t RCSB], [http://www.ebi.ac.uk/pdbsum/6t7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7t ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&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;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteopedia&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org&lt;/ins&gt;/fgij/fg.htm?mol=6t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7t OCA], [http://pdbe.org/6t7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7t RCSB], [http://www.ebi.ac.uk/pdbsum/6t7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7t ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&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;&amp;lt;/table&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;/table&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, 11 Apr 2020 06:23:59 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
		<item>
			<title>OCA at 00:58, 7 March 2020</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3170613&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;
			&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 00:58, 7 March 2020&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;/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;==Structure of yeast 80S ribosome stalled on poly(A) tract.==&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 of yeast 80S ribosome stalled on poly(A) tract.==&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;lt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;StructureSection &lt;/del&gt;load='6t7t' size='340' side='right'caption='[[6t7t]], [[Resolution|resolution]] 3.10&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: #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;SX &lt;/ins&gt;load='6t7t' size='340' side='right&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;' viewer='molstar&lt;/ins&gt;' caption='[[6t7t]], [[Resolution|resolution]] 3.10&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;== Structural highlights ==&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;== Structural highlights ==&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;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] is a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) Saccharomyces cerevisiae (strain atcc 204508 / s288c)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&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;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] is a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) Saccharomyces cerevisiae (strain atcc 204508 / s288c)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&amp;gt;&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 23:&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;&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: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;__TOC__&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;__TOC__&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;lt;/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;StructureSection&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;SX&lt;/ins&gt;&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;[[Category: Atcc 18824]]&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;[[Category: Atcc 18824]]&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;[[Category: Large Structures]]&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;[[Category: Large Structures]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Sat, 07 Mar 2020 00:58:21 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
		<item>
			<title>OCA at 07:45, 19 February 2020</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3158973&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;
			&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 07:45, 19 February 2020&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&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='6t7t' size='340' side='right'caption='[[6t7t]], [[Resolution|resolution]] 3.10&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='6t7t' size='340' side='right'caption='[[6t7t]], [[Resolution|resolution]] 3.10&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;== Structural highlights ==&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;== Structural highlights ==&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;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] is a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Saccharomyces_cerevisiae &lt;/del&gt;Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&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;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] is a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) &lt;/ins&gt;Saccharomyces cerevisiae &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(strain atcc 204508 / s288c)&lt;/ins&gt;]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&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;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7t OCA], [http://pdbe.org/6t7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7t RCSB], [http://www.ebi.ac.uk/pdbsum/6t7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7t ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&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;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7t OCA], [http://pdbe.org/6t7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7t RCSB], [http://www.ebi.ac.uk/pdbsum/6t7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7t ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&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;&amp;lt;/table&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;/table&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: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;GBLP_YEAST GBLP_YEAST&lt;/del&gt;]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Located at &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;head &lt;/del&gt;of the 40S ribosomal subunit in &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the vicinity of the mRNA exit channel, it serves as a scaffold &lt;/del&gt;protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;that can recruit other proteins to &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome&lt;/del&gt;. Involved in &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the negative regulation of translation of a specific subset &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteins&lt;/del&gt;.&amp;lt;ref&amp;gt;PMID:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;15340087&lt;/del&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RS31_YEAST RS31_YEAST&lt;/del&gt;]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;40S &lt;/del&gt;ribosomal protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;S31&lt;/del&gt;: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&amp;lt;ref&amp;gt;PMID&lt;/del&gt;:22096102&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/ref&amp;gt;  [[http://www&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;uniprot.org/uniprot/RS19A_YEAST RS19A_YEAST]] Required &lt;/del&gt;for &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proper maturation &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the small &lt;/del&gt;(&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;40S&lt;/del&gt;) &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA&lt;/del&gt;.