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<channel>
	<title>Autophagy Archives - Laboratory Notes</title>
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	<link>https://www.laboratorynotes.com/tag/autophagy/</link>
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	<item>
		<title>Leucine</title>
		<link>https://www.laboratorynotes.com/leucine/</link>
					<comments>https://www.laboratorynotes.com/leucine/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 17 Sep 2026 21:06:17 +0000</pubDate>
				<category><![CDATA[Database]]></category>
		<category><![CDATA[Database: Gene/Protein]]></category>
		<category><![CDATA[Amino acid metabolism]]></category>
		<category><![CDATA[Anabolic resistance]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Branched-chain amino acids]]></category>
		<category><![CDATA[Energy metabolism]]></category>
		<category><![CDATA[Essential amino acids]]></category>
		<category><![CDATA[Exercise physiology]]></category>
		<category><![CDATA[Insulin signaling]]></category>
		<category><![CDATA[L-leucine]]></category>
		<category><![CDATA[Leucine]]></category>
		<category><![CDATA[Leucine metabolism]]></category>
		<category><![CDATA[mTOR]]></category>
		<category><![CDATA[mTORC1]]></category>
		<category><![CDATA[Muscle growth]]></category>
		<category><![CDATA[Muscle metabolism]]></category>
		<category><![CDATA[Muscle protein synthesis]]></category>
		<category><![CDATA[Nutrient sensing]]></category>
		<category><![CDATA[Protein synthesis]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30323</guid>

					<description><![CDATA[<p>Leucine is an essential branched-chain amino acid that supports protein synthesis and muscle metabolism while also acting as a nutrient signal. Explore its roles in mTORC1 signaling, BCAA metabolism, energy metabolism, autophagy, exercise, aging, and metabolic health.</p>
<p>The post <a href="https://www.laboratorynotes.com/leucine/">Leucine</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Branched-Chain Amino Acid</title>
		<link>https://www.laboratorynotes.com/branched-chain-amino-acid/</link>
					<comments>https://www.laboratorynotes.com/branched-chain-amino-acid/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Wed, 02 Sep 2026 19:24:40 +0000</pubDate>
				<category><![CDATA[Database: Chemical]]></category>
		<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Biochemistry]]></category>
		<category><![CDATA[Amino acid metabolism]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Branched-chain amino acids]]></category>
		<category><![CDATA[Energy metabolism]]></category>
		<category><![CDATA[Essential amino acids]]></category>
		<category><![CDATA[Glucose metabolism]]></category>
		<category><![CDATA[Insulin signaling]]></category>
		<category><![CDATA[Isoleucine]]></category>
		<category><![CDATA[Leucine]]></category>
		<category><![CDATA[Metabolic health]]></category>
		<category><![CDATA[mTOR]]></category>
		<category><![CDATA[mTORC1]]></category>
		<category><![CDATA[Muscle growth]]></category>
		<category><![CDATA[Muscle metabolism]]></category>
		<category><![CDATA[Muscle protein synthesis]]></category>
		<category><![CDATA[Nitrogen metabolism]]></category>
		<category><![CDATA[Nutrient sensing]]></category>
		<category><![CDATA[Protein synthesis]]></category>
		<category><![CDATA[Valine]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30327</guid>

					<description><![CDATA[<p>Branched-chain amino acids (BCAAs) are the essential amino acids leucine, isoleucine, and valine. They play important roles in protein synthesis, muscle metabolism, energy production, nutrient sensing, mTOR signaling, nitrogen metabolism, exercise physiology, and metabolic health.</p>
<p>The post <a href="https://www.laboratorynotes.com/branched-chain-amino-acid/">Branched-Chain Amino Acid</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Protein Ubiquitination</title>
		<link>https://www.laboratorynotes.com/protein-ubiquitination/</link>
					<comments>https://www.laboratorynotes.com/protein-ubiquitination/#comments</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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			</item>
		<item>
		<title>Programmed Cell Death</title>
		<link>https://www.laboratorynotes.com/programmed-cell-death/</link>
					<comments>https://www.laboratorynotes.com/programmed-cell-death/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sat, 29 Aug 2026 09:14:14 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Apoptosis]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[Ferroptosis]]></category>
		<category><![CDATA[Necroptosis]]></category>
		<category><![CDATA[Programmed cell death]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Pyroptosis]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30054</guid>

