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	<title>Comments on: More new tricks: Thymus-specific proteasomes</title>
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	<link>http://www.iayork.com/MysteryRays/2007/06/27/more-new-tricks-thymus-specific-proteasomes/</link>
	<description>Meddling with things mankind is not meant to understand.  Also, pictures of my kids</description>
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		<title>By: Mystery Rays from Outer Space - Meddling with things mankind is not meant to understand. Also, pictures of my kids &#187; Proteasome subunit-dependent signaling in T cells?</title>
		<link>http://www.iayork.com/MysteryRays/2007/06/27/more-new-tricks-thymus-specific-proteasomes/comment-page-1/#comment-1210</link>
		<dc:creator>Mystery Rays from Outer Space - Meddling with things mankind is not meant to understand. Also, pictures of my kids &#187; Proteasome subunit-dependent signaling in T cells?</dc:creator>
		<pubDate>Thu, 24 Jan 2008 04:55:02 +0000</pubDate>
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		<description>[...] makes me wonder about the thymus-specific subunit that was recently identified. When that came out I found it hard to imagine that the very large effects associated with the knockout of this subunit could be explained by [...]</description>
		<content:encoded><![CDATA[<p>[...] makes me wonder about the thymus-specific subunit that was recently identified. When that came out I found it hard to imagine that the very large effects associated with the knockout of this subunit could be explained by [...]</p>
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		<title>By: Ubiquitin science on lake Garda &#171; Suicyte Notes</title>
		<link>http://www.iayork.com/MysteryRays/2007/06/27/more-new-tricks-thymus-specific-proteasomes/comment-page-1/#comment-121</link>
		<dc:creator>Ubiquitin science on lake Garda &#171; Suicyte Notes</dc:creator>
		<pubDate>Tue, 02 Oct 2007 22:31:12 +0000</pubDate>
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		<description>[...] The third day continued the &#8216;regulatory&#8217; session by a talk from Stefan Jentsch (MPI Martinsried). He was talking about recently published work on the sumoylation of PCNA and Rad52 in response to DNA double-strand breaks. It is known from previous work that PCNA ubiquitinatin regulates the switch from processive DNA polymerases to translesion repair polymerases, and the PCNA sumoylation competes with ubiquitination. According to Stefan, PCNA sumoylation acts as a &#8216;reset button&#8217; that facilitates new PCNA interactions. The sumoylation of Rad52 apparently plays a role in starting the &#8216;error free&#8217; repair pathway rather than the error-prone translesion synthesis. In the next talk, Maria Masucci (Karolinska, Stockholm) discussed the modulation of the ubiquitin pathway in Epstein-Barr virus infection. The GA-repeats in the EBNA1 proteins interfere with the proteasome and prevent EBNA1 degradation. In addition, the EBV and some other viruses appear to encode deubiquitinating enzymes that can be expected to mess up the cellular ubiquitin system. The last talk in this session was by Keiji Tanaka (Tokyo), who summarized his recently published data on a thymus-specific form of the proteasome. If you want to know more, read this blog entry on Mystery Rays. [...]</description>
		<content:encoded><![CDATA[<p>[...] The third day continued the &#8216;regulatory&#8217; session by a talk from Stefan Jentsch (MPI Martinsried). He was talking about recently published work on the sumoylation of PCNA and Rad52 in response to DNA double-strand breaks. It is known from previous work that PCNA ubiquitinatin regulates the switch from processive DNA polymerases to translesion repair polymerases, and the PCNA sumoylation competes with ubiquitination. According to Stefan, PCNA sumoylation acts as a &#8216;reset button&#8217; that facilitates new PCNA interactions. The sumoylation of Rad52 apparently plays a role in starting the &#8216;error free&#8217; repair pathway rather than the error-prone translesion synthesis. In the next talk, Maria Masucci (Karolinska, Stockholm) discussed the modulation of the ubiquitin pathway in Epstein-Barr virus infection. The GA-repeats in the EBNA1 proteins interfere with the proteasome and prevent EBNA1 degradation. In addition, the EBV and some other viruses appear to encode deubiquitinating enzymes that can be expected to mess up the cellular ubiquitin system. The last talk in this session was by Keiji Tanaka (Tokyo), who summarized his recently published data on a thymus-specific form of the proteasome. If you want to know more, read this blog entry on Mystery Rays. [...]</p>
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