&amp;lt;ref&amp;gt;PMID:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16159874&lt;/del&gt;&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;17726054&lt;/del&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL37A_YEAST RL37A_YEAST]] Binds to the 23S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RL40A_YEAST RL40A_YEAST&lt;/del&gt;]] Ubiquitin&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;: Exists &lt;/del&gt;either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;60S &lt;/del&gt;ribosomal protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;L40&lt;/del&gt;-&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;A&lt;/del&gt;: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(PubMed&lt;/del&gt;:22096102&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;)&lt;/del&gt;. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;eL40 is essential &lt;/del&gt;for &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;translation &lt;/del&gt;of a &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subset &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;cellular transcripts, including stress response transcripts, such as DDR2 (PubMed:23169626)&lt;/del&gt;.&amp;lt;ref&amp;gt;PMID:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;23169626&lt;/del&gt;&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;22096102&lt;/del&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS18A_YEAST RS18A_YEAST]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RS7A_YEAST RS7A_YEAST&lt;/del&gt;]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Involved in nucleolar processing &lt;/del&gt;of pre-&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;18S &lt;/del&gt;ribosomal &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RNA &lt;/del&gt;and &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome &lt;/del&gt;assembly.&amp;lt;ref&amp;gt;PMID:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;15590835&lt;/del&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RS27A_YEAST RS27A_YEAST&lt;/del&gt;]] Ubiquitin &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;exists &lt;/del&gt;either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31 &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;is a component of the 40S subunit of the ribosome (By similarity). [[http&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;//www.uniprot.org/uniprot/RL4A_YEAST RL4A_YEAST]] Participates in the regulation of the accumulation of its own mRNA.&amp;lt;ref&amp;gt;PMID:2065661&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL6B_YEAST RL6B_YEAST]] &lt;/del&gt;Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS9A_YEAST RS9A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS14A_YEAST RS14A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL5_YEAST RL5_YEAST]] Binds 5S RNA and is required for 60S subunit assembly. [[http://www.uniprot.org/uniprot/RL25_YEAST RL25_YEAST]] This protein binds to a specific region on the 26S rRNA. [[http://www.uniprot.org/uniprot/RL11A_YEAST RL11A_YEAST]] Binds to 5S ribosomal RNA. [[http://www.uniprot.org/uniprot/RS21A_YEAST RS21A_YEAST]] Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.&amp;lt;ref&amp;gt;PMID:14627813&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS6A_YEAST RS6A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS15_YEAST RS15_YEAST]] Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm.&amp;lt;ref&amp;gt;PMID:15167894&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS2_YEAST RS2_YEAST]] Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&lt;/del&gt;&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;[[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL37A_YEAST RL37A_YEAST&lt;/ins&gt;]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Binds to &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;23S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RS2_YEAST RS2_YEAST]] Important in the assembly and function &lt;/ins&gt;of the 40S ribosomal subunit&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. Mutations &lt;/ins&gt;in &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;this &lt;/ins&gt;protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;affects &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;control of translational fidelity&lt;/ins&gt;. Involved in &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;nucleolar processing &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;pre-18S ribosomal RNA and ribosome assembly&lt;/ins&gt;.&amp;lt;ref&amp;gt;PMID:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;15590835&lt;/ins&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL40A_YEAST RL40A_YEAST&lt;/ins&gt;]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;60S &lt;/ins&gt;ribosomal protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;L40-A&lt;/ins&gt;: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(PubMed&lt;/ins&gt;:22096102&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;)&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;eL40 is essential &lt;/ins&gt;for &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;translation &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;a subset of cellular transcripts, including stress response transcripts, such as DDR2 &lt;/ins&gt;(&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;PubMed:23169626&lt;/ins&gt;).&amp;lt;ref&amp;gt;PMID:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;23169626&lt;/ins&gt;&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;22096102&lt;/ins&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RS27A_YEAST RS27A_YEAST&lt;/ins&gt;]] Ubiquitin &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;exists &lt;/ins&gt;either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;40S &lt;/ins&gt;ribosomal protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;S31 is a component of the 40S subunit of the ribosome (By similarity). [[http://www.uniprot.org/uniprot/GBLP_YEAST GBLP_YEAST]] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.&amp;lt;ref&amp;gt;PMID:15340087&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS6A_YEAST RS6A_YEAST]] Involved in nucleolar processing of pre&lt;/ins&gt;-&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4A_YEAST RL4A_YEAST]] Participates in the regulation of the accumulation of its own mRNA.