					<description><![CDATA[<p>Programmed cell death (PCD) is a regulated biological process that eliminates damaged or unnecessary cells through apoptosis, autophagic cell death and regulated necrosis. By maintaining tissue homeostasis and supporting stress adaptation, PCD is essential for development and long‑term organismal health.</p>
<p>The post <a href="https://www.laboratorynotes.com/programmed-cell-death/">Programmed Cell Death</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Protein Misfolding</title>
		<link>https://www.laboratorynotes.com/protein-misfolding/</link>
					<comments>https://www.laboratorynotes.com/protein-misfolding/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 27 Aug 2026 18:20:27 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cancer Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cell biology]]></category>
		<category><![CDATA[Molecular chaperones]]></category>
		<category><![CDATA[Protein aggregation]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[Protein folding]]></category>
		<category><![CDATA[Protein homeostasis]]></category>
		<category><![CDATA[Protein misfolding]]></category>
		<category><![CDATA[Protein quality control]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30038</guid>

					<description><![CDATA[<p>Protein misfolding occurs when proteins fail to achieve or maintain their correct three-dimensional structures. Explore its causes, cellular consequences, quality-control mechanisms, and connection to disease.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-misfolding/">Protein Misfolding</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Protein Synthesis and Degradation</title>
		<link>https://www.laboratorynotes.com/protein-synthesis-and-degradation/</link>
					<comments>https://www.laboratorynotes.com/protein-synthesis-and-degradation/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 27 Aug 2026 15:52:23 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[Protein turnover]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30027</guid>

					<description><![CDATA[<p>Protein homeostasis is the process by which cells maintain a balance between protein synthesis and degradation. This balance is essential for protein quality, cellular function, growth, adaptation, and survival.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-synthesis-and-degradation/">Protein Synthesis and Degradation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Autophagy</title>
		<link>https://www.laboratorynotes.com/autophagy/</link>
					<comments>https://www.laboratorynotes.com/autophagy/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 27 Aug 2026 14:41:02 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cancer Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Aging]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular recycling]]></category>
		<category><![CDATA[Immunity]]></category>
		<category><![CDATA[Lysosomes]]></category>
		<category><![CDATA[Neurodegeneration]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=30020</guid>

					<description><![CDATA[<p>Autophagy is the cell’s built‑in recycling system, removing damaged proteins and organelles to maintain health and survive stress. This article explains how autophagy works, its role in immunity, aging, and disease, and why it is essential for cellular balance.</p>
<p>The post <a href="https://www.laboratorynotes.com/autophagy/">Autophagy</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Proteostasis Network</title>
		<link>https://www.laboratorynotes.com/proteostasis-network/</link>
					<comments>https://www.laboratorynotes.com/proteostasis-network/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Wed, 26 Aug 2026 23:35:50 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[Chaperones]]></category>
		<category><![CDATA[ER stress]]></category>
		<category><![CDATA[Protein quality control]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29997</guid>

					<description><![CDATA[<p>The proteostasis network is an integrated system of chaperones, degradation pathways and organelle‑specific quality‑control mechanisms that maintains protein folding, stability and function. By coordinating refolding, repair and degradation, cells prevent proteotoxic stress and preserve homeostasis.</p>
<p>The post <a href="https://www.laboratorynotes.com/proteostasis-network/">Proteostasis Network</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Cellular Stress Response</title>
		<link>https://www.laboratorynotes.com/cellular-stress-response/</link>
					<comments>https://www.laboratorynotes.com/cellular-stress-response/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Wed, 26 Aug 2026 22:19:52 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[Heat shock proteins]]></category>
		<category><![CDATA[Homeostasis]]></category>
		<category><![CDATA[Oxidative stress]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Unfolded protein response]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29982</guid>

