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	<title>Cell cycle regulation Archives - Laboratory Notes</title>
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		<title>Post-Translational Modifications in Cell-Cycle Regulation</title>
		<link>https://www.laboratorynotes.com/post-translational-modifications-in-cell-cycle-regulation/</link>
					<comments>https://www.laboratorynotes.com/post-translational-modifications-in-cell-cycle-regulation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Mon, 31 Aug 2026 09:29:07 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cancer Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Acetylation]]></category>
		<category><![CDATA[Cancer biology]]></category>
		<category><![CDATA[CDKs]]></category>
		<category><![CDATA[Cell cycle]]></category>
		<category><![CDATA[Cell cycle regulation]]></category>
		<category><![CDATA[Cyclins]]></category>
		<category><![CDATA[DNA damage response]]></category>
		<category><![CDATA[Methylation]]></category>
		<category><![CDATA[Mitosis]]></category>
		<category><![CDATA[Molecular biology]]></category>
		<category><![CDATA[Phosphorylation]]></category>
		<category><![CDATA[Post-translational modifications]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[SUMOylation]]></category>
		<category><![CDATA[Ubiquitination]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30113</guid>

					<description><![CDATA[<p>Post-translational modifications are essential regulators of cell-cycle progression. Learn how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and other PTMs control CDKs, cyclins, checkpoints, DNA replication, mitosis, and protein degradation.</p>
<p>The post <a href="https://www.laboratorynotes.com/post-translational-modifications-in-cell-cycle-regulation/">Post-Translational Modifications in Cell-Cycle Regulation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
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		<title>Timed Proteolysis as a Molecular Engine of Cell-Cycle Progression: Key Proteins Whose Degradation Drives Cell-Cycle Transitions</title>
		<link>https://www.laboratorynotes.com/timed-proteolysis-as-a-molecular-engine-of-cell-cycle-progression-key-proteins-whose-degradation-drives-cell-cycle-transitions/</link>
					<comments>https://www.laboratorynotes.com/timed-proteolysis-as-a-molecular-engine-of-cell-cycle-progression-key-proteins-whose-degradation-drives-cell-cycle-transitions/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sat, 22 Aug 2026 23:12:32 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cancer Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cancer biology]]></category>
		<category><![CDATA[Cell cycle]]></category>
		<category><![CDATA[Cell cycle regulation]]></category>
		<category><![CDATA[Cyclins]]></category>
		<category><![CDATA[Mitosis]]></category>
		<category><![CDATA[Proteasome]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[Ubiquitin]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29803</guid>

					<description><![CDATA[<p>Timely protein degradation is essential for orderly cell-cycle progression. Explore key cell-cycle regulators, their degradation mechanisms, and how their turnover controls G1/S transition, mitosis, chromosome segregation and mitotic exit.</p>
<p>The post <a href="https://www.laboratorynotes.com/timed-proteolysis-as-a-molecular-engine-of-cell-cycle-progression-key-proteins-whose-degradation-drives-cell-cycle-transitions/">Timed Proteolysis as a Molecular Engine of Cell-Cycle Progression: Key Proteins Whose Degradation Drives Cell-Cycle Transitions</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Mdm2 (Mouse Double Minute 2 Homologue)</title>
		<link>https://www.laboratorynotes.com/mdm2-mouse-double-minute-2-homologue/</link>
					<comments>https://www.laboratorynotes.com/mdm2-mouse-double-minute-2-homologue/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Fri, 21 Aug 2026 11:51:23 +0000</pubDate>
				<category><![CDATA[Database]]></category>
		<category><![CDATA[Database: Gene/Protein]]></category>
		<category><![CDATA[Cell cycle regulation]]></category>
		<category><![CDATA[DNA damage response]]></category>
		<category><![CDATA[Oncogenesis]]></category>
		<category><![CDATA[Ubiquitin signalling]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29798</guid>

					<description><![CDATA[<p>Mdm2 is a RING‑type E3 ubiquitin ligase that controls p53 stability through ubiquitination, nuclear export and proteasomal degradation. By interacting with p53, Mdmx/Mdm4 and ARF, Mdm2 regulates DNA‑damage responses, cell‑cycle progression and oncogenesis, making it a central determinant of tumour development and genome stability.</p>
<p>The post <a href="https://www.laboratorynotes.com/mdm2-mouse-double-minute-2-homologue/">Mdm2 (Mouse Double Minute 2 Homologue)</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>K48‑Linked Ubiquitination</title>
		<link>https://www.laboratorynotes.com/k48-linked-ubiquitination/</link>
					<comments>https://www.laboratorynotes.com/k48-linked-ubiquitination/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 20 Aug 2026 22:13:18 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cell cycle regulation]]></category>
		<category><![CDATA[DNA damage response]]></category>
		<category><![CDATA[K48‑linked ubiquitination]]></category>
		<category><![CDATA[Polyubiquitin chain]]></category>
		<category><![CDATA[Proteasomal degradation]]></category>
		<category><![CDATA[Protein turnover]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Ubiquitin signalling]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29770</guid>

					<description><![CDATA[<p>K48‑linked ubiquitination is the principal degradation signal in eukaryotic cells, directing proteins to the 26S proteasome. Built by E1, E2 and E3 enzymes, K48‑linked chains regulate protein turnover, cell‑cycle progression and DNA‑damage responses, forming a central mechanism for maintaining proteostasis and preventing toxic protein accumulation.</p>
<p>The post <a href="https://www.laboratorynotes.com/k48-linked-ubiquitination/">K48‑Linked Ubiquitination</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>RING Finger Ubiquitin Ligase</title>
		<link>https://www.laboratorynotes.com/ring-finger-ubiquitin-ligase/</link>
					<comments>https://www.laboratorynotes.com/ring-finger-ubiquitin-ligase/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Fri, 22 Aug 2025 19:39:42 +0000</pubDate>
				<category><![CDATA[Database: Enzyme]]></category>
		<category><![CDATA[Lab Notes: Cancer Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Cell cycle regulation]]></category>
		<category><![CDATA[DNA repair]]></category>
		<category><![CDATA[Neurodegeneration]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[RING ligases]]></category>
		<category><![CDATA[Ubiquitination]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=24043</guid>

					<description><![CDATA[<p>RING finger ubiquitin ligases are the largest class of E3 enzymes in the ubiquitin–proteasome system, defined by a zinc‑binding cross‑brace RING domain that positions E2~Ub for direct ubiquitin transfer. They regulate essential cellular processes including cell cycle progression, DNA repair, immunity, and neuronal function. Dysregulation of RING and RBR ligases such as MDM2 and Parkin contributes to cancer and neurodegeneration, while modern PROTAC therapeutics harness CRL4^CRBN and CRL2^VHL complexes to redirect ubiquitination toward disease‑associated proteins. </p>
<p>The post <a href="https://www.laboratorynotes.com/ring-finger-ubiquitin-ligase/">RING Finger Ubiquitin Ligase</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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