&amp;lt;ref&amp;gt;PMID:2065661&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL6B_YEAST RL6B_YEAST]] &lt;/ins&gt;Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&amp;lt;ref&amp;gt;PMID&lt;/ins&gt;:22096102&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/ref&amp;gt;  [[http://www&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;uniprot.org/uniprot/RS7A_YEAST RS7A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS14B_YEAST RS14B_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS21A_YEAST RS21A_YEAST]] Required &lt;/ins&gt;for &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the processing &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the 20S rRNA-precursor to mature 18S rRNA in &lt;/ins&gt;a &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;late step &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability&lt;/ins&gt;.&amp;lt;ref&amp;gt;PMID:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;14627813&lt;/ins&gt;&amp;lt;/ref&amp;gt; &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; [[http://www.uniprot.org/uniprot/RL5_YEAST RL5_YEAST]] Binds 5S RNA and is required for 60S subunit assembly. [[http://www.uniprot.org/uniprot/RS9A_YEAST RS9A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&lt;/ins&gt;&amp;lt;ref&amp;gt;PMID:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;15590835&lt;/ins&gt;&amp;lt;/ref&amp;gt;  &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/RL25_YEAST RL25_YEAST]] This protein binds to a specific region on the 26S rRNA. &lt;/ins&gt;[[http://www.uniprot.org/uniprot/RS18A_YEAST RS18A_YEAST]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL11B_YEAST RL11B_YEAST&lt;/ins&gt;]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Binds to 5S ribosomal RNA. [[http://www.uniprot.org/uniprot/RS19A_YEAST RS19A_YEAST]] Required for proper maturation &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the small (40S) ribosomal subunit. Binds to 40s &lt;/ins&gt;pre-ribosomal &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;particles, probably required after association of NOC4 but before association of ENP1, TSR1 &lt;/ins&gt;and &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RIO2 with 20/21S pre-rRNA.&amp;lt;ref&amp;gt;PMID:16159874&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:17726054&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS15_YEAST RS15_YEAST]] Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the &lt;/ins&gt;assembly &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;of pre-40S particles within the nucleus and controls their export to the cytoplasm&lt;/ins&gt;.&amp;lt;ref&amp;gt;PMID:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;15167894&lt;/ins&gt;&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RS31_YEAST RS31_YEAST&lt;/ins&gt;]] Ubiquitin&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;: Exists &lt;/ins&gt;either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&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;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&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;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&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: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&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;== Publication Abstract from PubMed ==&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 24:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 24:&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;__TOC__&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;__TOC__&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;/StructureSection&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&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;[[Category: Atcc 18824]]&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;[[Category: Large Structures]]&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;[[Category: Large Structures]]&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;[[Category: Saccharomyces cerevisiae]]&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: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Becker, R]]&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;[[Category: Becker, R]]&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;[[Category: Beckmann, R]]&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;[[Category: Beckmann, R]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 19 Feb 2020 07:45:31 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
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			<title>OCA at 12:17, 1 January 2020</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3138636&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 12:17, 1 January 2020&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;== 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;[[http://www.uniprot.org/uniprot/GBLP_YEAST GBLP_YEAST]] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.&amp;lt;ref&amp;gt;PMID:15340087&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS31_YEAST RS31_YEAST]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS19A_YEAST RS19A_YEAST]] Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.&amp;lt;ref&amp;gt;PMID:16159874&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:17726054&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL37A_YEAST RL37A_YEAST]] Binds to the 23S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RL40A_YEAST RL40A_YEAST]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  60S ribosomal protein L40-A: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eL40 is essential for translation of a subset of cellular transcripts, including stress response transcripts, such as DDR2 (PubMed:23169626).&amp;lt;ref&amp;gt;PMID:23169626&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS18A_YEAST RS18A_YEAST]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/RS7A_YEAST RS7A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS27A_YEAST RS27A_YEAST]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31 is a component of the 40S subunit of the ribosome (By similarity). [[http://www.uniprot.org/uniprot/RL4A_YEAST RL4A_YEAST]] Participates in the regulation of the accumulation of its own mRNA.&amp;lt;ref&amp;gt;PMID:2065661&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL6B_YEAST RL6B_YEAST]] Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS9A_YEAST RS9A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS14A_YEAST RS14A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL5_YEAST RL5_YEAST]] Binds 5S RNA and is required for 60S subunit assembly. [[http://www.uniprot.org/uniprot/RL25_YEAST RL25_YEAST]] This protein binds to a specific region on the 26S rRNA. [[http://www.uniprot.org/uniprot/RL11A_YEAST RL11A_YEAST]] Binds to 5S ribosomal RNA. [[http://www.uniprot.org/uniprot/RS21A_YEAST RS21A_YEAST]] Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.&amp;lt;ref&amp;gt;PMID:14627813&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS6A_YEAST RS6A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS15_YEAST RS15_YEAST]] Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm.&amp;lt;ref&amp;gt;PMID:15167894&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS2_YEAST RS2_YEAST]] Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&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;[[http://www.uniprot.org/uniprot/GBLP_YEAST GBLP_YEAST]] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.