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	<title>Post-translational modification Archives - Laboratory Notes</title>
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		<title>Protein S-Glutathionylation</title>
		<link>https://www.laboratorynotes.com/protein-s-glutathionylation/</link>
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		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 30 Aug 2026 15:43:02 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cancer biology]]></category>
		<category><![CDATA[Cysteine modification]]></category>
		<category><![CDATA[Deglutathionylation]]></category>
		<category><![CDATA[Glutaredoxin]]></category>
		<category><![CDATA[Glutathione]]></category>
		<category><![CDATA[Inflammation]]></category>
		<category><![CDATA[Mitochondrial biology]]></category>
		<category><![CDATA[Oxidative stress]]></category>
		<category><![CDATA[Post-translational modification]]></category>
		<category><![CDATA[Protein S-Glutathionylation]]></category>
		<category><![CDATA[Redox biology]]></category>
		<category><![CDATA[Redox signaling]]></category>
		<category><![CDATA[S-Glutathiolation]]></category>
		<category><![CDATA[S-Glutathionylation]]></category>
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					<description><![CDATA[<p>Protein S-glutathionylation is a reversible cysteine modification that connects glutathione metabolism with redox signaling, oxidative stress responses, protein function, mitochondrial biology and disease.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-s-glutathionylation/">Protein S-Glutathionylation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
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		<title>Protein Formylation</title>
		<link>https://www.laboratorynotes.com/protein-formylation/</link>
					<comments>https://www.laboratorynotes.com/protein-formylation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 30 Aug 2026 13:01:15 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Bacterial pathogenesis]]></category>
		<category><![CDATA[Bacterial protein synthesis]]></category>
		<category><![CDATA[Formyl peptide receptors]]></category>
		<category><![CDATA[Formylation]]></category>
		<category><![CDATA[Inflammation]]></category>
		<category><![CDATA[Innate immunity]]></category>
		<category><![CDATA[Methionyl-tRNA formyltransferase]]></category>
		<category><![CDATA[Molecular biology]]></category>
		<category><![CDATA[N-formylmethionine]]></category>
		<category><![CDATA[Peptide deformylase]]></category>
		<category><![CDATA[Post-translational modification]]></category>
		<category><![CDATA[Protein formylation]]></category>
		<category><![CDATA[Protein maturation]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30164</guid>

					<description><![CDATA[<p>Protein formylation is a chemical modification involved in bacterial and mitochondrial protein synthesis, protein maturation, innate immunity, inflammation and cellular signaling.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-formylation/">Protein Formylation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
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		<title>Lysine Malonylation</title>
		<link>https://www.laboratorynotes.com/lysine-malonylation/</link>
					<comments>https://www.laboratorynotes.com/lysine-malonylation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 30 Aug 2026 12:15:10 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Biochemistry]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cancer biology]]></category>
		<category><![CDATA[Demalonylation]]></category>
		<category><![CDATA[Epigenetics]]></category>
		<category><![CDATA[Histone malonylation]]></category>
		<category><![CDATA[Lysine acylation]]></category>
		<category><![CDATA[Lysine malonylation]]></category>
		<category><![CDATA[Malonyl-CoA]]></category>
		<category><![CDATA[Metabolic disease]]></category>
		<category><![CDATA[Metabolism]]></category>
		<category><![CDATA[Mitochondrial biology]]></category>
		<category><![CDATA[Molecular biology]]></category>
		<category><![CDATA[Post-translational modification]]></category>
		<category><![CDATA[Protein malonylation]]></category>
		<category><![CDATA[Protein regulation]]></category>
		<category><![CDATA[SIRT5]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30159</guid>

					<description><![CDATA[<p>Lysine malonylation is a metabolic post-translational modification that connects malonyl-CoA metabolism with protein function, mitochondrial activity, epigenetic regulation and cellular homeostasis.</p>
<p>The post <a href="https://www.laboratorynotes.com/lysine-malonylation/">Lysine Malonylation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
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		<title>Protein Lactylation</title>
		<link>https://www.laboratorynotes.com/protein-lactylation/</link>
					<comments>https://www.laboratorynotes.com/protein-lactylation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 30 Aug 2026 11:46:09 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cancer biology]]></category>
		<category><![CDATA[Cellular metabolism]]></category>
		<category><![CDATA[Epigenetics]]></category>
		<category><![CDATA[Gene expression]]></category>
		<category><![CDATA[Histone lactylation]]></category>
		<category><![CDATA[Inflammation]]></category>
		<category><![CDATA[Lactate metabolism]]></category>
		<category><![CDATA[Lactylation]]></category>
		<category><![CDATA[Lysine lactylation]]></category>
		<category><![CDATA[Macrophages]]></category>
		<category><![CDATA[Molecular biology]]></category>
		<category><![CDATA[Post-translational modification]]></category>
		<category><![CDATA[Protein lactylation]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30157</guid>

					<description><![CDATA[<p>Protein lactylation is an emerging post-translational modification that connects lactate metabolism with protein regulation, gene expression, inflammation, cellular signaling and disease.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-lactylation/">Protein Lactylation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
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			</item>
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		<title>Protein Ubiquitination</title>
		<link>https://www.laboratorynotes.com/protein-ubiquitination/</link>
					<comments>https://www.laboratorynotes.com/protein-ubiquitination/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 30 Aug 2026 10:34:07 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular homeostasis]]></category>
		<category><![CDATA[DNA damage response]]></category>
		<category><![CDATA[E3 ubiquitin ligases]]></category>
		<category><![CDATA[Molecular biology]]></category>
		<category><![CDATA[Post-translational modification]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[Protein ubiquitination]]></category>
		<category><![CDATA[Ubiquitin]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30155</guid>

					<description><![CDATA[<p>Protein ubiquitination is a fundamental post-translational modification that regulates protein degradation, cellular signaling, DNA repair, autophagy, protein trafficking and cellular homeostasis.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-ubiquitination/">Protein Ubiquitination</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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