					<description><![CDATA[<p>Cellular stress responses are adaptive defence mechanisms that protect cells from environmental, metabolic and proteotoxic stress. By activating heat‑shock proteins, unfolded protein responses, antioxidant pathways and autophagy, cells restore homeostasis and maintain functional integrity under adverse conditions.</p>
<p>The post <a href="https://www.laboratorynotes.com/cellular-stress-response/">Cellular Stress Response</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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			</item>
		<item>
		<title>Protein Quality Control</title>
		<link>https://www.laboratorynotes.com/protein-quality-control/</link>
					<comments>https://www.laboratorynotes.com/protein-quality-control/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Wed, 26 Aug 2026 00:02:22 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular stress responses]]></category>
		<category><![CDATA[Chaperones]]></category>
		<category><![CDATA[Misfolded proteins]]></category>
		<category><![CDATA[Protein quality control]]></category>
		<category><![CDATA[Proteostasis]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29884</guid>

					<description><![CDATA[<p>Protein quality control (PQC) is a cellular surveillance system that preserves proteome integrity by monitoring protein folding, repairing misfolded proteins and eliminating damaged or aggregated species. Through coordinated action of chaperones, the ubiquitin–proteasome system and autophagy, PQC protects cells from proteotoxic stress and maintains homeostasis.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-quality-control/">Protein Quality Control</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>TRIM Family</title>
		<link>https://www.laboratorynotes.com/trim-family/</link>
					<comments>https://www.laboratorynotes.com/trim-family/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 23 Aug 2026 20:20:49 +0000</pubDate>
				<category><![CDATA[Database]]></category>
		<category><![CDATA[Database: Gene/Protein]]></category>
		<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Biology]]></category>
		<category><![CDATA[Lab Notes: Cancer Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Lab Notes: Immunology]]></category>
		<category><![CDATA[Antiviral defence]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Innate immunity]]></category>
		<category><![CDATA[Protein quality control]]></category>
		<category><![CDATA[RING ligases]]></category>
		<category><![CDATA[TRIM family]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29825</guid>

					<description><![CDATA[<p>The TRIM family is a large group of single‑chain RING finger ubiquitin ligases that regulate innate immunity, antiviral defence, autophagy, transcription and protein quality control. Defined by their tripartite motif—RING, B‑box and coiled‑coil domains—TRIM proteins use diverse C‑terminal regions to achieve precise substrate specificity. Their roles in immunity, development and cancer make them key regulators of cellular homeostasis.</p>
<p>The post <a href="https://www.laboratorynotes.com/trim-family/">TRIM Family</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>K63‑Linked Ubiquitination</title>
		<link>https://www.laboratorynotes.com/k63-linked-ubiquitination/</link>
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		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sat, 22 Aug 2026 15:03:04 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular stress response]]></category>
		<category><![CDATA[DNA damage response]]></category>
		<category><![CDATA[K63‑linked ubiquitination]]></category>
		<category><![CDATA[NF‑κB signalling]]></category>
		<category><![CDATA[Ubiquitin signalling]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29773</guid>

					<description><![CDATA[<p>K63‑linked ubiquitination is a non‑degradative signalling modification that assembles scaffold‑like ubiquitin chains regulating DNA repair, NF‑κB activation, receptor endocytosis and autophagy. Built by UBE2N/UBE2V1 and specialised E3 ligases, K63 chains coordinate dynamic cellular responses without targeting proteins for proteasomal degradation.</p>
<p>The post <a href="https://www.laboratorynotes.com/k63-linked-ubiquitination/">K63‑Linked Ubiquitination</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>Premature Ageing</title>
		<link>https://www.laboratorynotes.com/premature-ageing/</link>
					<comments>https://www.laboratorynotes.com/premature-ageing/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 20 Aug 2026 19:46:08 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Ageing]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular senescence]]></category>
		<category><![CDATA[Mitochondrial dysfunction]]></category>
		<category><![CDATA[Oxidative stress]]></category>
		<category><![CDATA[Telomere shortening]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29753</guid>

					<description><![CDATA[<p>Premature ageing describes the accelerated decline of cellular and physiological functions caused by genomic instability, telomere attrition, mitochondrial dysfunction and chronic inflammation. These processes activate ageing pathways earlier than expected, leading to early onset of tissue deterioration, reduced homeostasis and increased vulnerability to age‑related diseases.</p>
<p>The post <a href="https://www.laboratorynotes.com/premature-ageing/">Premature Ageing</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>Ageing</title>
		<link>https://www.laboratorynotes.com/ageing/</link>
					<comments>https://www.laboratorynotes.com/ageing/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 20 Aug 2026 19:20:48 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Lab Notes: Developmental Biology]]></category>
		<category><![CDATA[Ageing]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular senescence]]></category>
		<category><![CDATA[Mitochondrial dysfunction]]></category>
		<category><![CDATA[Telomere shortening]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29749</guid>