&amp;lt;ref&amp;gt;PMID:15340087&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS31_YEAST RS31_YEAST]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS19A_YEAST RS19A_YEAST]] Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.&amp;lt;ref&amp;gt;PMID:16159874&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:17726054&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL37A_YEAST RL37A_YEAST]] Binds to the 23S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RL40A_YEAST RL40A_YEAST]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  60S ribosomal protein L40-A: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eL40 is essential for translation of a subset of cellular transcripts, including stress response transcripts, such as DDR2 (PubMed:23169626).&amp;lt;ref&amp;gt;PMID:23169626&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS18A_YEAST RS18A_YEAST]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/RS7A_YEAST RS7A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS27A_YEAST RS27A_YEAST]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31 is a component of the 40S subunit of the ribosome (By similarity). [[http://www.uniprot.org/uniprot/RL4A_YEAST RL4A_YEAST]] Participates in the regulation of the accumulation of its own mRNA.&amp;lt;ref&amp;gt;PMID:2065661&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL6B_YEAST RL6B_YEAST]] Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS9A_YEAST RS9A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS14A_YEAST RS14A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL5_YEAST RL5_YEAST]] Binds 5S RNA and is required for 60S subunit assembly. [[http://www.uniprot.org/uniprot/RL25_YEAST RL25_YEAST]] This protein binds to a specific region on the 26S rRNA. [[http://www.uniprot.org/uniprot/RL11A_YEAST RL11A_YEAST]] Binds to 5S ribosomal RNA. [[http://www.uniprot.org/uniprot/RS21A_YEAST RS21A_YEAST]] Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.&amp;lt;ref&amp;gt;PMID:14627813&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS6A_YEAST RS6A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS15_YEAST RS15_YEAST]] Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm.&amp;lt;ref&amp;gt;PMID:15167894&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS2_YEAST RS2_YEAST]] Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&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;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&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;== Publication Abstract from PubMed ==&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;Inhibitory codon pairs and poly(A) tracts within the translated mRNA cause ribosome stalling and reduce protein output. The molecular mechanisms that drive these stalling events, however, are still unknown. Here, we use a combination of in vitro biochemistry, ribosome profiling, and cryo-EM to define molecular mechanisms that lead to these ribosome stalls. First, we use an in vitro reconstituted yeast translation system to demonstrate that inhibitory codon pairs slow elongation rates which are partially rescued by increased tRNA concentration or by an artificial tRNA not dependent on wobble base-pairing. Ribosome profiling data extend these observations by revealing that paused ribosomes with empty A sites are enriched on these sequences. Cryo-EM structures of stalled ribosomes provide a structural explanation for the observed effects by showing decoding-incompatible conformations of mRNA in the A sites of all studied stall- and collision-inducing sequences. Interestingly, in the case of poly(A) tracts, the inhibitory conformation of the mRNA in the A site involves a nucleotide stacking array. Together, these data demonstrate a novel mRNA-induced mechanisms of translational stalling in eukaryotic ribosomes.&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;Molecular mechanism of translational stalling by inhibitory codon combinations and poly(A) tracts.,Tesina P, Lessen LN, Buschauer R, Cheng J, Wu CC, Berninghausen O, Buskirk AR, Becker T, Beckmann R, Green R EMBO J. 2019 Dec 20:e103365. doi: 10.15252/embj.2019103365. PMID:31858614&amp;lt;ref&amp;gt;PMID:31858614&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;From MEDLINE&amp;amp;reg;/PubMed&amp;amp;reg;, a database of the U.S. National Library of Medicine.&amp;lt;br&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;lt;/div&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;lt;div class=&amp;quot;pdbe-citations 6t7t&amp;quot; style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&amp;lt;/div&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;==See Also==&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;*[[Ribosome 3D structures|Ribosome 3D structures]]&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;== 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>Wed, 01 Jan 2020 12:17:37 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
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			<title>OCA at 09:19, 25 December 2019</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3132552&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 09:19, 25 December 2019&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;'''Unreleased structure'''&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: #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: #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;The entry &lt;/del&gt;6t7t is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ON HOLD &lt;/del&gt; &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;until Paper Publication&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;==Structure of yeast 80S ribosome stalled on poly(A) tract.==&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;&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;&amp;lt;StructureSection load='&lt;/ins&gt;6t7t&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;' size='340' side='right'caption='[[6t7t]], [[Resolution|resolution]] 3.10&amp;amp;Aring;' scene=''&amp;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: #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;Authors&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;== Structural highlights ==&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;&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;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[6t7t]] &lt;/ins&gt;is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;a 82 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7T OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7T FirstGlance]. &amp;lt;br&amp;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: #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;Description&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;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7t OCA], [http://pdbe.org/6t7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7t RCSB], [http://www.ebi.ac.uk/pdbsum/6t7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7t ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;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: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Unreleased 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;&amp;lt;/table&amp;gt;&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;== Function ==&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/GBLP_YEAST GBLP_YEAST]] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.