Neurodegeneration Archives - Laboratory Notes https://www.laboratorynotes.com/tag/neurodegeneration/ Wed, 23 Sep 2026 07:30:13 +0000 en hourly 1 https://wordpress.org/?v=7.1.2 Autophagy https://www.laboratorynotes.com/autophagy/ https://www.laboratorynotes.com/autophagy/#comments Thu, 27 Aug 2026 14:41:02 +0000 https://www.laboratorynotes.com/?p=30020 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.

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]]> https://www.laboratorynotes.com/autophagy/feed/ 1 Autophagosome https://www.laboratorynotes.com/autophagosome/ https://www.laboratorynotes.com/autophagosome/#comments Thu, 20 Aug 2026 12:49:39 +0000 https://www.laboratorynotes.com/?p=29728 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.

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]]> https://www.laboratorynotes.com/autophagosome/feed/ 2 RING Finger Ubiquitin Ligase https://www.laboratorynotes.com/ring-finger-ubiquitin-ligase/ https://www.laboratorynotes.com/ring-finger-ubiquitin-ligase/#comments Fri, 22 Aug 2025 19:39:42 +0000 https://www.laboratorynotes.com/?p=24043 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.

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