					<description><![CDATA[<p>Ageing is a gradual biological process driven by genomic instability, telomere shortening, mitochondrial dysfunction and cellular senescence. These changes reduce physiological resilience, impair tissue repair and increase susceptibility to chronic disease. Understanding the mechanisms of ageing provides insight into longevity, healthspan and the development of age‑related disorders.</p>
<p>The post <a href="https://www.laboratorynotes.com/ageing/">Ageing</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<title>Cellular Responses to Metabolic Stress During Nutrient Deprivation </title>
		<link>https://www.laboratorynotes.com/cellular-responses-to-metabolic-stress-during-nutrient-deprivation/</link>
					<comments>https://www.laboratorynotes.com/cellular-responses-to-metabolic-stress-during-nutrient-deprivation/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 20 Aug 2026 16:00:39 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[AMPK]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular homeostasis]]></category>
		<category><![CDATA[Metabolic stress]]></category>
		<category><![CDATA[Metabolism]]></category>
		<category><![CDATA[mTOR]]></category>
		<category><![CDATA[Nutrient deprivation]]></category>
		<category><![CDATA[Starvation response]]></category>
		<category><![CDATA[Stress signalling]]></category>
		<category><![CDATA[Transcriptional regulation]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29741</guid>

					<description><![CDATA[<p>Nutrient deprivation creates metabolic stress that suppresses mTOR, activates AMPK and induces autophagy. These pathways help cells conserve energy, recycle intracellular components and maintain homeostasis during starvation or limited nutrient availability. Prolonged nutrient deprivation influences gene expression, stress signalling and survival mechanisms across diverse cell types.</p>
<p>The post <a href="https://www.laboratorynotes.com/cellular-responses-to-metabolic-stress-during-nutrient-deprivation/">Cellular Responses to Metabolic Stress During Nutrient Deprivation </a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<title>Hydrolytic Enzymes in Cellular Homeostasis and Macromolecule Degradation</title>
		<link>https://www.laboratorynotes.com/hydrolytic-enzymes-in-cellular-homeostasis-and-macromolecule-degradation/</link>
					<comments>https://www.laboratorynotes.com/hydrolytic-enzymes-in-cellular-homeostasis-and-macromolecule-degradation/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 20 Aug 2026 13:09:47 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Biochemistry]]></category>
		<category><![CDATA[Lab Notes: Biology]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cellular homeostasis]]></category>
		<category><![CDATA[Digestion]]></category>
		<category><![CDATA[Glycosidases]]></category>
		<category><![CDATA[Hydrolytic enzyme]]></category>
		<category><![CDATA[Lipases]]></category>
		<category><![CDATA[Lysosomal hydrolases]]></category>
		<category><![CDATA[Metabolism]]></category>
		<category><![CDATA[Nucleases]]></category>
		<category><![CDATA[Proteases]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29736</guid>

					<description><![CDATA[<p>Hydrolytic enzymes catalyse the breakdown of macromolecules by adding water to chemical bonds. Found in lysosomes, digestive organs and immune cells, they degrade proteins, nucleic acids, lipids and carbohydrates. Their activity maintains cellular homeostasis, supports nutrient acquisition and protects against pathogens, while dysregulation contributes to metabolic and degenerative diseases.</p>
<p>The post <a href="https://www.laboratorynotes.com/hydrolytic-enzymes-in-cellular-homeostasis-and-macromolecule-degradation/">Hydrolytic Enzymes in Cellular Homeostasis and Macromolecule Degradation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>Autophagosome</title>
		<link>https://www.laboratorynotes.com/autophagosome/</link>
					<comments>https://www.laboratorynotes.com/autophagosome/#comments</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 20 Aug 2026 12:49:39 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagosome]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cancer biology]]></category>
		<category><![CDATA[Neurodegeneration]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29728</guid>