&amp;lt;ref&amp;gt;PMID:15340087&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS31_YEAST RS31_YEAST]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS19A_YEAST RS19A_YEAST]] Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.&amp;lt;ref&amp;gt;PMID:16159874&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:17726054&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL37A_YEAST RL37A_YEAST]] Binds to the 23S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RL40A_YEAST RL40A_YEAST]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  60S ribosomal protein L40-A: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eL40 is essential for translation of a subset of cellular transcripts, including stress response transcripts, such as DDR2 (PubMed:23169626).&amp;lt;ref&amp;gt;PMID:23169626&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS18A_YEAST RS18A_YEAST]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/RS7A_YEAST RS7A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS27A_YEAST RS27A_YEAST]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).  40S ribosomal protein S31 is a component of the 40S subunit of the ribosome (By similarity). [[http://www.uniprot.org/uniprot/RL4A_YEAST RL4A_YEAST]] Participates in the regulation of the accumulation of its own mRNA.&amp;lt;ref&amp;gt;PMID:2065661&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL6B_YEAST RL6B_YEAST]] Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.&amp;lt;ref&amp;gt;PMID:22096102&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS9A_YEAST RS9A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS14A_YEAST RS14A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL5_YEAST RL5_YEAST]] Binds 5S RNA and is required for 60S subunit assembly. [[http://www.uniprot.org/uniprot/RL25_YEAST RL25_YEAST]] This protein binds to a specific region on the 26S rRNA. [[http://www.uniprot.org/uniprot/RL11A_YEAST RL11A_YEAST]] Binds to 5S ribosomal RNA. [[http://www.uniprot.org/uniprot/RS21A_YEAST RS21A_YEAST]] Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.&amp;lt;ref&amp;gt;PMID:14627813&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS6A_YEAST RS6A_YEAST]] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS15_YEAST RS15_YEAST]] Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm.&amp;lt;ref&amp;gt;PMID:15167894&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RS2_YEAST RS2_YEAST]] Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.&amp;lt;ref&amp;gt;PMID:15590835&amp;lt;/ref&amp;gt; &lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;== References ==&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;references/&amp;gt;&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;__TOC__&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/StructureSection&amp;gt;&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category&lt;/ins&gt;: &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Large Structures]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Saccharomyces cerevisiae]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category&lt;/ins&gt;: &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Becker, R]]&lt;/ins&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;[[Category: &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Beckmann, R]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Berninghausen, O]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Buschauer, R]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Cheng, J]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Tesina, P]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Stalling dicodon codon pair]]&lt;/ins&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;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Translation&lt;/ins&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 25 Dec 2019 09:19:29 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
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			<title>OCA at 05:09, 6 November 2019</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3105081&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 05:09, 6 November 2019&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: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;'''Unreleased 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;'''Unreleased 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;/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: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The entry 6t7t is ON HOLD &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 entry 6t7t is ON HOLD &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; until Paper Publication&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;/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;Authors: &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;Authors: &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 06 Nov 2019 05:09:07 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
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			<title>OCA: Protected &quot;6t7t&quot; [edit=sysop:move=sysop]</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3102532&amp;oldid=prev</link>
			<description>&lt;p&gt;Protected &amp;quot;&lt;a href=&quot;/wiki/index.php/6t7t&quot; title=&quot;6t7t&quot;&gt;6t7t&lt;/a&gt;&amp;quot; [edit=sysop:move=sysop]&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 07:31, 30 October 2019&lt;/td&gt;
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			<pubDate>Wed, 30 Oct 2019 07:31:17 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
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			<title>OCA: New page: '''Unreleased structure'''  The entry 6t7t is ON HOLD   Authors:   Description:  Category: Unreleased Structures</title>
			<link>http://52.214.119.220/wiki/index.php?title=6t7t&amp;diff=3102531&amp;oldid=prev</link>
			<description>&lt;p&gt;New page: '''Unreleased structure'''  The entry 6t7t is ON HOLD   Authors:   Description:  &lt;a href=&quot;/wiki/index.php/Category:Unreleased_Structures&quot; title=&quot;Category:Unreleased Structures&quot;&gt;Category: Unreleased Structures&lt;/a&gt;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;'''Unreleased structure'''&lt;br /&gt;
&lt;br /&gt;
The entry 6t7t is ON HOLD &lt;br /&gt;
&lt;br /&gt;
Authors: &lt;br /&gt;
&lt;br /&gt;
Description: &lt;br /&gt;
[[Category: Unreleased Structures]]&lt;/div&gt;</description>
			<pubDate>Wed, 30 Oct 2019 07:31:15 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:6t7t</comments>		</item>
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