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	<title>ERAD Archives - Laboratory Notes</title>
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		<title>ATF6</title>
		<link>https://www.laboratorynotes.com/atf6/</link>
					<comments>https://www.laboratorynotes.com/atf6/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sat, 29 Aug 2026 09:58:21 +0000</pubDate>
				<category><![CDATA[Database]]></category>
		<category><![CDATA[Database: Gene/Protein]]></category>
		<category><![CDATA[ATF6]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[Chaperones]]></category>
		<category><![CDATA[ER stress]]></category>
		<category><![CDATA[ERAD]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Unfolded protein response]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30005</guid>

					<description><![CDATA[<p>ATF6 is an ER stress‑responsive transcription factor that enhances protein‑folding capacity and strengthens ER‑associated degradation. After trafficking to the Golgi and undergoing regulated proteolysis, ATF6 activates genes that restore ER proteostasis during unfolded protein accumulation.</p>
<p>The post <a href="https://www.laboratorynotes.com/atf6/">ATF6</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<title>Endoplasmic Reticulum Stress</title>
		<link>https://www.laboratorynotes.com/endoplasmic-reticulum-stress/</link>
					<comments>https://www.laboratorynotes.com/endoplasmic-reticulum-stress/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sat, 29 Aug 2026 09:50:51 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[ATF6]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[ER stress]]></category>
		<category><![CDATA[ERAD]]></category>
		<category><![CDATA[IRE1]]></category>
		<category><![CDATA[PERK]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Unfolded protein response]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29999</guid>

					<description><![CDATA[<p>ER stress arises when misfolded proteins accumulate in the endoplasmic reticulum, overwhelming its folding capacity. Through IRE1, PERK and ATF6 signalling, the unfolded protein response restores proteostasis, reduces protein load and protects cells from stress‑induced damage.</p>
<p>The post <a href="https://www.laboratorynotes.com/endoplasmic-reticulum-stress/">Endoplasmic Reticulum Stress</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
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		<title>Endoplasmic Reticulum Associated Degradation</title>
		<link>https://www.laboratorynotes.com/endoplasmic-reticulum-associated-degradation/</link>
					<comments>https://www.laboratorynotes.com/endoplasmic-reticulum-associated-degradation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 27 Aug 2026 00:18:51 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[Chaperones]]></category>
		<category><![CDATA[ER stress]]></category>
		<category><![CDATA[ERAD]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<category><![CDATA[Unfolded protein response]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30007</guid>

					<description><![CDATA[<p>ERAD is a central ER quality‑control pathway that recognises misfolded proteins, retrotranslocates them to the cytosol, ubiquitinates them and directs them to the proteasome. By preventing proteotoxic accumulation, ERAD preserves ER homeostasis and supports cellular proteostasis.</p>
<p>The post <a href="https://www.laboratorynotes.com/endoplasmic-reticulum-associated-degradation/">Endoplasmic Reticulum Associated Degradation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
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		<title>Unfolded Protein Response</title>
		<link>https://www.laboratorynotes.com/unfolded-protein-response/</link>
					<comments>https://www.laboratorynotes.com/unfolded-protein-response/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Wed, 26 Aug 2026 23:29:46 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[ATF6]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[ER stress]]></category>
		<category><![CDATA[ERAD]]></category>
		<category><![CDATA[IRE1]]></category>
		<category><![CDATA[PERK]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Unfolded protein response]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29995</guid>

					<description><![CDATA[<p>The unfolded protein response (UPR) is a conserved ER stress pathway that detects misfolded proteins and restores proteostasis. Through IRE1, PERK and ATF6 signalling, cells expand folding capacity, reduce protein load and maintain homeostasis under conditions of ER stress.</p>
<p>The post <a href="https://www.laboratorynotes.com/unfolded-protein-response/">Unfolded Protein Response</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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