					<description><![CDATA[<p>Autophagosomes are double‑membrane vesicles that capture cytoplasmic material for lysosomal degradation. Formed from expanding phagophores and marked by LC3 lipidation, autophagosomes are central to autophagy, enabling cells to recycle nutrients, remove damaged organelles and maintain homeostasis. Their dysfunction contributes to neurodegenerative, metabolic and cancerous diseases.</p>
<p>The post <a href="https://www.laboratorynotes.com/autophagosome/">Autophagosome</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<title>Autophagy-Lysosome Pathway</title>
		<link>https://www.laboratorynotes.com/autophagy-lysosome-pathway/</link>
					<comments>https://www.laboratorynotes.com/autophagy-lysosome-pathway/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Thu, 13 Aug 2026 13:56:25 +0000</pubDate>
				<category><![CDATA[Lab Notes]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cancer research]]></category>
		<category><![CDATA[Lysosome]]></category>
		<category><![CDATA[Neurodegenerative disease]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=29089</guid>

					<description><![CDATA[<p>The autophagy-lysosome pathway is the cell's primary degradation and recycling system, responsible for clearing damaged proteins, dysfunctional organelles, and intracellular pathogens. Dysfunction in this pathway has been linked to neurodegenerative disorders, cancer, and metabolic syndromes. This article explores how the process works, its role in disease prevention, and emerging therapeutic strategies targeting this vital cellular mechanism.</p>
<p>The post <a href="https://www.laboratorynotes.com/autophagy-lysosome-pathway/">Autophagy-Lysosome Pathway</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>Protein Degradation</title>
		<link>https://www.laboratorynotes.com/protein-degradation/</link>
					<comments>https://www.laboratorynotes.com/protein-degradation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Sun, 02 Aug 2026 16:57:52 +0000</pubDate>
				<category><![CDATA[Lab Notes: Biochemistry]]></category>
		<category><![CDATA[Lab Notes: Cell Biology]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[Cyclins]]></category>
		<category><![CDATA[E3 ubiquitin ligase]]></category>
		<category><![CDATA[Proteasome]]></category>
		<category><![CDATA[Protein degradation]]></category>
		<category><![CDATA[Ubiquitin]]></category>
		<category><![CDATA[Ubiquitin-Proteasome system]]></category>
		<category><![CDATA[Ubiquitination]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=28434</guid>

					<description><![CDATA[<p>Protein degradation is a vital cellular process that removes damaged or unnecessary proteins to maintain homeostasis. This article explains the ubiquitin–proteasome system, autophagy, and their roles in cellular regulation and disease.</p>
<p>The post <a href="https://www.laboratorynotes.com/protein-degradation/">Protein Degradation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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		<item>
		<title>Picric Acid [C6H3N3O7] Molecular Weight Calculation</title>
		<link>https://www.laboratorynotes.com/picric-acid-c6h3n3o7-molecular-weight-calculation/</link>
					<comments>https://www.laboratorynotes.com/picric-acid-c6h3n3o7-molecular-weight-calculation/#respond</comments>
		
		<dc:creator><![CDATA[admin]]></dc:creator>
		<pubDate>Wed, 11 Jan 2023 01:20:36 +0000</pubDate>
				<category><![CDATA[Database: Molecular Weight Calculations]]></category>
		<category><![CDATA[Lab Notes: Laboratory Calculations]]></category>
		<category><![CDATA[Autophagy]]></category>
		<category><![CDATA[C6H3N3O7]]></category>
		<category><![CDATA[Carbon (c)]]></category>
		<category><![CDATA[Hydrogen (H)]]></category>
		<category><![CDATA[Nitrogen (N)]]></category>
		<category><![CDATA[Oxygen (O)]]></category>
		<guid isPermaLink="false">https://www.laboratorynotes.com/?p=11033</guid>

					<description><![CDATA[<p>Picric acid (C6H3N3O7) is an organic compound of four elements: Carbon, Hydrogen, Nitrogen, and Oxygen. The molecular weight of Picric acid is 229.10422 which can be calculated by adding up the total weight (atomic weight multiplied by their number) of all its elements.</p>
<p>The post <a href="https://www.laboratorynotes.com/picric-acid-c6h3n3o7-molecular-weight-calculation/">Picric Acid [C6H3N3O7] Molecular Weight Calculation</a> appeared first on <a href="https://www.laboratorynotes.com">Laboratory Notes</a>.</p>
]]></description>
		
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